path: root/plip/test/pdb/4rao.pdb

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-SEP-14   4RAO              
TITLE     AZA-ACYCLIC NUCLEOSIDE PHOSPHONATES CONTAINING A SECOND PHOSPHONATE   
TITLE    2 GROUP AS INHIBITORS OF THE HUMAN, PLASMODIUM FALCIPARUM AND VIVAX 6- 
TITLE    3 OXOPURINE PHOSPHORIBOSYLTRANSFERASES AND THEIR PRO-DRUGS AS          
TITLE    4 ANTIMALARIAL AGENTS                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE;            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HGPRT, HGPRTASE;                                            
COMPND   5 EC: 2.4.2.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HPRT1, HPRT;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    6-OXOPURINE PHOSPHORIBOSYLTRANSFERASE, 9-[(N-PHOSPHONOETHYL-N-        
KEYWDS   2 PHOSPHONOETHOXYETHYL)-2-AMINOETHYL]HYPOXANTHINE, CYTOPLASMIC,        
KEYWDS   3 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.T.KEOUGH,D.HOCKOV,Z.JANEBA,T-H.WANG,L.NAESENS,M.D.EDSTEIN,          
AUTHOR   2 M.CHAVCHICH,L.W.GUDDAT                                               
REVDAT   1   07-JAN-15 4RAO    0                                                
JRNL        AUTH   D.T.KEOUGH,D.HOCKOVA,Z.JANEBA,T.WANG,L.NAESENS,M.D.EDSTEIN,  
JRNL        AUTH 2 M.CHAVCHICH,L.W.GUDDAT                                       
JRNL        TITL   AZA-ACYCLIC NUCLEOSIDE PHOSPHONATES CONTAINING A SECOND      
JRNL        TITL 2 PHOSPHONATE GROUP AS INHIBITORS OF THE HUMAN, PLASMODIUM     
JRNL        TITL 3 FALCIPARUM AND VIVAX 6-OXOPURINE PHOSPHORIBOSYLTRANSFERASES  
JRNL        TITL 4 AND THEIR PRODRUGS AS ANTIMALARIAL AGENTS.                   
JRNL        REF    J.MED.CHEM.                                2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25494538                                                     
JRNL        DOI    10.1021/JM501416T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 68117                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 35.4134 -  4.5060    0.99     4936   149  0.1807 0.2057        
REMARK   3     2  4.5060 -  3.5776    1.00     4836   146  0.1615 0.1763        
REMARK   3     3  3.5776 -  3.1257    1.00     4767   145  0.1953 0.2231        
REMARK   3     4  3.1257 -  2.8400    1.00     4737   143  0.2116 0.2582        
REMARK   3     5  2.8400 -  2.6365    1.00     4706   143  0.2255 0.2502        
REMARK   3     6  2.6365 -  2.4811    1.00     4727   142  0.2233 0.2280        
REMARK   3     7  2.4811 -  2.3569    1.00     4713   143  0.2191 0.2645        
REMARK   3     8  2.3569 -  2.2543    1.00     4684   142  0.2253 0.2528        
REMARK   3     9  2.2543 -  2.1676    1.00     4694   142  0.2235 0.2826        
REMARK   3    10  2.1676 -  2.0928    1.00     4710   142  0.2168 0.2730        
REMARK   3    11  2.0928 -  2.0273    1.00     4653   141  0.2352 0.2856        
REMARK   3    12  2.0273 -  1.9694    1.00     4654   141  0.2295 0.2647        
REMARK   3    13  1.9694 -  1.9176    1.00     4669   141  0.2360 0.2575        
REMARK   3    14  1.9176 -  1.8710    0.99     4631   140  0.2623 0.2810        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.440           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           6832                                  
REMARK   3   ANGLE     :  1.222           9287                                  
REMARK   3   CHIRALITY :  0.078           1037                                  
REMARK   3   PLANARITY :  0.004           1170                                  
REMARK   3   DIHEDRAL  : 15.853           2652                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 1 through 24 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4722   2.5508  -3.4232              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2761 T22:   0.3888                                     
REMARK   3      T33:   0.1914 T12:  -0.0331                                     
REMARK   3      T13:   0.0513 T23:  -0.0546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9643 L22:   4.4104                                     
REMARK   3      L33:   1.8046 L12:  -1.1905                                     
REMARK   3      L13:   1.0296 L23:  -1.2136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3593 S12:   0.5049 S13:  -0.0274                       
REMARK   3      S21:  -0.2290 S22:  -0.3701 S23:  -0.2974                       
REMARK   3      S31:   0.0652 S32:   0.6322 S33:  -0.0160                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 25 through 37 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5740  15.0112  -2.1731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5345 T22:   0.3390                                     
REMARK   3      T33:   0.2732 T12:  -0.1146                                     
REMARK   3      T13:   0.0131 T23:   0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3478 L22:   9.3251                                     
REMARK   3      L33:   5.4894 L12:  -1.6751                                     
REMARK   3      L13:  -1.3368 L23:   2.9191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1374 S12:   0.4752 S13:   0.8809                       
REMARK   3      S21:  -0.2252 S22:   0.0174 S23:  -0.9703                       
REMARK   3      S31:  -1.4878 S32:   0.5679 S33:  -0.1024                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 38 through 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0299  -4.8692  13.7308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1921 T22:   0.2423                                     
REMARK   3      T33:   0.1793 T12:   0.0057                                     
REMARK   3      T13:   0.0041 T23:  -0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8229 L22:   3.0929                                     
REMARK   3      L33:   2.8758 L12:   1.0899                                     
REMARK   3      L13:   0.2587 L23:  -0.0075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1555 S12:  -0.0781 S13:   0.0165                       
REMARK   3      S21:   0.1337 S22:  -0.1202 S23:   0.0458                       
REMARK   3      S31:   0.0627 S32:   0.1012 S33:  -0.0399                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 87 through 100 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8742  -4.6966  22.3544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4573 T22:   0.3327                                     
REMARK   3      T33:   0.2715 T12:  -0.0363                                     
REMARK   3      T13:   0.0154 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3739 L22:   4.9720                                     
REMARK   3      L33:   0.0627 L12:   6.7926                                     
REMARK   3      L13:   0.7814 L23:   0.4067                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1087 S12:   0.0667 S13:  -0.3674                       
REMARK   3      S21:  -0.4185 S22:   0.1934 S23:  -0.1040                       
REMARK   3      S31:   0.0179 S32:   0.2954 S33:  -0.0951                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 101 through 152 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3619  -1.1903  21.8612              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2424 T22:   0.3030                                     
REMARK   3      T33:   0.1570 T12:  -0.0124                                     
REMARK   3      T13:  -0.0384 T23:  -0.0567                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9774 L22:   3.5114                                     
REMARK   3      L33:   8.1942 L12:   0.2834                                     
REMARK   3      L13:   2.3189 L23:  -2.3631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0385 S12:   0.0995 S13:   0.1632                       
REMARK   3      S21:   0.0202 S22:  -0.0321 S23:  -0.3284                       
REMARK   3      S31:   0.0388 S32:   0.4188 S33:   0.0812                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 153 through 216 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1693   6.2682   7.3597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2550 T22:   0.4224                                     
REMARK   3      T33:   0.2827 T12:  -0.0986                                     
REMARK   3      T13:   0.0189 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0134 L22:   3.7565                                     
REMARK   3      L33:   3.6492 L12:  -0.4347                                     
REMARK   3      L13:   0.0531 L23:  -0.8514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0897 S12:   0.0177 S13:   0.2839                       
REMARK   3      S21:   0.0164 S22:  -0.1132 S23:  -0.6065                       
REMARK   3      S31:  -0.3736 S32:   0.7221 S33:   0.0633                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 4 through 37 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7905  -9.3190  -7.9593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2025 T22:   0.3236                                     
REMARK   3      T33:   0.2550 T12:   0.0481                                     
REMARK   3      T13:   0.0364 T23:  -0.0647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6287 L22:   3.1423                                     
REMARK   3      L33:   3.0007 L12:   1.0484                                     
REMARK   3      L13:   0.3472 L23:  -1.0446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0960 S12:   0.3007 S13:  -0.3171                       
REMARK   3      S21:  -0.1329 S22:  -0.0124 S23:  -0.3755                       
REMARK   3      S31:   0.1412 S32:   0.4958 S33:  -0.0539                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 38 through 56 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1620   9.1215  -7.3183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2348 T22:   0.2147                                     
REMARK   3      T33:   0.2739 T12:  -0.0059                                     
REMARK   3      T13:  -0.0091 T23:   0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0545 L22:   6.2816                                     
REMARK   3      L33:   7.7011 L12:  -4.0601                                     
REMARK   3      L13:   2.7727 L23:  -2.8739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0759 S12:  -0.0991 S13:   0.3418                       
REMARK   3      S21:  -0.0425 S22:   0.2800 S23:   0.2201                       
REMARK   3      S31:  -0.6067 S32:  -0.3073 S33:  -0.1197                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid 57 through 87 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0721   5.0697  -6.7935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1976 T22:   0.1806                                     
REMARK   3      T33:   0.2866 T12:   0.0082                                     
REMARK   3      T13:  -0.0307 T23:   0.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2939 L22:   3.1853                                     
REMARK   3      L33:   4.5097 L12:   0.4367                                     
REMARK   3      L13:  -0.1908 L23:   0.9722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0591 S12:   0.0989 S13:   0.3597                       
REMARK   3      S21:  -0.1435 S22:  -0.0041 S23:   0.5650                       
REMARK   3      S31:  -0.4725 S32:  -0.0689 S33:  -0.0009                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid 88 through 100 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6201   5.4722  -8.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3285 T22:   0.2809                                     
REMARK   3      T33:   0.4418 T12:   0.0033                                     
REMARK   3      T13:  -0.0756 T23:   0.0819                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7080 L22:   6.5543                                     
REMARK   3      L33:   9.0136 L12:  -0.2897                                     
REMARK   3      L13:   0.5454 L23:   2.9229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0167 S12:   0.1832 S13:   0.6399                       
REMARK   3      S21:   0.1989 S22:  -0.1656 S23:   0.1336                       
REMARK   3      S31:  -0.4471 S32:  -0.2982 S33:   0.0286                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resid 101 through 127 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4581   1.0517 -17.8888              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4451 T22:   0.5360                                     
REMARK   3      T33:   0.7020 T12:  -0.0544                                     
REMARK   3      T13:  -0.1737 T23:   0.0758                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6249 L22:   4.2114                                     
REMARK   3      L33:   4.7536 L12:  -2.4673                                     
REMARK   3      L13:  -1.0265 L23:  -1.0321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3066 S12:   0.1490 S13:  -0.3129                       
REMARK   3      S21:   0.3123 S22:   0.3331 S23:   1.8742                       
REMARK   3      S31:   0.5098 S32:  -1.0567 S33:  -0.4721                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resid 128 through 165 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0289   2.8212 -20.8366              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3105 T22:   0.2046                                     
REMARK   3      T33:   0.2996 T12:  -0.0078                                     
REMARK   3      T13:  -0.1292 T23:   0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4033 L22:   3.3607                                     
REMARK   3      L33:   3.1928 L12:  -3.0711                                     
REMARK   3      L13:  -0.1955 L23:  -0.2494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0449 S12:   0.2226 S13:  -0.2503                       
REMARK   3      S21:  -0.4713 S22:   0.0433 S23:   0.6805                       
REMARK   3      S31:  -0.1652 S32:   0.0517 S33:  -0.0899                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'B' and (resid 166 through 179 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7217   3.5405 -22.9572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3020 T22:   0.2842                                     
REMARK   3      T33:   0.2183 T12:  -0.0475                                     
REMARK   3      T13:  -0.0280 T23:   0.0484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8428 L22:   3.4867                                     
REMARK   3      L33:   2.6575 L12:  -2.1537                                     
REMARK   3      L13:  -1.8438 L23:   1.4901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1121 S12:   0.2952 S13:   0.1938                       
REMARK   3      S21:  -0.1234 S22:   0.1184 S23:   0.0988                       
REMARK   3      S31:  -0.1890 S32:   0.0746 S33:   0.0474                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'B' and (resid 180 through 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7454 -13.7514 -12.7741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2674 T22:   0.2860                                     
REMARK   3      T33:   0.2342 T12:   0.0261                                     
REMARK   3      T13:   0.0026 T23:  -0.0712                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6259 L22:   6.6450                                     
REMARK   3      L33:   3.8025 L12:   1.7450                                     
REMARK   3      L13:   0.3382 L23:  -0.8431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0850 S12:   0.4215 S13:  -0.4131                       
REMARK   3      S21:  -0.4885 S22:   0.1456 S23:  -0.0432                       
REMARK   3      S31:   0.5445 S32:   0.0073 S33:  -0.0711                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'C' and (resid 4 through 17 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8002   5.2641  25.7419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4519 T22:   0.5025                                     
REMARK   3      T33:   0.5261 T12:  -0.1123                                     
REMARK   3      T13:   0.2360 T23:  -0.1521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4939 L22:   0.2716                                     
REMARK   3      L33:   4.0367 L12:  -0.7858                                     
REMARK   3      L13:  -1.2106 L23:   0.1507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2196 S12:  -0.1074 S13:  -0.3731                       
REMARK   3      S21:   1.2339 S22:  -0.6445 S23:   1.0583                       
REMARK   3      S31:  -0.1297 S32:  -0.6932 S33:   0.3067                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'C' and (resid 18 through 37 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2078  -8.0140  25.2309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4199 T22:   0.2999                                     
REMARK   3      T33:   0.3372 T12:  -0.1174                                     
REMARK   3      T13:   0.0404 T23:   0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5958 L22:   2.0855                                     
REMARK   3      L33:   5.3145 L12:   1.4540                                     
REMARK   3      L13:   1.9488 L23:   0.0979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4184 S12:  -0.3626 S13:  -0.5220                       
REMARK   3      S21:   0.4671 S22:  -0.1381 S23:   0.1603                       
REMARK   3      S31:   0.6002 S32:  -0.2884 S33:  -0.2772                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'C' and (resid 38 through 56 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5354  14.3474  13.8291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3400 T22:   0.2063                                     
REMARK   3      T33:   0.3313 T12:  -0.0001                                     
REMARK   3      T13:   0.1224 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7932 L22:   6.3044                                     
REMARK   3      L33:   3.8763 L12:   4.2064                                     
REMARK   3      L13:   0.0905 L23:  -0.0663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1031 S12:   0.0624 S13:   0.7132                       
REMARK   3      S21:  -0.5421 S22:   0.0949 S23:   0.1644                       
REMARK   3      S31:  -0.6505 S32:  -0.1254 S33:  -0.1066                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain 'C' and (resid 57 through 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0027  13.8690  15.5492              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3351 T22:   0.2157                                     
REMARK   3      T33:   0.2640 T12:  -0.1063                                     
REMARK   3      T13:   0.0809 T23:  -0.0342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6491 L22:   0.5365                                     
REMARK   3      L33:   3.0010 L12:  -0.6665                                     
REMARK   3      L13:   1.3498 L23:   0.8748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0577 S12:   0.0339 S13:   0.4225                       
REMARK   3      S21:   0.0477 S22:  -0.1015 S23:   0.1085                       
REMARK   3      S31:  -0.5330 S32:   0.3055 S33:   0.0232                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: chain 'C' and (resid 86 through 100 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0002  17.3071  12.2154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5092 T22:   0.3385                                     
REMARK   3      T33:   0.4654 T12:  -0.0712                                     
REMARK   3      T13:   0.0850 T23:  -0.0447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7662 L22:   3.8053                                     
REMARK   3      L33:   3.8671 L12:   2.5060                                     
REMARK   3      L13:   0.2796 L23:   3.0611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3232 S12:  -0.0318 S13:   0.7002                       
REMARK   3      S21:  -0.2447 S22:   0.1126 S23:   0.2700                       
REMARK   3      S31:  -1.6107 S32:  -0.1009 S33:   0.3292                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: chain 'C' and (resid 101 through 127 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2858  21.2308  25.1680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5071 T22:   0.4735                                     
REMARK   3      T33:   0.5341 T12:  -0.0457                                     
REMARK   3      T13:   0.1161 T23:   0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1569 L22:   3.0106                                     
REMARK   3      L33:   9.6358 L12:  -2.9825                                     
REMARK   3      L13:   3.6773 L23:  -4.6960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2981 S12:  -0.3220 S13:   0.7213                       
REMARK   3      S21:   0.1061 S22:  -0.8327 S23:  -1.2978                       
REMARK   3      S31:   0.4972 S32:   1.0513 S33:   0.3472                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: chain 'C' and (resid 128 through 152 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6286  19.9185  29.9169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2659 T22:   0.2222                                     
REMARK   3      T33:   0.2617 T12:  -0.0345                                     
REMARK   3      T13:   0.0677 T23:  -0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7029 L22:   7.0638                                     
REMARK   3      L33:   8.3276 L12:   2.4706                                     
REMARK   3      L13:  -2.0266 L23:  -2.9262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:  -0.4065 S13:   0.1586                       
REMARK   3      S21:   0.2687 S22:  -0.3832 S23:  -0.2002                       
REMARK   3      S31:  -0.0449 S32:   0.0873 S33:   0.3842                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: chain 'C' and (resid 153 through 165 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9947  20.8924  24.2281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3617 T22:   0.2000                                     
REMARK   3      T33:   0.3001 T12:  -0.0679                                     
REMARK   3      T13:   0.1359 T23:  -0.0704                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2222 L22:   7.6794                                     
REMARK   3      L33:   2.9007 L12:   4.8860                                     
REMARK   3      L13:   0.0328 L23:  -0.2847                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0094 S12:   0.3612 S13:   0.2829                       
REMARK   3      S21:   0.0456 S22:   0.0181 S23:  -0.0041                       
REMARK   3      S31:  -0.3718 S32:  -0.1961 S33:   0.0242                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: chain 'C' and (resid 166 through 179 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6439  17.6761  31.3303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5744 T22:   0.4890                                     
REMARK   3      T33:   0.4615 T12:  -0.0777                                     
REMARK   3      T13:   0.2231 T23:  -0.1319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2801 L22:   0.4819                                     
REMARK   3      L33:   6.0005 L12:   0.3319                                     
REMARK   3      L13:  -1.2257 L23:  -1.6367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3794 S12:  -0.5828 S13:   0.4005                       
REMARK   3      S21:   0.6050 S22:  -0.0997 S23:   0.3705                       
REMARK   3      S31:  -1.4104 S32:  -0.1493 S33:  -0.3174                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: chain 'C' and (resid 180 through 197 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2843   2.6492  30.3826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3827 T22:   0.3258                                     
REMARK   3      T33:   0.2227 T12:  -0.1238                                     
REMARK   3      T13:   0.0693 T23:  -0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1945 L22:   5.2026                                     
REMARK   3      L33:   2.8929 L12:  -2.5123                                     
REMARK   3      L13:   1.4510 L23:  -1.7782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0302 S12:  -0.5840 S13:  -0.0394                       
REMARK   3      S21:   0.7396 S22:  -0.0750 S23:   0.0436                       
REMARK   3      S31:  -0.1888 S32:   0.2572 S33:   0.0432                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: chain 'C' and (resid 198 through 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2277  -4.9589  31.0597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3256 T22:   0.3494                                     
REMARK   3      T33:   0.2430 T12:  -0.1166                                     
REMARK   3      T13:   0.0292 T23:   0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5854 L22:   7.0219                                     
REMARK   3      L33:   3.8471 L12:  -0.9788                                     
REMARK   3      L13:  -0.0121 L23:  -1.6477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2853 S12:  -1.1363 S13:  -0.3380                       
REMARK   3      S21:   0.7591 S22:  -0.0161 S23:  -0.1311                       
REMARK   3      S31:  -0.1604 S32:   0.0951 S33:  -0.2664                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: chain 'D' and (resid 4 through 37 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -19.7687   7.9262  12.3306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2938 T22:   0.3022                                     
REMARK   3      T33:   0.5025 T12:   0.0628                                     
REMARK   3      T13:   0.1000 T23:  -0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0154 L22:   1.4706                                     
REMARK   3      L33:   4.9327 L12:   1.5759                                     
REMARK   3      L13:   0.6482 L23:   1.6684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2635 S12:  -0.1958 S13:   0.3666                       
REMARK   3      S21:   0.2279 S22:  -0.2062 S23:   0.6715                       
REMARK   3      S31:  -0.6958 S32:  -0.4394 S33:  -0.1152                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: chain 'D' and (resid 38 through 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3180 -11.1190   4.8960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2029 T22:   0.1682                                     
REMARK   3      T33:   0.2818 T12:  -0.0174                                     
REMARK   3      T13:  -0.0111 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6384 L22:   0.7363                                     
REMARK   3      L33:   3.0040 L12:  -0.4053                                     
REMARK   3      L13:   0.0498 L23:   0.9104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0868 S12:  -0.0227 S13:  -0.2157                       
REMARK   3      S21:   0.0834 S22:   0.0141 S23:   0.1540                       
REMARK   3      S31:   0.1725 S32:   0.1730 S33:  -0.0901                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: chain 'D' and (resid 86 through 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3858 -15.3306  -2.4011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2033 T22:   0.2437                                     
REMARK   3      T33:   0.2731 T12:  -0.0290                                     
REMARK   3      T13:   0.0366 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8711 L22:   2.5353                                     
REMARK   3      L33:   6.1068 L12:   3.2149                                     
REMARK   3      L13:   3.3977 L23:   1.6686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0517 S12:  -0.1318 S13:  -0.3811                       
REMARK   3      S21:   0.0170 S22:   0.1104 S23:   0.0416                       
REMARK   3      S31:   0.2354 S32:  -0.2260 S33:  -0.2115                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: chain 'D' and (resid 103 through 127 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1679 -17.6624 -10.5807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4050 T22:   0.4330                                     
REMARK   3      T33:   0.4386 T12:  -0.0910                                     
REMARK   3      T13:  -0.0558 T23:  -0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8089 L22:   4.6034                                     
REMARK   3      L33:   5.8075 L12:  -4.9288                                     
REMARK   3      L13:   4.0693 L23:  -4.6891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1487 S12:   0.7254 S13:   0.6893                       
REMARK   3      S21:  -1.1507 S22:  -0.5453 S23:  -0.6519                       
REMARK   3      S31:   0.3356 S32:   0.0048 S33:   0.4885                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: chain 'D' and (resid 128 through 165 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0224 -16.9523   0.6254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1555 T22:   0.1799                                     
REMARK   3      T33:   0.2530 T12:  -0.0535                                     
REMARK   3      T13:  -0.0014 T23:   0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1201 L22:   7.1702                                     
REMARK   3      L33:   3.9062 L12:  -2.9147                                     
REMARK   3      L13:  -2.0855 L23:   4.8093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0171 S12:   0.1705 S13:   0.0210                       
REMARK   3      S21:   0.1975 S22:  -0.1344 S23:   0.1069                       
REMARK   3      S31:   0.1501 S32:  -0.2435 S33:   0.1238                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: chain 'D' and (resid 166 through 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6784   0.8813   5.0001              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2228 T22:   0.3741                                     
REMARK   3      T33:   0.4971 T12:   0.0658                                     
REMARK   3      T13:   0.0159 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1335 L22:   3.0594                                     
REMARK   3      L33:   3.5083 L12:   0.5127                                     
REMARK   3      L13:  -0.4859 L23:  -0.3460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0416 S12:   0.1868 S13:   0.2085                       
REMARK   3      S21:   0.0127 S22:  -0.0363 S23:   0.6115                       
REMARK   3      S31:  -0.3381 S32:  -0.6544 S33:  -0.0106                       
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 4RAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087110.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95369                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68208                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       38.30100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.42450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.42650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.42450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.30100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.42650            
REMARK 290   SMTRY3   4  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A    89                                                      
REMARK 465     SER A   103                                                      
REMARK 465     TYR A   104                                                      
REMARK 465     CYS A   105                                                      
REMARK 465     ASN A   106                                                      
REMARK 465     ASP A   107                                                      
REMARK 465     GLN A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     THR A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ILE A   113                                                      
REMARK 465     LYS A   114                                                      
REMARK 465     VAL A   115                                                      
REMARK 465     ILE A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     ASP A   120                                                      
REMARK 465     ALA A   217                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B   103                                                      
REMARK 465     TYR B   104                                                      
REMARK 465     CYS B   105                                                      
REMARK 465     ASN B   106                                                      
REMARK 465     ASP B   107                                                      
REMARK 465     GLN B   108                                                      
REMARK 465     SER B   109                                                      
REMARK 465     THR B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     ILE B   113                                                      
REMARK 465     LYS B   114                                                      
REMARK 465     LEU B   121                                                      
REMARK 465     SER B   122                                                      
REMARK 465     VAL B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     SER C   103                                                      
REMARK 465     TYR C   104                                                      
REMARK 465     CYS C   105                                                      
REMARK 465     ASN C   106                                                      
REMARK 465     ASP C   107                                                      
REMARK 465     GLN C   108                                                      
REMARK 465     SER C   109                                                      
REMARK 465     THR C   110                                                      
REMARK 465     GLY C   111                                                      
REMARK 465     ASP C   112                                                      
REMARK 465     ILE C   113                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     CYS D   105                                                      
REMARK 465     ASN D   106                                                      
REMARK 465     ASP D   107                                                      
REMARK 465     GLN D   108                                                      
REMARK 465     SER D   109                                                      
REMARK 465     THR D   110                                                      
REMARK 465     GLY D   111                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     CYS A  22    SG                                                  
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 102    CG   CD   CE   NZ                                   
REMARK 470     CYS A 205    SG                                                  
REMARK 470     CYS B  22    SG                                                  
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B  92    CG1  CG2  CD1                                       
REMARK 470     LYS B 102    CG   CD   CE   NZ                                   
REMARK 470     ASP B 120    CG   OD1  OD2                                       
REMARK 470     LYS B 174    CG   CD   CE   NZ                                   
REMARK 470     CYS B 205    SG                                                  
REMARK 470     CYS C  22    SG                                                  
REMARK 470     ILE C  92    CG1  CG2  CD1                                       
REMARK 470     LYS C 102    CG   CD   CE   NZ                                   
REMARK 470     LYS C 114    CG   CD   CE   NZ                                   
REMARK 470     CYS C 205    SG                                                  
REMARK 470     CYS D  22    SG                                                  
REMARK 470     ASP D 112    CG   OD1  OD2                                       
REMARK 470     CYS D 205    SG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS B   165     NH2  ARG B   169              2.17            
REMARK 500   O    HOH C   450     O    HOH C   451              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B  93   C   -  N   -  CA  ANGL. DEV. =  20.8 DEGREES          
REMARK 500    PRO B  93   C   -  N   -  CD  ANGL. DEV. = -17.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 137      -79.98   -119.09                                   
REMARK 500    ASN A 153       68.36     38.12                                   
REMARK 500    ALA A 191      -12.06     80.32                                   
REMARK 500    GLU A 196      -11.43     79.36                                   
REMARK 500    SER B  88     -162.73   -106.70                                   
REMARK 500    ILE B  92     -121.61    -71.69                                   
REMARK 500    ASP B 137      -83.44   -122.03                                   
REMARK 500    VAL B 149      -58.67     60.92                                   
REMARK 500    ALA B 191      -10.33     82.40                                   
REMARK 500    GLU B 196      -11.77     80.16                                   
REMARK 500    ASP B 200       46.15    -89.31                                   
REMARK 500    ASP C  12       33.68    -97.04                                   
REMARK 500    LEU C 121        0.11    -65.26                                   
REMARK 500    ASP C 137      -81.36   -118.99                                   
REMARK 500    ALA C 191       -8.59     79.91                                   
REMARK 500    GLU C 196      -12.94     75.85                                   
REMARK 500    PHE C 198       -0.28     77.73                                   
REMARK 500    ASP C 200       42.51    -89.00                                   
REMARK 500    ASP D 137      -85.06   -118.19                                   
REMARK 500    ALA D 191      -14.39     82.21                                   
REMARK 500    GLU D 196      -10.81     78.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B   58     HIS B   59                  145.45                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 450   O                                                      
REMARK 620 2 GLU C 133   OE1 133.0                                              
REMARK 620 3 HOH C 448   O    66.1  88.1                                        
REMARK 620 4 ASP C 134   OD1 126.1  81.1 167.6                                  
REMARK 620 5 HOH C 405   O    99.4 120.5  90.6  89.5                            
REMARK 620 6 HOH C 411   O    63.6  79.1  90.8  93.2 160.4                      
REMARK 620 7 HOH C 451   O    56.2 146.0 119.2  73.1  81.7  80.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 447   O                                                      
REMARK 620 2 HOH D 445   O    93.6                                              
REMARK 620 3 GLU D 133   OE1 101.7  85.8                                        
REMARK 620 4 HOH D 410   O    86.5 163.2 110.7                                  
REMARK 620 5 HOH D 401   O   113.3  76.9 141.5  87.6                            
REMARK 620 6 ASP D 134   OD1 171.0  94.4  74.8  87.0  72.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 447   O                                                      
REMARK 620 2 ASP B 193   OD1  91.9                                              
REMARK 620 3 HOH B 448   O    90.0 171.7                                        
REMARK 620 4 3L7 B 301   OAE  84.5  83.8 104.4                                  
REMARK 620 5 HOH B 446   O   170.5  85.3  91.6 104.2                            
REMARK 620 6 HOH B 421   O    90.8  81.0  90.9 164.0  79.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 133   OE1                                                    
REMARK 620 2 ASP B 134   OD1  81.8                                              
REMARK 620 3 3L7 B 301   OAU 137.1 136.3                                        
REMARK 620 4 GLU B 133   OE2  50.5 116.2 106.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 452   O                                                      
REMARK 620 2 ASP C 193   OD1  97.6                                              
REMARK 620 3 HOH C 453   O    67.3 149.1                                        
REMARK 620 4 HOH C 421   O   159.3  99.0 102.9                                  
REMARK 620 5 HOH C 412   O    87.8  82.9 121.3  82.0                            
REMARK 620 6 3L7 C 301   OAB  93.7  86.0  69.1  99.7 168.9                      
REMARK 620 7 HOH C 438   O    78.0 154.4  52.1  81.7  71.7 119.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 193   OD1                                                    
REMARK 620 2 HOH D 425   O    82.9                                              
REMARK 620 3 HOH D 446   O    98.2 109.9                                        
REMARK 620 4 3L7 D 301   OAE  73.3 155.3  80.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 449   O                                                      
REMARK 620 2 HOH A 450   O    96.0                                              
REMARK 620 3 HOH A 418   O    86.1  77.4                                        
REMARK 620 4 GLU A 133   OE1 109.5 145.7  81.8                                  
REMARK 620 5 ASP A 134   OD1 176.1  80.4  94.3  74.3                            
REMARK 620 6 HOH A 426   O    94.9  80.7 158.1 118.1  83.3                      
REMARK 620 7 GLU A 133   OE2  78.5 161.4 119.5  51.2 104.6  82.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 193   OD1                                                    
REMARK 620 2 3L7 A 301   OAD  83.9                                              
REMARK 620 3 HOH A 451   O    79.1 157.1                                        
REMARK 620 4 HOH A 452   O    86.1  88.1  75.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 303                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4RAB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RAC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RAD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RAN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RAQ   RELATED DB: PDB                                   
DBREF  4RAO A    1   217  UNP    P00492   HPRT_HUMAN       2    218             
DBREF  4RAO B    1   217  UNP    P00492   HPRT_HUMAN       2    218             
DBREF  4RAO C    1   217  UNP    P00492   HPRT_HUMAN       2    218             
DBREF  4RAO D    1   217  UNP    P00492   HPRT_HUMAN       2    218             
SEQRES   1 A  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
SEQRES   2 A  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
SEQRES   3 A  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
SEQRES   4 A  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
SEQRES   5 A  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
SEQRES   6 A  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
SEQRES   7 A  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
SEQRES   8 A  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
SEQRES   9 A  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
SEQRES  10 A  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
SEQRES  11 A  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
SEQRES  12 A  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
SEQRES  13 A  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
SEQRES  14 A  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
SEQRES  15 A  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
SEQRES  16 A  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
SEQRES  17 A  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
SEQRES   1 B  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
SEQRES   2 B  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
SEQRES   3 B  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
SEQRES   4 B  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
SEQRES   5 B  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
SEQRES   6 B  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
SEQRES   7 B  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
SEQRES   8 B  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
SEQRES   9 B  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
SEQRES  10 B  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
SEQRES  11 B  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
SEQRES  12 B  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
SEQRES  13 B  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
SEQRES  14 B  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
SEQRES  15 B  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
SEQRES  16 B  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
SEQRES  17 B  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
SEQRES   1 C  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
SEQRES   2 C  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
SEQRES   3 C  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
SEQRES   4 C  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
SEQRES   5 C  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
SEQRES   6 C  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
SEQRES   7 C  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
SEQRES   8 C  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
SEQRES   9 C  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
SEQRES  10 C  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
SEQRES  11 C  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
SEQRES  12 C  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
SEQRES  13 C  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
SEQRES  14 C  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
SEQRES  15 C  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
SEQRES  16 C  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
SEQRES  17 C  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
SEQRES   1 D  217  ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU          
SEQRES   2 D  217  PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS          
SEQRES   3 D  217  TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY          
SEQRES   4 D  217  LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL          
SEQRES   5 D  217  MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS          
SEQRES   6 D  217  VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU          
SEQRES   7 D  217  ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER          
SEQRES   8 D  217  ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR          
SEQRES   9 D  217  CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY          
SEQRES  10 D  217  GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU          
SEQRES  11 D  217  ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN          
SEQRES  12 D  217  THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET          
SEQRES  13 D  217  VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG          
SEQRES  14 D  217  SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE          
SEQRES  15 D  217  PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN          
SEQRES  16 D  217  GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER          
SEQRES  17 D  217  GLU THR GLY LYS ALA LYS TYR LYS ALA                          
HET    3L7  A 301      28                                                       
HET     MG  A 302       1                                                       
HET     MG  A 303       1                                                       
HET    3L7  B 301      56                                                       
HET     MG  B 302       1                                                       
HET     MG  B 303       1                                                       
HET    3L7  C 301      28                                                       
HET     MG  C 302       1                                                       
HET     MG  C 303       1                                                       
HET    3L7  D 301      28                                                       
HET     MG  D 302       1                                                       
HET     MG  D 303       1                                                       
HETNAM     3L7 (2-{[2-(6-OXO-1,6-DIHYDRO-9H-PURIN-9-YL)ETHYL](2-{[(E)-          
HETNAM   2 3L7  2-PHOSPHONOETHENYL]OXY}ETHYL)AMINO}ETHYL)PHOSPHONIC             
HETNAM   3 3L7  ACID                                                            
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5  3L7    4(C13 H21 N5 O8 P2)                                          
FORMUL   6   MG    8(MG 2+)                                                     
FORMUL  17  HOH   *201(H2 O)                                                    
HELIX    1   1 ASP A   17  PHE A   21  5                                   5    
HELIX    2   2 PRO A   24  ALA A   28  5                                   5    
HELIX    3   3 PRO A   37  GLY A   57  1                                  21    
HELIX    4   4 GLY A   70  ASN A   87  1                                  18    
HELIX    5   5 LEU A  121  THR A  125  5                                   5    
HELIX    6   6 GLY A  139  ARG A  150  1                                  12    
HELIX    7   7 GLN A  151  ASN A  153  5                                   3    
HELIX    8   8 SER A  208  LYS A  216  1                                   9    
HELIX    9   9 ASP B   17  PHE B   21  5                                   5    
HELIX   10  10 PRO B   24  ALA B   28  5                                   5    
HELIX   11  11 PRO B   37  GLY B   57  1                                  21    
HELIX   12  12 GLY B   70  SER B   88  1                                  19    
HELIX   13  13 GLY B  139  GLN B  151  1                                  13    
HELIX   14  14 SER B  208  TYR B  215  1                                   8    
HELIX   15  15 ASP C   17  PHE C   21  5                                   5    
HELIX   16  16 PRO C   24  ALA C   28  5                                   5    
HELIX   17  17 PRO C   37  GLY C   57  1                                  21    
HELIX   18  18 GLY C   70  ARG C   86  1                                  17    
HELIX   19  19 ASP C  120  THR C  125  5                                   6    
HELIX   20  20 GLY C  139  GLN C  151  1                                  13    
HELIX   21  21 SER C  208  TYR C  215  1                                   8    
HELIX   22  22 ASP D   17  PHE D   21  5                                   5    
HELIX   23  23 PRO D   24  ALA D   28  5                                   5    
HELIX   24  24 PRO D   37  GLY D   57  1                                  21    
HELIX   25  25 GLY D   70  ARG D   86  1                                  17    
HELIX   26  26 ASP D  120  THR D  125  5                                   6    
HELIX   27  27 GLY D  139  ARG D  150  1                                  12    
HELIX   28  28 GLN D  151  ASN D  153  5                                   3    
HELIX   29  29 SER D  208  LYS D  216  1                                   9    
SHEET    1   A 6 VAL A   7  VAL A   8  0                                        
SHEET    2   A 6 PHE A 177  ILE A 182  1  O  GLU A 181   N  VAL A   7           
SHEET    3   A 6 MET A 156  LYS A 165  1  N  SER A 161   O  PHE A 177           
SHEET    4   A 6 ASN A 128  ILE A 136  1  N  ILE A 131   O  ALA A 160           
SHEET    5   A 6 ILE A  61  LEU A  67  1  N  LEU A  64   O  LEU A 130           
SHEET    6   A 6 MET A  94  ARG A 100  1  O  ASP A  97   N  CYS A  65           
SHEET    1   B 3 LEU A  31  ILE A  36  0                                        
SHEET    2   B 3 VAL A 204  ILE A 207 -1  O  VAL A 206   N  GLU A  32           
SHEET    3   B 3 VAL A 187  VAL A 188 -1  N  VAL A 188   O  CYS A 205           
SHEET    1   C 7 VAL B   7  VAL B   8  0                                        
SHEET    2   C 7 PHE B 177  ILE B 182  1  O  GLU B 181   N  VAL B   7           
SHEET    3   C 7 MET B 156  LYS B 165  1  N  SER B 161   O  PHE B 177           
SHEET    4   C 7 ASN B 128  ILE B 136  1  N  ILE B 131   O  ALA B 160           
SHEET    5   C 7 ILE B  61  LEU B  67  1  N  LEU B  64   O  LEU B 130           
SHEET    6   C 7 MET B  94  ARG B 100  1  O  ILE B  99   N  LEU B  67           
SHEET    7   C 7 ILE B 116  GLY B 117 -1  O  ILE B 116   N  ARG B 100           
SHEET    1   D 3 LEU B  31  ILE B  36  0                                        
SHEET    2   D 3 VAL B 204  ILE B 207 -1  O  VAL B 206   N  GLU B  32           
SHEET    3   D 3 VAL B 187  VAL B 188 -1  N  VAL B 188   O  CYS B 205           
SHEET    1   E 6 VAL C   7  VAL C   8  0                                        
SHEET    2   E 6 PHE C 177  ILE C 182  1  O  GLU C 181   N  VAL C   7           
SHEET    3   E 6 MET C 156  LYS C 165  1  N  SER C 161   O  PHE C 177           
SHEET    4   E 6 ASN C 128  ILE C 136  1  N  VAL C 129   O  MET C 156           
SHEET    5   E 6 ILE C  61  LEU C  67  1  N  LEU C  64   O  LEU C 130           
SHEET    6   E 6 MET C  94  ARG C 100  1  O  ILE C  99   N  LEU C  67           
SHEET    1   F 3 LEU C  31  ILE C  36  0                                        
SHEET    2   F 3 VAL C 204  ILE C 207 -1  O  VAL C 206   N  GLU C  32           
SHEET    3   F 3 VAL C 187  VAL C 188 -1  N  VAL C 188   O  CYS C 205           
SHEET    1   G 7 VAL D   7  VAL D   8  0                                        
SHEET    2   G 7 PHE D 177  ILE D 182  1  O  GLU D 181   N  VAL D   7           
SHEET    3   G 7 MET D 156  LYS D 165  1  N  SER D 161   O  PHE D 177           
SHEET    4   G 7 ASN D 128  ILE D 136  1  N  VAL D 129   O  MET D 156           
SHEET    5   G 7 ILE D  61  VAL D  66  1  N  LEU D  64   O  LEU D 130           
SHEET    6   G 7 MET D  94  LYS D 102  1  O  ASP D  97   N  CYS D  65           
SHEET    7   G 7 LYS D 114  ILE D 116 -1  O  ILE D 116   N  ARG D 100           
SHEET    1   H 3 LEU D  31  ILE D  36  0                                        
SHEET    2   H 3 VAL D 204  ILE D 207 -1  O  VAL D 206   N  GLU D  32           
SHEET    3   H 3 VAL D 187  VAL D 188 -1  N  VAL D 188   O  CYS D 205           
LINK        MG    MG C 302                 O   HOH C 450     1555   1555  1.80  
LINK        MG    MG D 302                 O   HOH D 447     1555   1555  1.91  
LINK        MG    MG B 303                 O   HOH B 447     1555   1555  1.96  
LINK         OE1AGLU B 133                MG    MG B 302     1555   1555  2.06  
LINK         OD1 ASP B 134                MG    MG B 302     1555   1555  2.10  
LINK        MG    MG C 303                 O   HOH C 452     1555   1555  2.11  
LINK        MG    MG D 302                 O   HOH D 445     1555   1555  2.14  
LINK         OE1 GLU D 133                MG    MG D 302     1555   1555  2.15  
LINK         OD1 ASP B 193                MG    MG B 303     1555   1555  2.16  
LINK         OD1 ASP D 193                MG    MG D 303     1555   1555  2.18  
LINK         OE1BGLU B 133                MG    MG B 302     1555   1555  2.18  
LINK         OE1 GLU C 133                MG    MG C 302     1555   1555  2.19  
LINK         OD1 ASP C 193                MG    MG C 303     1555   1555  2.21  
LINK        MG    MG A 302                 O   HOH A 449     1555   1555  2.21  
LINK        MG    MG C 302                 O   HOH C 448     1555   1555  2.25  
LINK        MG    MG C 303                 O   HOH C 453     1555   1555  2.25  
LINK         OD1 ASP C 134                MG    MG C 302     1555   1555  2.26  
LINK        MG    MG D 302                 O   HOH D 410     1555   1555  2.26  
LINK        MG    MG B 303                 O   HOH B 448     1555   1555  2.27  
LINK         OD1 ASP A 193                MG    MG A 303     1555   1555  2.27  
LINK        MG    MG C 303                 O   HOH C 421     1555   1555  2.28  
LINK         OAEB3L7 B 301                MG    MG B 303     1555   1555  2.28  
LINK        MG    MG A 302                 O   HOH A 450     1555   1555  2.28  
LINK        MG    MG A 302                 O   HOH A 418     1555   1555  2.29  
LINK        MG    MG D 303                 O   HOH D 425     1555   1555  2.30  
LINK        MG    MG C 302                 O   HOH C 405     1555   1555  2.31  
LINK         OE1 GLU A 133                MG    MG A 302     1555   1555  2.33  
LINK        MG    MG B 303                 O   HOH B 446     1555   1555  2.34  
LINK        MG    MG D 303                 O   HOH D 446     1555   1555  2.35  
LINK        MG    MG D 302                 O   HOH D 401     1555   1555  2.35  
LINK         OD1 ASP A 134                MG    MG A 302     1555   1555  2.35  
LINK         OD1 ASP D 134                MG    MG D 302     1555   1555  2.36  
LINK         OAD 3L7 A 301                MG    MG A 303     1555   1555  2.41  
LINK        MG    MG A 302                 O   HOH A 426     1555   1555  2.42  
LINK        MG    MG C 302                 O   HOH C 411     1555   1555  2.45  
LINK        MG    MG C 303                 O   HOH C 412     1555   1555  2.45  
LINK        MG    MG B 303                 O   HOH B 421     1555   1555  2.48  
LINK         OAB 3L7 C 301                MG    MG C 303     1555   1555  2.52  
LINK        MG    MG C 302                 O   HOH C 451     1555   1555  2.60  
LINK        MG    MG A 303                 O   HOH A 451     1555   1555  2.61  
LINK         OAUB3L7 B 301                MG    MG B 302     1555   1555  2.63  
LINK         OE2 GLU A 133                MG    MG A 302     1555   1555  2.69  
LINK        MG    MG C 303                 O   HOH C 438     1555   1555  2.70  
LINK        MG    MG A 303                 O   HOH A 452     1555   1555  2.74  
LINK         OAE 3L7 D 301                MG    MG D 303     1555   1555  2.75  
LINK         OE2AGLU B 133                MG    MG B 302     1555   1555  2.82  
CISPEP   1 LEU A   67    LYS A   68          0        -2.10                     
CISPEP   2 GLY B   57    GLY B   58          0         9.27                     
CISPEP   3 LEU B   67    LYS B   68          0        -4.05                     
CISPEP   4 ILE B   92    PRO B   93          0         0.30                     
CISPEP   5 LEU C   67    LYS C   68          0        -2.75                     
CISPEP   6 LEU D   67    LYS D   68          0        -8.23                     
SITE     1 AC1 19 LYS A  68  GLY A  69  ASP A 137  THR A 138                    
SITE     2 AC1 19 GLY A 139  LYS A 140  THR A 141  LYS A 165                    
SITE     3 AC1 19 LYS A 185  PHE A 186  VAL A 187  ASP A 193                    
SITE     4 AC1 19 ARG A 199   MG A 303  HOH A 412  HOH A 418                    
SITE     5 AC1 19 HOH A 426  HOH A 450  HOH A 452                               
SITE     1 AC2  6 GLU A 133  ASP A 134  HOH A 418  HOH A 426                    
SITE     2 AC2  6 HOH A 449  HOH A 450                                          
SITE     1 AC3  4 ASP A 193  3L7 A 301  HOH A 451  HOH A 452                    
SITE     1 AC4 22 LYS B  68  GLY B  69  GLU B 133  ASP B 137                    
SITE     2 AC4 22 THR B 138  GLY B 139  LYS B 140  THR B 141                    
SITE     3 AC4 22 LYS B 165  LYS B 185  PHE B 186  VAL B 187                    
SITE     4 AC4 22 ASP B 193  ARG B 199   MG B 302   MG B 303                    
SITE     5 AC4 22 HOH B 401  HOH B 414  HOH B 430  HOH B 446                    
SITE     6 AC4 22 HOH B 447  HOH B 448                                          
SITE     1 AC5  3 GLU B 133  ASP B 134  3L7 B 301                               
SITE     1 AC6  6 ASP B 193  3L7 B 301  HOH B 421  HOH B 446                    
SITE     2 AC6  6 HOH B 447  HOH B 448                                          
SITE     1 AC7 25 LYS C  68  GLY C  69  ARG C 100  ASP C 137                    
SITE     2 AC7 25 THR C 138  GLY C 139  LYS C 140  THR C 141                    
SITE     3 AC7 25 LYS C 165  LYS C 185  PHE C 186  VAL C 187                    
SITE     4 AC7 25 ASP C 193  ARG C 199   MG C 303  HOH C 402                    
SITE     5 AC7 25 HOH C 405  HOH C 411  HOH C 413  HOH C 418                    
SITE     6 AC7 25 HOH C 421  HOH C 449  HOH C 450  HOH C 451                    
SITE     7 AC7 25 HOH C 453                                                     
SITE     1 AC8  7 GLU C 133  ASP C 134  HOH C 405  HOH C 411                    
SITE     2 AC8  7 HOH C 448  HOH C 450  HOH C 451                               
SITE     1 AC9  7 ASP C 193  3L7 C 301  HOH C 412  HOH C 421                    
SITE     2 AC9  7 HOH C 438  HOH C 452  HOH C 453                               
SITE     1 BC1 19 LYS D  68  GLY D  69  ASP D 137  THR D 138                    
SITE     2 BC1 19 GLY D 139  LYS D 140  THR D 141  LYS D 165                    
SITE     3 BC1 19 LYS D 185  PHE D 186  VAL D 187  ASP D 193                    
SITE     4 BC1 19 ARG D 199   MG D 303  HOH D 401  HOH D 405                    
SITE     5 BC1 19 HOH D 410  HOH D 432  HOH D 445                               
SITE     1 BC2  6 GLU D 133  ASP D 134  HOH D 401  HOH D 410                    
SITE     2 BC2  6 HOH D 445  HOH D 447                                          
SITE     1 BC3  4 ASP D 193  3L7 D 301  HOH D 425  HOH D 446                    
CRYST1   76.602   92.853  114.849  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013054  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008707        0.00000                         
ATOM      1  N   ALA A   1      29.351 -15.299  10.549  1.00 74.92           N  
ANISOU    1  N   ALA A   1     7124   9614  11727    415  -2282   2479       N  
ATOM      2  CA  ALA A   1      28.468 -14.947   9.436  1.00 73.31           C  
ANISOU    2  CA  ALA A   1     7090   9292  11472    457  -2044   2081       C  
ATOM      3  C   ALA A   1      27.420 -13.904   9.827  1.00 70.93           C  
ANISOU    3  C   ALA A   1     7078   9180  10693    224  -1925   2028       C  
ATOM      4  O   ALA A   1      26.898 -13.915  10.943  1.00 70.22           O  
ANISOU    4  O   ALA A   1     7090   9184  10407     75  -2003   2318       O  
ATOM      5  CB  ALA A   1      27.789 -16.190   8.876  1.00 72.44           C  
ANISOU    5  CB  ALA A   1     6943   8763  11820    639  -2052   2026       C  
ATOM      6  N   THR A   2      27.118 -13.006   8.896  1.00 68.65           N  
ANISOU    6  N   THR A   2     6912   8955  10215    211  -1725   1667       N  
ATOM      7  CA  THR A   2      26.058 -12.025   9.086  1.00 67.59           C  
ANISOU    7  CA  THR A   2     7040   8946   9696     24  -1591   1568       C  
ATOM      8  C   THR A   2      24.709 -12.738   9.002  1.00 65.98           C  
ANISOU    8  C   THR A   2     6940   8476   9654     47  -1545   1596       C  
ATOM      9  O   THR A   2      24.376 -13.318   7.963  1.00 65.77           O  
ANISOU    9  O   THR A   2     6881   8188   9921    208  -1498   1377       O  
ATOM     10  CB  THR A   2      26.121 -10.925   8.005  1.00 67.81           C  
ANISOU   10  CB  THR A   2     7139   9079   9545     22  -1398   1203       C  
ATOM     11  OG1 THR A   2      27.483 -10.518   7.811  1.00 70.55           O  
ANISOU   11  OG1 THR A   2     7304   9595   9908     54  -1433   1186       O  
ATOM     12  CG2 THR A   2      25.271  -9.717   8.403  1.00 64.90           C  
ANISOU   12  CG2 THR A   2     7011   8877   8770   -192  -1293   1135       C  
ATOM     13  N   ARG A   3      23.943 -12.700  10.094  1.00 59.98           N  
ANISOU   13  N   ARG A   3     6293   7790   8707   -105  -1564   1865       N  
ATOM     14  CA  ARG A   3      22.657 -13.400  10.173  1.00 57.18           C  
ANISOU   14  CA  ARG A   3     5991   7188   8549   -107  -1525   1981       C  
ATOM     15  C   ARG A   3      21.689 -12.952   9.078  1.00 54.95           C  
ANISOU   15  C   ARG A   3     5835   6771   8272    -91  -1357   1618       C  
ATOM     16  O   ARG A   3      20.867 -13.734   8.585  1.00 54.27           O  
ANISOU   16  O   ARG A   3     5721   6371   8530    -18  -1370   1583       O  
ATOM     17  CB  ARG A   3      22.017 -13.199  11.553  1.00 54.82           C  
ANISOU   17  CB  ARG A   3     5798   7085   7946   -275  -1510   2338       C  
ATOM     18  CG  ARG A   3      20.755 -14.030  11.792  1.00 54.28           C  
ANISOU   18  CG  ARG A   3     5718   6766   8139   -284  -1468   2575       C  
ATOM     19  CD  ARG A   3      21.063 -15.516  11.680  1.00 62.24           C  
ANISOU   19  CD  ARG A   3     6498   7425   9728   -146  -1653   2800       C  
ATOM     20  NE  ARG A   3      19.883 -16.359  11.857  1.00 66.19           N  
ANISOU   20  NE  ARG A   3     6942   7630  10577   -166  -1638   3050       N  
ATOM     21  CZ  ARG A   3      18.925 -16.507  10.946  1.00 65.34           C  
ANISOU   21  CZ  ARG A   3     6854   7229  10744   -139  -1575   2799       C  
ATOM     22  NH1 ARG A   3      18.997 -15.853   9.791  1.00 61.70           N  
ANISOU   22  NH1 ARG A   3     6491   6763  10190    -78  -1509   2294       N  
ATOM     23  NH2 ARG A   3      17.889 -17.302  11.190  1.00 66.44           N  
ANISOU   23  NH2 ARG A   3     6901   7085  11258   -175  -1588   3075       N  
ATOM     24  N   SER A   4      21.789 -11.689   8.693  1.00 50.57           N  
ANISOU   24  N   SER A   4     5408   6441   7364   -162  -1225   1359       N  
ATOM     25  CA  SER A   4      20.893 -11.170   7.671  1.00 50.99           C  
ANISOU   25  CA  SER A   4     5584   6402   7389   -149  -1077   1044       C  
ATOM     26  C   SER A   4      21.570 -10.070   6.858  1.00 49.88           C  
ANISOU   26  C   SER A   4     5484   6454   7016   -138   -977    752       C  
ATOM     27  O   SER A   4      21.272  -8.888   7.053  1.00 43.16           O  
ANISOU   27  O   SER A   4     4768   5789   5841   -281   -866    681       O  
ATOM     28  CB  SER A   4      19.597 -10.666   8.315  1.00 48.54           C  
ANISOU   28  CB  SER A   4     5428   6135   6880   -308   -963   1149       C  
ATOM     29  OG  SER A   4      18.556 -10.565   7.364  1.00 50.34           O  
ANISOU   29  OG  SER A   4     5723   6177   7228   -275   -876    919       O  
ATOM     30  N   PRO A   5      22.484 -10.460   5.935  1.00 54.89           N  
ANISOU   30  N   PRO A   5     5985   7037   7836     43  -1004    591       N  
ATOM     31  CA  PRO A   5      23.197  -9.503   5.079  1.00 52.90           C  
ANISOU   31  CA  PRO A   5     5724   6973   7402     76   -886    367       C  
ATOM     32  C   PRO A   5      22.193  -8.758   4.215  1.00 51.34           C  
ANISOU   32  C   PRO A   5     5696   6760   7052     54   -737    127       C  
ATOM     33  O   PRO A   5      21.062  -9.227   4.042  1.00 54.58           O  
ANISOU   33  O   PRO A   5     6190   6968   7581     70   -750     80       O  
ATOM     34  CB  PRO A   5      24.098 -10.397   4.215  1.00 53.45           C  
ANISOU   34  CB  PRO A   5     5612   6940   7757    332   -921    253       C  
ATOM     35  CG  PRO A   5      23.392 -11.705   4.179  1.00 56.28           C  
ANISOU   35  CG  PRO A   5     5958   6970   8457    447  -1039    264       C  
ATOM     36  CD  PRO A   5      22.788 -11.852   5.552  1.00 57.48           C  
ANISOU   36  CD  PRO A   5     6156   7099   8585    250  -1129    597       C  
ATOM     37  N   GLY A   6      22.587  -7.614   3.674  1.00 42.12           N  
ANISOU   37  N   GLY A   6     4555   5789   5658     12   -609      2       N  
ATOM     38  CA  GLY A   6      21.591  -6.699   3.161  1.00 35.03           C  
ANISOU   38  CA  GLY A   6     3826   4906   4580    -64   -483   -145       C  
ATOM     39  C   GLY A   6      21.459  -6.620   1.659  1.00 30.98           C  
ANISOU   39  C   GLY A   6     3331   4377   4064    110   -386   -393       C  
ATOM     40  O   GLY A   6      22.131  -7.327   0.913  1.00 30.10           O  
ANISOU   40  O   GLY A   6     3112   4247   4079    323   -397   -496       O  
ATOM     41  N   VAL A   7      20.556  -5.746   1.230  1.00 26.95           N  
ANISOU   41  N   VAL A   7     2962   3884   3393     33   -292   -488       N  
ATOM     42  CA  VAL A   7      20.394  -5.398  -0.174  1.00 27.17           C  
ANISOU   42  CA  VAL A   7     3032   3964   3328    173   -194   -691       C  
ATOM     43  C   VAL A   7      21.639  -4.624  -0.584  1.00 27.34           C  
ANISOU   43  C   VAL A   7     2938   4232   3217    192    -68   -651       C  
ATOM     44  O   VAL A   7      21.919  -3.550  -0.038  1.00 28.85           O  
ANISOU   44  O   VAL A   7     3123   4540   3301      0    -17   -528       O  
ATOM     45  CB  VAL A   7      19.142  -4.513  -0.360  1.00 25.01           C  
ANISOU   45  CB  VAL A   7     2918   3656   2930     51   -137   -737       C  
ATOM     46  CG1 VAL A   7      19.019  -4.013  -1.810  1.00 26.04           C  
ANISOU   46  CG1 VAL A   7     3094   3886   2913    187    -43   -901       C  
ATOM     47  CG2 VAL A   7      17.892  -5.277   0.059  1.00 27.68           C  
ANISOU   47  CG2 VAL A   7     3325   3747   3445     24   -250   -740       C  
ATOM     48  N   VAL A   8      22.389  -5.164  -1.537  1.00 29.05           N  
ANISOU   48  N   VAL A   8     3053   4523   3463    431    -19   -757       N  
ATOM     49  CA  VAL A   8      23.618  -4.519  -1.977  1.00 34.59           C  
ANISOU   49  CA  VAL A   8     3596   5469   4078    472    129   -677       C  
ATOM     50  C   VAL A   8      23.278  -3.426  -2.989  1.00 36.07           C  
ANISOU   50  C   VAL A   8     3859   5806   4038    471    295   -716       C  
ATOM     51  O   VAL A   8      22.765  -3.710  -4.068  1.00 33.00           O  
ANISOU   51  O   VAL A   8     3564   5433   3542    663    336   -895       O  
ATOM     52  CB  VAL A   8      24.608  -5.530  -2.605  1.00 39.10           C  
ANISOU   52  CB  VAL A   8     4002   6089   4764    762    159   -761       C  
ATOM     53  CG1 VAL A   8      25.800  -4.806  -3.208  1.00 42.06           C  
ANISOU   53  CG1 VAL A   8     4189   6744   5049    822    361   -654       C  
ATOM     54  CG2 VAL A   8      25.089  -6.547  -1.562  1.00 37.62           C  
ANISOU   54  CG2 VAL A   8     3699   5750   4846    756    -14   -663       C  
ATOM     55  N   ILE A   9      23.552  -2.175  -2.636  1.00 31.74           N  
ANISOU   55  N   ILE A   9     3272   5361   3428    256    366   -548       N  
ATOM     56  CA  ILE A   9      23.335  -1.068  -3.561  1.00 32.85           C  
ANISOU   56  CA  ILE A   9     3446   5636   3397    242    526   -517       C  
ATOM     57  C   ILE A   9      24.676  -0.718  -4.215  1.00 37.50           C  
ANISOU   57  C   ILE A   9     3805   6470   3973    341    701   -376       C  
ATOM     58  O   ILE A   9      25.654  -0.412  -3.534  1.00 31.73           O  
ANISOU   58  O   ILE A   9     2888   5781   3386    213    686   -209       O  
ATOM     59  CB  ILE A   9      22.681   0.131  -2.840  1.00 34.84           C  
ANISOU   59  CB  ILE A   9     3794   5801   3643    -46    495   -427       C  
ATOM     60  CG1 ILE A   9      21.286  -0.280  -2.352  1.00 33.10           C  
ANISOU   60  CG1 ILE A   9     3779   5368   3429    -96    373   -555       C  
ATOM     61  CG2 ILE A   9      22.611   1.351  -3.752  1.00 37.59           C  
ANISOU   61  CG2 ILE A   9     4132   6269   3880    -76    653   -333       C  
ATOM     62  CD1 ILE A   9      20.430   0.848  -1.871  1.00 37.12           C  
ANISOU   62  CD1 ILE A   9     4402   5790   3911   -311    379   -518       C  
ATOM     63  N   SER A  10      24.742  -0.800  -5.541  1.00 32.59           N  
ANISOU   63  N   SER A  10     3181   6026   3177    583    865   -436       N  
ATOM     64  CA  SER A  10      26.027  -0.667  -6.224  1.00 38.67           C  
ANISOU   64  CA  SER A  10     3708   7058   3928    735   1074   -293       C  
ATOM     65  C   SER A  10      26.538   0.770  -6.236  1.00 35.77           C  
ANISOU   65  C   SER A  10     3187   6808   3596    523   1203      6       C  
ATOM     66  O   SER A  10      25.772   1.707  -6.025  1.00 35.31           O  
ANISOU   66  O   SER A  10     3252   6646   3517    312   1156     59       O  
ATOM     67  CB  SER A  10      25.930  -1.189  -7.660  1.00 47.07           C  
ANISOU   67  CB  SER A  10     4831   8321   4733   1091   1230   -455       C  
ATOM     68  OG  SER A  10      24.866  -0.538  -8.324  1.00 52.65           O  
ANISOU   68  OG  SER A  10     5740   9050   5216   1066   1244   -489       O  
ATOM     69  N   ASP A  11      27.833   0.927  -6.510  1.00 38.36           N  
ANISOU   69  N   ASP A  11     3224   7334   4016    588   1367    208       N  
ATOM     70  CA  ASP A  11      28.466   2.236  -6.557  1.00 42.68           C  
ANISOU   70  CA  ASP A  11     3562   7974   4679    388   1485    531       C  
ATOM     71  C   ASP A  11      27.835   3.139  -7.623  1.00 46.68           C  
ANISOU   71  C   ASP A  11     4166   8605   4966    417   1657    637       C  
ATOM     72  O   ASP A  11      27.788   4.357  -7.464  1.00 50.77           O  
ANISOU   72  O   ASP A  11     4635   9041   5613    171   1653    849       O  
ATOM     73  CB  ASP A  11      29.966   2.100  -6.838  1.00 43.26           C  
ANISOU   73  CB  ASP A  11     3267   8264   4906    505   1663    748       C  
ATOM     74  CG  ASP A  11      30.751   1.550  -5.652  1.00 45.72           C  
ANISOU   74  CG  ASP A  11     3413   8444   5515    397   1460    749       C  
ATOM     75  OD1 ASP A  11      30.200   1.504  -4.533  1.00 45.38           O  
ANISOU   75  OD1 ASP A  11     3534   8161   5549    183   1188    632       O  
ATOM     76  OD2 ASP A  11      31.937   1.187  -5.848  1.00 48.95           O  
ANISOU   76  OD2 ASP A  11     3514   9010   6076    535   1583    888       O  
ATOM     77  N   ASP A  12      27.345   2.536  -8.703  1.00 46.50           N  
ANISOU   77  N   ASP A  12     4347   8653   4670    695   1715    460       N  
ATOM     78  CA AASP A  12      26.799   3.335  -9.800  0.59 46.31           C  
ANISOU   78  CA AASP A  12     4472   8657   4468    719   1786    557       C  
ATOM     79  CA BASP A  12      26.795   3.266  -9.842  0.41 46.48           C  
ANISOU   79  CA BASP A  12     4501   8684   4477    737   1787    543       C  
ATOM     80  C   ASP A  12      25.283   3.452  -9.763  1.00 45.82           C  
ANISOU   80  C   ASP A  12     4691   8452   4264    662   1641    380       C  
ATOM     81  O   ASP A  12      24.665   3.874 -10.736  1.00 50.19           O  
ANISOU   81  O   ASP A  12     5389   9037   4643    730   1661    409       O  
ATOM     82  CB AASP A  12      27.258   2.810 -11.159  0.59 49.62           C  
ANISOU   82  CB AASP A  12     4917   9270   4667   1029   1925    524       C  
ATOM     83  CB BASP A  12      27.121   2.528 -11.140  0.41 49.33           C  
ANISOU   83  CB BASP A  12     4922   9222   4601   1070   1898    443       C  
ATOM     84  CG AASP A  12      26.948   1.342 -11.359  0.59 50.57           C  
ANISOU   84  CG AASP A  12     5190   9385   4640   1295   1840    155       C  
ATOM     85  CG BASP A  12      28.592   2.194 -11.270  0.41 54.02           C  
ANISOU   85  CG BASP A  12     5247   9965   5312   1186   2059    574       C  
ATOM     86  OD1AASP A  12      26.046   0.807 -10.682  0.59 47.79           O  
ANISOU   86  OD1AASP A  12     4990   8864   4306   1254   1655    -83       O  
ATOM     87  OD1BASP A  12      29.433   3.056 -10.933  0.41 54.05           O  
ANISOU   87  OD1BASP A  12     5007   9982   5548   1003   2139    881       O  
ATOM     88  OD2AASP A  12      27.615   0.715 -12.210  0.59 58.64           O  
ANISOU   88  OD2AASP A  12     6174  10562   5545   1549   1954     98       O  
ATOM     89  OD2BASP A  12      28.912   1.067 -11.713  0.41 59.24           O  
ANISOU   89  OD2BASP A  12     5935  10708   5866   1460   2093    363       O  
ATOM     90  N   GLU A  13      24.691   3.100  -8.626  1.00 40.11           N  
ANISOU   90  N   GLU A  13     4028   7589   3625    529   1491    213       N  
ATOM     91  CA  GLU A  13      23.244   3.239  -8.440  1.00 41.06           C  
ANISOU   91  CA  GLU A  13     4409   7505   3688    437   1326     52       C  
ATOM     92  C   GLU A  13      22.844   4.690  -8.662  1.00 39.88           C  
ANISOU   92  C   GLU A  13     4253   7334   3565    247   1389    294       C  
ATOM     93  O   GLU A  13      23.339   5.580  -7.977  1.00 40.63           O  
ANISOU   93  O   GLU A  13     4204   7331   3903      3   1393    487       O  
ATOM     94  CB  GLU A  13      22.828   2.795  -7.038  1.00 44.57           C  
ANISOU   94  CB  GLU A  13     4936   7648   4349    249   1100   -106       C  
ATOM     95  CG  GLU A  13      21.370   3.106  -6.688  1.00 47.84           C  
ANISOU   95  CG  GLU A  13     5572   7833   4771    115    959   -217       C  
ATOM     96  CD  GLU A  13      20.377   2.332  -7.537  1.00 53.92           C  
ANISOU   96  CD  GLU A  13     6526   8607   5357    334    893   -434       C  
ATOM     97  OE1 GLU A  13      20.623   1.134  -7.792  1.00 60.41           O  
ANISOU   97  OE1 GLU A  13     7358   9466   6130    546    848   -620       O  
ATOM     98  OE2 GLU A  13      19.357   2.928  -7.949  1.00 52.41           O  
ANISOU   98  OE2 GLU A  13     6457   8361   5097    296    865   -426       O  
ATOM     99  N   PRO A  14      21.965   4.937  -9.647  1.00 44.06           N  
ANISOU   99  N   PRO A  14     4951   7876   3913    354   1382    277       N  
ATOM    100  CA  PRO A  14      21.609   6.314 -10.006  1.00 43.53           C  
ANISOU  100  CA  PRO A  14     4867   7775   3900    207   1438    537       C  
ATOM    101  C   PRO A  14      20.482   6.857  -9.142  1.00 42.19           C  
ANISOU  101  C   PRO A  14     4809   7357   3865    -19   1306    471       C  
ATOM    102  O   PRO A  14      20.275   8.066  -9.107  1.00 47.99           O  
ANISOU  102  O   PRO A  14     5493   7990   4750   -194   1335    682       O  
ATOM    103  CB  PRO A  14      21.139   6.180 -11.458  1.00 45.41           C  
ANISOU  103  CB  PRO A  14     5239   8147   3869    443   1452    524       C  
ATOM    104  CG  PRO A  14      20.558   4.804 -11.523  1.00 50.07           C  
ANISOU  104  CG  PRO A  14     6006   8707   4311    629   1304    158       C  
ATOM    105  CD  PRO A  14      21.376   3.951 -10.571  1.00 48.12           C  
ANISOU  105  CD  PRO A  14     5654   8431   4198    621   1302     33       C  
ATOM    106  N   GLY A  15      19.771   5.977  -8.448  1.00 38.82           N  
ANISOU  106  N   GLY A  15     4539   6747   3462    -17   1131    175       N  
ATOM    107  CA  GLY A  15      18.619   6.393  -7.673  1.00 32.91           C  
ANISOU  107  CA  GLY A  15     3924   5709   2873   -199    992     83       C  
ATOM    108  C   GLY A  15      17.504   6.859  -8.594  1.00 36.41           C  
ANISOU  108  C   GLY A  15     4482   6154   3200   -128    976    121       C  
ATOM    109  O   GLY A  15      17.548   6.621  -9.808  1.00 41.10           O  
ANISOU  109  O   GLY A  15     5095   6987   3534     87   1032    163       O  
ATOM    110  N   TYR A  16      16.521   7.542  -8.017  1.00 32.48           N  
ANISOU  110  N   TYR A  16     4053   5403   2884   -294    898    110       N  
ATOM    111  CA  TYR A  16      15.303   7.914  -8.729  1.00 32.38           C  
ANISOU  111  CA  TYR A  16     4143   5339   2822   -239    838    130       C  
ATOM    112  C   TYR A  16      15.120   9.430  -8.774  1.00 35.84           C  
ANISOU  112  C   TYR A  16     4508   5664   3447   -398    905    385       C  
ATOM    113  O   TYR A  16      15.432  10.140  -7.804  1.00 33.88           O  
ANISOU  113  O   TYR A  16     4191   5229   3453   -602    927    417       O  
ATOM    114  CB  TYR A  16      14.085   7.271  -8.047  1.00 31.78           C  
ANISOU  114  CB  TYR A  16     4197   5027   2852   -265    678   -115       C  
ATOM    115  CG  TYR A  16      14.138   5.758  -7.960  1.00 32.53           C  
ANISOU  115  CG  TYR A  16     4352   5161   2848   -124    578   -354       C  
ATOM    116  CD1 TYR A  16      13.722   4.962  -9.027  1.00 41.14           C  
ANISOU  116  CD1 TYR A  16     5523   6369   3738     98    476   -480       C  
ATOM    117  CD2 TYR A  16      14.610   5.127  -6.811  1.00 33.82           C  
ANISOU  117  CD2 TYR A  16     4490   5231   3127   -207    563   -457       C  
ATOM    118  CE1 TYR A  16      13.778   3.581  -8.947  1.00 41.90           C  
ANISOU  118  CE1 TYR A  16     5663   6448   3807    229    362   -718       C  
ATOM    119  CE2 TYR A  16      14.662   3.754  -6.720  1.00 32.38           C  
ANISOU  119  CE2 TYR A  16     4341   5046   2914    -82    463   -643       C  
ATOM    120  CZ  TYR A  16      14.243   2.989  -7.778  1.00 36.73           C  
ANISOU  120  CZ  TYR A  16     4962   5671   3323    132    362   -781       C  
ATOM    121  OH  TYR A  16      14.308   1.622  -7.681  1.00 37.92           O  
ANISOU  121  OH  TYR A  16     5136   5769   3503    257    242   -985       O  
ATOM    122  N   ASP A  17      14.609   9.907  -9.907  1.00 32.85           N  
ANISOU  122  N   ASP A  17     4146   5391   2944   -295    914    556       N  
ATOM    123  CA  ASP A  17      14.235  11.302 -10.094  1.00 34.06           C  
ANISOU  123  CA  ASP A  17     4231   5407   3302   -418    951    820       C  
ATOM    124  C   ASP A  17      13.229  11.695  -9.022  1.00 30.20           C  
ANISOU  124  C   ASP A  17     3801   4552   3121   -579    857    659       C  
ATOM    125  O   ASP A  17      12.251  10.978  -8.789  1.00 28.08           O  
ANISOU  125  O   ASP A  17     3649   4195   2826   -521    742    436       O  
ATOM    126  CB  ASP A  17      13.615  11.474 -11.486  1.00 38.85           C  
ANISOU  126  CB  ASP A  17     4883   6204   3675   -241    925    995       C  
ATOM    127  CG  ASP A  17      13.383  12.926 -11.860  1.00 47.28           C  
ANISOU  127  CG  ASP A  17     5847   7165   4954   -345    977   1354       C  
ATOM    128  OD1 ASP A  17      13.072  13.749 -10.975  1.00 45.32           O  
ANISOU  128  OD1 ASP A  17     5551   6579   5089   -544    959   1352       O  
ATOM    129  OD2 ASP A  17      13.506  13.245 -13.057  1.00 59.31           O  
ANISOU  129  OD2 ASP A  17     7336   8945   6254   -213   1033   1643       O  
ATOM    130  N   LEU A  18      13.469  12.831  -8.364  1.00 32.50           N  
ANISOU  130  N   LEU A  18     4000   4625   3724   -773    906    768       N  
ATOM    131  CA  LEU A  18      12.600  13.270  -7.269  1.00 33.00           C  
ANISOU  131  CA  LEU A  18     4118   4355   4064   -904    848    587       C  
ATOM    132  C   LEU A  18      11.183  13.484  -7.768  1.00 27.01           C  
ANISOU  132  C   LEU A  18     3419   3482   3360   -827    779    607       C  
ATOM    133  O   LEU A  18      10.229  13.322  -7.016  1.00 30.63           O  
ANISOU  133  O   LEU A  18     3946   3742   3950   -852    732    406       O  
ATOM    134  CB  LEU A  18      13.113  14.581  -6.670  1.00 30.87           C  
ANISOU  134  CB  LEU A  18     3737   3860   4132  -1100    891    693       C  
ATOM    135  CG  LEU A  18      14.514  14.565  -6.077  1.00 35.64           C  
ANISOU  135  CG  LEU A  18     4246   4524   4770  -1216    921    686       C  
ATOM    136  CD1 LEU A  18      15.013  15.989  -5.841  1.00 41.06           C  
ANISOU  136  CD1 LEU A  18     4786   4976   5837  -1401    929    855       C  
ATOM    137  CD2 LEU A  18      14.493  13.779  -4.783  1.00 35.34           C  
ANISOU  137  CD2 LEU A  18     4320   4436   4673  -1258    860    348       C  
ATOM    138  N   ASP A  19      11.055  13.859  -9.047  1.00 28.84           N  
ANISOU  138  N   ASP A  19     3611   3858   3490   -725    775    875       N  
ATOM    139  CA  ASP A  19       9.756  14.207  -9.621  1.00 32.50           C  
ANISOU  139  CA  ASP A  19     4102   4215   4032   -656    681    951       C  
ATOM    140  C   ASP A  19       8.797  13.029  -9.743  1.00 30.19           C  
ANISOU  140  C   ASP A  19     3926   3971   3574   -524    541    713       C  
ATOM    141  O   ASP A  19       7.603  13.222 -10.008  1.00 30.01           O  
ANISOU  141  O   ASP A  19     3911   3815   3675   -484    434    730       O  
ATOM    142  CB  ASP A  19       9.930  14.889 -10.978  1.00 39.01           C  
ANISOU  142  CB  ASP A  19     4854   5223   4746   -572    697   1336       C  
ATOM    143  CG  ASP A  19      10.532  16.282 -10.858  1.00 49.12           C  
ANISOU  143  CG  ASP A  19     5977   6336   6349   -729    806   1632       C  
ATOM    144  OD1 ASP A  19      10.018  17.078 -10.041  1.00 50.40           O  
ANISOU  144  OD1 ASP A  19     6106   6135   6910   -862    791   1563       O  
ATOM    145  OD2 ASP A  19      11.520  16.573 -11.573  1.00 55.44           O  
ANISOU  145  OD2 ASP A  19     6677   7362   7028   -711    908   1932       O  
ATOM    146  N   LEU A  20       9.324  11.825  -9.529  1.00 27.04           N  
ANISOU  146  N   LEU A  20     3593   3732   2947   -464    527    503       N  
ATOM    147  CA  LEU A  20       8.550  10.584  -9.604  1.00 26.86           C  
ANISOU  147  CA  LEU A  20     3663   3728   2814   -349    374    266       C  
ATOM    148  C   LEU A  20       7.935  10.219  -8.244  1.00 28.66           C  
ANISOU  148  C   LEU A  20     3904   3696   3290   -459    374     50       C  
ATOM    149  O   LEU A  20       7.099   9.313  -8.139  1.00 27.12           O  
ANISOU  149  O   LEU A  20     3745   3434   3125   -401    251   -107       O  
ATOM    150  CB  LEU A  20       9.434   9.429 -10.124  1.00 29.63           C  
ANISOU  150  CB  LEU A  20     4069   4366   2823   -204    353    152       C  
ATOM    151  CG  LEU A  20       9.982   9.537 -11.553  1.00 36.15           C  
ANISOU  151  CG  LEU A  20     4903   5526   3305    -31    365    328       C  
ATOM    152  CD1 LEU A  20      11.024   8.458 -11.827  1.00 41.31           C  
ANISOU  152  CD1 LEU A  20     5592   6441   3664    113    403    181       C  
ATOM    153  CD2 LEU A  20       8.869   9.441 -12.572  1.00 38.36           C  
ANISOU  153  CD2 LEU A  20     5251   5854   3469    109    167    339       C  
ATOM    154  N   PHE A  21       8.340  10.941  -7.208  1.00 24.46           N  
ANISOU  154  N   PHE A  21     3335   3020   2941   -612    508     52       N  
ATOM    155  CA  PHE A  21       7.842  10.688  -5.860  1.00 25.87           C  
ANISOU  155  CA  PHE A  21     3534   3004   3293   -701    546   -135       C  
ATOM    156  C   PHE A  21       7.221  11.897  -5.182  1.00 26.99           C  
ANISOU  156  C   PHE A  21     3637   2890   3729   -802    632   -114       C  
ATOM    157  O   PHE A  21       7.301  13.019  -5.676  1.00 25.61           O  
ANISOU  157  O   PHE A  21     3405   2646   3679   -832    656     55       O  
ATOM    158  CB  PHE A  21       8.963  10.109  -4.996  1.00 29.32           C  
ANISOU  158  CB  PHE A  21     3996   3537   3608   -761    603   -249       C  
ATOM    159  CG  PHE A  21       9.461   8.803  -5.504  1.00 33.97           C  
ANISOU  159  CG  PHE A  21     4615   4327   3965   -643    522   -312       C  
ATOM    160  CD1 PHE A  21       8.820   7.625  -5.149  1.00 38.92           C  
ANISOU  160  CD1 PHE A  21     5278   4902   4606   -590    434   -460       C  
ATOM    161  CD2 PHE A  21      10.528   8.746  -6.388  1.00 33.27           C  
ANISOU  161  CD2 PHE A  21     4502   4468   3670   -570    538   -215       C  
ATOM    162  CE1 PHE A  21       9.251   6.403  -5.648  1.00 39.47           C  
ANISOU  162  CE1 PHE A  21     5374   5112   4512   -467    335   -546       C  
ATOM    163  CE2 PHE A  21      10.961   7.529  -6.893  1.00 38.63           C  
ANISOU  163  CE2 PHE A  21     5212   5324   4140   -425    469   -313       C  
ATOM    164  CZ  PHE A  21      10.324   6.357  -6.521  1.00 43.53           C  
ANISOU  164  CZ  PHE A  21     5882   5856   4801   -374    353   -497       C  
ATOM    165  N   CYS A  22       6.576  11.632  -4.050  1.00 28.80           N  
ANISOU  165  N   CYS A  22     3889   2979   4076   -839    684   -279       N  
ATOM    166  CA  CYS A  22       6.040  12.666  -3.185  1.00 30.99           C  
ANISOU  166  CA  CYS A  22     4147   3026   4604   -909    794   -336       C  
ATOM    167  C   CYS A  22       7.160  13.096  -2.248  1.00 31.10           C  
ANISOU  167  C   CYS A  22     4202   3050   4566  -1024    867   -441       C  
ATOM    168  O   CYS A  22       7.619  12.298  -1.427  1.00 34.81           O  
ANISOU  168  O   CYS A  22     4731   3629   4867  -1047    882   -571       O  
ATOM    169  CB  CYS A  22       4.877  12.111  -2.392  1.00 31.59           C  
ANISOU  169  CB  CYS A  22     4222   3000   4783   -871    844   -455       C  
ATOM    170  N   ILE A  23       7.601  14.343  -2.392  1.00 27.70           N  
ANISOU  170  N   ILE A  23     3726   2493   4304  -1099    887   -370       N  
ATOM    171  CA  ILE A  23       8.719  14.909  -1.633  1.00 32.34           C  
ANISOU  171  CA  ILE A  23     4327   3055   4906  -1225    903   -462       C  
ATOM    172  C   ILE A  23       8.238  16.171  -0.914  1.00 35.70           C  
ANISOU  172  C   ILE A  23     4746   3214   5606  -1248    936   -579       C  
ATOM    173  O   ILE A  23       7.518  16.975  -1.510  1.00 43.40           O  
ANISOU  173  O   ILE A  23     5650   4026   6814  -1199    931   -455       O  
ATOM    174  CB  ILE A  23       9.861  15.292  -2.599  1.00 36.18           C  
ANISOU  174  CB  ILE A  23     4721   3643   5384  -1275    855   -227       C  
ATOM    175  CG1 ILE A  23      10.357  14.059  -3.357  1.00 39.08           C  
ANISOU  175  CG1 ILE A  23     5093   4316   5441  -1184    820   -133       C  
ATOM    176  CG2 ILE A  23      11.005  15.953  -1.869  1.00 41.27           C  
ANISOU  176  CG2 ILE A  23     5336   4219   6127  -1426    836   -298       C  
ATOM    177  CD1 ILE A  23      10.915  12.981  -2.448  1.00 39.84           C  
ANISOU  177  CD1 ILE A  23     5258   4552   5327  -1196    807   -319       C  
ATOM    178  N   PRO A  24       8.642  16.369   0.359  1.00 37.87           N  
ANISOU  178  N   PRO A  24     5087   3484   5817  -1276    933   -806       N  
ATOM    179  CA  PRO A  24       8.285  17.639   1.015  1.00 41.16           C  
ANISOU  179  CA  PRO A  24     5498   3685   6458  -1254    929   -934       C  
ATOM    180  C   PRO A  24       8.841  18.851   0.262  1.00 41.55           C  
ANISOU  180  C   PRO A  24     5438   3562   6787  -1324    831   -754       C  
ATOM    181  O   PRO A  24      10.022  18.859  -0.110  1.00 37.51           O  
ANISOU  181  O   PRO A  24     4873   3118   6259  -1435    756   -630       O  
ATOM    182  CB  PRO A  24       8.939  17.520   2.399  1.00 42.30           C  
ANISOU  182  CB  PRO A  24     5745   3906   6423  -1296    908  -1194       C  
ATOM    183  CG  PRO A  24       9.990  16.453   2.245  1.00 40.80           C  
ANISOU  183  CG  PRO A  24     5568   3945   5988  -1377    857  -1128       C  
ATOM    184  CD  PRO A  24       9.435  15.494   1.241  1.00 34.59           C  
ANISOU  184  CD  PRO A  24     4757   3258   5128  -1327    920   -953       C  
ATOM    185  N   ASN A  25       7.995  19.863   0.060  1.00 50.72           N  
ANISOU  185  N   ASN A  25     9844   4248   5180    740   -103    514       N  
ATOM    186  CA  ASN A  25       8.343  21.058  -0.700  1.00 56.54           C  
ANISOU  186  CA  ASN A  25    10832   4687   5963    691    -73    757       C  
ATOM    187  C   ASN A  25       9.607  21.746  -0.213  1.00 56.00           C  
ANISOU  187  C   ASN A  25    10920   4332   6025    220      1    750       C  
ATOM    188  O   ASN A  25      10.417  22.210  -1.015  1.00 51.94           O  
ANISOU  188  O   ASN A  25    10441   3741   5554     -3    101    979       O  
ATOM    189  CB  ASN A  25       7.192  22.065  -0.651  1.00 66.10           C  
ANISOU  189  CB  ASN A  25    12196   5640   7281   1070   -101    711       C  
ATOM    190  CG  ASN A  25       6.743  22.503  -2.027  1.00 75.99           C  
ANISOU  190  CG  ASN A  25    13479   6938   8455   1350   -161    986       C  
ATOM    191  OD1 ASN A  25       6.071  21.750  -2.734  1.00 77.48           O  
ANISOU  191  OD1 ASN A  25    13454   7471   8514   1641   -281    998       O  
ATOM    192  ND2 ASN A  25       7.098  23.730  -2.415  1.00 84.14           N  
ANISOU  192  ND2 ASN A  25    14784   7620   9566   1271    -88   1191       N  
ATOM    193  N   HIS A  26       9.767  21.810   1.107  1.00 53.49           N  
ANISOU  193  N   HIS A  26    10672   3872   5778     73    -41    451       N  
ATOM    194  CA  HIS A  26      10.884  22.539   1.698  1.00 51.75           C  
ANISOU  194  CA  HIS A  26    10553   3384   5725   -353    -40    337       C  
ATOM    195  C   HIS A  26      12.248  21.890   1.429  1.00 48.55           C  
ANISOU  195  C   HIS A  26     9952   3142   5352   -790    -56    398       C  
ATOM    196  O   HIS A  26      13.282  22.476   1.727  1.00 51.15           O  
ANISOU  196  O   HIS A  26    10262   3278   5895  -1176    -58    295       O  
ATOM    197  CB  HIS A  26      10.654  22.806   3.202  1.00 52.50           C  
ANISOU  197  CB  HIS A  26    10742   3379   5827   -350   -126    -51       C  
ATOM    198  CG  HIS A  26      10.406  21.576   4.025  1.00 52.69           C  
ANISOU  198  CG  HIS A  26    10641   3748   5632   -263   -206   -252       C  
ATOM    199  ND1 HIS A  26       9.152  21.022   4.188  1.00 48.64           N  
ANISOU  199  ND1 HIS A  26    10064   3413   5004    123   -121   -299       N  
ATOM    200  CD2 HIS A  26      11.250  20.810   4.760  1.00 51.50           C  
ANISOU  200  CD2 HIS A  26    10381   3813   5374   -502   -354   -423       C  
ATOM    201  CE1 HIS A  26       9.240  19.956   4.963  1.00 47.01           C  
ANISOU  201  CE1 HIS A  26     9736   3504   4620     96   -148   -448       C  
ATOM    202  NE2 HIS A  26      10.500  19.806   5.326  1.00 47.48           N  
ANISOU  202  NE2 HIS A  26     9787   3604   4649   -249   -317   -512       N  
ATOM    203  N   TYR A  27      12.242  20.692   0.845  1.00 44.81           N  
ANISOU  203  N   TYR A  27     9175   3132   4719   -703    -60    516       N  
ATOM    204  CA  TYR A  27      13.478  19.983   0.501  1.00 44.35           C  
ANISOU  204  CA  TYR A  27     8768   3367   4718  -1043    -51    550       C  
ATOM    205  C   TYR A  27      13.623  19.748  -1.005  1.00 46.60           C  
ANISOU  205  C   TYR A  27     8969   3821   4916  -1014    144    891       C  
ATOM    206  O   TYR A  27      14.556  19.076  -1.435  1.00 47.45           O  
ANISOU  206  O   TYR A  27     8757   4208   5064  -1247    210    918       O  
ATOM    207  CB  TYR A  27      13.557  18.630   1.219  1.00 41.46           C  
ANISOU  207  CB  TYR A  27     8068   3445   4239   -982   -218    341       C  
ATOM    208  CG  TYR A  27      13.776  18.693   2.718  1.00 38.89           C  
ANISOU  208  CG  TYR A  27     7828   3036   3911  -1065   -426     13       C  
ATOM    209  CD1 TYR A  27      14.600  19.655   3.284  1.00 41.25           C  
ANISOU  209  CD1 TYR A  27     8257   3013   4401  -1390   -525   -167       C  
ATOM    210  CD2 TYR A  27      13.163  17.775   3.560  1.00 36.36           C  
ANISOU  210  CD2 TYR A  27     7481   2952   3381   -822   -510   -129       C  
ATOM    211  CE1 TYR A  27      14.800  19.707   4.658  1.00 45.08           C  
ANISOU  211  CE1 TYR A  27     8859   3461   4809  -1432   -773   -510       C  
ATOM    212  CE2 TYR A  27      13.353  17.815   4.931  1.00 35.32           C  
ANISOU  212  CE2 TYR A  27     7519   2766   3135   -855   -693   -405       C  
ATOM    213  CZ  TYR A  27      14.170  18.780   5.475  1.00 38.69           C  
ANISOU  213  CZ  TYR A  27     8088   2920   3692  -1141   -859   -609       C  
ATOM    214  OH  TYR A  27      14.359  18.817   6.842  1.00 40.74           O  
ANISOU  214  OH  TYR A  27     8463   3220   3798  -1106  -1064   -881       O  
ATOM    215  N   ALA A  28      12.706  20.294  -1.799  1.00 48.00           N  
ANISOU  215  N   ALA A  28     9413   3862   4961   -689    221   1120       N  
ATOM    216  CA  ALA A  28      12.686  20.044  -3.245  1.00 52.74           C  
ANISOU  216  CA  ALA A  28     9900   4740   5401   -547    351   1377       C  
ATOM    217  C   ALA A  28      14.002  20.387  -3.950  1.00 57.49           C  
ANISOU  217  C   ALA A  28    10447   5277   6118   -947    614   1556       C  
ATOM    218  O   ALA A  28      14.413  19.696  -4.885  1.00 58.65           O  
ANISOU  218  O   ALA A  28    10390   5766   6128   -968    743   1672       O  
ATOM    219  CB  ALA A  28      11.529  20.784  -3.901  1.00 54.14           C  
ANISOU  219  CB  ALA A  28    10290   4806   5477   -111    309   1515       C  
ATOM    220  N   GLU A  29      14.649  21.463  -3.509  1.00 60.50           N  
ANISOU  220  N   GLU A  29    10979   5222   6786  -1263    719   1538       N  
ATOM    221  CA  GLU A  29      15.904  21.903  -4.115  1.00 64.79           C  
ANISOU  221  CA  GLU A  29    11421   5652   7543  -1673   1020   1673       C  
ATOM    222  C   GLU A  29      17.134  21.314  -3.429  1.00 62.88           C  
ANISOU  222  C   GLU A  29    10798   5512   7581  -2163   1012   1409       C  
ATOM    223  O   GLU A  29      18.222  21.295  -4.006  1.00 64.62           O  
ANISOU  223  O   GLU A  29    10760   5796   7998  -2487   1274   1466       O  
ATOM    224  CB  GLU A  29      16.002  23.424  -4.078  1.00 74.42           C  
ANISOU  224  CB  GLU A  29    12929   6333   9015  -1778   1152   1769       C  
ATOM    225  CG  GLU A  29      15.484  24.054  -2.788  1.00 84.40           C  
ANISOU  225  CG  GLU A  29    14368   7257  10445  -1734    918   1491       C  
ATOM    226  CD  GLU A  29      16.045  25.446  -2.548  1.00100.40           C  
ANISOU  226  CD  GLU A  29    16537   8744  12866  -2021   1063   1471       C  
ATOM    227  OE1 GLU A  29      15.390  26.245  -1.839  1.00104.96           O  
ANISOU  227  OE1 GLU A  29    17356   8991  13533  -1864    934   1333       O  
ATOM    228  OE2 GLU A  29      17.147  25.738  -3.061  1.00108.34           O  
ANISOU  228  OE2 GLU A  29    17385   9656  14123  -2409   1322   1573       O  
ATOM    229  N   ASP A  30      16.956  20.840  -2.199  1.00 54.78           N  
ANISOU  229  N   ASP A  30     9713   4516   6584  -2196    692   1100       N  
ATOM    230  CA  ASP A  30      18.080  20.418  -1.370  1.00 52.43           C  
ANISOU  230  CA  ASP A  30     8983   4350   6588  -2572    529    755       C  
ATOM    231  C   ASP A  30      18.491  18.971  -1.604  1.00 50.31           C  
ANISOU  231  C   ASP A  30     8219   4666   6230  -2494    459    689       C  
ATOM    232  O   ASP A  30      19.574  18.556  -1.191  1.00 52.21           O  
ANISOU  232  O   ASP A  30     8017   5071   6751  -2768    350    446       O  
ATOM    233  CB  ASP A  30      17.748  20.632   0.110  1.00 52.79           C  
ANISOU  233  CB  ASP A  30     9132   4261   6665  -2501    147    395       C  
ATOM    234  CG  ASP A  30      17.343  22.060   0.409  1.00 58.61           C  
ANISOU  234  CG  ASP A  30    10305   4433   7530  -2524    210    385       C  
ATOM    235  OD1 ASP A  30      17.810  22.962  -0.312  1.00 59.76           O  
ANISOU  235  OD1 ASP A  30    10468   4321   7915  -2697    501    566       O  
ATOM    236  OD2 ASP A  30      16.559  22.276   1.359  1.00 60.73           O  
ANISOU  236  OD2 ASP A  30    10819   4587   7671  -2287     -9    186       O  
ATOM    237  N   LEU A  31      17.619  18.201  -2.248  1.00 41.71           N  
ANISOU  237  N   LEU A  31     7183   3877   4788  -2101    492    867       N  
ATOM    238  CA  LEU A  31      17.910  16.806  -2.545  1.00 38.73           C  
ANISOU  238  CA  LEU A  31     6377   4002   4335  -1997    456    798       C  
ATOM    239  C   LEU A  31      18.245  16.648  -4.019  1.00 44.86           C  
ANISOU  239  C   LEU A  31     7102   4937   5005  -2050    837   1052       C  
ATOM    240  O   LEU A  31      17.827  17.456  -4.851  1.00 47.71           O  
ANISOU  240  O   LEU A  31     7866   5076   5184  -1999   1076   1347       O  
ATOM    241  CB  LEU A  31      16.720  15.916  -2.178  1.00 35.22           C  
ANISOU  241  CB  LEU A  31     5980   3790   3612  -1550    236    736       C  
ATOM    242  CG  LEU A  31      16.263  16.041  -0.723  1.00 34.22           C  
ANISOU  242  CG  LEU A  31     5990   3516   3496  -1455    -61    511       C  
ATOM    243  CD1 LEU A  31      15.022  15.201  -0.434  1.00 33.99           C  
ANISOU  243  CD1 LEU A  31     6010   3670   3234  -1050   -151    472       C  
ATOM    244  CD2 LEU A  31      17.396  15.670   0.217  1.00 35.88           C  
ANISOU  244  CD2 LEU A  31     5897   3812   3922  -1693   -288    256       C  
ATOM    245  N   GLU A  32      19.013  15.614  -4.343  1.00 44.74           N  
ANISOU  245  N   GLU A  32     6625   5293   5079  -2125    903    941       N  
ATOM    246  CA  GLU A  32      19.406  15.393  -5.727  1.00 44.28           C  
ANISOU  246  CA  GLU A  32     6513   5423   4887  -2180   1310   1133       C  
ATOM    247  C   GLU A  32      18.601  14.245  -6.331  1.00 40.09           C  
ANISOU  247  C   GLU A  32     5945   5291   3996  -1766   1238   1126       C  
ATOM    248  O   GLU A  32      18.103  14.348  -7.453  1.00 44.22           O  
ANISOU  248  O   GLU A  32     6748   5900   4154  -1588   1438   1342       O  
ATOM    249  CB  GLU A  32      20.902  15.097  -5.837  1.00 50.98           C  
ANISOU  249  CB  GLU A  32     6832   6397   6141  -2572   1525    972       C  
ATOM    250  CG  GLU A  32      21.419  15.127  -7.272  1.00 59.39           C  
ANISOU  250  CG  GLU A  32     7882   7578   7108  -2610   2019   1165       C  
ATOM    251  CD  GLU A  32      21.208  16.480  -7.937  1.00 72.51           C  
ANISOU  251  CD  GLU A  32    10024   8868   8657  -2610   2256   1496       C  
ATOM    252  OE1 GLU A  32      21.350  17.517  -7.250  1.00 75.16           O  
ANISOU  252  OE1 GLU A  32    10498   8794   9266  -2841   2199   1495       O  
ATOM    253  OE2 GLU A  32      20.894  16.505  -9.147  1.00 78.88           O  
ANISOU  253  OE2 GLU A  32    11067   9804   9099  -2364   2463   1740       O  
ATOM    254  N   ARG A  33      18.497  13.151  -5.582  1.00 37.59           N  
ANISOU  254  N   ARG A  33     5301   5200   3783  -1613    944    867       N  
ATOM    255  CA  ARG A  33      17.800  11.947  -6.033  1.00 37.32           C  
ANISOU  255  CA  ARG A  33     5155   5501   3524  -1273    877    782       C  
ATOM    256  C   ARG A  33      17.254  11.205  -4.832  1.00 32.02           C  
ANISOU  256  C   ARG A  33     4370   4841   2955  -1087    530    581       C  
ATOM    257  O   ARG A  33      17.802  11.295  -3.738  1.00 30.58           O  
ANISOU  257  O   ARG A  33     4077   4534   3008  -1227    346    471       O  
ATOM    258  CB  ARG A  33      18.758  10.994  -6.766  1.00 41.98           C  
ANISOU  258  CB  ARG A  33     5329   6409   4212  -1362   1102    668       C  
ATOM    259  CG  ARG A  33      19.514  11.567  -7.941  1.00 46.99           C  
ANISOU  259  CG  ARG A  33     6023   7069   4762  -1593   1558    842       C  
ATOM    260  CD  ARG A  33      18.645  11.673  -9.177  1.00 52.69           C  
ANISOU  260  CD  ARG A  33     7133   7866   5020  -1259   1664   1011       C  
ATOM    261  NE  ARG A  33      18.485  10.386  -9.846  1.00 47.68           N  
ANISOU  261  NE  ARG A  33     6284   7558   4275   -999   1652    795       N  
ATOM    262  CZ  ARG A  33      17.968  10.244 -11.061  1.00 51.82           C  
ANISOU  262  CZ  ARG A  33     7071   8167   4451   -708   1734    833       C  
ATOM    263  NH1 ARG A  33      17.562  11.312 -11.729  1.00 50.60           N  
ANISOU  263  NH1 ARG A  33     7357   7876   3993   -566   1824   1142       N  
ATOM    264  NH2 ARG A  33      17.864   9.039 -11.612  1.00 49.71           N  
ANISOU  264  NH2 ARG A  33     6615   8128   4147   -542   1699    568       N  
ATOM    265  N   VAL A  34      16.182  10.449  -5.034  1.00 27.22           N  
ANISOU  265  N   VAL A  34     3795   4381   2166   -772    449    518       N  
ATOM    266  CA  VAL A  34      15.789   9.444  -4.056  1.00 26.06           C  
ANISOU  266  CA  VAL A  34     3493   4270   2140   -618    248    336       C  
ATOM    267  C   VAL A  34      16.747   8.263  -4.215  1.00 26.01           C  
ANISOU  267  C   VAL A  34     3073   4482   2330   -662    291    195       C  
ATOM    268  O   VAL A  34      16.980   7.782  -5.333  1.00 30.06           O  
ANISOU  268  O   VAL A  34     3424   5216   2782   -640    484    159       O  
ATOM    269  CB  VAL A  34      14.337   9.008  -4.263  1.00 28.90           C  
ANISOU  269  CB  VAL A  34     3955   4682   2342   -315    205    272       C  
ATOM    270  CG1 VAL A  34      13.977   7.832  -3.349  1.00 29.16           C  
ANISOU  270  CG1 VAL A  34     3825   4718   2535   -197    116    102       C  
ATOM    271  CG2 VAL A  34      13.406  10.182  -3.984  1.00 35.08           C  
ANISOU  271  CG2 VAL A  34     5102   5229   2999   -225    138    380       C  
ATOM    272  N   PHE A  35      17.320   7.808  -3.105  1.00 26.75           N  
ANISOU  272  N   PHE A  35     3016   4511   2636   -692    101    107       N  
ATOM    273  CA  PHE A  35      18.332   6.757  -3.167  1.00 26.42           C  
ANISOU  273  CA  PHE A  35     2566   4634   2837   -695     97    -24       C  
ATOM    274  C   PHE A  35      17.711   5.414  -2.788  1.00 30.97           C  
ANISOU  274  C   PHE A  35     3094   5228   3445   -427     29   -119       C  
ATOM    275  O   PHE A  35      17.842   4.427  -3.524  1.00 31.82           O  
ANISOU  275  O   PHE A  35     2956   5491   3644   -332    166   -236       O  
ATOM    276  CB  PHE A  35      19.498   7.100  -2.252  1.00 29.90           C  
ANISOU  276  CB  PHE A  35     2841   4999   3522   -865   -121    -72       C  
ATOM    277  CG  PHE A  35      20.752   6.359  -2.569  1.00 34.90           C  
ANISOU  277  CG  PHE A  35     2974   5813   4473   -906    -93   -214       C  
ATOM    278  CD1 PHE A  35      21.340   6.461  -3.829  1.00 36.84           C  
ANISOU  278  CD1 PHE A  35     2972   6228   4799  -1065    260   -237       C  
ATOM    279  CD2 PHE A  35      21.365   5.571  -1.603  1.00 36.99           C  
ANISOU  279  CD2 PHE A  35     3031   6076   4947   -759   -409   -322       C  
ATOM    280  CE1 PHE A  35      22.515   5.786  -4.115  1.00 44.82           C  
ANISOU  280  CE1 PHE A  35     3467   7406   6156  -1096    330   -410       C  
ATOM    281  CE2 PHE A  35      22.545   4.890  -1.885  1.00 39.70           C  
ANISOU  281  CE2 PHE A  35     2858   6579   5646   -749   -413   -481       C  
ATOM    282  CZ  PHE A  35      23.114   4.996  -3.143  1.00 44.53           C  
ANISOU  282  CZ  PHE A  35     3188   7339   6394   -916    -25   -536       C  
ATOM    283  N   ILE A  36      17.036   5.384  -1.641  1.00 30.70           N  
ANISOU  283  N   ILE A  36     3318   5005   3342   -318   -137    -80       N  
ATOM    284  CA  ILE A  36      16.247   4.216  -1.241  1.00 26.69           C  
ANISOU  284  CA  ILE A  36     2849   4430   2864    -97   -108   -131       C  
ATOM    285  C   ILE A  36      14.836   4.635  -0.865  1.00 28.05           C  
ANISOU  285  C   ILE A  36     3339   4456   2862    -26    -46    -97       C  
ATOM    286  O   ILE A  36      14.629   5.223   0.200  1.00 26.81           O  
ANISOU  286  O   ILE A  36     3466   4131   2590    -31   -153    -23       O  
ATOM    287  CB  ILE A  36      16.880   3.475  -0.045  1.00 25.56           C  
ANISOU  287  CB  ILE A  36     2712   4169   2829     14   -312   -106       C  
ATOM    288  CG1 ILE A  36      18.368   3.225  -0.297  1.00 27.97           C  
ANISOU  288  CG1 ILE A  36     2637   4618   3370    -37   -442   -174       C  
ATOM    289  CG2 ILE A  36      16.167   2.144   0.201  1.00 26.13           C  
ANISOU  289  CG2 ILE A  36     2824   4116   2986    219   -182   -128       C  
ATOM    290  CD1 ILE A  36      19.150   2.864   0.987  1.00 32.00           C  
ANISOU  290  CD1 ILE A  36     3183   5035   3942     98   -794   -142       C  
ATOM    291  N   PRO A  37      13.857   4.329  -1.732  1.00 23.86           N  
ANISOU  291  N   PRO A  37     2740   4003   2323     57    117   -197       N  
ATOM    292  CA  PRO A  37      12.462   4.688  -1.459  1.00 22.73           C  
ANISOU  292  CA  PRO A  37     2790   3743   2102    147    181   -225       C  
ATOM    293  C   PRO A  37      11.992   4.136  -0.128  1.00 24.94           C  
ANISOU  293  C   PRO A  37     3245   3793   2440    215    238   -203       C  
ATOM    294  O   PRO A  37      12.369   3.011   0.236  1.00 23.55           O  
ANISOU  294  O   PRO A  37     2989   3555   2404    261    280   -208       O  
ATOM    295  CB  PRO A  37      11.692   3.988  -2.582  1.00 22.78           C  
ANISOU  295  CB  PRO A  37     2559   3906   2192    245    292   -428       C  
ATOM    296  CG  PRO A  37      12.699   3.874  -3.712  1.00 26.92           C  
ANISOU  296  CG  PRO A  37     2892   4668   2667    183    287   -448       C  
ATOM    297  CD  PRO A  37      14.006   3.603  -3.008  1.00 26.13           C  
ANISOU  297  CD  PRO A  37     2736   4506   2685     87    232   -346       C  
ATOM    298  N   HIS A  38      11.181   4.921   0.576  1.00 24.19           N  
ANISOU  298  N   HIS A  38     3622   3048   2522    -96   -326    494       N  
ATOM    299  CA  HIS A  38      10.599   4.522   1.852  1.00 22.50           C  
ANISOU  299  CA  HIS A  38     3258   2823   2468      8   -307    407       C  
ATOM    300  C   HIS A  38      10.006   3.120   1.792  1.00 22.40           C  
ANISOU  300  C   HIS A  38     3166   2895   2451     61   -335    349       C  
ATOM    301  O   HIS A  38      10.228   2.288   2.674  1.00 21.00           O  
ANISOU  301  O   HIS A  38     2891   2780   2309     87   -257    260       O  
ATOM    302  CB  HIS A  38       9.482   5.496   2.251  1.00 23.79           C  
ANISOU  302  CB  HIS A  38     3407   2834   2798     98   -401    448       C  
ATOM    303  CG  HIS A  38       8.790   5.113   3.524  1.00 27.52           C  
ANISOU  303  CG  HIS A  38     3731   3303   3424    193   -360    352       C  
ATOM    304  ND1 HIS A  38       7.515   4.586   3.551  1.00 26.71           N  
ANISOU  304  ND1 HIS A  38     3526   3200   3424    283   -442    344       N  
ATOM    305  CD2 HIS A  38       9.196   5.177   4.818  1.00 27.18           C  
ANISOU  305  CD2 HIS A  38     3628   3265   3435    192   -243    262       C  
ATOM    306  CE1 HIS A  38       7.167   4.341   4.802  1.00 27.64           C  
ANISOU  306  CE1 HIS A  38     3528   3323   3649    332   -358    251       C  
ATOM    307  NE2 HIS A  38       8.162   4.694   5.592  1.00 29.83           N  
ANISOU  307  NE2 HIS A  38     3841   3601   3892    279   -241    200       N  
ATOM    308  N   GLY A  39       9.250   2.861   0.733  1.00 24.98           N  
ANISOU  308  N   GLY A  39     3552   3215   2725     63   -461    408       N  
ATOM    309  CA  GLY A  39       8.557   1.590   0.632  1.00 29.03           C  
ANISOU  309  CA  GLY A  39     4004   3787   3237     94   -509    358       C  
ATOM    310  C   GLY A  39       9.511   0.424   0.510  1.00 24.25           C  
ANISOU  310  C   GLY A  39     3418   3288   2509     53   -397    274       C  
ATOM    311  O   GLY A  39       9.235  -0.662   1.000  1.00 23.94           O  
ANISOU  311  O   GLY A  39     3308   3283   2505     86   -382    201       O  
ATOM    312  N   LEU A  40      10.636   0.640  -0.162  1.00 23.98           N  
ANISOU  312  N   LEU A  40     3480   3300   2332    -21   -314    284       N  
ATOM    313  CA  LEU A  40      11.657  -0.403  -0.245  1.00 26.06           C  
ANISOU  313  CA  LEU A  40     3738   3661   2502    -37   -185    193       C  
ATOM    314  C   LEU A  40      12.255  -0.672   1.146  1.00 23.61           C  
ANISOU  314  C   LEU A  40     3288   3375   2308     15    -87    124       C  
ATOM    315  O   LEU A  40      12.544  -1.817   1.525  1.00 21.19           O  
ANISOU  315  O   LEU A  40     2931   3110   2009     58    -39     45       O  
ATOM    316  CB  LEU A  40      12.723  -0.008  -1.274  1.00 27.57           C  
ANISOU  316  CB  LEU A  40     4040   3910   2524   -134    -96    217       C  
ATOM    317  CG  LEU A  40      13.958  -0.904  -1.385  1.00 33.10           C  
ANISOU  317  CG  LEU A  40     4709   4719   3149   -137     71    117       C  
ATOM    318  CD1 LEU A  40      13.547  -2.349  -1.637  1.00 36.51           C  
ANISOU  318  CD1 LEU A  40     5163   5161   3550    -79     53     30       C  
ATOM    319  CD2 LEU A  40      14.907  -0.401  -2.463  1.00 26.13           C  
ANISOU  319  CD2 LEU A  40     3928   3904   2095   -251    176    142       C  
ATOM    320  N   ILE A  41      12.407   0.390   1.924  1.00 21.18           N  
ANISOU  320  N   ILE A  41     2936   3025   2087      7    -73    156       N  
ATOM    321  CA  ILE A  41      12.903   0.257   3.289  1.00 20.06           C  
ANISOU  321  CA  ILE A  41     2682   2901   2038     35     -5    100       C  
ATOM    322  C   ILE A  41      11.943  -0.614   4.090  1.00 21.78           C  
ANISOU  322  C   ILE A  41     2835   3096   2346    107    -50     55       C  
ATOM    323  O   ILE A  41      12.371  -1.522   4.811  1.00 19.59           O  
ANISOU  323  O   ILE A  41     2499   2860   2083    133     -6     -2       O  
ATOM    324  CB  ILE A  41      13.089   1.634   3.961  1.00 23.66           C  
ANISOU  324  CB  ILE A  41     3136   3296   2559     -3      8    136       C  
ATOM    325  CG1 ILE A  41      14.204   2.435   3.284  1.00 23.20           C  
ANISOU  325  CG1 ILE A  41     3137   3269   2407   -107     68    180       C  
ATOM    326  CG2 ILE A  41      13.403   1.477   5.465  1.00 21.49           C  
ANISOU  326  CG2 ILE A  41     2765   3034   2365     13     55     75       C  
ATOM    327  CD1 ILE A  41      14.307   3.895   3.788  1.00 25.30           C  
ANISOU  327  CD1 ILE A  41     3444   3441   2728   -166     63    224       C  
ATOM    328  N   MET A  42      10.644  -0.350   3.942  1.00 20.09           N  
ANISOU  328  N   MET A  42     2624   2814   2194    134   -145     88       N  
ATOM    329  CA  MET A  42       9.611  -1.104   4.651  1.00 20.55           C  
ANISOU  329  CA  MET A  42     2609   2859   2342    179   -181     51       C  
ATOM    330  C   MET A  42       9.682  -2.583   4.278  1.00 20.08           C  
ANISOU  330  C   MET A  42     2570   2845   2214    178   -188      7       C  
ATOM    331  O   MET A  42       9.679  -3.452   5.157  1.00 19.55           O  
ANISOU  331  O   MET A  42     2458   2789   2183    194   -157    -41       O  
ATOM    332  CB  MET A  42       8.218  -0.577   4.301  1.00 21.82           C  
ANISOU  332  CB  MET A  42     2745   2956   2587    208   -289    100       C  
ATOM    333  CG  MET A  42       7.949   0.823   4.804  1.00 25.68           C  
ANISOU  333  CG  MET A  42     3211   3365   3181    239   -282    129       C  
ATOM    334  SD  MET A  42       8.244   0.981   6.578  1.00 34.50           S  
ANISOU  334  SD  MET A  42     4256   4478   4376    247   -153     46       S  
ATOM    335  CE  MET A  42       6.759   0.238   7.263  1.00 52.39           C  
ANISOU  335  CE  MET A  42     6396   6749   6759    290   -168      3       C  
ATOM    336  N   ASP A  43       9.748  -2.870   2.981  1.00 19.02           N  
ANISOU  336  N   ASP A  43     2528   2727   1972    153   -230     24       N  
ATOM    337  CA  ASP A  43       9.774  -4.276   2.543  1.00 19.87           C  
ANISOU  337  CA  ASP A  43     2686   2856   2009    150   -236    -33       C  
ATOM    338  C   ASP A  43      10.990  -5.025   3.061  1.00 23.61           C  
ANISOU  338  C   ASP A  43     3144   3364   2463    183   -124    -98       C  
ATOM    339  O   ASP A  43      10.900  -6.197   3.438  1.00 21.44           O  
ANISOU  339  O   ASP A  43     2872   3071   2203    209   -124   -148       O  
ATOM    340  CB  ASP A  43       9.732  -4.369   1.020  1.00 21.07           C  
ANISOU  340  CB  ASP A  43     2968   3019   2018    103   -287    -16       C  
ATOM    341  CG  ASP A  43       8.402  -3.946   0.455  1.00 26.75           C  
ANISOU  341  CG  ASP A  43     3701   3704   2760     73   -445     54       C  
ATOM    342  OD1 ASP A  43       7.371  -4.102   1.155  1.00 29.97           O  
ANISOU  342  OD1 ASP A  43     4005   4085   3297     95   -509     59       O  
ATOM    343  OD2 ASP A  43       8.393  -3.447  -0.679  1.00 28.42           O  
ANISOU  343  OD2 ASP A  43     4021   3918   2860     24   -505    109       O  
ATOM    344  N   ARG A  44      12.144  -4.362   3.062  1.00 22.17           N  
ANISOU  344  N   ARG A  44     2943   3227   2252    180    -37    -92       N  
ATOM    345  CA  ARG A  44      13.352  -4.997   3.577  1.00 20.08           C  
ANISOU  345  CA  ARG A  44     2628   3008   1995    223     56   -145       C  
ATOM    346  C   ARG A  44      13.216  -5.196   5.079  1.00 23.64           C  
ANISOU  346  C   ARG A  44     2994   3436   2552    249     40   -146       C  
ATOM    347  O   ARG A  44      13.563  -6.252   5.620  1.00 23.28           O  
ANISOU  347  O   ARG A  44     2932   3384   2530    298     48   -184       O  
ATOM    348  CB  ARG A  44      14.598  -4.157   3.236  1.00 19.96           C  
ANISOU  348  CB  ARG A  44     2583   3065   1934    190    150   -131       C  
ATOM    349  CG  ARG A  44      15.876  -4.699   3.830  1.00 21.29           C  
ANISOU  349  CG  ARG A  44     2652   3296   2141    241    231   -176       C  
ATOM    350  CD  ARG A  44      16.181  -6.117   3.358  1.00 25.89           C  
ANISOU  350  CD  ARG A  44     3265   3876   2698    323    267   -253       C  
ATOM    351  NE  ARG A  44      17.410  -6.611   3.991  1.00 28.49           N  
ANISOU  351  NE  ARG A  44     3472   4257   3096    397    328   -287       N  
ATOM    352  CZ  ARG A  44      17.604  -7.863   4.401  1.00 33.52           C  
ANISOU  352  CZ  ARG A  44     4098   4850   3787    500    313   -333       C  
ATOM    353  NH1 ARG A  44      16.656  -8.779   4.230  1.00 29.37           N  
ANISOU  353  NH1 ARG A  44     3690   4226   3244    523    253   -360       N  
ATOM    354  NH2 ARG A  44      18.757  -8.202   4.968  1.00 34.74           N  
ANISOU  354  NH2 ARG A  44     4124   5055   4020    577    347   -347       N  
ATOM    355  N   THR A  45      12.682  -4.186   5.760  1.00 20.09           N  
ANISOU  355  N   THR A  45     2508   2965   2162    216     16   -107       N  
ATOM    356  CA  THR A  45      12.536  -4.244   7.212  1.00 19.95           C  
ANISOU  356  CA  THR A  45     2431   2931   2216    218     15   -114       C  
ATOM    357  C   THR A  45      11.589  -5.374   7.612  1.00 23.89           C  
ANISOU  357  C   THR A  45     2945   3390   2743    231    -30   -133       C  
ATOM    358  O   THR A  45      11.783  -6.024   8.642  1.00 22.60           O  
ANISOU  358  O   THR A  45     2767   3220   2599    236    -25   -145       O  
ATOM    359  CB  THR A  45      12.057  -2.894   7.780  1.00 20.78           C  
ANISOU  359  CB  THR A  45     2516   3007   2374    181     18    -88       C  
ATOM    360  OG1 THR A  45      13.015  -1.881   7.442  1.00 23.00           O  
ANISOU  360  OG1 THR A  45     2802   3314   2624    146     56    -65       O  
ATOM    361  CG2 THR A  45      11.904  -2.947   9.318  1.00 22.04           C  
ANISOU  361  CG2 THR A  45     2640   3157   2580    165     37   -110       C  
ATOM    362  N   GLU A  46      10.578  -5.633   6.786  1.00 20.49           N  
ANISOU  362  N   GLU A  46     2550   2930   2304    223    -84   -130       N  
ATOM    363  CA  GLU A  46       9.669  -6.744   7.071  1.00 17.67           C  
ANISOU  363  CA  GLU A  46     2208   2536   1971    208   -129   -147       C  
ATOM    364  C   GLU A  46      10.423  -8.071   7.142  1.00 22.81           C  
ANISOU  364  C   GLU A  46     2917   3167   2581    240   -118   -182       C  
ATOM    365  O   GLU A  46      10.200  -8.872   8.056  1.00 20.73           O  
ANISOU  365  O   GLU A  46     2663   2870   2345    227   -130   -185       O  
ATOM    366  CB  GLU A  46       8.557  -6.858   6.019  1.00 21.19           C  
ANISOU  366  CB  GLU A  46     2681   2964   2407    179   -210   -136       C  
ATOM    367  CG  GLU A  46       7.571  -8.000   6.335  1.00 21.03           C  
ANISOU  367  CG  GLU A  46     2666   2909   2415    133   -260   -153       C  
ATOM    368  CD  GLU A  46       6.402  -8.072   5.357  1.00 32.29           C  
ANISOU  368  CD  GLU A  46     4094   4331   3843     84   -364   -137       C  
ATOM    369  OE1 GLU A  46       5.548  -8.962   5.508  1.00 31.60           O  
ANISOU  369  OE1 GLU A  46     4005   4222   3779     22   -414   -148       O  
ATOM    370  OE2 GLU A  46       6.336  -7.241   4.428  1.00 36.92           O  
ANISOU  370  OE2 GLU A  46     4689   4934   4403     95   -410   -104       O  
ATOM    371  N   ARG A  47      11.318  -8.296   6.183  1.00 21.89           N  
ANISOU  371  N   ARG A  47     2848   3068   2402    283    -91   -209       N  
ATOM    372  CA  ARG A  47      12.069  -9.550   6.142  1.00 24.30           C  
ANISOU  372  CA  ARG A  47     3206   3338   2689    344    -73   -255       C  
ATOM    373  C   ARG A  47      13.043  -9.550   7.304  1.00 25.52           C  
ANISOU  373  C   ARG A  47     3288   3515   2895    388    -46   -238       C  
ATOM    374  O   ARG A  47      13.244 -10.574   7.963  1.00 24.00           O  
ANISOU  374  O   ARG A  47     3125   3265   2730    425    -73   -242       O  
ATOM    375  CB  ARG A  47      12.816  -9.709   4.821  1.00 25.74           C  
ANISOU  375  CB  ARG A  47     3444   3543   2792    384    -19   -306       C  
ATOM    376  CG  ARG A  47      13.781 -10.896   4.812  1.00 28.90           C  
ANISOU  376  CG  ARG A  47     3876   3904   3200    483     26   -368       C  
ATOM    377  CD  ARG A  47      13.040 -12.195   5.065  1.00 32.91           C  
ANISOU  377  CD  ARG A  47     4489   4294   3723    480    -44   -391       C  
ATOM    378  NE  ARG A  47      13.950 -13.326   5.264  1.00 37.36           N  
ANISOU  378  NE  ARG A  47     5086   4786   4324    596    -18   -439       N  
ATOM    379  CZ  ARG A  47      14.142 -14.301   4.386  1.00 35.97           C  
ANISOU  379  CZ  ARG A  47     5029   4530   4106    651     12   -527       C  
ATOM    380  NH1 ARG A  47      13.477 -14.305   3.229  1.00 32.81           N  
ANISOU  380  NH1 ARG A  47     4741   4123   3601    577     12   -574       N  
ATOM    381  NH2 ARG A  47      14.990 -15.289   4.666  1.00 34.61           N  
ANISOU  381  NH2 ARG A  47     4876   4277   3997    782     34   -569       N  
ATOM    382  N   LEU A  48      13.634  -8.390   7.571  1.00 21.61           N  
ANISOU  382  N   LEU A  48     2709   3092   2409    374     -7   -211       N  
ATOM    383  CA  LEU A  48      14.561  -8.276   8.699  1.00 23.33           C  
ANISOU  383  CA  LEU A  48     2854   3344   2667    392     -4   -189       C  
ATOM    384  C   LEU A  48      13.910  -8.674  10.021  1.00 23.21           C  
ANISOU  384  C   LEU A  48     2863   3281   2677    351    -58   -160       C  
ATOM    385  O   LEU A  48      14.539  -9.324  10.853  1.00 24.60           O  
ANISOU  385  O   LEU A  48     3034   3443   2868    382    -93   -141       O  
ATOM    386  CB  LEU A  48      15.133  -6.861   8.818  1.00 28.00           C  
ANISOU  386  CB  LEU A  48     3369   4012   3257    344     36   -166       C  
ATOM    387  CG  LEU A  48      16.333  -6.513   7.954  1.00 35.63           C  
ANISOU  387  CG  LEU A  48     4278   5056   4203    370    104   -181       C  
ATOM    388  CD1 LEU A  48      17.002  -5.248   8.450  1.00 31.23           C  
ANISOU  388  CD1 LEU A  48     3645   4566   3656    298    124   -148       C  
ATOM    389  CD2 LEU A  48      17.329  -7.654   7.932  1.00 36.55           C  
ANISOU  389  CD2 LEU A  48     4350   5187   4351    474    116   -213       C  
ATOM    390  N   ALA A  49      12.662  -8.260  10.227  1.00 21.05           N  
ANISOU  390  N   ALA A  49     2608   2984   2404    280    -63   -153       N  
ATOM    391  CA  ALA A  49      11.957  -8.575  11.465  1.00 22.85           C  
ANISOU  391  CA  ALA A  49     2859   3181   2641    218    -83   -133       C  
ATOM    392  C   ALA A  49      11.815 -10.076  11.623  1.00 21.61           C  
ANISOU  392  C   ALA A  49     2784   2950   2478    232   -133   -128       C  
ATOM    393  O   ALA A  49      11.940 -10.612  12.727  1.00 21.96           O  
ANISOU  393  O   ALA A  49     2867   2966   2510    202   -164    -95       O  
ATOM    394  CB  ALA A  49      10.603  -7.911  11.482  1.00 24.59           C  
ANISOU  394  CB  ALA A  49     3058   3399   2887    154    -60   -140       C  
ATOM    395  N   ARG A  50      11.543 -10.768  10.519  1.00 21.68           N  
ANISOU  395  N   ARG A  50     2841   2914   2482    266   -149   -159       N  
ATOM    396  CA  ARG A  50      11.395 -12.212  10.598  1.00 24.36           C  
ANISOU  396  CA  ARG A  50     3284   3153   2816    275   -198   -161       C  
ATOM    397  C   ARG A  50      12.728 -12.875  10.948  1.00 28.01           C  
ANISOU  397  C   ARG A  50     3763   3583   3295    381   -222   -150       C  
ATOM    398  O   ARG A  50      12.773 -13.828  11.744  1.00 30.29           O  
ANISOU  398  O   ARG A  50     4130   3789   3589    378   -280   -113       O  
ATOM    399  CB  ARG A  50      10.853 -12.782   9.282  1.00 30.91           C  
ANISOU  399  CB  ARG A  50     4184   3935   3626    278   -212   -211       C  
ATOM    400  CG  ARG A  50      10.316 -14.202   9.436  1.00 38.70           C  
ANISOU  400  CG  ARG A  50     5299   4797   4607    240   -269   -215       C  
ATOM    401  CD  ARG A  50       9.586 -14.645   8.189  1.00 43.51           C  
ANISOU  401  CD  ARG A  50     5984   5365   5183    201   -295   -267       C  
ATOM    402  NE  ARG A  50      10.520 -14.969   7.121  1.00 45.92           N  
ANISOU  402  NE  ARG A  50     6349   5644   5453    311   -266   -334       N  
ATOM    403  CZ  ARG A  50      10.255 -14.844   5.825  1.00 47.01           C  
ANISOU  403  CZ  ARG A  50     6535   5798   5529    293   -262   -388       C  
ATOM    404  NH1 ARG A  50       9.079 -14.386   5.421  1.00 46.12           N  
ANISOU  404  NH1 ARG A  50     6401   5726   5397    179   -314   -369       N  
ATOM    405  NH2 ARG A  50      11.173 -15.169   4.931  1.00 49.43           N  
ANISOU  405  NH2 ARG A  50     6905   6084   5791    390   -206   -462       N  
ATOM    406  N   ASP A  51      13.809 -12.370  10.354  1.00 23.79           N  
ANISOU  406  N   ASP A  51     3150   3115   2773    470   -180   -176       N  
ATOM    407  CA  ASP A  51      15.152 -12.886  10.614  1.00 22.46           C  
ANISOU  407  CA  ASP A  51     2944   2941   2650    590   -199   -169       C  
ATOM    408  C   ASP A  51      15.511 -12.680  12.082  1.00 25.15           C  
ANISOU  408  C   ASP A  51     3250   3306   3001    552   -264    -92       C  
ATOM    409  O   ASP A  51      16.095 -13.553  12.718  1.00 25.18           O  
ANISOU  409  O   ASP A  51     3284   3245   3036    616   -341    -52       O  
ATOM    410  CB  ASP A  51      16.183 -12.178   9.716  1.00 25.87           C  
ANISOU  410  CB  ASP A  51     3262   3474   3093    661   -118   -212       C  
ATOM    411  CG  ASP A  51      16.028 -12.535   8.233  1.00 31.39           C  
ANISOU  411  CG  ASP A  51     4023   4147   3755    702    -50   -294       C  
ATOM    412  OD1 ASP A  51      15.317 -13.506   7.921  1.00 28.96           O  
ANISOU  412  OD1 ASP A  51     3847   3728   3430    702    -81   -324       O  
ATOM    413  OD2 ASP A  51      16.642 -11.859   7.378  1.00 27.89           O  
ANISOU  413  OD2 ASP A  51     3513   3794   3290    721     36   -330       O  
ATOM    414  N   VAL A  52      15.155 -11.516  12.611  1.00 25.09           N  
ANISOU  414  N   VAL A  52     3192   3380   2959    446   -239    -72       N  
ATOM    415  CA  VAL A  52      15.411 -11.218  14.020  1.00 23.93           C  
ANISOU  415  CA  VAL A  52     3041   3263   2790    378   -293    -11       C  
ATOM    416  C   VAL A  52      14.680 -12.219  14.895  1.00 27.83           C  
ANISOU  416  C   VAL A  52     3667   3658   3250    319   -356     35       C  
ATOM    417  O   VAL A  52      15.252 -12.812  15.804  1.00 25.44           O  
ANISOU  417  O   VAL A  52     3407   3321   2937    329   -449    101       O  
ATOM    418  CB  VAL A  52      14.955  -9.799  14.386  1.00 27.72           C  
ANISOU  418  CB  VAL A  52     3479   3821   3232    267   -234    -21       C  
ATOM    419  CG1 VAL A  52      14.870  -9.640  15.902  1.00 26.10           C  
ANISOU  419  CG1 VAL A  52     3324   3624   2967    162   -277     25       C  
ATOM    420  CG2 VAL A  52      15.892  -8.751  13.772  1.00 29.09           C  
ANISOU  420  CG2 VAL A  52     3537   4088   3429    297   -191    -43       C  
ATOM    421  N   MET A  53      13.411 -12.437  14.597  1.00 27.48           N  
ANISOU  421  N   MET A  53     3688   3567   3186    248   -314     10       N  
ATOM    422  CA AMET A  53      12.607 -13.333  15.412  0.64 28.63           C  
ANISOU  422  CA AMET A  53     3960   3628   3290    154   -353     54       C  
ATOM    423  CA BMET A  53      12.599 -13.336  15.408  0.36 28.70           C  
ANISOU  423  CA BMET A  53     3969   3637   3300    154   -353     54       C  
ATOM    424  C   MET A  53      13.095 -14.772  15.334  1.00 30.63           C  
ANISOU  424  C   MET A  53     4319   3750   3569    238   -446     89       C  
ATOM    425  O   MET A  53      13.069 -15.505  16.328  1.00 32.28           O  
ANISOU  425  O   MET A  53     4641   3886   3740    184   -522    163       O  
ATOM    426  CB AMET A  53      11.127 -13.202  15.047  0.64 28.63           C  
ANISOU  426  CB AMET A  53     3969   3626   3283     51   -285     16       C  
ATOM    427  CB BMET A  53      11.115 -13.238  15.021  0.36 28.51           C  
ANISOU  427  CB BMET A  53     3956   3607   3268     52   -286     16       C  
ATOM    428  CG AMET A  53      10.511 -11.959  15.652  0.64 25.87           C  
ANISOU  428  CG AMET A  53     3545   3372   2911    -44   -202      0       C  
ATOM    429  CG BMET A  53      10.173 -14.095  15.872  0.36 30.65           C  
ANISOU  429  CG BMET A  53     4343   3810   3493    -84   -301     59       C  
ATOM    430  SD AMET A  53      10.681 -11.950  17.458  0.64 42.46           S  
ANISOU  430  SD AMET A  53     5729   5488   4916   -163   -213     60       S  
ATOM    431  SD BMET A  53       9.775 -13.512  17.547  0.36 53.46           S  
ANISOU  431  SD BMET A  53     7257   6765   6292   -244   -251    100       S  
ATOM    432  CE AMET A  53       9.694 -13.392  17.849  0.64 53.64           C  
ANISOU  432  CE AMET A  53     7285   6800   6294   -274   -239    105       C  
ATOM    433  CE BMET A  53      10.496 -11.866  17.615  0.36 42.00           C  
ANISOU  433  CE BMET A  53     5674   5437   4849   -189   -198     58       C  
ATOM    434  N   LYS A  54      13.566 -15.175  14.161  1.00 28.38           N  
ANISOU  434  N   LYS A  54     4014   3426   3342    370   -439     33       N  
ATOM    435  CA  LYS A  54      14.128 -16.508  14.019  1.00 31.47           C  
ANISOU  435  CA  LYS A  54     4506   3673   3779    483   -516     47       C  
ATOM    436  C   LYS A  54      15.356 -16.674  14.917  1.00 34.25           C  
ANISOU  436  C   LYS A  54     4822   4025   4165    573   -613    124       C  
ATOM    437  O   LYS A  54      15.554 -17.717  15.540  1.00 33.83           O  
ANISOU  437  O   LYS A  54     4889   3840   4124    603   -721    194       O  
ATOM    438  CB  LYS A  54      14.498 -16.782  12.560  1.00 32.32           C  
ANISOU  438  CB  LYS A  54     4593   3753   3935    615   -460    -51       C  
ATOM    439  CG  LYS A  54      14.781 -18.248  12.277  1.00 44.31           C  
ANISOU  439  CG  LYS A  54     6252   5083   5500    724   -518    -66       C  
ATOM    440  CD  LYS A  54      13.521 -19.087  12.486  1.00 52.91           C  
ANISOU  440  CD  LYS A  54     7526   6039   6538    579   -559    -45       C  
ATOM    441  CE  LYS A  54      13.791 -20.573  12.276  1.00 58.88           C  
ANISOU  441  CE  LYS A  54     8460   6571   7339    677   -628    -56       C  
ATOM    442  NZ  LYS A  54      14.723 -21.115  13.298  1.00 64.93           N  
ANISOU  442  NZ  LYS A  54     9252   7254   8163    782   -739     42       N  
ATOM    443  N   GLU A  55      16.169 -15.628  15.006  1.00 32.10           N  
ANISOU  443  N   GLU A  55     4389   3899   3909    605   -589    120       N  
ATOM    444  CA  GLU A  55      17.415 -15.701  15.774  1.00 32.98           C  
ANISOU  444  CA  GLU A  55     4428   4038   4066    688   -697    193       C  
ATOM    445  C   GLU A  55      17.212 -15.439  17.272  1.00 32.76           C  
ANISOU  445  C   GLU A  55     4469   4036   3943    538   -787    294       C  
ATOM    446  O   GLU A  55      17.862 -16.061  18.115  1.00 35.55           O  
ANISOU  446  O   GLU A  55     4867   4334   4306    576   -933    390       O  
ATOM    447  CB  GLU A  55      18.435 -14.707  15.198  1.00 38.73           C  
ANISOU  447  CB  GLU A  55     4946   4920   4850    763   -635    144       C  
ATOM    448  CG  GLU A  55      19.751 -14.607  15.972  1.00 48.12           C  
ANISOU  448  CG  GLU A  55     6011   6175   6096    830   -754    218       C  
ATOM    449  CD  GLU A  55      20.746 -15.703  15.616  1.00 57.96           C  
ANISOU  449  CD  GLU A  55     7203   7338   7482   1052   -821    224       C  
ATOM    450  OE1 GLU A  55      20.429 -16.554  14.754  1.00 59.45           O  
ANISOU  450  OE1 GLU A  55     7474   7402   7710   1152   -762    157       O  
ATOM    451  OE2 GLU A  55      21.854 -15.707  16.200  1.00 61.60           O  
ANISOU  451  OE2 GLU A  55     7533   7853   8017   1128   -937    291       O  
ATOM    452  N   MET A  56      16.308 -14.522  17.603  1.00 35.13           N  
ANISOU  452  N   MET A  56     4784   4413   4149    370   -702    271       N  
ATOM    453  CA  MET A  56      16.251 -13.996  18.972  1.00 35.87           C  
ANISOU  453  CA  MET A  56     4928   4565   4136    220   -751    338       C  
ATOM    454  C   MET A  56      14.935 -14.239  19.700  1.00 38.83           C  
ANISOU  454  C   MET A  56     5464   4890   4398     43   -708    357       C  
ATOM    455  O   MET A  56      14.786 -13.827  20.851  1.00 40.34           O  
ANISOU  455  O   MET A  56     5723   5128   4475   -100   -724    399       O  
ATOM    456  CB  MET A  56      16.526 -12.486  18.973  1.00 32.64           C  
ANISOU  456  CB  MET A  56     4388   4308   3708    165   -675    286       C  
ATOM    457  CG  MET A  56      17.802 -12.067  18.279  1.00 34.54           C  
ANISOU  457  CG  MET A  56     4449   4627   4047    297   -693    264       C  
ATOM    458  SD  MET A  56      17.982 -10.281  18.260  1.00 33.35           S  
ANISOU  458  SD  MET A  56     4185   4625   3863    194   -599    207       S  
ATOM    459  CE  MET A  56      18.436  -9.990  19.970  1.00 38.79           C  
ANISOU  459  CE  MET A  56     4945   5358   4437     49   -731    289       C  
ATOM    460  N   GLY A  57      13.985 -14.890  19.039  1.00 37.47           N  
ANISOU  460  N   GLY A  57     5354   4633   4251     36   -649    322       N  
ATOM    461  CA  GLY A  57      12.645 -15.025  19.586  1.00 36.49           C  
ANISOU  461  CA  GLY A  57     5337   4489   4039   -145   -577    325       C  
ATOM    462  C   GLY A  57      12.447 -16.084  20.656  1.00 42.22           C  
ANISOU  462  C   GLY A  57     6259   5109   4672   -253   -671    433       C  
ATOM    463  O   GLY A  57      11.326 -16.308  21.107  1.00 47.31           O  
ANISOU  463  O   GLY A  57     6995   5739   5241   -421   -599    439       O  
ATOM    464  N   GLY A  58      13.525 -16.738  21.073  1.00 41.08           N  
ANISOU  464  N   GLY A  58     6177   4894   4538   -163   -833    526       N  
ATOM    465  CA  GLY A  58      13.425 -17.782  22.081  1.00 45.59           C  
ANISOU  465  CA  GLY A  58     6962   5343   5017   -260   -953    653       C  
ATOM    466  C   GLY A  58      13.445 -17.256  23.508  1.00 47.05           C  
ANISOU  466  C   GLY A  58     7233   5611   5032   -439   -979    723       C  
ATOM    467  O   GLY A  58      13.256 -18.006  24.467  1.00 45.66           O  
ANISOU  467  O   GLY A  58     7260   5351   4737   -567  -1067    837       O  
ATOM    468  N   HIS A  59      13.684 -15.960  23.660  1.00 44.90           N  
ANISOU  468  N   HIS A  59     6829   5498   4734   -461   -904    656       N  
ATOM    469  CA  HIS A  59      13.776 -15.372  24.989  1.00 44.18           C  
ANISOU  469  CA  HIS A  59     6830   5490   4467   -634   -923    701       C  
ATOM    470  C   HIS A  59      13.419 -13.892  24.923  1.00 42.30           C  
ANISOU  470  C   HIS A  59     6465   5400   4207   -693   -748    571       C  
ATOM    471  O   HIS A  59      13.522 -13.283  23.868  1.00 43.00           O  
ANISOU  471  O   HIS A  59     6376   5531   4431   -565   -674    479       O  
ATOM    472  CB  HIS A  59      15.188 -15.555  25.548  1.00 49.42           C  
ANISOU  472  CB  HIS A  59     7505   6149   5122   -557  -1154    814       C  
ATOM    473  CG  HIS A  59      15.350 -15.092  26.965  1.00 56.52           C  
ANISOU  473  CG  HIS A  59     8542   7121   5811   -755  -1216    878       C  
ATOM    474  ND1 HIS A  59      14.929 -15.838  28.046  1.00 60.12           N  
ANISOU  474  ND1 HIS A  59     9251   7506   6086   -933  -1284    993       N  
ATOM    475  CD2 HIS A  59      15.899 -13.964  27.480  1.00 58.33           C  
ANISOU  475  CD2 HIS A  59     8714   7484   5965   -821  -1223    842       C  
ATOM    476  CE1 HIS A  59      15.207 -15.189  29.164  1.00 61.88           C  
ANISOU  476  CE1 HIS A  59     9569   7822   6119  -1099  -1327   1022       C  
ATOM    477  NE2 HIS A  59      15.797 -14.050  28.849  1.00 59.83           N  
ANISOU  477  NE2 HIS A  59     9125   7685   5924  -1034  -1294    927       N  
ATOM    478  N   HIS A  60      12.989 -13.336  26.056  1.00 37.20           N  
ANISOU  478  N   HIS A  60     5930   4820   3384   -892   -679    563       N  
ATOM    479  CA  HIS A  60      12.658 -11.922  26.192  1.00 34.32           C  
ANISOU  479  CA  HIS A  60     5484   4571   2985   -958   -513    437       C  
ATOM    480  C   HIS A  60      13.660 -11.035  25.446  1.00 36.70           C  
ANISOU  480  C   HIS A  60     5602   4932   3410   -805   -558    388       C  
ATOM    481  O   HIS A  60      14.863 -11.095  25.703  1.00 36.61           O  
ANISOU  481  O   HIS A  60     5577   4937   3395   -759   -734    462       O  
ATOM    482  CB  HIS A  60      12.641 -11.577  27.683  1.00 38.63           C  
ANISOU  482  CB  HIS A  60     6214   5167   3296  -1174   -511    462       C  
ATOM    483  CG  HIS A  60      12.123 -10.209  28.002  1.00 47.66           C  
ANISOU  483  CG  HIS A  60     7327   6402   4380  -1267   -313    317       C  
ATOM    484  ND1 HIS A  60      11.320  -9.962  29.100  1.00 51.86           N  
ANISOU  484  ND1 HIS A  60     8017   6968   4718  -1478   -167    273       N  
ATOM    485  CD2 HIS A  60      12.323  -9.009  27.405  1.00 46.42           C  
ANISOU  485  CD2 HIS A  60     7016   6295   4325  -1180   -233    205       C  
ATOM    486  CE1 HIS A  60      11.032  -8.675  29.147  1.00 52.15           C  
ANISOU  486  CE1 HIS A  60     7992   7066   4756  -1497      0    127       C  
ATOM    487  NE2 HIS A  60      11.623  -8.073  28.133  1.00 48.85           N  
ANISOU  487  NE2 HIS A  60     7392   6650   4518  -1320    -47     91       N  
ATOM    488  N   ILE A  61      13.158 -10.234  24.511  1.00 32.61           N  
ANISOU  488  N   ILE A  61     4937   4445   3007   -734   -407    272       N  
ATOM    489  CA  ILE A  61      13.997  -9.311  23.742  1.00 32.47           C  
ANISOU  489  CA  ILE A  61     4758   4482   3097   -617   -421    223       C  
ATOM    490  C   ILE A  61      13.904  -7.899  24.330  1.00 37.20           C  
ANISOU  490  C   ILE A  61     5368   5151   3616   -728   -320    135       C  
ATOM    491  O   ILE A  61      12.806  -7.421  24.628  1.00 36.57           O  
ANISOU  491  O   ILE A  61     5331   5071   3492   -813   -152     53       O  
ATOM    492  CB  ILE A  61      13.563  -9.266  22.254  1.00 35.50           C  
ANISOU  492  CB  ILE A  61     4998   4844   3648   -471   -335    161       C  
ATOM    493  CG1 ILE A  61      13.805 -10.615  21.571  1.00 36.90           C  
ANISOU  493  CG1 ILE A  61     5173   4940   3906   -350   -435    227       C  
ATOM    494  CG2 ILE A  61      14.306  -8.171  21.486  1.00 28.30           C  
ANISOU  494  CG2 ILE A  61     3941   3991   2822   -388   -320    108       C  
ATOM    495  CD1 ILE A  61      13.306 -10.661  20.132  1.00 39.37           C  
ANISOU  495  CD1 ILE A  61     5382   5229   4347   -236   -356    163       C  
ATOM    496  N   VAL A  62      15.052  -7.250  24.524  1.00 34.71           N  
ANISOU  496  N   VAL A  62     5012   4889   3286   -732   -419    149       N  
ATOM    497  CA  VAL A  62      15.086  -5.817  24.812  1.00 37.92           C  
ANISOU  497  CA  VAL A  62     5420   5340   3647   -818   -328     52       C  
ATOM    498  C   VAL A  62      15.607  -5.120  23.572  1.00 34.07           C  
ANISOU  498  C   VAL A  62     4756   4869   3318   -690   -312     15       C  
ATOM    499  O   VAL A  62      16.746  -5.353  23.177  1.00 30.26           O  
ANISOU  499  O   VAL A  62     4173   4426   2899   -619   -444     78       O  
ATOM    500  CB  VAL A  62      16.041  -5.470  25.959  1.00 40.23           C  
ANISOU  500  CB  VAL A  62     5810   5686   3789   -959   -461     91       C  
ATOM    501  CG1 VAL A  62      16.106  -3.966  26.159  1.00 40.75           C  
ANISOU  501  CG1 VAL A  62     5891   5776   3817  -1050   -365    -22       C  
ATOM    502  CG2 VAL A  62      15.579  -6.113  27.227  1.00 44.62           C  
ANISOU  502  CG2 VAL A  62     6573   6228   4151  -1112   -483    137       C  
ATOM    503  N   ALA A  63      14.784  -4.271  22.962  1.00 28.57           N  
ANISOU  503  N   ALA A  63     4019   4146   2689   -661   -151    -82       N  
ATOM    504  CA  ALA A  63      15.208  -3.519  21.778  1.00 27.30           C  
ANISOU  504  CA  ALA A  63     3724   3992   2657   -564   -130   -109       C  
ATOM    505  C   ALA A  63      15.751  -2.162  22.221  1.00 29.13           C  
ANISOU  505  C   ALA A  63     3988   4243   2839   -669   -115   -164       C  
ATOM    506  O   ALA A  63      15.056  -1.382  22.877  1.00 29.59           O  
ANISOU  506  O   ALA A  63     4150   4262   2830   -758     -5   -249       O  
ATOM    507  CB  ALA A  63      14.055  -3.350  20.800  1.00 27.80           C  
ANISOU  507  CB  ALA A  63     3734   4003   2825   -473      0   -164       C  
ATOM    508  N   LEU A  64      17.008  -1.892  21.879  1.00 24.60           N  
ANISOU  508  N   LEU A  64     3324   3726   2298   -666   -220   -121       N  
ATOM    509  CA  LEU A  64      17.661  -0.653  22.278  1.00 27.28           C  
ANISOU  509  CA  LEU A  64     3694   4084   2588   -791   -230   -163       C  
ATOM    510  C   LEU A  64      17.797   0.285  21.065  1.00 27.80           C  
ANISOU  510  C   LEU A  64     3667   4126   2770   -734   -158   -194       C  
ATOM    511  O   LEU A  64      18.538  -0.004  20.126  1.00 26.63           O  
ANISOU  511  O   LEU A  64     3379   4032   2709   -655   -206   -140       O  
ATOM    512  CB  LEU A  64      19.026  -0.979  22.875  1.00 31.36           C  
ANISOU  512  CB  LEU A  64     4168   4695   3051   -865   -417    -81       C  
ATOM    513  CG  LEU A  64      19.883   0.141  23.457  1.00 36.03           C  
ANISOU  513  CG  LEU A  64     4794   5326   3571  -1036   -476   -108       C  
ATOM    514  CD1 LEU A  64      19.158   0.868  24.593  1.00 38.00           C  
ANISOU  514  CD1 LEU A  64     5266   5510   3662  -1192   -397   -203       C  
ATOM    515  CD2 LEU A  64      21.202  -0.430  23.962  1.00 39.19           C  
ANISOU  515  CD2 LEU A  64     5105   5839   3946  -1084   -693     -4       C  
ATOM    516  N   CYS A  65      17.076   1.405  21.084  1.00 27.57           N  
ANISOU  516  N   CYS A  65     3726   4009   2739   -774    -37   -283       N  
ATOM    517  CA  CYS A  65      17.091   2.352  19.975  1.00 25.75           C  
ANISOU  517  CA  CYS A  65     3447   3730   2608   -731     23   -301       C  
ATOM    518  C   CYS A  65      18.256   3.333  20.102  1.00 23.97           C  
ANISOU  518  C   CYS A  65     3225   3531   2352   -869    -34   -298       C  
ATOM    519  O   CYS A  65      18.387   4.000  21.123  1.00 25.94           O  
ANISOU  519  O   CYS A  65     3599   3753   2505  -1011    -41   -354       O  
ATOM    520  CB  CYS A  65      15.786   3.148  19.963  1.00 29.40           C  
ANISOU  520  CB  CYS A  65     4003   4063   3104   -698    164   -390       C  
ATOM    521  SG  CYS A  65      15.756   4.446  18.689  1.00 28.02           S  
ANISOU  521  SG  CYS A  65     3814   3791   3041   -655    214   -397       S  
ATOM    522  N   VAL A  66      19.101   3.436  19.076  1.00 25.02           N  
ANISOU  522  N   VAL A  66     3229   3720   2556   -845    -69   -241       N  
ATOM    523  CA  VAL A  66      20.176   4.433  19.121  1.00 25.41           C  
ANISOU  523  CA  VAL A  66     3270   3798   2585  -1000   -113   -236       C  
ATOM    524  C   VAL A  66      19.708   5.753  18.494  1.00 30.51           C  
ANISOU  524  C   VAL A  66     4014   4308   3270  -1027    -14   -282       C  
ATOM    525  O   VAL A  66      19.659   5.884  17.270  1.00 25.00           O  
ANISOU  525  O   VAL A  66     3253   3596   2648   -951     28   -243       O  
ATOM    526  CB  VAL A  66      21.469   3.953  18.416  1.00 30.32           C  
ANISOU  526  CB  VAL A  66     3688   4568   3263   -992   -191   -152       C  
ATOM    527  CG1 VAL A  66      22.588   4.943  18.667  1.00 32.08           C  
ANISOU  527  CG1 VAL A  66     3892   4840   3457  -1190   -247   -146       C  
ATOM    528  CG2 VAL A  66      21.884   2.565  18.920  1.00 30.64           C  
ANISOU  528  CG2 VAL A  66     3625   4717   3299   -918   -299    -98       C  
ATOM    529  N   LEU A  67      19.362   6.710  19.356  1.00 28.98           N  
ANISOU  529  N   LEU A  67     3992   4003   3015  -1137     21   -365       N  
ATOM    530  CA  LEU A  67      18.895   8.040  18.959  1.00 27.02           C  
ANISOU  530  CA  LEU A  67     3873   3586   2808  -1163    105   -417       C  
ATOM    531  C   LEU A  67      20.050   8.855  18.393  1.00 29.89           C  
ANISOU  531  C   LEU A  67     4208   3971   3177  -1309     58   -368       C  
ATOM    532  O   LEU A  67      21.204   8.576  18.732  1.00 31.73           O  
ANISOU  532  O   LEU A  67     4345   4350   3363  -1433    -40   -327       O  
ATOM    533  CB  LEU A  67      18.325   8.749  20.193  1.00 26.02           C  
ANISOU  533  CB  LEU A  67     3947   3337   2605  -1247    160   -539       C  
ATOM    534  CG  LEU A  67      17.074   8.087  20.745  1.00 28.51           C  
ANISOU  534  CG  LEU A  67     4294   3624   2915  -1120    246   -600       C  
ATOM    535  CD1 LEU A  67      16.631   8.724  22.060  1.00 28.89           C  
ANISOU  535  CD1 LEU A  67     4543   3576   2860  -1224    321   -736       C  
ATOM    536  CD2 LEU A  67      15.961   8.120  19.709  1.00 26.56           C  
ANISOU  536  CD2 LEU A  67     3996   3284   2810   -923    332   -592       C  
ATOM    537  N   LYS A  68      19.767   9.854  17.546  1.00 28.86           N  
ANISOU  537  N   LYS A  68     4157   3701   3107  -1305    116   -363       N  
ATOM    538  CA  LYS A  68      18.409  10.183  17.095  1.00 26.76           C  
ANISOU  538  CA  LYS A  68     3982   3266   2921  -1141    206   -397       C  
ATOM    539  C   LYS A  68      18.056   9.431  15.831  1.00 28.61           C  
ANISOU  539  C   LYS A  68     4083   3559   3227   -977    211   -311       C  
ATOM    540  O   LYS A  68      16.889   9.085  15.602  1.00 25.96           O  
ANISOU  540  O   LYS A  68     3748   3163   2954   -812    253   -328       O  
ATOM    541  CB  LYS A  68      18.296  11.679  16.800  1.00 27.05           C  
ANISOU  541  CB  LYS A  68     4192   3094   2990  -1215    240   -420       C  
ATOM    542  CG  LYS A  68      18.362  12.618  18.000  1.00 28.68           C  
ANISOU  542  CG  LYS A  68     4592   3173   3133  -1361    259   -537       C  
ATOM    543  CD  LYS A  68      18.368  14.049  17.463  1.00 31.53           C  
ANISOU  543  CD  LYS A  68     5123   3313   3542  -1429    280   -536       C  
ATOM    544  CE  LYS A  68      18.528  15.095  18.519  1.00 40.91           C  
ANISOU  544  CE  LYS A  68     6533   4345   4667  -1593    300   -657       C  
ATOM    545  NZ  LYS A  68      18.287  16.416  17.870  1.00 42.88           N  
ANISOU  545  NZ  LYS A  68     6963   4335   4996  -1605    325   -650       N  
ATOM    546  N   GLY A  69      19.074   9.181  15.008  1.00 26.17           N  
ANISOU  546  N   GLY A  69     3659   3377   2908  -1034    172   -225       N  
ATOM    547  CA  GLY A  69      18.892   8.680  13.654  1.00 23.46           C  
ANISOU  547  CA  GLY A  69     3229   3077   2607   -919    186   -148       C  
ATOM    548  C   GLY A  69      18.256   7.304  13.577  1.00 24.57           C  
ANISOU  548  C   GLY A  69     3266   3300   2769   -748    184   -149       C  
ATOM    549  O   GLY A  69      17.649   6.935  12.567  1.00 25.17           O  
ANISOU  549  O   GLY A  69     3320   3363   2880   -631    199   -110       O  
ATOM    550  N   GLY A  70      18.385   6.527  14.641  1.00 21.95           N  
ANISOU  550  N   GLY A  70     2887   3048   2404   -748    156   -187       N  
ATOM    551  CA  GLY A  70      17.788   5.200  14.625  1.00 22.42           C  
ANISOU  551  CA  GLY A  70     2870   3169   2480   -605    149   -184       C  
ATOM    552  C   GLY A  70      16.280   5.147  14.854  1.00 23.64           C  
ANISOU  552  C   GLY A  70     3095   3211   2676   -496    197   -233       C  
ATOM    553  O   GLY A  70      15.682   4.071  14.731  1.00 22.33           O  
ANISOU  553  O   GLY A  70     2871   3085   2527   -392    193   -225       O  
ATOM    554  N   TYR A  71      15.651   6.273  15.188  1.00 23.52           N  
ANISOU  554  N   TYR A  71     3196   3052   2687   -518    245   -286       N  
ATOM    555  CA  TYR A  71      14.288   6.210  15.738  1.00 25.86           C  
ANISOU  555  CA  TYR A  71     3532   3263   3029   -426    307   -355       C  
ATOM    556  C   TYR A  71      13.235   5.666  14.760  1.00 21.87           C  
ANISOU  556  C   TYR A  71     2954   2743   2613   -272    309   -318       C  
ATOM    557  O   TYR A  71      12.316   4.948  15.167  1.00 23.98           O  
ANISOU  557  O   TYR A  71     3180   3027   2905   -203    340   -352       O  
ATOM    558  CB  TYR A  71      13.854   7.556  16.350  1.00 26.17           C  
ANISOU  558  CB  TYR A  71     3710   3139   3094   -465    374   -440       C  
ATOM    559  CG  TYR A  71      12.933   8.398  15.486  1.00 27.52           C  
ANISOU  559  CG  TYR A  71     3914   3154   3390   -349    399   -430       C  
ATOM    560  CD1 TYR A  71      11.559   8.173  15.466  1.00 26.33           C  
ANISOU  560  CD1 TYR A  71     3714   2951   3340   -201    449   -466       C  
ATOM    561  CD2 TYR A  71      13.436   9.440  14.717  1.00 25.96           C  
ANISOU  561  CD2 TYR A  71     3794   2857   3211   -397    365   -378       C  
ATOM    562  CE1 TYR A  71      10.722   8.937  14.682  1.00 27.90           C  
ANISOU  562  CE1 TYR A  71     3924   3007   3670    -82    445   -445       C  
ATOM    563  CE2 TYR A  71      12.611  10.209  13.923  1.00 29.00           C  
ANISOU  563  CE2 TYR A  71     4225   3084   3710   -287    360   -350       C  
ATOM    564  CZ  TYR A  71      11.255   9.953  13.908  1.00 31.91           C  
ANISOU  564  CZ  TYR A  71     4528   3405   4191   -119    391   -382       C  
ATOM    565  OH  TYR A  71      10.428  10.722  13.119  1.00 32.79           O  
ANISOU  565  OH  TYR A  71     4669   3358   4433      3    361   -341       O  
ATOM    566  N   LYS A  72      13.352   6.013  13.481  1.00 22.38           N  
ANISOU  566  N   LYS A  72     3011   2780   2714   -237    271   -246       N  
ATOM    567  CA  LYS A  72      12.397   5.532  12.474  1.00 23.03           C  
ANISOU  567  CA  LYS A  72     3037   2852   2863   -112    245   -202       C  
ATOM    568  C   LYS A  72      12.523   4.034  12.210  1.00 25.35           C  
ANISOU  568  C   LYS A  72     3236   3280   3115    -79    214   -177       C  
ATOM    569  O   LYS A  72      11.534   3.302  12.258  1.00 25.33           O  
ANISOU  569  O   LYS A  72     3184   3284   3154     -3    214   -192       O  
ATOM    570  CB  LYS A  72      12.552   6.304  11.154  1.00 26.87           C  
ANISOU  570  CB  LYS A  72     3572   3273   3366   -107    199   -120       C  
ATOM    571  CG  LYS A  72      11.754   7.594  11.105  1.00 36.92           C  
ANISOU  571  CG  LYS A  72     4931   4361   4736    -59    204   -128       C  
ATOM    572  CD  LYS A  72      10.260   7.310  11.152  1.00 44.86           C  
ANISOU  572  CD  LYS A  72     5866   5319   5859     88    204   -156       C  
ATOM    573  CE  LYS A  72       9.778   6.692   9.852  1.00 49.93           C  
ANISOU  573  CE  LYS A  72     6452   6006   6513    157    112    -66       C  
ATOM    574  NZ  LYS A  72       8.423   6.081   9.989  1.00 51.61           N  
ANISOU  574  NZ  LYS A  72     6552   6229   6829    271    103    -94       N  
ATOM    575  N   PHE A  73      13.738   3.588  11.905  1.00 20.75           N  
ANISOU  575  N   PHE A  73     2625   2800   2460   -136    190   -141       N  
ATOM    576  CA  PHE A  73      14.013   2.174  11.703  1.00 19.77           C  
ANISOU  576  CA  PHE A  73     2426   2783   2303    -96    164   -127       C  
ATOM    577  C   PHE A  73      13.567   1.365  12.916  1.00 21.76           C  
ANISOU  577  C   PHE A  73     2664   3053   2550    -87    171   -172       C  
ATOM    578  O   PHE A  73      12.945   0.305  12.784  1.00 22.96           O  
ANISOU  578  O   PHE A  73     2786   3223   2713    -27    155   -169       O  
ATOM    579  CB  PHE A  73      15.511   1.977  11.408  1.00 22.76           C  
ANISOU  579  CB  PHE A  73     2756   3264   2626   -153    155    -98       C  
ATOM    580  CG  PHE A  73      15.899   0.556  11.085  1.00 22.83           C  
ANISOU  580  CG  PHE A  73     2692   3364   2618    -88    136    -90       C  
ATOM    581  CD1 PHE A  73      15.189  -0.192  10.152  1.00 22.30           C  
ANISOU  581  CD1 PHE A  73     2634   3284   2557     -4    128    -83       C  
ATOM    582  CD2 PHE A  73      17.006  -0.018  11.684  1.00 21.49           C  
ANISOU  582  CD2 PHE A  73     2450   3284   2430   -109    114    -89       C  
ATOM    583  CE1 PHE A  73      15.579  -1.510   9.848  1.00 22.68           C  
ANISOU  583  CE1 PHE A  73     2638   3390   2589     59    117    -89       C  
ATOM    584  CE2 PHE A  73      17.395  -1.334  11.389  1.00 22.21           C  
ANISOU  584  CE2 PHE A  73     2479   3435   2526    -25     96    -85       C  
ATOM    585  CZ  PHE A  73      16.687  -2.069  10.470  1.00 23.71           C  
ANISOU  585  CZ  PHE A  73     2697   3593   2717     59    106    -92       C  
ATOM    586  N   PHE A  74      13.860   1.887  14.098  1.00 19.78           N  
ANISOU  586  N   PHE A  74     2456   2791   2270   -167    192   -211       N  
ATOM    587  CA  PHE A  74      13.454   1.255  15.351  1.00 21.07           C  
ANISOU  587  CA  PHE A  74     2639   2968   2397   -191    206   -251       C  
ATOM    588  C   PHE A  74      11.931   1.110  15.443  1.00 23.55           C  
ANISOU  588  C   PHE A  74     2952   3224   2773   -129    264   -289       C  
ATOM    589  O   PHE A  74      11.441   0.019  15.694  1.00 21.64           O  
ANISOU  589  O   PHE A  74     2686   3016   2520   -111    257   -284       O  
ATOM    590  CB  PHE A  74      14.008   2.066  16.518  1.00 20.56           C  
ANISOU  590  CB  PHE A  74     2649   2892   2269   -309    222   -295       C  
ATOM    591  CG  PHE A  74      13.627   1.548  17.885  1.00 23.16           C  
ANISOU  591  CG  PHE A  74     3036   3237   2526   -365    244   -337       C  
ATOM    592  CD1 PHE A  74      14.287   0.459  18.449  1.00 28.82           C  
ANISOU  592  CD1 PHE A  74     3741   4040   3170   -399    164   -291       C  
ATOM    593  CD2 PHE A  74      12.662   2.201  18.632  1.00 26.05           C  
ANISOU  593  CD2 PHE A  74     3478   3528   2892   -389    347   -423       C  
ATOM    594  CE1 PHE A  74      13.959   0.011  19.728  1.00 27.60           C  
ANISOU  594  CE1 PHE A  74     3670   3895   2922   -476    176   -315       C  
ATOM    595  CE2 PHE A  74      12.324   1.756  19.921  1.00 31.66           C  
ANISOU  595  CE2 PHE A  74     4261   4262   3507   -467    389   -467       C  
ATOM    596  CZ  PHE A  74      12.979   0.659  20.461  1.00 28.03           C  
ANISOU  596  CZ  PHE A  74     3809   3889   2952   -522    296   -405       C  
ATOM    597  N   ALA A  75      11.185   2.196  15.221  1.00 22.14           N  
ANISOU  597  N   ALA A  75     2792   2952   2668    -96    316   -324       N  
ATOM    598  CA  ALA A  75       9.731   2.144  15.371  1.00 23.94           C  
ANISOU  598  CA  ALA A  75     2981   3134   2980    -30    377   -367       C  
ATOM    599  C   ALA A  75       9.153   1.134  14.384  1.00 25.15           C  
ANISOU  599  C   ALA A  75     3050   3327   3177     41    316   -311       C  
ATOM    600  O   ALA A  75       8.282   0.309  14.726  1.00 24.30           O  
ANISOU  600  O   ALA A  75     2895   3248   3089     47    341   -328       O  
ATOM    601  CB  ALA A  75       9.105   3.538  15.164  1.00 24.67           C  
ANISOU  601  CB  ALA A  75     3094   3103   3176     25    425   -405       C  
ATOM    602  N   ASP A  76       9.656   1.179  13.161  1.00 22.09           N  
ANISOU  602  N   ASP A  76     2658   2945   2790     73    241   -247       N  
ATOM    603  CA  ASP A  76       9.147   0.321  12.092  1.00 21.86           C  
ANISOU  603  CA  ASP A  76     2579   2943   2783    128    175   -201       C  
ATOM    604  C   ASP A  76       9.529  -1.143  12.256  1.00 25.29           C  
ANISOU  604  C   ASP A  76     3009   3451   3148    105    148   -191       C  
ATOM    605  O   ASP A  76       8.683  -2.041  12.113  1.00 22.70           O  
ANISOU  605  O   ASP A  76     2647   3133   2844    119    128   -191       O  
ATOM    606  CB  ASP A  76       9.613   0.851  10.732  1.00 24.06           C  
ANISOU  606  CB  ASP A  76     2885   3204   3051    151    113   -140       C  
ATOM    607  CG  ASP A  76       8.891   2.119  10.322  1.00 27.14           C  
ANISOU  607  CG  ASP A  76     3286   3494   3534    198    102   -125       C  
ATOM    608  OD1 ASP A  76       7.837   2.415  10.915  1.00 29.23           O  
ANISOU  608  OD1 ASP A  76     3501   3709   3897    243    139   -167       O  
ATOM    609  OD2 ASP A  76       9.369   2.807   9.395  1.00 28.30           O  
ANISOU  609  OD2 ASP A  76     3490   3606   3656    191     59    -68       O  
ATOM    610  N   LEU A  77      10.801  -1.392  12.556  1.00 20.51           N  
ANISOU  610  N   LEU A  77     2434   2891   2468     68    140   -181       N  
ATOM    611  CA  LEU A  77      11.246  -2.763  12.805  1.00 20.00           C  
ANISOU  611  CA  LEU A  77     2373   2873   2353     66    106   -169       C  
ATOM    612  C   LEU A  77      10.453  -3.364  13.976  1.00 19.10           C  
ANISOU  612  C   LEU A  77     2274   2751   2233     22    133   -193       C  
ATOM    613  O   LEU A  77       9.997  -4.513  13.904  1.00 19.88           O  
ANISOU  613  O   LEU A  77     2378   2848   2328     26    105   -181       O  
ATOM    614  CB  LEU A  77      12.757  -2.803  13.096  1.00 21.22           C  
ANISOU  614  CB  LEU A  77     2528   3080   2453     43     85   -152       C  
ATOM    615  CG  LEU A  77      13.390  -4.153  13.456  1.00 24.74           C  
ANISOU  615  CG  LEU A  77     2976   3559   2867     63     34   -131       C  
ATOM    616  CD1 LEU A  77      13.288  -5.128  12.306  1.00 24.18           C  
ANISOU  616  CD1 LEU A  77     2901   3477   2810    140     10   -125       C  
ATOM    617  CD2 LEU A  77      14.858  -3.978  13.859  1.00 26.66           C  
ANISOU  617  CD2 LEU A  77     3182   3864   3084     44      2   -111       C  
ATOM    618  N   LEU A  78      10.257  -2.597  15.041  1.00 18.84           N  
ANISOU  618  N   LEU A  78     2264   2706   2189    -34    197   -232       N  
ATOM    619  CA ALEU A  78       9.499  -3.128  16.175  0.72 22.44           C  
ANISOU  619  CA ALEU A  78     2745   3164   2615    -97    248   -259       C  
ATOM    620  CA BLEU A  78       9.487  -3.085  16.187  0.28 22.37           C  
ANISOU  620  CA BLEU A  78     2737   3155   2608    -97    251   -261       C  
ATOM    621  C   LEU A  78       8.045  -3.371  15.795  1.00 23.63           C  
ANISOU  621  C   LEU A  78     2828   3298   2851    -72    287   -278       C  
ATOM    622  O   LEU A  78       7.432  -4.332  16.264  1.00 22.55           O  
ANISOU  622  O   LEU A  78     2698   3176   2694   -123    301   -274       O  
ATOM    623  CB ALEU A  78       9.590  -2.223  17.407  0.72 23.19           C  
ANISOU  623  CB ALEU A  78     2899   3254   2660   -174    327   -315       C  
ATOM    624  CB BLEU A  78       9.509  -2.083  17.342  0.28 23.73           C  
ANISOU  624  CB BLEU A  78     2961   3316   2740   -167    335   -321       C  
ATOM    625  CG ALEU A  78      10.559  -2.727  18.466  0.72 27.52           C  
ANISOU  625  CG ALEU A  78     3533   3841   3081   -264    281   -290       C  
ATOM    626  CG BLEU A  78      10.676  -2.162  18.315  0.28 27.68           C  
ANISOU  626  CG BLEU A  78     3546   3850   3120   -254    294   -306       C  
ATOM    627  CD1ALEU A  78      11.963  -2.773  17.875  0.72 27.08           C  
ANISOU  627  CD1ALEU A  78     3456   3816   3018   -229    174   -234       C  
ATOM    628  CD1BLEU A  78      10.323  -1.456  19.604  0.28 31.52           C  
ANISOU  628  CD1BLEU A  78     4116   4323   3538   -352    394   -381       C  
ATOM    629  CD2ALEU A  78      10.528  -1.834  19.691  0.72 32.44           C  
ANISOU  629  CD2ALEU A  78     4241   4455   3629   -364    362   -358       C  
ATOM    630  CD2BLEU A  78      11.032  -3.593  18.598  0.28 26.45           C  
ANISOU  630  CD2BLEU A  78     3419   3729   2904   -273    211   -241       C  
ATOM    631  N   ASP A  79       7.491  -2.517  14.944  1.00 20.71           N  
ANISOU  631  N   ASP A  79     2393   2897   2579     -2    292   -288       N  
ATOM    632  CA  ASP A  79       6.105  -2.729  14.523  1.00 22.41           C  
ANISOU  632  CA  ASP A  79     2511   3108   2894     26    304   -297       C  
ATOM    633  C   ASP A  79       5.961  -4.042  13.759  1.00 20.98           C  
ANISOU  633  C   ASP A  79     2327   2949   2696     18    212   -248       C  
ATOM    634  O   ASP A  79       4.965  -4.760  13.911  1.00 21.90           O  
ANISOU  634  O   ASP A  79     2392   3082   2846    -24    223   -254       O  
ATOM    635  CB  ASP A  79       5.595  -1.557  13.680  1.00 27.90           C  
ANISOU  635  CB  ASP A  79     3141   3755   3706    117    290   -298       C  
ATOM    636  CG  ASP A  79       5.073  -0.420  14.526  1.00 32.20           C  
ANISOU  636  CG  ASP A  79     3660   4255   4321    136    407   -371       C  
ATOM    637  OD1 ASP A  79       4.966  -0.592  15.757  1.00 32.13           O  
ANISOU  637  OD1 ASP A  79     3679   4269   4260     65    515   -430       O  
ATOM    638  OD2 ASP A  79       4.748   0.638  13.956  1.00 32.29           O  
ANISOU  638  OD2 ASP A  79     3636   4198   4434    221    393   -370       O  
ATOM    639  N   TYR A  80       6.943  -4.355  12.925  1.00 19.31           N  
ANISOU  639  N   TYR A  80     2172   2736   2431     51    131   -209       N  
ATOM    640  CA  TYR A  80       6.911  -5.628  12.193  1.00 19.11           C  
ANISOU  640  CA  TYR A  80     2174   2711   2376     47     52   -181       C  
ATOM    641  C   TYR A  80       7.100  -6.820  13.121  1.00 23.96           C  
ANISOU  641  C   TYR A  80     2853   3324   2928    -18     59   -177       C  
ATOM    642  O   TYR A  80       6.465  -7.863  12.948  1.00 21.45           O  
ANISOU  642  O   TYR A  80     2550   2988   2611    -60     24   -167       O  
ATOM    643  CB  TYR A  80       7.967  -5.668  11.069  1.00 18.82           C  
ANISOU  643  CB  TYR A  80     2186   2673   2290    104     -7   -158       C  
ATOM    644  CG  TYR A  80       7.540  -4.928   9.812  1.00 21.36           C  
ANISOU  644  CG  TYR A  80     2480   2987   2648    144    -52   -140       C  
ATOM    645  CD1 TYR A  80       6.532  -5.437   9.001  1.00 24.65           C  
ANISOU  645  CD1 TYR A  80     2876   3397   3093    134   -124   -129       C  
ATOM    646  CD2 TYR A  80       8.156  -3.738   9.429  1.00 20.33           C  
ANISOU  646  CD2 TYR A  80     2357   2853   2515    174    -39   -125       C  
ATOM    647  CE1 TYR A  80       6.132  -4.781   7.836  1.00 26.18           C  
ANISOU  647  CE1 TYR A  80     3058   3584   3306    162   -195    -96       C  
ATOM    648  CE2 TYR A  80       7.765  -3.070   8.266  1.00 24.00           C  
ANISOU  648  CE2 TYR A  80     2823   3299   2999    201    -98    -89       C  
ATOM    649  CZ  TYR A  80       6.746  -3.599   7.487  1.00 24.30           C  
ANISOU  649  CZ  TYR A  80     2840   3332   3059    199   -181    -72       C  
ATOM    650  OH  TYR A  80       6.340  -2.963   6.338  1.00 23.37           O  
ANISOU  650  OH  TYR A  80     2735   3196   2947    218   -267    -22       O  
ATOM    651  N   ILE A  81       8.002  -6.687  14.083  1.00 21.07           N  
ANISOU  651  N   ILE A  81     2539   2967   2501    -37     86   -174       N  
ATOM    652  CA  ILE A  81       8.198  -7.744  15.079  1.00 20.77           C  
ANISOU  652  CA  ILE A  81     2581   2917   2394   -105     75   -151       C  
ATOM    653  C   ILE A  81       6.920  -7.999  15.866  1.00 24.27           C  
ANISOU  653  C   ILE A  81     3011   3365   2844   -207    146   -168       C  
ATOM    654  O   ILE A  81       6.542  -9.148  16.087  1.00 24.40           O  
ANISOU  654  O   ILE A  81     3083   3355   2832   -273    119   -141       O  
ATOM    655  CB  ILE A  81       9.360  -7.407  16.040  1.00 25.31           C  
ANISOU  655  CB  ILE A  81     3209   3512   2897   -120     71   -137       C  
ATOM    656  CG1 ILE A  81      10.691  -7.494  15.291  1.00 26.29           C  
ANISOU  656  CG1 ILE A  81     3325   3641   3021    -29     -2   -113       C  
ATOM    657  CG2 ILE A  81       9.374  -8.382  17.220  1.00 24.76           C  
ANISOU  657  CG2 ILE A  81     3239   3425   2745   -210     51   -100       C  
ATOM    658  CD1 ILE A  81      11.890  -6.995  16.109  1.00 27.49           C  
ANISOU  658  CD1 ILE A  81     3488   3832   3124    -47    -24    -96       C  
ATOM    659  N   LYS A  82       6.246  -6.923  16.274  1.00 21.37           N  
ANISOU  659  N   LYS A  82     2570   3028   2521   -222    246   -218       N  
ATOM    660  CA  LYS A  82       4.989  -7.031  17.006  1.00 19.32           C  
ANISOU  660  CA  LYS A  82     2263   2794   2285   -314    349   -252       C  
ATOM    661  C   LYS A  82       3.912  -7.753  16.199  1.00 23.63           C  
ANISOU  661  C   LYS A  82     2724   3341   2913   -330    312   -238       C  
ATOM    662  O   LYS A  82       3.143  -8.541  16.738  1.00 25.65           O  
ANISOU  662  O   LYS A  82     2981   3612   3153   -444    354   -234       O  
ATOM    663  CB  LYS A  82       4.504  -5.643  17.412  1.00 22.82           C  
ANISOU  663  CB  LYS A  82     2626   3256   2790   -287    472   -325       C  
ATOM    664  CG  LYS A  82       5.241  -5.097  18.635  1.00 28.24           C  
ANISOU  664  CG  LYS A  82     3421   3946   3364   -343    541   -357       C  
ATOM    665  CD  LYS A  82       5.355  -3.588  18.608  1.00 33.21           C  
ANISOU  665  CD  LYS A  82     4017   4552   4051   -272    605   -422       C  
ATOM    666  CE  LYS A  82       3.999  -2.922  18.620  1.00 39.23           C  
ANISOU  666  CE  LYS A  82     4647   5314   4947   -235    732   -497       C  
ATOM    667  NZ  LYS A  82       4.140  -1.425  18.588  1.00 40.92           N  
ANISOU  667  NZ  LYS A  82     4854   5468   5226   -150    787   -561       N  
ATOM    668  N   ALA A  83       3.854  -7.469  14.903  1.00 19.60           N  
ANISOU  668  N   ALA A  83     2149   2818   2479   -236    229   -229       N  
ATOM    669  CA  ALA A  83       2.902  -8.144  14.020  1.00 21.94           C  
ANISOU  669  CA  ALA A  83     2376   3118   2842   -262    160   -213       C  
ATOM    670  C   ALA A  83       3.159  -9.649  14.036  1.00 24.23           C  
ANISOU  670  C   ALA A  83     2793   3365   3047   -343     93   -176       C  
ATOM    671  O   ALA A  83       2.222 -10.457  14.086  1.00 27.44           O  
ANISOU  671  O   ALA A  83     3176   3776   3475   -451     87   -169       O  
ATOM    672  CB  ALA A  83       3.014  -7.601  12.610  1.00 21.61           C  
ANISOU  672  CB  ALA A  83     2294   3065   2853   -157     60   -199       C  
ATOM    673  N   LEU A  84       4.433 -10.032  13.987  1.00 20.28           N  
ANISOU  673  N   LEU A  84     2426   2816   2462   -292     41   -153       N  
ATOM    674  CA  LEU A  84       4.779 -11.449  14.045  1.00 22.74           C  
ANISOU  674  CA  LEU A  84     2877   3057   2707   -341    -27   -119       C  
ATOM    675  C   LEU A  84       4.365 -12.039  15.387  1.00 29.51           C  
ANISOU  675  C   LEU A  84     3792   3909   3510   -480     33    -96       C  
ATOM    676  O   LEU A  84       3.902 -13.177  15.470  1.00 27.67           O  
ANISOU  676  O   LEU A  84     3637   3622   3253   -582     -2    -67       O  
ATOM    677  CB  LEU A  84       6.281 -11.652  13.842  1.00 24.18           C  
ANISOU  677  CB  LEU A  84     3159   3195   2835   -234    -83   -103       C  
ATOM    678  CG  LEU A  84       6.857 -11.314  12.473  1.00 25.58           C  
ANISOU  678  CG  LEU A  84     3315   3372   3033   -116   -131   -125       C  
ATOM    679  CD1 LEU A  84       8.360 -11.413  12.521  1.00 24.30           C  
ANISOU  679  CD1 LEU A  84     3209   3192   2832    -19   -150   -115       C  
ATOM    680  CD2 LEU A  84       6.303 -12.265  11.423  1.00 27.59           C  
ANISOU  680  CD2 LEU A  84     3622   3571   3291   -140   -202   -137       C  
ATOM    681  N   ASN A  85       4.530 -11.261  16.447  1.00 25.75           N  
ANISOU  681  N   ASN A  85     3300   3484   3001   -501    126   -107       N  
ATOM    682  CA  ASN A  85       4.204 -11.758  17.775  1.00 25.30           C  
ANISOU  682  CA  ASN A  85     3325   3430   2857   -650    194    -84       C  
ATOM    683  C   ASN A  85       2.714 -11.939  18.040  1.00 33.11           C  
ANISOU  683  C   ASN A  85     4219   4469   3891   -789    294   -108       C  
ATOM    684  O   ASN A  85       2.336 -12.722  18.908  1.00 37.97           O  
ANISOU  684  O   ASN A  85     4926   5073   4426   -946    335    -74       O  
ATOM    685  CB  ASN A  85       4.844 -10.867  18.852  1.00 34.19           C  
ANISOU  685  CB  ASN A  85     4486   4599   3907   -650    266    -99       C  
ATOM    686  CG  ASN A  85       6.240 -11.332  19.235  1.00 45.52           C  
ANISOU  686  CG  ASN A  85     6068   5979   5247   -613    154    -35       C  
ATOM    687  OD1 ASN A  85       6.400 -12.287  20.004  1.00 50.99           O  
ANISOU  687  OD1 ASN A  85     6904   6625   5845   -708    110     31       O  
ATOM    688  ND2 ASN A  85       7.254 -10.665  18.704  1.00 53.52           N  
ANISOU  688  ND2 ASN A  85     7043   7002   6291   -479    100    -46       N  
ATOM    689  N   ARG A  86       1.851 -11.241  17.306  1.00 31.15           N  
ANISOU  689  N   ARG A  86     3784   4278   3772   -742    329   -158       N  
ATOM    690  CA  ARG A  86       0.416 -11.372  17.597  1.00 36.61           C  
ANISOU  690  CA  ARG A  86     4340   5040   4532   -871    431   -185       C  
ATOM    691  C   ARG A  86      -0.354 -12.236  16.590  1.00 39.78           C  
ANISOU  691  C   ARG A  86     4684   5425   5007   -928    327   -160       C  
ATOM    692  O   ARG A  86      -1.552 -12.501  16.758  1.00 43.62           O  
ANISOU  692  O   ARG A  86     5042   5975   5557  -1058    391   -172       O  
ATOM    693  CB  ARG A  86      -0.252 -10.001  17.766  1.00 35.67           C  
ANISOU  693  CB  ARG A  86     4022   5006   4526   -802    565   -263       C  
ATOM    694  CG  ARG A  86      -0.257  -9.171  16.501  1.00 31.24           C  
ANISOU  694  CG  ARG A  86     3335   4439   4095   -632    472   -277       C  
ATOM    695  CD  ARG A  86      -0.969  -7.834  16.646  1.00 31.78           C  
ANISOU  695  CD  ARG A  86     3211   4562   4301   -545    590   -348       C  
ATOM    696  NE  ARG A  86      -0.867  -7.095  15.392  1.00 29.74           N  
ANISOU  696  NE  ARG A  86     2874   4276   4148   -388    466   -333       N  
ATOM    697  CZ  ARG A  86      -0.010  -6.109  15.168  1.00 32.09           C  
ANISOU  697  CZ  ARG A  86     3230   4527   4436   -261    448   -342       C  
ATOM    698  NH1 ARG A  86       0.805  -5.706  16.134  1.00 26.98           N  
ANISOU  698  NH1 ARG A  86     2702   3861   3687   -269    541   -373       N  
ATOM    699  NH2 ARG A  86       0.015  -5.514  13.981  1.00 31.77           N  
ANISOU  699  NH2 ARG A  86     3135   4459   4477   -143    329   -313       N  
ATOM    700  N   ASN A  87       0.326 -12.682  15.547  1.00 44.19           N  
ANISOU  700  N   ASN A  87     7468   4672   4648  -1100   -470   -251       N  
ATOM    701  CA  ASN A  87      -0.333 -13.483  14.528  1.00 55.45           C  
ANISOU  701  CA  ASN A  87     8993   6158   5916  -1372   -453   -360       C  
ATOM    702  C   ASN A  87       0.308 -14.859  14.518  1.00 61.70           C  
ANISOU  702  C   ASN A  87     9626   6892   6923  -1284   -152   -781       C  
ATOM    703  O   ASN A  87       0.451 -15.498  13.478  1.00 71.73           O  
ANISOU  703  O   ASN A  87    10918   8292   8043  -1616     43  -1108       O  
ATOM    704  CB  ASN A  87      -0.229 -12.805  13.164  1.00 62.64           C  
ANISOU  704  CB  ASN A  87    10077   7349   6374  -1926   -505   -329       C  
ATOM    705  CG  ASN A  87      -0.963 -11.465  13.109  1.00 62.79           C  
ANISOU  705  CG  ASN A  87    10184   7338   6338  -2038   -887    168       C  
ATOM    706  OD1 ASN A  87      -2.194 -11.408  13.183  1.00 61.69           O  
ANISOU  706  OD1 ASN A  87    10069   7041   6329  -2004  -1147    458       O  
ATOM    707  ND2 ASN A  87      -0.206 -10.386  12.957  1.00 59.76           N  
ANISOU  707  ND2 ASN A  87     9807   7067   5832  -2183   -931    265       N  
ATOM    708  N   SER A  88       0.678 -15.298  15.717  1.00 62.36           N  
ANISOU  708  N   SER A  88     9513   6775   7405   -879   -129   -764       N  
ATOM    709  CA ASER A  88       1.399 -16.547  15.895  0.47 64.86           C  
ANISOU  709  CA ASER A  88     9577   6935   8131   -749     90  -1085       C  
ATOM    710  CA BSER A  88       1.426 -16.532  15.911  0.53 64.20           C  
ANISOU  710  CA BSER A  88     9491   6851   8050   -746     91  -1084       C  
ATOM    711  C   SER A  88       0.907 -17.306  17.123  1.00 65.33           C  
ANISOU  711  C   SER A  88     9476   6752   8593   -389    -74   -856       C  
ATOM    712  O   SER A  88       0.905 -16.786  18.242  1.00 64.37           O  
ANISOU  712  O   SER A  88     9327   6618   8511   -192   -240   -558       O  
ATOM    713  CB ASER A  88       2.898 -16.273  15.999  0.47 63.72           C  
ANISOU  713  CB ASER A  88     9271   6819   8121   -742    285  -1295       C  
ATOM    714  CB BSER A  88       2.898 -16.199  16.116  0.53 61.35           C  
ANISOU  714  CB BSER A  88     8971   6514   7823   -714    262  -1256       C  
ATOM    715  OG ASER A  88       3.355 -15.577  14.849  0.47 62.96           O  
ANISOU  715  OG ASER A  88     9326   6992   7604  -1138    441  -1512       O  
ATOM    716  OG BSER A  88       3.047 -15.240  17.147  0.53 52.64           O  
ANISOU  716  OG BSER A  88     7896   5434   6671   -514     77   -910       O  
ATOM    717  N   ARG A  90       2.346 -18.673  20.317  1.00 59.41           N  
ANISOU  717  N   ARG A  90     8019   5576   8976    204   -365   -369       N  
ATOM    718  CA  ARG A  90       3.792 -18.570  20.156  1.00 57.77           C  
ANISOU  718  CA  ARG A  90     7610   5316   9022    187   -207   -565       C  
ATOM    719  C   ARG A  90       4.271 -17.113  20.129  1.00 60.98           C  
ANISOU  719  C   ARG A  90     8225   5992   8951    105   -152   -540       C  
ATOM    720  O   ARG A  90       4.403 -16.518  19.049  1.00 61.54           O  
ANISOU  720  O   ARG A  90     8474   6204   8704    -69     37   -808       O  
ATOM    721  CB  ARG A  90       4.228 -19.286  18.893  1.00 59.64           C  
ANISOU  721  CB  ARG A  90     7717   5414   9530     68    102  -1088       C  
ATOM    722  N   SER A  91       4.538 -16.543  21.306  1.00 53.54           N  
ANISOU  722  N   SER A  91     7250   5143   7951    173   -325   -215       N  
ATOM    723  CA  SER A  91       5.064 -15.175  21.382  1.00 54.85           C  
ANISOU  723  CA  SER A  91     7563   5529   7748    108   -270   -203       C  
ATOM    724  C   SER A  91       6.028 -14.958  22.551  1.00 55.98           C  
ANISOU  724  C   SER A  91     7516   5714   8041    145   -377     26       C  
ATOM    725  O   SER A  91       6.104 -15.760  23.484  1.00 53.81           O  
ANISOU  725  O   SER A  91     7018   5343   8084    179   -572    289       O  
ATOM    726  CB  SER A  91       3.937 -14.139  21.426  1.00 52.42           C  
ANISOU  726  CB  SER A  91     7532   5392   6994     51   -344    -83       C  
ATOM    727  OG  SER A  91       3.358 -14.051  22.713  1.00 53.26           O  
ANISOU  727  OG  SER A  91     7596   5561   7077     87   -512    187       O  
ATOM    728  N   ILE A  92       6.759 -13.849  22.479  1.00 52.24           N  
ANISOU  728  N   ILE A  92     7125   5400   7324     92   -279    -37       N  
ATOM    729  CA  ILE A  92       7.872 -13.574  23.380  1.00 48.48           C  
ANISOU  729  CA  ILE A  92     6471   4979   6968     87   -343    127       C  
ATOM    730  C   ILE A  92       7.768 -12.120  23.846  1.00 44.97           C  
ANISOU  730  C   ILE A  92     6218   4804   6065      6   -331    194       C  
ATOM    731  O   ILE A  92       7.549 -11.217  23.032  1.00 43.48           O  
ANISOU  731  O   ILE A  92     6231   4685   5606    -29   -206     17       O  
ATOM    732  CB  ILE A  92       9.222 -13.886  22.656  1.00 75.81           C  
ANISOU  732  CB  ILE A  92     9738   8282  10786    109   -166   -135       C  
ATOM    733  CG1 ILE A  92      10.153 -12.669  22.590  1.00 73.96           C  
ANISOU  733  CG1 ILE A  92     9589   8232  10279     51    -50   -209       C  
ATOM    734  CG2 ILE A  92       8.946 -14.415  21.243  1.00 76.69           C  
ANISOU  734  CG2 ILE A  92     9900   8274  10964     72     63   -544       C  
ATOM    735  CD1 ILE A  92      10.129 -11.935  21.248  1.00 71.75           C  
ANISOU  735  CD1 ILE A  92     9545   8064   9654    -57    185   -548       C  
ATOM    736  N   PRO A  93       7.868 -11.885  25.162  1.00 41.28           N  
ANISOU  736  N   PRO A  93     5664   4496   5523    -80   -473    455       N  
ATOM    737  CA  PRO A  93       7.709 -10.488  25.583  1.00 43.58           C  
ANISOU  737  CA  PRO A  93     6096   5022   5442   -181   -401    418       C  
ATOM    738  C   PRO A  93       8.852  -9.610  25.073  1.00 38.45           C  
ANISOU  738  C   PRO A  93     5473   4410   4729   -166   -261    272       C  
ATOM    739  O   PRO A  93       9.954 -10.103  24.838  1.00 40.10           O  
ANISOU  739  O   PRO A  93     5537   4522   5178   -120   -243    259       O  
ATOM    740  CB  PRO A  93       7.716 -10.569  27.112  1.00 47.79           C  
ANISOU  740  CB  PRO A  93     6497   5774   5886   -376   -548    679       C  
ATOM    741  CG  PRO A  93       8.389 -11.866  27.436  1.00 53.60           C  
ANISOU  741  CG  PRO A  93     6993   6377   6995   -373   -753    947       C  
ATOM    742  CD  PRO A  93       8.073 -12.803  26.296  1.00 49.47           C  
ANISOU  742  CD  PRO A  93     6464   5534   6798   -162   -711    793       C  
ATOM    743  N   MET A  94       8.584  -8.325  24.881  1.00 34.61           N  
ANISOU  743  N   MET A  94     5132   4026   3992   -213   -167    157       N  
ATOM    744  CA  MET A  94       9.621  -7.411  24.423  1.00 31.90           C  
ANISOU  744  CA  MET A  94     4820   3737   3564   -224    -54     45       C  
ATOM    745  C   MET A  94       9.554  -6.089  25.186  1.00 34.71           C  
ANISOU  745  C   MET A  94     5188   4261   3740   -326    -16     38       C  
ATOM    746  O   MET A  94       8.467  -5.568  25.430  1.00 30.61           O  
ANISOU  746  O   MET A  94     4704   3739   3187   -375    -17     -4       O  
ATOM    747  CB  MET A  94       9.493  -7.182  22.914  1.00 37.65           C  
ANISOU  747  CB  MET A  94     5702   4371   4234   -221     25   -126       C  
ATOM    748  CG  MET A  94      10.504  -6.193  22.347  1.00 42.83           C  
ANISOU  748  CG  MET A  94     6405   5110   4758   -288    129   -228       C  
ATOM    749  SD  MET A  94      10.644  -6.313  20.548  1.00 51.02           S  
ANISOU  749  SD  MET A  94     7585   6131   5669   -436    225   -427       S  
ATOM    750  CE  MET A  94       8.914  -6.250  20.069  1.00 65.71           C  
ANISOU  750  CE  MET A  94     9596   7916   7454   -504     62   -305       C  
ATOM    751  N   THR A  95      10.713  -5.563  25.583  1.00 28.83           N  
ANISOU  751  N   THR A  95     4376   3639   2940   -372     35     45       N  
ATOM    752  CA  THR A  95      10.787  -4.259  26.225  1.00 31.06           C  
ANISOU  752  CA  THR A  95     4645   4075   3081   -488    115    -27       C  
ATOM    753  C   THR A  95      11.682  -3.348  25.395  1.00 33.18           C  
ANISOU  753  C   THR A  95     4975   4317   3313   -449    196   -122       C  
ATOM    754  O   THR A  95      12.426  -3.822  24.530  1.00 32.50           O  
ANISOU  754  O   THR A  95     4922   4161   3266   -378    212   -139       O  
ATOM    755  CB  THR A  95      11.306  -4.353  27.671  1.00 31.68           C  
ANISOU  755  CB  THR A  95     4581   4407   3050   -677     90     90       C  
ATOM    756  OG1 THR A  95      12.507  -5.129  27.698  1.00 35.87           O  
ANISOU  756  OG1 THR A  95     5015   4927   3687   -639     -4    271       O  
ATOM    757  CG2 THR A  95      10.278  -5.022  28.556  1.00 34.70           C  
ANISOU  757  CG2 THR A  95     4909   4889   3388   -826     13    175       C  
ATOM    758  N   VAL A  96      11.593  -2.043  25.636  1.00 31.74           N  
ANISOU  758  N   VAL A  96     4783   4184   3094   -524    265   -219       N  
ATOM    759  CA  VAL A  96      12.324  -1.084  24.808  1.00 33.36           C  
ANISOU  759  CA  VAL A  96     5045   4356   3274   -516    305   -270       C  
ATOM    760  C   VAL A  96      13.161  -0.174  25.681  1.00 36.58           C  
ANISOU  760  C   VAL A  96     5355   4928   3615   -599    401   -328       C  
ATOM    761  O   VAL A  96      12.816   0.084  26.834  1.00 35.41           O  
ANISOU  761  O   VAL A  96     5097   4908   3451   -723    462   -395       O  
ATOM    762  CB  VAL A  96      11.377  -0.218  23.932  1.00 36.92           C  
ANISOU  762  CB  VAL A  96     5551   4622   3855   -543    232   -281       C  
ATOM    763  CG1 VAL A  96      10.407  -1.083  23.188  1.00 36.45           C  
ANISOU  763  CG1 VAL A  96     5585   4432   3832   -514    124   -209       C  
ATOM    764  CG2 VAL A  96      10.607   0.787  24.784  1.00 40.45           C  
ANISOU  764  CG2 VAL A  96     5842   5010   4518   -610    279   -394       C  
ATOM    765  N   ASP A  97      14.279   0.295  25.141  1.00 27.36           N  
ANISOU  765  N   ASP A  97     4223   3792   2382   -582    437   -332       N  
ATOM    766  CA  ASP A  97      15.023   1.367  25.787  1.00 30.55           C  
ANISOU  766  CA  ASP A  97     4546   4325   2736   -663    528   -401       C  
ATOM    767  C   ASP A  97      15.704   2.219  24.723  1.00 31.26           C  
ANISOU  767  C   ASP A  97     4710   4353   2813   -649    528   -412       C  
ATOM    768  O   ASP A  97      15.747   1.842  23.541  1.00 31.60           O  
ANISOU  768  O   ASP A  97     4870   4320   2817   -632    471   -369       O  
ATOM    769  CB  ASP A  97      16.036   0.837  26.801  1.00 35.86           C  
ANISOU  769  CB  ASP A  97     5129   5212   3284   -725    551   -323       C  
ATOM    770  CG  ASP A  97      16.206   1.771  27.993  1.00 47.23           C  
ANISOU  770  CG  ASP A  97     6456   6863   4625   -923    656   -424       C  
ATOM    771  OD1 ASP A  97      15.930   2.986  27.848  1.00 45.00           O  
ANISOU  771  OD1 ASP A  97     6145   6514   4438   -951    751   -603       O  
ATOM    772  OD2 ASP A  97      16.611   1.290  29.072  1.00 55.55           O  
ANISOU  772  OD2 ASP A  97     7423   8151   5534  -1096    631   -317       O  
ATOM    773  N   PHE A  98      16.228   3.364  25.147  1.00 27.74           N  
ANISOU  773  N   PHE A  98     4189   3971   2379   -712    598   -482       N  
ATOM    774  CA  PHE A  98      16.791   4.328  24.212  1.00 31.51           C  
ANISOU  774  CA  PHE A  98     4717   4392   2864   -740    567   -460       C  
ATOM    775  C   PHE A  98      18.130   4.797  24.731  1.00 32.01           C  
ANISOU  775  C   PHE A  98     4733   4629   2801   -760    677   -507       C  
ATOM    776  O   PHE A  98      18.320   4.954  25.933  1.00 32.80           O  
ANISOU  776  O   PHE A  98     4720   4865   2878   -812    770   -581       O  
ATOM    777  CB  PHE A  98      15.848   5.529  24.056  1.00 32.19           C  
ANISOU  777  CB  PHE A  98     4701   4268   3260   -803    489   -474       C  
ATOM    778  CG  PHE A  98      14.484   5.155  23.574  1.00 29.26           C  
ANISOU  778  CG  PHE A  98     4344   3695   3080   -799    349   -395       C  
ATOM    779  CD1 PHE A  98      13.510   4.730  24.474  1.00 29.24           C  
ANISOU  779  CD1 PHE A  98     4240   3652   3216   -772    416   -516       C  
ATOM    780  CD2 PHE A  98      14.173   5.215  22.227  1.00 30.02           C  
ANISOU  780  CD2 PHE A  98     4552   3675   3181   -881    142   -190       C  
ATOM    781  CE1 PHE A  98      12.249   4.374  24.035  1.00 29.62           C  
ANISOU  781  CE1 PHE A  98     4291   3499   3464   -760    285   -443       C  
ATOM    782  CE2 PHE A  98      12.909   4.851  21.772  1.00 31.07           C  
ANISOU  782  CE2 PHE A  98     4695   3626   3486   -905    -17    -79       C  
ATOM    783  CZ  PHE A  98      11.947   4.424  22.678  1.00 30.22           C  
ANISOU  783  CZ  PHE A  98     4479   3432   3572   -810     58   -210       C  
ATOM    784  N   ILE A  99      19.066   5.024  23.822  1.00 29.93           N  
ANISOU  784  N   ILE A  99     4553   4394   2425   -772    671   -472       N  
ATOM    785  CA  ILE A  99      20.367   5.517  24.232  1.00 31.89           C  
ANISOU  785  CA  ILE A  99     4754   4789   2575   -785    769   -510       C  
ATOM    786  C   ILE A  99      20.847   6.490  23.184  1.00 33.39           C  
ANISOU  786  C   ILE A  99     5010   4952   2722   -868    727   -481       C  
ATOM    787  O   ILE A  99      20.481   6.381  22.008  1.00 32.08           O  
ANISOU  787  O   ILE A  99     4954   4727   2506   -959    626   -409       O  
ATOM    788  CB  ILE A  99      21.372   4.354  24.446  1.00 44.19           C  
ANISOU  788  CB  ILE A  99     6289   6445   4055   -723    826   -496       C  
ATOM    789  CG1 ILE A  99      22.585   4.834  25.244  1.00 50.99           C  
ANISOU  789  CG1 ILE A  99     7056   7460   4859   -752    896   -492       C  
ATOM    790  CG2 ILE A  99      21.765   3.707  23.124  1.00 44.46           C  
ANISOU  790  CG2 ILE A  99     6410   6427   4054   -726    852   -551       C  
ATOM    791  CD1 ILE A  99      23.579   3.744  25.556  1.00 55.84           C  
ANISOU  791  CD1 ILE A  99     7565   8103   5546   -708    894   -417       C  
ATOM    792  N   ARG A 100      21.627   7.476  23.604  1.00 31.75           N  
ANISOU  792  N   ARG A 100     4734   4815   2516   -896    786   -517       N  
ATOM    793  CA  ARG A 100      22.166   8.424  22.645  1.00 34.54           C  
ANISOU  793  CA  ARG A 100     5139   5161   2824  -1006    721   -452       C  
ATOM    794  C   ARG A 100      23.667   8.569  22.866  1.00 41.23           C  
ANISOU  794  C   ARG A 100     5979   6185   3502   -994    856   -520       C  
ATOM    795  O   ARG A 100      24.118   8.661  24.008  1.00 38.56           O  
ANISOU  795  O   ARG A 100     5538   5930   3182   -934    955   -584       O  
ATOM    796  CB  ARG A 100      21.475   9.784  22.772  1.00 42.29           C  
ANISOU  796  CB  ARG A 100     5991   5957   4121  -1068    609   -403       C  
ATOM    797  CG  ARG A 100      22.191  10.880  22.001  1.00 47.33           C  
ANISOU  797  CG  ARG A 100     6637   6597   4749  -1204    509   -285       C  
ATOM    798  CD  ARG A 100      21.260  11.625  21.091  1.00 54.64           C  
ANISOU  798  CD  ARG A 100     7514   7289   5957  -1370    215    -37       C  
ATOM    799  NE  ARG A 100      20.665  12.784  21.739  1.00 59.61           N  
ANISOU  799  NE  ARG A 100     7868   7633   7147  -1340    160    -69       N  
ATOM    800  CZ  ARG A 100      20.895  14.040  21.372  1.00 62.72           C  
ANISOU  800  CZ  ARG A 100     8119   7869   7843  -1461    -10     84       C  
ATOM    801  NH1 ARG A 100      21.703  14.302  20.356  1.00 61.58           N  
ANISOU  801  NH1 ARG A 100     8122   7882   7393  -1653   -161    319       N  
ATOM    802  NH2 ARG A 100      20.311  15.037  22.018  1.00 68.74           N  
ANISOU  802  NH2 ARG A 100     8556   8308   9254  -1426    -19    -22       N  
ATOM    803  N   LEU A 101      24.418   8.554  21.765  1.00 45.55           N  
ANISOU  803  N   LEU A 101     6927   5196   5183   -621  -1167   -462       N  
ATOM    804  CA  LEU A 101      25.864   8.751  21.768  1.00 49.37           C  
ANISOU  804  CA  LEU A 101     7348   5720   5691   -978  -1304   -337       C  
ATOM    805  C   LEU A 101      26.201  10.015  20.975  1.00 56.85           C  
ANISOU  805  C   LEU A 101     8493   6446   6662  -1239  -1505   -171       C  
ATOM    806  O   LEU A 101      25.604  10.271  19.926  1.00 57.98           O  
ANISOU  806  O   LEU A 101     8642   6563   6826  -1188  -1454    -88       O  
ATOM    807  CB  LEU A 101      26.567   7.547  21.130  1.00 45.67           C  
ANISOU  807  CB  LEU A 101     6470   5636   5246  -1058  -1124   -231       C  
ATOM    808  CG  LEU A 101      27.033   6.384  22.004  1.00 51.17           C  
ANISOU  808  CG  LEU A 101     6974   6540   5926   -976  -1040   -310       C  
ATOM    809  CD1 LEU A 101      25.899   5.817  22.842  1.00 48.44           C  
ANISOU  809  CD1 LEU A 101     6730   6143   5532   -682   -949   -497       C  
ATOM    810  CD2 LEU A 101      27.650   5.291  21.141  1.00 51.11           C  
ANISOU  810  CD2 LEU A 101     6631   6862   5926   -975   -864   -210       C  
ATOM    811  N   LYS A 102      27.152  10.799  21.476  1.00 63.96           N  
ANISOU  811  N   LYS A 102     9570   7185   7548  -1552  -1763   -100       N  
ATOM    812  CA  LYS A 102      27.630  11.985  20.761  1.00 72.44           C  
ANISOU  812  CA  LYS A 102    10847   8047   8630  -1905  -2007    111       C  
ATOM    813  C   LYS A 102      29.132  12.190  20.961  1.00 77.93           C  
ANISOU  813  C   LYS A 102    11375   8913   9321  -2326  -2142    336       C  
ATOM    814  O   LYS A 102      29.915  12.083  20.017  1.00 82.23           O  
ANISOU  814  O   LYS A 102    11607   9760   9877  -2607  -2096    596       O  
ATOM    815  CB  LYS A 102      26.864  13.223  21.198  1.00 73.98           C  
ANISOU  815  CB  LYS A 102    11615   7709   8786  -1756  -2233    -11       C  
ATOM    816  N   LEU A 121      19.760   0.952  32.614  1.00 58.91           N  
ANISOU  816  N   LEU A 121     8208   8523   5654    434   -277   -985       N  
ATOM    817  CA  LEU A 121      20.020  -0.059  31.586  1.00 51.73           C  
ANISOU  817  CA  LEU A 121     7140   7634   4882    266   -330   -865       C  
ATOM    818  C   LEU A 121      20.154  -1.469  32.159  1.00 50.31           C  
ANISOU  818  C   LEU A 121     6915   7548   4653     93   -372   -730       C  
ATOM    819  O   LEU A 121      20.531  -2.412  31.454  1.00 48.06           O  
ANISOU  819  O   LEU A 121     6576   7209   4476    -36   -446   -641       O  
ATOM    820  CB  LEU A 121      21.251   0.298  30.751  1.00 53.09           C  
ANISOU  820  CB  LEU A 121     7363   7561   5246    174   -462   -914       C  
ATOM    821  CG  LEU A 121      21.037   1.212  29.539  1.00 52.91           C  
ANISOU  821  CG  LEU A 121     7330   7446   5326    257   -449   -956       C  
ATOM    822  CD1 LEU A 121      22.275   1.229  28.651  1.00 52.58           C  
ANISOU  822  CD1 LEU A 121     7264   7244   5471     99   -558   -925       C  
ATOM    823  CD2 LEU A 121      19.810   0.789  28.743  1.00 51.69           C  
ANISOU  823  CD2 LEU A 121     6994   7466   5178    306   -325   -841       C  
ATOM    824  N   SER A 122      19.823  -1.616  33.438  1.00 49.91           N  
ANISOU  824  N   SER A 122     6921   7617   4423    108   -333   -713       N  
ATOM    825  CA  SER A 122      19.655  -2.932  34.039  1.00 48.94           C  
ANISOU  825  CA  SER A 122     6765   7610   4218    -47   -371   -553       C  
ATOM    826  C   SER A 122      18.493  -3.635  33.348  1.00 51.14           C  
ANISOU  826  C   SER A 122     6845   8107   4479   -129   -296   -382       C  
ATOM    827  O   SER A 122      18.259  -4.819  33.557  1.00 53.31           O  
ANISOU  827  O   SER A 122     7098   8436   4722   -315   -358   -212       O  
ATOM    828  CB  SER A 122      19.380  -2.801  35.537  1.00 52.00           C  
ANISOU  828  CB  SER A 122     7246   8128   4384     -8   -319   -561       C  
ATOM    829  OG  SER A 122      18.375  -1.833  35.775  1.00 54.23           O  
ANISOU  829  OG  SER A 122     7474   8598   4532    200   -130   -633       O  
ATOM    830  N   THR A 123      17.774  -2.884  32.517  1.00 57.73           N  
ANISOU  830  N   THR A 123     7550   9049   5335     -5   -190   -412       N  
ATOM    831  CA  THR A 123      16.712  -3.411  31.671  1.00 66.59           C  
ANISOU  831  CA  THR A 123     8466  10381   6454   -110   -151   -232       C  
ATOM    832  C   THR A 123      17.238  -4.459  30.679  1.00 67.01           C  
ANISOU  832  C   THR A 123     8591  10205   6663   -333   -312   -152       C  
ATOM    833  O   THR A 123      16.454  -5.170  30.049  1.00 71.13           O  
ANISOU  833  O   THR A 123     9020  10821   7187   -509   -344     24       O  
ATOM    834  CB  THR A 123      16.020  -2.264  30.891  1.00 72.44           C  
ANISOU  834  CB  THR A 123     9075  11249   7200    117    -34   -293       C  
ATOM    835  OG1 THR A 123      16.971  -1.614  30.036  1.00 74.29           O  
ANISOU  835  OG1 THR A 123     9452  11148   7628    182   -111   -454       O  
ATOM    836  CG2 THR A 123      15.440  -1.237  31.854  1.00 75.96           C  
ANISOU  836  CG2 THR A 123     9497  11867   7497    423    131   -387       C  
ATOM    837  N   LEU A 124      18.562  -4.550  30.551  1.00 59.07           N  
ANISOU  837  N   LEU A 124     7759   8898   5786   -313   -417   -276       N  
ATOM    838  CA  LEU A 124      19.205  -5.439  29.579  1.00 47.60           C  
ANISOU  838  CA  LEU A 124     6402   7213   4471   -412   -541   -248       C  
ATOM    839  C   LEU A 124      19.637  -6.783  30.168  1.00 41.86           C  
ANISOU  839  C   LEU A 124     5813   6362   3729   -523   -672   -157       C  
ATOM    840  O   LEU A 124      19.760  -7.773  29.445  1.00 37.78           O  
ANISOU  840  O   LEU A 124     5402   5684   3269   -606   -768    -97       O  
ATOM    841  CB  LEU A 124      20.445  -4.769  28.985  1.00 46.09           C  
ANISOU  841  CB  LEU A 124     6258   6835   4417   -288   -563   -413       C  
ATOM    842  CG  LEU A 124      20.356  -3.375  28.378  1.00 43.58           C  
ANISOU  842  CG  LEU A 124     5862   6538   4158   -167   -474   -522       C  
ATOM    843  CD1 LEU A 124      21.733  -2.919  27.928  1.00 44.05           C  
ANISOU  843  CD1 LEU A 124     5959   6414   4364   -120   -526   -620       C  
ATOM    844  CD2 LEU A 124      19.405  -3.366  27.204  1.00 43.50           C  
ANISOU  844  CD2 LEU A 124     5764   6585   4180   -201   -424   -439       C  
ATOM    845  N   THR A 125      19.889  -6.814  31.475  1.00 39.49           N  
ANISOU  845  N   THR A 125     5545   6120   3341   -509   -684   -154       N  
ATOM    846  CA  THR A 125      20.520  -7.981  32.102  1.00 39.99           C  
ANISOU  846  CA  THR A 125     5745   6050   3399   -580   -826    -81       C  
ATOM    847  C   THR A 125      19.745  -9.292  31.886  1.00 46.17           C  
ANISOU  847  C   THR A 125     6605   6789   4148   -801   -908    115       C  
ATOM    848  O   THR A 125      18.526  -9.350  32.082  1.00 45.49           O  
ANISOU  848  O   THR A 125     6408   6914   3963   -965   -845    259       O  
ATOM    849  CB  THR A 125      20.779  -7.725  33.593  1.00 47.34           C  
ANISOU  849  CB  THR A 125     6693   7082   4212   -552   -826    -93       C  
ATOM    850  OG1 THR A 125      21.515  -6.500  33.723  1.00 50.73           O  
ANISOU  850  OG1 THR A 125     7107   7490   4678   -388   -792   -273       O  
ATOM    851  CG2 THR A 125      21.584  -8.856  34.204  1.00 46.72           C  
ANISOU  851  CG2 THR A 125     6750   6858   4142   -606   -991    -16       C  
ATOM    852  N   GLY A 126      20.459 -10.328  31.443  1.00 44.86           N  
ANISOU  852  N   GLY A 126     6635   6352   4056   -809  -1057    128       N  
ATOM    853  CA  GLY A 126      19.866 -11.632  31.215  1.00 41.60           C  
ANISOU  853  CA  GLY A 126     6401   5790   3616  -1036  -1188    301       C  
ATOM    854  C   GLY A 126      18.877 -11.702  30.061  1.00 45.74           C  
ANISOU  854  C   GLY A 126     6898   6322   4159  -1181  -1167    365       C  
ATOM    855  O   GLY A 126      18.120 -12.671  29.950  1.00 47.63           O  
ANISOU  855  O   GLY A 126     7261   6482   4356  -1456  -1283    543       O  
ATOM    856  N   LYS A 127      18.867 -10.694  29.190  1.00 41.59           N  
ANISOU  856  N   LYS A 127     6226   5881   3694  -1036  -1046    238       N  
ATOM    857  CA  LYS A 127      17.906 -10.694  28.088  1.00 42.50           C  
ANISOU  857  CA  LYS A 127     6298   6029   3821  -1178  -1036    313       C  
ATOM    858  C   LYS A 127      18.602 -10.668  26.731  1.00 37.14           C  
ANISOU  858  C   LYS A 127     5759   5120   3232  -1024  -1054    163       C  
ATOM    859  O   LYS A 127      19.805 -10.431  26.652  1.00 41.22           O  
ANISOU  859  O   LYS A 127     6331   5530   3801   -790  -1037      1       O  
ATOM    860  CB  LYS A 127      16.912  -9.530  28.224  1.00 42.45           C  
ANISOU  860  CB  LYS A 127     5969   6394   3765  -1186   -875    356       C  
ATOM    861  CG  LYS A 127      16.090  -9.585  29.533  1.00 50.36           C  
ANISOU  861  CG  LYS A 127     6801   7707   4627  -1329   -825    521       C  
ATOM    862  CD  LYS A 127      15.066  -8.457  29.632  1.00 52.49           C  
ANISOU  862  CD  LYS A 127     6733   8399   4810  -1267   -649    567       C  
ATOM    863  CE  LYS A 127      14.411  -8.390  31.010  1.00 55.73           C  
ANISOU  863  CE  LYS A 127     6956   9170   5049  -1312   -552    689       C  
ATOM    864  NZ  LYS A 127      15.403  -8.079  32.067  1.00 54.31           N  
ANISOU  864  NZ  LYS A 127     6919   8886   4831  -1117   -517    521       N  
ATOM    865  N   ASN A 128      17.839 -10.943  25.680  1.00 35.79           N  
ANISOU  865  N   ASN A 128     5638   4900   3061  -1175  -1093    237       N  
ATOM    866  CA  ASN A 128      18.340 -10.849  24.316  1.00 35.73           C  
ANISOU  866  CA  ASN A 128     5755   4720   3102  -1039  -1087    105       C  
ATOM    867  C   ASN A 128      18.262  -9.409  23.821  1.00 36.80           C  
ANISOU  867  C   ASN A 128     5626   5072   3285   -910   -930     18       C  
ATOM    868  O   ASN A 128      17.187  -8.932  23.450  1.00 41.65           O  
ANISOU  868  O   ASN A 128     6076   5865   3885  -1041   -900    126       O  
ATOM    869  CB  ASN A 128      17.546 -11.775  23.396  1.00 39.22           C  
ANISOU  869  CB  ASN A 128     6412   4987   3502  -1279  -1222    228       C  
ATOM    870  CG  ASN A 128      17.820 -13.242  23.680  1.00 46.40           C  
ANISOU  870  CG  ASN A 128     7714   5560   4358  -1381  -1420    288       C  
ATOM    871  OD1 ASN A 128      18.592 -13.576  24.584  1.00 46.70           O  
ANISOU  871  OD1 ASN A 128     7836   5516   4394  -1260  -1455    246       O  
ATOM    872  ND2 ASN A 128      17.184 -14.125  22.913  1.00 49.03           N  
ANISOU  872  ND2 ASN A 128     8323   5672   4636  -1614  -1577    399       N  
ATOM    873  N   VAL A 129      19.408  -8.731  23.812  1.00 37.52           N  
ANISOU  873  N   VAL A 129     5683   5147   3426   -671   -851   -154       N  
ATOM    874  CA  VAL A 129      19.476  -7.312  23.472  1.00 31.83           C  
ANISOU  874  CA  VAL A 129     4762   4583   2747   -569   -727   -233       C  
ATOM    875  C   VAL A 129      19.636  -7.104  21.971  1.00 35.30           C  
ANISOU  875  C   VAL A 129     5263   4946   3205   -533   -703   -286       C  
ATOM    876  O   VAL A 129      20.574  -7.636  21.358  1.00 33.27           O  
ANISOU  876  O   VAL A 129     5174   4530   2937   -420   -714   -381       O  
ATOM    877  CB  VAL A 129      20.626  -6.627  24.224  1.00 32.36           C  
ANISOU  877  CB  VAL A 129     4770   4674   2851   -404   -677   -361       C  
ATOM    878  CG1 VAL A 129      20.701  -5.135  23.872  1.00 31.47           C  
ANISOU  878  CG1 VAL A 129     4477   4659   2821   -316   -557   -426       C  
ATOM    879  CG2 VAL A 129      20.435  -6.790  25.724  1.00 37.99           C  
ANISOU  879  CG2 VAL A 129     5441   5474   3522   -438   -699   -310       C  
ATOM    880  N   LEU A 130      18.701  -6.366  21.370  1.00 28.68           N  
ANISOU  880  N   LEU A 130     4293   4240   2366   -616   -671   -214       N  
ATOM    881  CA  LEU A 130      18.818  -6.000  19.968  1.00 26.57           C  
ANISOU  881  CA  LEU A 130     4070   3926   2100   -595   -647   -249       C  
ATOM    882  C   LEU A 130      19.120  -4.510  19.900  1.00 28.39           C  
ANISOU  882  C   LEU A 130     4116   4272   2397   -489   -539   -303       C  
ATOM    883  O   LEU A 130      18.287  -3.688  20.272  1.00 30.28           O  
ANISOU  883  O   LEU A 130     4178   4657   2670   -488   -508   -233       O  
ATOM    884  CB  LEU A 130      17.533  -6.321  19.192  1.00 27.07           C  
ANISOU  884  CB  LEU A 130     4136   4022   2127   -788   -724    -95       C  
ATOM    885  CG  LEU A 130      17.474  -5.884  17.724  1.00 33.40           C  
ANISOU  885  CG  LEU A 130     4981   4799   2911   -794   -715   -103       C  
ATOM    886  CD1 LEU A 130      18.530  -6.606  16.895  1.00 32.31           C  
ANISOU  886  CD1 LEU A 130     5098   4458   2720   -688   -703   -237       C  
ATOM    887  CD2 LEU A 130      16.096  -6.098  17.132  1.00 37.37           C  
ANISOU  887  CD2 LEU A 130     5439   5375   3385  -1013   -814     80       C  
ATOM    888  N   ILE A 131      20.322  -4.164  19.457  1.00 26.27           N  
ANISOU  888  N   ILE A 131     3869   3928   2185   -360   -466   -406       N  
ATOM    889  CA  ILE A 131      20.681  -2.759  19.269  1.00 28.27           C  
ANISOU  889  CA  ILE A 131     3973   4226   2542   -292   -385   -421       C  
ATOM    890  C   ILE A 131      20.207  -2.340  17.874  1.00 24.32           C  
ANISOU  890  C   ILE A 131     3490   3742   2009   -357   -383   -357       C  
ATOM    891  O   ILE A 131      20.472  -3.029  16.892  1.00 25.31           O  
ANISOU  891  O   ILE A 131     3754   3826   2035   -385   -387   -371       O  
ATOM    892  CB  ILE A 131      22.204  -2.539  19.428  1.00 31.05           C  
ANISOU  892  CB  ILE A 131     4289   4555   2954   -193   -331   -499       C  
ATOM    893  CG1 ILE A 131      22.657  -2.914  20.836  1.00 27.97           C  
ANISOU  893  CG1 ILE A 131     3883   4155   2591   -143   -366   -544       C  
ATOM    894  CG2 ILE A 131      22.582  -1.103  19.161  1.00 31.29           C  
ANISOU  894  CG2 ILE A 131     4211   4604   3072   -208   -300   -476       C  
ATOM    895  CD1 ILE A 131      24.168  -2.846  21.041  1.00 31.06           C  
ANISOU  895  CD1 ILE A 131     4195   4572   3035    -60   -344   -581       C  
ATOM    896  N   VAL A 132      19.470  -1.234  17.788  1.00 25.72           N  
ANISOU  896  N   VAL A 132     3557   3970   2244   -358   -387   -287       N  
ATOM    897  CA  VAL A 132      18.915  -0.812  16.495  1.00 23.71           C  
ANISOU  897  CA  VAL A 132     3317   3738   1956   -429   -416   -193       C  
ATOM    898  C   VAL A 132      19.539   0.516  16.060  1.00 27.67           C  
ANISOU  898  C   VAL A 132     3785   4190   2540   -389   -382   -184       C  
ATOM    899  O   VAL A 132      19.346   1.536  16.716  1.00 28.78           O  
ANISOU  899  O   VAL A 132     3872   4290   2773   -305   -397   -182       O  
ATOM    900  CB  VAL A 132      17.386  -0.689  16.522  1.00 23.91           C  
ANISOU  900  CB  VAL A 132     3240   3882   1961   -471   -490    -59       C  
ATOM    901  CG1 VAL A 132      16.865  -0.375  15.112  1.00 21.87           C  
ANISOU  901  CG1 VAL A 132     3009   3647   1652   -567   -556     57       C  
ATOM    902  CG2 VAL A 132      16.745  -1.986  17.044  1.00 28.31           C  
ANISOU  902  CG2 VAL A 132     3819   4515   2424   -593   -557    -14       C  
ATOM    903  N   GLU A 133      20.261   0.493  14.946  1.00 27.49           N  
ANISOU  903  N   GLU A 133     3823   4165   2456   -453   -347   -170       N  
ATOM    904  CA  GLU A 133      21.042   1.645  14.489  1.00 28.58           C  
ANISOU  904  CA  GLU A 133     3931   4280   2646   -487   -327   -120       C  
ATOM    905  C   GLU A 133      20.633   2.089  13.085  1.00 24.78           C  
ANISOU  905  C   GLU A 133     3504   3823   2087   -587   -360      3       C  
ATOM    906  O   GLU A 133      20.085   1.305  12.312  1.00 26.27           O  
ANISOU  906  O   GLU A 133     3772   4063   2146   -634   -374     21       O  
ATOM    907  CB  GLU A 133      22.540   1.294  14.534  1.00 37.50           C  
ANISOU  907  CB  GLU A 133     5017   5478   3753   -482   -231   -175       C  
ATOM    908  CG  GLU A 133      23.524   2.384  14.082  1.00 40.47           C  
ANISOU  908  CG  GLU A 133     5320   5897   4160   -594   -219    -74       C  
ATOM    909  CD  GLU A 133      23.566   3.588  15.011  1.00 42.18           C  
ANISOU  909  CD  GLU A 133     5540   5967   4521   -639   -335    -51       C  
ATOM    910  OE1 GLU A 133      22.512   4.225  15.214  1.00 40.89           O  
ANISOU  910  OE1 GLU A 133     5468   5659   4409   -590   -426    -43       O  
ATOM    911  OE2 GLU A 133      24.657   3.908  15.529  1.00 44.72           O  
ANISOU  911  OE2 GLU A 133     5783   6320   4887   -714   -349    -36       O  
ATOM    912  N   ASP A 134      20.908   3.347  12.743  1.00 23.62           N  
ANISOU  912  N   ASP A 134     3355   3621   2001   -648   -402    102       N  
ATOM    913  CA  ASP A 134      20.605   3.830  11.406  1.00 27.25           C  
ANISOU  913  CA  ASP A 134     3876   4103   2374   -762   -447    246       C  
ATOM    914  C   ASP A 134      21.706   3.468  10.393  1.00 26.28           C  
ANISOU  914  C   ASP A 134     3763   4133   2090   -870   -328    272       C  
ATOM    915  O   ASP A 134      21.424   2.974   9.291  1.00 28.00           O  
ANISOU  915  O   ASP A 134     4072   4436   2131   -922   -308    306       O  
ATOM    916  CB  ASP A 134      20.344   5.351  11.402  1.00 29.50           C  
ANISOU  916  CB  ASP A 134     4205   4230   2772   -784   -578    370       C  
ATOM    917  CG  ASP A 134      21.471   6.163  12.045  1.00 29.83           C  
ANISOU  917  CG  ASP A 134     4256   4175   2904   -853   -594    365       C  
ATOM    918  OD1 ASP A 134      22.337   5.602  12.752  1.00 28.74           O  
ANISOU  918  OD1 ASP A 134     4032   4112   2778   -845   -507    262       O  
ATOM    919  OD2 ASP A 134      21.484   7.397  11.834  1.00 37.95           O  
ANISOU  919  OD2 ASP A 134     5398   5035   3987   -933   -730    486       O  
ATOM    920  N   ILE A 135      22.958   3.726  10.763  1.00 27.06           N  
ANISOU  920  N   ILE A 135     3762   4297   2224   -901   -251    267       N  
ATOM    921  CA  ILE A 135      24.049   3.512   9.811  1.00 27.98           C  
ANISOU  921  CA  ILE A 135     3817   4646   2169   -976   -108    331       C  
ATOM    922  C   ILE A 135      25.358   3.132  10.508  1.00 26.32           C  
ANISOU  922  C   ILE A 135     3423   4592   1985   -911     10    276       C  
ATOM    923  O   ILE A 135      25.695   3.648  11.581  1.00 26.27           O  
ANISOU  923  O   ILE A 135     3337   4499   2147   -945    -71    276       O  
ATOM    924  CB  ILE A 135      24.225   4.737   8.866  1.00 31.80           C  
ANISOU  924  CB  ILE A 135     4315   5159   2610  -1208   -172    559       C  
ATOM    925  CG1 ILE A 135      25.254   4.446   7.755  1.00 30.21           C  
ANISOU  925  CG1 ILE A 135     4024   5288   2168  -1282     13    649       C  
ATOM    926  CG2 ILE A 135      24.567   5.980   9.670  1.00 30.78           C  
ANISOU  926  CG2 ILE A 135     4156   4866   2671  -1341   -320    656       C  
ATOM    927  CD1 ILE A 135      25.244   5.456   6.599  1.00 32.44           C  
ANISOU  927  CD1 ILE A 135     4360   5630   2337  -1539    -48    897       C  
ATOM    928  N   ILE A 136      26.060   2.178   9.914  1.00 29.20           N  
ANISOU  928  N   ILE A 136     3742   5190   2164   -785    192    222       N  
ATOM    929  CA  ILE A 136      27.414   1.855  10.321  1.00 33.38           C  
ANISOU  929  CA  ILE A 136     4036   5964   2682   -694    325    224       C  
ATOM    930  C   ILE A 136      28.347   2.310   9.218  1.00 34.16           C  
ANISOU  930  C   ILE A 136     3966   6412   2600   -814    467    414       C  
ATOM    931  O   ILE A 136      28.135   2.001   8.038  1.00 34.46           O  
ANISOU  931  O   ILE A 136     4124   6561   2407   -776    574    417       O  
ATOM    932  CB  ILE A 136      27.572   0.366  10.613  1.00 36.65           C  
ANISOU  932  CB  ILE A 136     4517   6396   3012   -375    432     17       C  
ATOM    933  CG1 ILE A 136      26.754   0.019  11.856  1.00 39.64           C  
ANISOU  933  CG1 ILE A 136     5013   6477   3573   -328    278   -113       C  
ATOM    934  CG2 ILE A 136      29.051   0.004  10.822  1.00 36.22           C  
ANISOU  934  CG2 ILE A 136     4179   6673   2911   -214    595     48       C  
ATOM    935  CD1 ILE A 136      26.707  -1.438  12.168  1.00 45.61           C  
ANISOU  935  CD1 ILE A 136     5918   7163   4248    -70    315   -294       C  
ATOM    936  N   ASP A 137      29.356   3.090   9.591  1.00 33.33           N  
ANISOU  936  N   ASP A 137     3590   6496   2579   -999    450    598       N  
ATOM    937  CA  ASP A 137      30.325   3.583   8.622  1.00 36.81           C  
ANISOU  937  CA  ASP A 137     3799   7348   2840  -1170    583    843       C  
ATOM    938  C   ASP A 137      31.708   3.068   9.003  1.00 47.48           C  
ANISOU  938  C   ASP A 137     4769   9123   4150  -1024    752    894       C  
ATOM    939  O   ASP A 137      32.177   2.090   8.437  1.00 48.20           O  
ANISOU  939  O   ASP A 137     4779   9511   4026   -699   1003    807       O  
ATOM    940  CB  ASP A 137      30.272   5.117   8.532  1.00 39.84           C  
ANISOU  940  CB  ASP A 137     4195   7616   3325  -1616    366   1109       C  
ATOM    941  CG  ASP A 137      31.287   5.697   7.565  1.00 45.85           C  
ANISOU  941  CG  ASP A 137     4696   8834   3891  -1884    476   1427       C  
ATOM    942  OD1 ASP A 137      31.810   4.965   6.694  1.00 51.06           O  
ANISOU  942  OD1 ASP A 137     5231   9814   4357  -1641    711   1380       O  
ATOM    943  OD2 ASP A 137      31.542   6.913   7.656  1.00 50.08           O  
ANISOU  943  OD2 ASP A 137     5217   9284   4528  -2276    258   1669       O  
ATOM    944  N   THR A 138      32.357   3.709   9.972  1.00 42.43           N  
ANISOU  944  N   THR A 138     3912   8510   3698  -1238    603   1033       N  
ATOM    945  CA  THR A 138      33.682   3.253  10.382  1.00 47.94           C  
ANISOU  945  CA  THR A 138     4188   9655   4370  -1115    732   1126       C  
ATOM    946  C   THR A 138      33.518   2.054  11.306  1.00 45.26           C  
ANISOU  946  C   THR A 138     3934   9144   4119   -697    757    838       C  
ATOM    947  O   THR A 138      34.352   1.146  11.327  1.00 48.78           O  
ANISOU  947  O   THR A 138     4141   9927   4466   -358    946    806       O  
ATOM    948  CB  THR A 138      34.491   4.351  11.103  1.00 43.92           C  
ANISOU  948  CB  THR A 138     3419   9255   4014  -1556    513   1412       C  
ATOM    949  OG1 THR A 138      33.798   4.754  12.295  1.00 42.95           O  
ANISOU  949  OG1 THR A 138     3581   8606   4134  -1664    225   1273       O  
ATOM    950  CG2 THR A 138      34.695   5.549  10.189  1.00 46.62           C  
ANISOU  950  CG2 THR A 138     3788   9633   4293  -1949    394   1679       C  
ATOM    951  N   GLY A 139      32.426   2.050  12.057  1.00 36.31           N  
ANISOU  951  N   GLY A 139     3143   7499   3154   -704    566    644       N  
ATOM    952  CA  GLY A 139      32.173   0.994  13.018  1.00 35.51           C  
ANISOU  952  CA  GLY A 139     3157   7199   3136   -389    544    407       C  
ATOM    953  C   GLY A 139      32.553   1.416  14.427  1.00 36.36           C  
ANISOU  953  C   GLY A 139     3146   7215   3453   -542    339    453       C  
ATOM    954  O   GLY A 139      32.266   0.702  15.391  1.00 36.51           O  
ANISOU  954  O   GLY A 139     3281   7033   3557   -350    274    282       O  
ATOM    955  N   LYS A 140      33.197   2.576  14.554  1.00 39.98           N  
ANISOU  955  N   LYS A 140     3406   7811   3973   -920    212    697       N  
ATOM    956  CA  LYS A 140      33.651   3.065  15.869  1.00 44.31           C  
ANISOU  956  CA  LYS A 140     3876   8276   4684  -1120    -23    758       C  
ATOM    957  C   LYS A 140      32.529   3.218  16.877  1.00 41.86           C  
ANISOU  957  C   LYS A 140     3951   7451   4502  -1112   -209    541       C  
ATOM    958  O   LYS A 140      32.654   2.796  18.029  1.00 44.41           O  
ANISOU  958  O   LYS A 140     4282   7690   4901  -1016   -302    445       O  
ATOM    959  CB  LYS A 140      34.359   4.416  15.751  1.00 53.22           C  
ANISOU  959  CB  LYS A 140     4844   9542   5834  -1617   -199   1068       C  
ATOM    960  CG  LYS A 140      35.770   4.376  15.206  1.00 64.17           C  
ANISOU  960  CG  LYS A 140     5709  11561   7114  -1715    -72   1371       C  
ATOM    961  CD  LYS A 140      36.456   5.715  15.469  1.00 71.76           C  
ANISOU  961  CD  LYS A 140     6663  12489   8115  -2224   -358   1657       C  
ATOM    962  CE  LYS A 140      37.709   5.906  14.626  1.00 81.08           C  
ANISOU  962  CE  LYS A 140     7512  14160   9135  -2289   -256   1954       C  
ATOM    963  NZ  LYS A 140      37.386   6.239  13.205  1.00 83.31           N  
ANISOU  963  NZ  LYS A 140     7850  14536   9267  -2344   -117   2031       N  
ATOM    964  N   THR A 141      31.442   3.851  16.449  1.00 36.66           N  
ANISOU  964  N   THR A 141     3595   6484   3850  -1204   -263    485       N  
ATOM    965  CA  THR A 141      30.300   4.081  17.321  1.00 36.59           C  
ANISOU  965  CA  THR A 141     3918   6051   3932  -1156   -406    299       C  
ATOM    966  C   THR A 141      29.743   2.772  17.871  1.00 38.62           C  
ANISOU  966  C   THR A 141     4244   6247   4183   -821   -309     83       C  
ATOM    967  O   THR A 141      29.479   2.644  19.073  1.00 39.36           O  
ANISOU  967  O   THR A 141     4440   6177   4340   -773   -416    -27       O  
ATOM    968  CB  THR A 141      29.176   4.820  16.592  1.00 35.38           C  
ANISOU  968  CB  THR A 141     4025   5647   3770  -1219   -442    292       C  
ATOM    969  OG1 THR A 141      29.671   6.061  16.080  1.00 43.75           O  
ANISOU  969  OG1 THR A 141     5083   6711   4830  -1557   -572    514       O  
ATOM    970  CG2 THR A 141      28.012   5.083  17.539  1.00 39.63           C  
ANISOU  970  CG2 THR A 141     4850   5824   4384  -1110   -563    117       C  
ATOM    971  N   MET A 142      29.559   1.798  16.988  1.00 29.73           N  
ANISOU  971  N   MET A 142     3100   5241   2953   -609   -123     29       N  
ATOM    972  CA  MET A 142      28.990   0.521  17.415  1.00 29.74           C  
ANISOU  972  CA  MET A 142     3232   5139   2928   -339    -74   -152       C  
ATOM    973  C   MET A 142      29.921  -0.238  18.374  1.00 26.77           C  
ANISOU  973  C   MET A 142     2704   4884   2582   -195    -89   -173       C  
ATOM    974  O   MET A 142      29.474  -0.761  19.399  1.00 30.25           O  
ANISOU  974  O   MET A 142     3274   5156   3064   -114   -172   -281       O  
ATOM    975  CB  MET A 142      28.599  -0.338  16.203  1.00 36.09           C  
ANISOU  975  CB  MET A 142     4141   5989   3581   -170     80   -210       C  
ATOM    976  CG  MET A 142      27.653  -1.470  16.567  1.00 42.16           C  
ANISOU  976  CG  MET A 142     5155   6547   4316     -5     52   -371       C  
ATOM    977  SD  MET A 142      26.391  -1.006  17.790  1.00 47.20           S  
ANISOU  977  SD  MET A 142     5929   6927   5079   -130   -115   -417       S  
ATOM    978  CE  MET A 142      25.471   0.251  16.902  1.00 25.99           C  
ANISOU  978  CE  MET A 142     3301   4169   2403   -306   -144   -333       C  
ATOM    979  N   GLN A 143      31.211  -0.269  18.064  1.00 33.22           N  
ANISOU  979  N   GLN A 143     3222   6029   3370   -168    -15    -41       N  
ATOM    980  CA  GLN A 143      32.179  -0.899  18.965  1.00 36.66           C  
ANISOU  980  CA  GLN A 143     3461   6624   3844    -23    -52    -18       C  
ATOM    981  C   GLN A 143      32.168  -0.238  20.336  1.00 39.87           C  
ANISOU  981  C   GLN A 143     3901   6876   4371   -249   -282     -2       C  
ATOM    982  O   GLN A 143      32.273  -0.904  21.371  1.00 40.08           O  
ANISOU  982  O   GLN A 143     3960   6841   4428   -125   -364    -68       O  
ATOM    983  CB  GLN A 143      33.581  -0.881  18.355  1.00 43.96           C  
ANISOU  983  CB  GLN A 143     3974   8019   4710     31     70    175       C  
ATOM    984  CG  GLN A 143      33.747  -1.848  17.183  1.00 49.71           C  
ANISOU  984  CG  GLN A 143     4694   8931   5264    398    326    110       C  
ATOM    985  CD  GLN A 143      35.192  -2.004  16.744  1.00 59.79           C  
ANISOU  985  CD  GLN A 143     5507  10757   6455    565    485    299       C  
ATOM    986  OE1 GLN A 143      36.013  -1.102  16.931  1.00 61.63           O  
ANISOU  986  OE1 GLN A 143     5380  11291   6746    266    414    548       O  
ATOM    987  NE2 GLN A 143      35.513  -3.156  16.159  1.00 64.76           N  
ANISOU  987  NE2 GLN A 143     6150  11531   6927   1048    690    192       N  
ATOM    988  N   THR A 144      32.023   1.081  20.337  1.00 38.85           N  
ANISOU  988  N   THR A 144     3815   6658   4287   -578   -403     84       N  
ATOM    989  CA  THR A 144      31.944   1.838  21.577  1.00 42.90           C  
ANISOU  989  CA  THR A 144     4459   6972   4870   -792   -638     70       C  
ATOM    990  C   THR A 144      30.702   1.418  22.343  1.00 37.80           C  
ANISOU  990  C   THR A 144     4127   6017   4218   -636   -655   -145       C  
ATOM    991  O   THR A 144      30.767   1.107  23.537  1.00 35.44           O  
ANISOU  991  O   THR A 144     3887   5654   3925   -604   -763   -207       O  
ATOM    992  CB  THR A 144      31.878   3.343  21.302  1.00 44.07           C  
ANISOU  992  CB  THR A 144     4713   6991   5040  -1141   -782    179       C  
ATOM    993  OG1 THR A 144      33.133   3.782  20.764  1.00 45.13           O  
ANISOU  993  OG1 THR A 144     4519   7462   5166  -1379   -809    440       O  
ATOM    994  CG2 THR A 144      31.575   4.106  22.577  1.00 49.99           C  
ANISOU  994  CG2 THR A 144     5738   7440   5816  -1296  -1027     96       C  
ATOM    995  N   LEU A 145      29.571   1.389  21.646  1.00 34.17           N  
ANISOU  995  N   LEU A 145     3845   5407   3730   -553   -552   -232       N  
ATOM    996  CA  LEU A 145      28.307   1.044  22.279  1.00 31.40           C  
ANISOU  996  CA  LEU A 145     3732   4842   3357   -434   -556   -386       C  
ATOM    997  C   LEU A 145      28.302  -0.402  22.776  1.00 37.48           C  
ANISOU  997  C   LEU A 145     4497   5656   4089   -234   -511   -452       C  
ATOM    998  O   LEU A 145      27.857  -0.681  23.898  1.00 38.58           O  
ANISOU  998  O   LEU A 145     4752   5701   4207   -207   -584   -523       O  
ATOM    999  CB  LEU A 145      27.130   1.306  21.344  1.00 33.60           C  
ANISOU  999  CB  LEU A 145     4141   5015   3612   -408   -475   -413       C  
ATOM   1000  CG  LEU A 145      25.770   1.014  21.981  1.00 39.41           C  
ANISOU 1000  CG  LEU A 145     5047   5616   4313   -304   -475   -520       C  
ATOM   1001  CD1 LEU A 145      25.620   1.774  23.291  1.00 40.65           C  
ANISOU 1001  CD1 LEU A 145     5319   5656   4470   -331   -591   -584       C  
ATOM   1002  CD2 LEU A 145      24.636   1.361  21.033  1.00 40.83           C  
ANISOU 1002  CD2 LEU A 145     5298   5739   4475   -290   -423   -502       C  
ATOM   1003  N   LEU A 146      28.811  -1.315  21.954  1.00 31.28           N  
ANISOU 1003  N   LEU A 146     3609   5007   3269    -83   -399   -427       N  
ATOM   1004  CA  LEU A 146      28.896  -2.716  22.355  1.00 32.83           C  
ANISOU 1004  CA  LEU A 146     3867   5188   3421    128   -393   -484       C  
ATOM   1005  C   LEU A 146      29.702  -2.866  23.652  1.00 34.31           C  
ANISOU 1005  C   LEU A 146     3958   5429   3649    131   -523   -451       C  
ATOM   1006  O   LEU A 146      29.315  -3.620  24.544  1.00 34.58           O  
ANISOU 1006  O   LEU A 146     4136   5351   3652    194   -597   -502       O  
ATOM   1007  CB  LEU A 146      29.511  -3.563  21.236  1.00 32.90           C  
ANISOU 1007  CB  LEU A 146     3815   5326   3360    351   -257   -477       C  
ATOM   1008  CG  LEU A 146      28.544  -3.914  20.109  1.00 33.18           C  
ANISOU 1008  CG  LEU A 146     4063   5244   3298    382   -169   -544       C  
ATOM   1009  CD1 LEU A 146      29.288  -4.384  18.867  1.00 29.06           C  
ANISOU 1009  CD1 LEU A 146     3485   4891   2668    590    -13   -541       C  
ATOM   1010  CD2 LEU A 146      27.565  -4.980  20.575  1.00 34.59           C  
ANISOU 1010  CD2 LEU A 146     4530   5191   3420    428   -253   -628       C  
ATOM   1011  N   SER A 147      30.801  -2.130  23.770  1.00 36.31           N  
ANISOU 1011  N   SER A 147     3970   5869   3958     20   -577   -338       N  
ATOM   1012  CA  SER A 147      31.669  -2.260  24.945  1.00 38.98           C  
ANISOU 1012  CA  SER A 147     4189   6296   4326     -3   -733   -275       C  
ATOM   1013  C   SER A 147      30.982  -1.841  26.248  1.00 43.49           C  
ANISOU 1013  C   SER A 147     4987   6663   4874   -157   -886   -354       C  
ATOM   1014  O   SER A 147      31.412  -2.243  27.334  1.00 43.57           O  
ANISOU 1014  O   SER A 147     4993   6693   4867   -146  -1020   -334       O  
ATOM   1015  CB  SER A 147      32.976  -1.490  24.762  1.00 45.84           C  
ANISOU 1015  CB  SER A 147     4723   7448   5245   -163   -793    -90       C  
ATOM   1016  OG  SER A 147      32.800  -0.109  25.004  1.00 52.25           O  
ANISOU 1016  OG  SER A 147     5620   8154   6078   -503   -924    -60       O  
ATOM   1017  N   LEU A 148      29.924  -1.040  26.134  1.00 42.09           N  
ANISOU 1017  N   LEU A 148     5009   6310   4675   -268   -861   -439       N  
ATOM   1018  CA  LEU A 148      29.121  -0.630  27.288  1.00 41.66           C  
ANISOU 1018  CA  LEU A 148     5188   6090   4550   -337   -952   -538       C  
ATOM   1019  C   LEU A 148      28.014  -1.637  27.587  1.00 40.79           C  
ANISOU 1019  C   LEU A 148     5224   5912   4362   -194   -871   -612       C  
ATOM   1020  O   LEU A 148      27.832  -2.066  28.731  1.00 41.52           O  
ANISOU 1020  O   LEU A 148     5416   5987   4373   -187   -946   -636       O  
ATOM   1021  CB  LEU A 148      28.496   0.752  27.055  1.00 41.44           C  
ANISOU 1021  CB  LEU A 148     5311   5917   4518   -460   -966   -589       C  
ATOM   1022  CG  LEU A 148      27.493   1.198  28.128  1.00 45.09           C  
ANISOU 1022  CG  LEU A 148     6038   6229   4866   -429  -1003   -722       C  
ATOM   1023  CD1 LEU A 148      28.156   1.344  29.498  1.00 43.81           C  
ANISOU 1023  CD1 LEU A 148     5967   6056   4624   -526  -1188   -742       C  
ATOM   1024  CD2 LEU A 148      26.782   2.492  27.742  1.00 51.11           C  
ANISOU 1024  CD2 LEU A 148     6978   6822   5620   -445  -1000   -783       C  
ATOM   1025  N   VAL A 149      27.275  -2.003  26.545  1.00 34.42           N  
ANISOU 1025  N   VAL A 149     4435   5082   3562   -118   -736   -623       N  
ATOM   1026  CA  VAL A 149      26.139  -2.915  26.658  1.00 34.60           C  
ANISOU 1026  CA  VAL A 149     4589   5055   3503    -59   -687   -647       C  
ATOM   1027  C   VAL A 149      26.534  -4.260  27.277  1.00 43.81           C  
ANISOU 1027  C   VAL A 149     5805   6216   4627     15   -763   -613       C  
ATOM   1028  O   VAL A 149      25.775  -4.846  28.063  1.00 40.99           O  
ANISOU 1028  O   VAL A 149     5572   5829   4171    -22   -802   -602       O  
ATOM   1029  CB  VAL A 149      25.469  -3.117  25.289  1.00 36.53           C  
ANISOU 1029  CB  VAL A 149     4846   5278   3756    -33   -578   -638       C  
ATOM   1030  CG1 VAL A 149      24.448  -4.268  25.329  1.00 37.53           C  
ANISOU 1030  CG1 VAL A 149     5111   5361   3790    -35   -583   -616       C  
ATOM   1031  CG2 VAL A 149      24.805  -1.832  24.863  1.00 34.69           C  
ANISOU 1031  CG2 VAL A 149     4604   5029   3547    -96   -531   -653       C  
ATOM   1032  N   ARG A 150      27.734  -4.730  26.945  1.00 39.44           N  
ANISOU 1032  N   ARG A 150     5143   5710   4133    129   -789   -576       N  
ATOM   1033  CA  ARG A 150      28.213  -6.001  27.474  1.00 40.59           C  
ANISOU 1033  CA  ARG A 150     5358   5818   4247    262   -883   -539       C  
ATOM   1034  C   ARG A 150      28.378  -5.964  28.995  1.00 42.90           C  
ANISOU 1034  C   ARG A 150     5681   6127   4492    173  -1029   -508       C  
ATOM   1035  O   ARG A 150      28.298  -6.999  29.657  1.00 41.03           O  
ANISOU 1035  O   ARG A 150     5583   5817   4189    217  -1130   -465       O  
ATOM   1036  CB  ARG A 150      29.521  -6.413  26.794  1.00 41.73           C  
ANISOU 1036  CB  ARG A 150     5335   6065   4455    483   -860   -501       C  
ATOM   1037  CG  ARG A 150      29.332  -6.675  25.301  1.00 44.65           C  
ANISOU 1037  CG  ARG A 150     5744   6414   4807    609   -709   -547       C  
ATOM   1038  CD  ARG A 150      30.389  -7.589  24.715  1.00 49.34           C  
ANISOU 1038  CD  ARG A 150     6285   7076   5387    944   -670   -537       C  
ATOM   1039  NE  ARG A 150      30.080  -7.908  23.321  1.00 54.90           N  
ANISOU 1039  NE  ARG A 150     7116   7730   6013   1071   -529   -610       N  
ATOM   1040  CZ  ARG A 150      30.696  -7.373  22.268  1.00 59.78           C  
ANISOU 1040  CZ  ARG A 150     7520   8567   6627   1154   -366   -594       C  
ATOM   1041  NH1 ARG A 150      31.676  -6.490  22.443  1.00 60.40           N  
ANISOU 1041  NH1 ARG A 150     7220   8940   6791   1093   -338   -481       N  
ATOM   1042  NH2 ARG A 150      30.338  -7.727  21.036  1.00 57.07           N  
ANISOU 1042  NH2 ARG A 150     7352   8162   6170   1265   -249   -672       N  
ATOM   1043  N   GLN A 151      28.594  -4.773  29.545  1.00 39.84           N  
ANISOU 1043  N   GLN A 151     5212   5811   4114     33  -1064   -526       N  
ATOM   1044  CA  GLN A 151      28.791  -4.636  30.985  1.00 42.55           C  
ANISOU 1044  CA  GLN A 151     5621   6173   4373    -63  -1214   -512       C  
ATOM   1045  C   GLN A 151      27.504  -4.848  31.783  1.00 44.87           C  
ANISOU 1045  C   GLN A 151     6122   6420   4505   -130  -1187   -550       C  
ATOM   1046  O   GLN A 151      27.552  -5.042  32.992  1.00 42.42           O  
ANISOU 1046  O   GLN A 151     5881   6136   4100   -194  -1260   -514       O  
ATOM   1047  CB  GLN A 151      29.429  -3.290  31.315  1.00 41.61           C  
ANISOU 1047  CB  GLN A 151     5427   6105   4276   -214  -1298   -528       C  
ATOM   1048  CG  GLN A 151      30.806  -3.116  30.696  1.00 42.44           C  
ANISOU 1048  CG  GLN A 151     5258   6350   4516   -209  -1353   -420       C  
ATOM   1049  CD  GLN A 151      31.401  -1.748  30.942  1.00 42.66           C  
ANISOU 1049  CD  GLN A 151     5242   6410   4558   -450  -1484   -395       C  
ATOM   1050  OE1 GLN A 151      31.470  -1.283  32.079  1.00 41.81           O  
ANISOU 1050  OE1 GLN A 151     5285   6249   4350   -597  -1654   -423       O  
ATOM   1051  NE2 GLN A 151      31.838  -1.092  29.867  1.00 40.48           N  
ANISOU 1051  NE2 GLN A 151     4790   6209   4380   -518  -1426   -333       N  
ATOM   1052  N   TYR A 152      26.356  -4.812  31.107  1.00 43.32           N  
ANISOU 1052  N   TYR A 152     5973   6199   4288   -129  -1042   -582       N  
ATOM   1053  CA  TYR A 152      25.072  -5.123  31.757  1.00 45.96           C  
ANISOU 1053  CA  TYR A 152     6396   6579   4486   -202   -963   -549       C  
ATOM   1054  C   TYR A 152      24.739  -6.622  31.685  1.00 41.51           C  
ANISOU 1054  C   TYR A 152     5916   5964   3890   -212  -1013   -439       C  
ATOM   1055  O   TYR A 152      23.619  -7.037  32.002  1.00 44.73           O  
ANISOU 1055  O   TYR A 152     6363   6425   4209   -285   -961   -368       O  
ATOM   1056  CB  TYR A 152      23.934  -4.256  31.183  1.00 42.72           C  
ANISOU 1056  CB  TYR A 152     5984   6186   4063   -196   -818   -595       C  
ATOM   1057  CG  TYR A 152      24.065  -2.811  31.602  1.00 42.73           C  
ANISOU 1057  CG  TYR A 152     6004   6174   4056   -175   -788   -696       C  
ATOM   1058  CD1 TYR A 152      23.449  -2.346  32.762  1.00 39.32           C  
ANISOU 1058  CD1 TYR A 152     5678   5794   3467   -165   -747   -726       C  
ATOM   1059  CD2 TYR A 152      24.843  -1.922  30.866  1.00 42.70           C  
ANISOU 1059  CD2 TYR A 152     5950   6101   4173   -168   -825   -761       C  
ATOM   1060  CE1 TYR A 152      23.587  -1.037  33.167  1.00 41.24           C  
ANISOU 1060  CE1 TYR A 152     6008   5988   3674   -135   -739   -845       C  
ATOM   1061  CE2 TYR A 152      24.984  -0.608  31.260  1.00 40.51           C  
ANISOU 1061  CE2 TYR A 152     5764   5756   3873   -185   -852   -847       C  
ATOM   1062  CZ  TYR A 152      24.350  -0.171  32.415  1.00 45.00           C  
ANISOU 1062  CZ  TYR A 152     6468   6342   4287   -153   -807   -903       C  
ATOM   1063  OH  TYR A 152      24.485   1.135  32.828  1.00 46.03           O  
ANISOU 1063  OH  TYR A 152     6747   6361   4382   -136   -846  -1013       O  
ATOM   1064  N   ASN A 153      25.742  -7.408  31.296  1.00 63.94           N  
ANISOU 1064  N   ASN A 153     9290   9908   5097    505  -2450    561       N  
ATOM   1065  CA  ASN A 153      25.635  -8.857  31.123  1.00 59.88           C  
ANISOU 1065  CA  ASN A 153     8810   9296   4644    701  -2406    748       C  
ATOM   1066  C   ASN A 153      24.318  -9.370  30.527  1.00 54.75           C  
ANISOU 1066  C   ASN A 153     8312   8461   4030    749  -2112    786       C  
ATOM   1067  O   ASN A 153      23.514 -10.016  31.200  1.00 56.46           O  
ANISOU 1067  O   ASN A 153     8773   8573   4104    796  -1972    899       O  
ATOM   1068  CB  ASN A 153      26.010  -9.585  32.410  1.00 64.90           C  
ANISOU 1068  CB  ASN A 153     9600   9971   5090    793  -2539    895       C  
ATOM   1069  CG  ASN A 153      27.491  -9.428  32.749  1.00 71.94           C  
ANISOU 1069  CG  ASN A 153    10265  11054   6014    793  -2863    910       C  
ATOM   1070  OD1 ASN A 153      28.359  -9.668  31.906  1.00 71.94           O  
ANISOU 1070  OD1 ASN A 153     9976  11103   6255    853  -2979    935       O  
ATOM   1071  ND2 ASN A 153      27.784  -9.002  33.978  1.00 77.57           N  
ANISOU 1071  ND2 ASN A 153    11100  11884   6489    731  -3004    894       N  
ATOM   1072  N   PRO A 154      24.094  -9.060  29.249  1.00 46.22           N  
ANISOU 1072  N   PRO A 154     7072   7347   3141    726  -2015    696       N  
ATOM   1073  CA  PRO A 154      22.950  -9.608  28.517  1.00 44.35           C  
ANISOU 1073  CA  PRO A 154     6935   6951   2967    773  -1766    741       C  
ATOM   1074  C   PRO A 154      23.184 -11.084  28.238  1.00 43.88           C  
ANISOU 1074  C   PRO A 154     6876   6793   3003    968  -1781    910       C  
ATOM   1075  O   PRO A 154      24.318 -11.544  28.327  1.00 49.94           O  
ANISOU 1075  O   PRO A 154     7500   7636   3840   1083  -1977    963       O  
ATOM   1076  CB  PRO A 154      22.999  -8.844  27.195  1.00 43.82           C  
ANISOU 1076  CB  PRO A 154     6610   6905   3133    680  -1693    589       C  
ATOM   1077  CG  PRO A 154      24.455  -8.526  27.034  1.00 42.45           C  
ANISOU 1077  CG  PRO A 154     6182   6906   3040    709  -1958    542       C  
ATOM   1078  CD  PRO A 154      24.935  -8.201  28.397  1.00 45.42           C  
ANISOU 1078  CD  PRO A 154     6678   7365   3215    649  -2138    559       C  
ATOM   1079  N   LYS A 155      22.122 -11.807  27.899  1.00 48.24           N  
ANISOU 1079  N   LYS A 155     7565   7161   3602    977  -1556    992       N  
ATOM   1080  CA  LYS A 155      22.240 -13.197  27.492  1.00 52.73           C  
ANISOU 1080  CA  LYS A 155     8158   7581   4297   1136  -1540   1132       C  
ATOM   1081  C   LYS A 155      22.903 -13.213  26.119  1.00 48.86           C  
ANISOU 1081  C   LYS A 155     7372   7106   4087   1185  -1555   1032       C  
ATOM   1082  O   LYS A 155      23.766 -14.039  25.821  1.00 51.53           O  
ANISOU 1082  O   LYS A 155     7626   7430   4521   1378  -1667   1099       O  
ATOM   1083  CB  LYS A 155      20.844 -13.816  27.410  1.00 59.69           C  
ANISOU 1083  CB  LYS A 155     9235   8248   5198   1056  -1279   1221       C  
ATOM   1084  CG  LYS A 155      20.794 -15.331  27.270  1.00 67.43           C  
ANISOU 1084  CG  LYS A 155    10347   9019   6254   1194  -1260   1392       C  
ATOM   1085  CD  LYS A 155      19.755 -15.912  28.229  1.00 72.51           C  
ANISOU 1085  CD  LYS A 155    11297   9527   6726   1138  -1115   1570       C  
ATOM   1086  CE  LYS A 155      19.507 -17.394  27.984  1.00 75.52           C  
ANISOU 1086  CE  LYS A 155    11832   9646   7214   1222  -1062   1738       C  
ATOM   1087  NZ  LYS A 155      18.843 -17.627  26.670  1.00 74.59           N  
ANISOU 1087  NZ  LYS A 155    11600   9372   7369   1111   -913   1651       N  
ATOM   1088  N   MET A 156      22.492 -12.262  25.292  1.00 41.91           N  
ANISOU 1088  N   MET A 156     6342   6257   3325   1023  -1431    874       N  
ATOM   1089  CA  MET A 156      22.893 -12.213  23.899  1.00 40.64           C  
ANISOU 1089  CA  MET A 156     5938   6094   3408   1044  -1386    777       C  
ATOM   1090  C   MET A 156      22.803 -10.747  23.456  1.00 42.92           C  
ANISOU 1090  C   MET A 156     6066   6505   3738    857  -1343    609       C  
ATOM   1091  O   MET A 156      21.939 -10.009  23.942  1.00 41.24           O  
ANISOU 1091  O   MET A 156     5976   6283   3411    709  -1255    567       O  
ATOM   1092  CB  MET A 156      21.926 -13.087  23.088  1.00 43.14           C  
ANISOU 1092  CB  MET A 156     6358   6180   3851   1039  -1192    811       C  
ATOM   1093  CG  MET A 156      22.048 -12.977  21.593  1.00 44.49           C  
ANISOU 1093  CG  MET A 156     6345   6323   4234   1034  -1108    695       C  
ATOM   1094  SD  MET A 156      20.578 -13.602  20.721  1.00 54.41           S  
ANISOU 1094  SD  MET A 156     7747   7326   5601    925   -897    693       S  
ATOM   1095  CE  MET A 156      20.441 -15.256  21.417  1.00 40.68           C  
ANISOU 1095  CE  MET A 156     6278   5369   3811   1066   -928    886       C  
ATOM   1096  N   VAL A 157      23.703 -10.322  22.564  1.00 39.46           N  
ANISOU 1096  N   VAL A 157     5362   6175   3456    875  -1394    523       N  
ATOM   1097  CA  VAL A 157      23.621  -9.001  21.934  1.00 35.38           C  
ANISOU 1097  CA  VAL A 157     4696   5736   3010    698  -1332    376       C  
ATOM   1098  C   VAL A 157      23.711  -9.162  20.431  1.00 34.38           C  
ANISOU 1098  C   VAL A 157     4406   5566   3092    729  -1205    323       C  
ATOM   1099  O   VAL A 157      24.623  -9.826  19.939  1.00 39.10           O  
ANISOU 1099  O   VAL A 157     4864   6202   3792    892  -1255    360       O  
ATOM   1100  CB  VAL A 157      24.784  -8.072  22.316  1.00 41.07           C  
ANISOU 1100  CB  VAL A 157     5231   6664   3710    643  -1530    318       C  
ATOM   1101  CG1 VAL A 157      24.452  -6.632  21.908  1.00 39.14           C  
ANISOU 1101  CG1 VAL A 157     4928   6447   3495    427  -1453    177       C  
ATOM   1102  CG2 VAL A 157      25.057  -8.124  23.756  1.00 45.83           C  
ANISOU 1102  CG2 VAL A 157     5980   7335   4098    664  -1723    378       C  
ATOM   1103  N   LYS A 158      22.772  -8.552  19.711  1.00 30.40           N  
ANISOU 1103  N   LYS A 158     3926   4986   2639    590  -1041    242       N  
ATOM   1104  CA  LYS A 158      22.785  -8.533  18.261  1.00 29.14           C  
ANISOU 1104  CA  LYS A 158     3640   4791   2639    598   -924    180       C  
ATOM   1105  C   LYS A 158      22.617  -7.091  17.852  1.00 31.00           C  
ANISOU 1105  C   LYS A 158     3781   5097   2901    418   -871     74       C  
ATOM   1106  O   LYS A 158      22.030  -6.300  18.594  1.00 31.33           O  
ANISOU 1106  O   LYS A 158     3923   5140   2842    293   -872     45       O  
ATOM   1107  CB  LYS A 158      21.618  -9.340  17.689  1.00 32.68           C  
ANISOU 1107  CB  LYS A 158     4252   5041   3124    604   -786    202       C  
ATOM   1108  CG  LYS A 158      21.647 -10.822  18.021  1.00 36.87           C  
ANISOU 1108  CG  LYS A 158     4926   5444   3640    764   -821    311       C  
ATOM   1109  CD  LYS A 158      22.869 -11.508  17.434  1.00 45.04           C  
ANISOU 1109  CD  LYS A 158     5838   6514   4759    971   -875    321       C  
ATOM   1110  CE  LYS A 158      22.811 -13.011  17.683  1.00 47.96           C  
ANISOU 1110  CE  LYS A 158     6394   6706   5120   1144   -898    426       C  
ATOM   1111  NZ  LYS A 158      24.085 -13.669  17.317  1.00 47.29           N  
ANISOU 1111  NZ  LYS A 158     6193   6670   5107   1393   -957    450       N  
ATOM   1112  N   VAL A 159      23.130  -6.750  16.677  1.00 27.40           N  
ANISOU 1112  N   VAL A 159     3154   4689   2570    418   -812     20       N  
ATOM   1113  CA  VAL A 159      22.976  -5.401  16.145  1.00 26.35           C  
ANISOU 1113  CA  VAL A 159     2943   4595   2471    251   -748    -66       C  
ATOM   1114  C   VAL A 159      22.286  -5.441  14.792  1.00 26.09           C  
ANISOU 1114  C   VAL A 159     2931   4465   2517    245   -589   -101       C  
ATOM   1115  O   VAL A 159      22.710  -6.160  13.889  1.00 30.21           O  
ANISOU 1115  O   VAL A 159     3394   4976   3107    367   -543    -91       O  
ATOM   1116  CB  VAL A 159      24.346  -4.700  15.997  1.00 27.67           C  
ANISOU 1116  CB  VAL A 159     2869   4937   2709    215   -832    -86       C  
ATOM   1117  CG1 VAL A 159      24.199  -3.327  15.322  1.00 28.04           C  
ANISOU 1117  CG1 VAL A 159     2857   4993   2805     35   -750   -162       C  
ATOM   1118  CG2 VAL A 159      25.006  -4.566  17.352  1.00 29.47           C  
ANISOU 1118  CG2 VAL A 159     3080   5269   2848    194  -1033    -61       C  
ATOM   1119  N   ALA A 160      21.206  -4.664  14.668  1.00 26.46           N  
ANISOU 1119  N   ALA A 160     3071   4439   2542    118   -510   -141       N  
ATOM   1120  CA  ALA A 160      20.547  -4.424  13.398  1.00 25.25           C  
ANISOU 1120  CA  ALA A 160     2928   4216   2451     86   -391   -177       C  
ATOM   1121  C   ALA A 160      20.865  -2.999  12.946  1.00 25.28           C  
ANISOU 1121  C   ALA A 160     2836   4283   2485    -36   -356   -230       C  
ATOM   1122  O   ALA A 160      20.638  -2.053  13.685  1.00 26.37           O  
ANISOU 1122  O   ALA A 160     3014   4427   2579   -144   -382   -257       O  
ATOM   1123  CB  ALA A 160      19.043  -4.611  13.536  1.00 22.00           C  
ANISOU 1123  CB  ALA A 160     2669   3676   2014     43   -334   -162       C  
ATOM   1124  N   SER A 161      21.374  -2.839  11.730  1.00 23.59           N  
ANISOU 1124  N   SER A 161     2524   4103   2336    -18   -287   -243       N  
ATOM   1125  CA  SER A 161      21.627  -1.501  11.202  1.00 23.23           C  
ANISOU 1125  CA  SER A 161     2408   4095   2324   -145   -237   -273       C  
ATOM   1126  C   SER A 161      20.937  -1.388   9.879  1.00 26.29           C  
ANISOU 1126  C   SER A 161     2857   4409   2725   -135   -124   -282       C  
ATOM   1127  O   SER A 161      21.074  -2.278   9.035  1.00 24.14           O  
ANISOU 1127  O   SER A 161     2589   4127   2456    -20    -80   -274       O  
ATOM   1128  CB  SER A 161      23.128  -1.250  11.038  1.00 28.63           C  
ANISOU 1128  CB  SER A 161     2881   4925   3072   -155   -259   -258       C  
ATOM   1129  OG  SER A 161      23.385   0.076  10.611  1.00 26.62           O  
ANISOU 1129  OG  SER A 161     2569   4689   2857   -311   -211   -274       O  
ATOM   1130  N   LEU A 162      20.173  -0.312   9.699  1.00 22.74           N  
ANISOU 1130  N   LEU A 162     2475   3896   2267   -240    -84   -299       N  
ATOM   1131  CA  LEU A 162      19.447  -0.104   8.446  1.00 23.76           C  
ANISOU 1131  CA  LEU A 162     2672   3959   2396   -231     -2   -296       C  
ATOM   1132  C   LEU A 162      20.440  -0.047   7.296  1.00 22.85           C  
ANISOU 1132  C   LEU A 162     2469   3917   2296   -201     77   -283       C  
ATOM   1133  O   LEU A 162      20.250  -0.680   6.255  1.00 25.75           O  
ANISOU 1133  O   LEU A 162     2892   4260   2632   -111    127   -284       O  
ATOM   1134  CB  LEU A 162      18.660   1.211   8.483  1.00 25.38           C  
ANISOU 1134  CB  LEU A 162     2946   4095   2601   -334     27   -302       C  
ATOM   1135  CG  LEU A 162      18.029   1.540   7.119  1.00 26.52           C  
ANISOU 1135  CG  LEU A 162     3151   4187   2737   -319     92   -283       C  
ATOM   1136  CD1 LEU A 162      16.947   0.530   6.750  1.00 24.81           C  
ANISOU 1136  CD1 LEU A 162     3009   3913   2503   -241     59   -278       C  
ATOM   1137  CD2 LEU A 162      17.479   2.958   7.113  1.00 25.51           C  
ANISOU 1137  CD2 LEU A 162     3082   3989   2620   -402    125   -275       C  
ATOM   1138  N   LEU A 163      21.510   0.719   7.492  1.00 22.11           N  
ANISOU 1138  N   LEU A 163     2242   3912   2247   -285     90   -271       N  
ATOM   1139  CA  LEU A 163      22.512   0.884   6.444  1.00 24.22           C  
ANISOU 1139  CA  LEU A 163     2394   4267   2540   -271    198   -238       C  
ATOM   1140  C   LEU A 163      23.893   0.503   6.939  1.00 26.13           C  
ANISOU 1140  C   LEU A 163     2421   4658   2849   -243    171   -215       C  
ATOM   1141  O   LEU A 163      24.215   0.684   8.111  1.00 26.30           O  
ANISOU 1141  O   LEU A 163     2375   4716   2901   -314     49   -224       O  
ATOM   1142  CB  LEU A 163      22.555   2.334   5.978  1.00 23.99           C  
ANISOU 1142  CB  LEU A 163     2371   4213   2532   -427    266   -213       C  
ATOM   1143  CG  LEU A 163      21.230   2.966   5.551  1.00 27.47           C  
ANISOU 1143  CG  LEU A 163     3004   4512   2921   -454    281   -219       C  
ATOM   1144  CD1 LEU A 163      21.420   4.456   5.289  1.00 28.57           C  
ANISOU 1144  CD1 LEU A 163     3158   4606   3092   -608    337   -185       C  
ATOM   1145  CD2 LEU A 163      20.650   2.275   4.314  1.00 25.68           C  
ANISOU 1145  CD2 LEU A 163     2882   4257   2619   -328    340   -209       C  
ATOM   1146  N   VAL A 164      24.709  -0.014   6.022  1.00 25.42           N  
ANISOU 1146  N   VAL A 164     2226   4658   2774   -130    285   -182       N  
ATOM   1147  CA  VAL A 164      26.137  -0.241   6.257  1.00 27.43           C  
ANISOU 1147  CA  VAL A 164     2217   5085   3120    -94    293   -136       C  
ATOM   1148  C   VAL A 164      26.878   0.300   5.053  1.00 28.91           C  
ANISOU 1148  C   VAL A 164     2287   5362   3338   -116    485    -78       C  
ATOM   1149  O   VAL A 164      26.579  -0.076   3.917  1.00 28.83           O  
ANISOU 1149  O   VAL A 164     2399   5311   3243      4    625    -81       O  
ATOM   1150  CB  VAL A 164      26.483  -1.735   6.406  1.00 28.01           C  
ANISOU 1150  CB  VAL A 164     2263   5194   3184    146    273   -138       C  
ATOM   1151  CG1 VAL A 164      27.997  -1.921   6.474  1.00 30.51           C  
ANISOU 1151  CG1 VAL A 164     2269   5712   3611    216    305    -72       C  
ATOM   1152  CG2 VAL A 164      25.807  -2.310   7.641  1.00 26.87           C  
ANISOU 1152  CG2 VAL A 164     2239   4965   3006    163     94   -171       C  
ATOM   1153  N   LYS A 165      27.833   1.188   5.294  1.00 30.54           N  
ANISOU 1153  N   LYS A 165     2266   5684   3656   -281    489    -22       N  
ATOM   1154  CA  LYS A 165      28.599   1.787   4.213  1.00 32.64           C  
ANISOU 1154  CA  LYS A 165     2394   6043   3965   -333    692     59       C  
ATOM   1155  C   LYS A 165      29.769   0.914   3.836  1.00 39.41           C  
ANISOU 1155  C   LYS A 165     3000   7088   4885   -144    809    117       C  
ATOM   1156  O   LYS A 165      30.469   0.388   4.715  1.00 36.03           O  
ANISOU 1156  O   LYS A 165     2365   6774   4550    -88    686    127       O  
ATOM   1157  CB  LYS A 165      29.129   3.159   4.615  1.00 40.03           C  
ANISOU 1157  CB  LYS A 165     3186   7009   5017   -625    649    106       C  
ATOM   1158  CG  LYS A 165      28.123   4.286   4.521  1.00 42.69           C  
ANISOU 1158  CG  LYS A 165     3776   7152   5294   -801    631     78       C  
ATOM   1159  CD  LYS A 165      28.830   5.592   4.135  1.00 43.52           C  
ANISOU 1159  CD  LYS A 165     3760   7278   5499  -1051    722    165       C  
ATOM   1160  CE  LYS A 165      27.829   6.718   4.163  1.00 39.09           C  
ANISOU 1160  CE  LYS A 165     3472   6497   4883  -1204    686    135       C  
ATOM   1161  NZ  LYS A 165      28.438   8.055   4.224  1.00 35.03           N  
ANISOU 1161  NZ  LYS A 165     2884   5946   4482  -1493    698    195       N  
ATOM   1162  N   ARG A 166      29.991   0.772   2.529  1.00 38.92           N  
ANISOU 1162  N   ARG A 166     2963   7062   4762    -29   1052    159       N  
ATOM   1163  CA  ARG A 166      31.211   0.162   2.026  1.00 44.24           C  
ANISOU 1163  CA  ARG A 166     3373   7932   5504    149   1229    233       C  
ATOM   1164  C   ARG A 166      32.330   1.178   2.076  1.00 50.28           C  
ANISOU 1164  C   ARG A 166     3789   8872   6444    -69   1298    353       C  
ATOM   1165  O   ARG A 166      32.350   2.145   1.312  1.00 53.45           O  
ANISOU 1165  O   ARG A 166     4217   9258   6833   -233   1453    418       O  
ATOM   1166  CB  ARG A 166      31.041  -0.304   0.582  1.00 43.64           C  
ANISOU 1166  CB  ARG A 166     3482   7829   5271    351   1487    232       C  
ATOM   1167  CG  ARG A 166      30.252  -1.582   0.439  1.00 40.39           C  
ANISOU 1167  CG  ARG A 166     3359   7277   4711    604   1434    119       C  
ATOM   1168  CD  ARG A 166      30.468  -2.167  -0.954  1.00 45.33           C  
ANISOU 1168  CD  ARG A 166     4116   7919   5188    841   1701    117       C  
ATOM   1169  NE  ARG A 166      30.036  -1.226  -1.979  1.00 39.17           N  
ANISOU 1169  NE  ARG A 166     3505   7093   4286    707   1837    152       N  
ATOM   1170  CZ  ARG A 166      28.764  -0.983  -2.271  1.00 36.98           C  
ANISOU 1170  CZ  ARG A 166     3557   6628   3866    629   1730     85       C  
ATOM   1171  NH1 ARG A 166      27.806  -1.620  -1.617  1.00 34.75           N  
ANISOU 1171  NH1 ARG A 166     3451   6195   3558    657   1502    -20       N  
ATOM   1172  NH2 ARG A 166      28.452  -0.114  -3.222  1.00 45.44           N  
ANISOU 1172  NH2 ARG A 166     4773   7667   4824    528   1851    136       N  
ATOM   1173  N   THR A 167      33.270   0.964   2.978  1.00 53.89           N  
ANISOU 1173  N   THR A 167     3915   9492   7067    -81   1173    392       N  
ATOM   1174  CA  THR A 167      34.372   1.889   3.090  1.00 61.36           C  
ANISOU 1174  CA  THR A 167     4557  10547   8211   -311   1186    495       C  
ATOM   1175  C   THR A 167      35.630   1.116   3.456  1.00 67.97           C  
ANISOU 1175  C   THR A 167     5087  11530   9210   -143   1152    544       C  
ATOM   1176  O   THR A 167      35.583   0.200   4.279  1.00 68.48           O  
ANISOU 1176  O   THR A 167     5122  11632   9266     27    978    500       O  
ATOM   1177  CB  THR A 167      34.043   3.030   4.104  1.00 64.29           C  
ANISOU 1177  CB  THR A 167     4940  10847   8639   -665    938    466       C  
ATOM   1178  OG1 THR A 167      35.081   4.016   4.094  1.00 60.12           O  
ANISOU 1178  OG1 THR A 167     4196  10343   8304   -907    947    552       O  
ATOM   1179  CG2 THR A 167      33.853   2.489   5.519  1.00 62.71           C  
ANISOU 1179  CG2 THR A 167     4720  10665   8441   -635    628    386       C  
ATOM   1180  N   PRO A 168      36.756   1.454   2.810  1.00 74.81           N  
ANISOU 1180  N   PRO A 168     5728  12477  10220   -178   1331    638       N  
ATOM   1181  CA  PRO A 168      38.057   0.945   3.255  1.00 80.25           C  
ANISOU 1181  CA  PRO A 168     6069  13319  11102    -78   1276    692       C  
ATOM   1182  C   PRO A 168      38.340   1.429   4.679  1.00 83.00           C  
ANISOU 1182  C   PRO A 168     6254  13697  11585   -308    926    681       C  
ATOM   1183  O   PRO A 168      39.174   0.853   5.381  1.00 84.16           O  
ANISOU 1183  O   PRO A 168     6161  13960  11858   -205    779    704       O  
ATOM   1184  CB  PRO A 168      39.047   1.571   2.257  1.00 83.41           C  
ANISOU 1184  CB  PRO A 168     6277  13789  11627   -170   1543    789       C  
ATOM   1185  CG  PRO A 168      38.300   2.694   1.598  1.00 80.57           C  
ANISOU 1185  CG  PRO A 168     6151  13292  11170   -410   1657    796       C  
ATOM   1186  CD  PRO A 168      36.867   2.264   1.584  1.00 76.96           C  
ANISOU 1186  CD  PRO A 168     6064  12706  10472   -292   1608    701       C  
ATOM   1187  N   ARG A 169      37.622   2.477   5.087  1.00 80.97           N  
ANISOU 1187  N   ARG A 169     6159  13322  11284   -608    790    640       N  
ATOM   1188  CA  ARG A 169      37.713   3.058   6.427  1.00 80.44           C  
ANISOU 1188  CA  ARG A 169     6040  13234  11291   -850    450    598       C  
ATOM   1189  C   ARG A 169      37.097   2.178   7.520  1.00 77.06           C  
ANISOU 1189  C   ARG A 169     5736  12800  10743   -696    196    515       C  
ATOM   1190  O   ARG A 169      37.248   2.468   8.708  1.00 75.38           O  
ANISOU 1190  O   ARG A 169     5497  12579  10565   -845   -100    475       O  
ATOM   1191  CB  ARG A 169      37.039   4.440   6.452  1.00 79.63           C  
ANISOU 1191  CB  ARG A 169     6142  12965  11149  -1194    409    563       C  
ATOM   1192  CG  ARG A 169      37.992   5.627   6.576  1.00 82.91           C  
ANISOU 1192  CG  ARG A 169     6362  13371  11769  -1512    361    615       C  
ATOM   1193  CD  ARG A 169      37.342   6.938   6.120  1.00 81.36           C  
ANISOU 1193  CD  ARG A 169     6402  12982  11529  -1790    443    611       C  
ATOM   1194  NE  ARG A 169      36.492   7.561   7.136  1.00 78.57           N  
ANISOU 1194  NE  ARG A 169     6309  12465  11080  -1981    179    496       N  
ATOM   1195  CZ  ARG A 169      35.172   7.702   7.033  1.00 78.12           C  
ANISOU 1195  CZ  ARG A 169     6589  12265  10829  -1973    202    425       C  
ATOM   1196  NH1 ARG A 169      34.529   7.257   5.959  1.00 75.90           N  
ANISOU 1196  NH1 ARG A 169     6425  11988  10425  -1791    458    458       N  
ATOM   1197  NH2 ARG A 169      34.487   8.288   8.008  1.00 78.34           N  
ANISOU 1197  NH2 ARG A 169     6848  12140  10777  -2140    -28    312       N  
ATOM   1198  N   SER A 170      36.397   1.117   7.124  1.00 77.02           N  
ANISOU 1198  N   SER A 170     5893  12786  10587   -401    309    485       N  
ATOM   1199  CA  SER A 170      35.765   0.219   8.090  1.00 75.31           C  
ANISOU 1199  CA  SER A 170     5811  12552  10251   -238     96    416       C  
ATOM   1200  C   SER A 170      36.803  -0.457   8.974  1.00 77.12           C  
ANISOU 1200  C   SER A 170     5803  12896  10603   -113   -100    463       C  
ATOM   1201  O   SER A 170      37.749  -1.069   8.476  1.00 78.31           O  
ANISOU 1201  O   SER A 170     5734  13150  10870     88     35    538       O  
ATOM   1202  CB  SER A 170      34.916  -0.843   7.387  1.00 73.77           C  
ANISOU 1202  CB  SER A 170     5824  12313   9894     71    274    377       C  
ATOM   1203  OG  SER A 170      34.597  -1.906   8.273  1.00 71.07           O  
ANISOU 1203  OG  SER A 170     5587  11937   9478    278     87    336       O  
ATOM   1204  N   VAL A 171      36.615  -0.345  10.288  1.00 77.07           N  
ANISOU 1204  N   VAL A 171     5862  12865  10558   -222   -416    415       N  
ATOM   1205  CA  VAL A 171      37.514  -0.972  11.259  1.00 80.05           C  
ANISOU 1205  CA  VAL A 171     6054  13338  11024   -109   -646    457       C  
ATOM   1206  C   VAL A 171      37.277  -2.486  11.238  1.00 75.62           C  
ANISOU 1206  C   VAL A 171     5571  12784  10377    286   -602    476       C  
ATOM   1207  O   VAL A 171      37.998  -3.267  11.870  1.00 75.49           O  
ANISOU 1207  O   VAL A 171     5419  12838  10425    467   -746    529       O  
ATOM   1208  CB  VAL A 171      37.328  -0.371  12.682  1.00 88.36           C  
ANISOU 1208  CB  VAL A 171     7220  14335  12019   -342   -999    391       C  
ATOM   1209  CG1 VAL A 171      38.440  -0.817  13.616  1.00 91.70           C  
ANISOU 1209  CG1 VAL A 171     7416  14870  12557   -267  -1246    443       C  
ATOM   1210  CG2 VAL A 171      37.314   1.148  12.615  1.00 87.42           C  
ANISOU 1210  CG2 VAL A 171     7123  14143  11951   -724  -1017    346       C  
ATOM   1211  N   GLY A 172      36.262  -2.890  10.482  1.00 69.75           N  
ANISOU 1211  N   GLY A 172     5059  11953   9489    422   -404    430       N  
ATOM   1212  CA  GLY A 172      36.001  -4.294  10.249  1.00 69.66           C  
ANISOU 1212  CA  GLY A 172     5160  11907   9400    800   -319    436       C  
ATOM   1213  C   GLY A 172      34.777  -4.820  10.967  1.00 68.25           C  
ANISOU 1213  C   GLY A 172     5322  11581   9030    860   -466    361       C  
ATOM   1214  O   GLY A 172      34.461  -6.003  10.838  1.00 67.85           O  
ANISOU 1214  O   GLY A 172     5452  11419   8909   1149   -411    356       O  
ATOM   1215  N   TYR A 173      34.086  -3.959  11.717  1.00 65.29           N  
ANISOU 1215  N   TYR A 173     5126  11111   8571    573   -634    293       N  
ATOM   1216  CA  TYR A 173      32.894  -4.403  12.442  1.00 56.37           C  
ANISOU 1216  CA  TYR A 173     4394   9764   7261    596   -743    222       C  
ATOM   1217  C   TYR A 173      31.699  -4.654  11.517  1.00 53.22           C  
ANISOU 1217  C   TYR A 173     4326   9140   6756    647   -525    148       C  
ATOM   1218  O   TYR A 173      31.380  -3.828  10.662  1.00 48.58           O  
ANISOU 1218  O   TYR A 173     3770   8513   6174    495   -368    110       O  
ATOM   1219  CB  TYR A 173      32.487  -3.446  13.575  1.00 52.69           C  
ANISOU 1219  CB  TYR A 173     4042   9264   6716    308   -971    167       C  
ATOM   1220  CG  TYR A 173      31.163  -3.874  14.159  1.00 46.60           C  
ANISOU 1220  CG  TYR A 173     3678   8270   5759    341  -1008    105       C  
ATOM   1221  CD1 TYR A 173      31.093  -4.935  15.053  1.00 45.05           C  
ANISOU 1221  CD1 TYR A 173     3590   8047   5480    530  -1151    148       C  
ATOM   1222  CD2 TYR A 173      29.973  -3.265  13.763  1.00 41.64           C  
ANISOU 1222  CD2 TYR A 173     3315   7460   5047    198   -883     21       C  
ATOM   1223  CE1 TYR A 173      29.877  -5.365  15.553  1.00 41.80           C  
ANISOU 1223  CE1 TYR A 173     3536   7436   4911    551  -1154    113       C  
ATOM   1224  CE2 TYR A 173      28.756  -3.685  14.263  1.00 37.58           C  
ANISOU 1224  CE2 TYR A 173     3128   6763   4388    230   -895    -18       C  
ATOM   1225  CZ  TYR A 173      28.715  -4.735  15.152  1.00 40.28           C  
ANISOU 1225  CZ  TYR A 173     3566   7084   4654    396  -1021     30       C  
ATOM   1226  OH  TYR A 173      27.499  -5.151  15.642  1.00 45.55           O  
ANISOU 1226  OH  TYR A 173     4545   7574   5188    410  -1010     10       O  
ATOM   1227  N   LYS A 174      31.037  -5.793  11.726  1.00 53.07           N  
ANISOU 1227  N   LYS A 174     4557   8967   6640    849   -536    136       N  
ATOM   1228  CA  LYS A 174      29.872  -6.206  10.946  1.00 48.95           C  
ANISOU 1228  CA  LYS A 174     4352   8225   6020    899   -378     68       C  
ATOM   1229  C   LYS A 174      28.657  -6.437  11.841  1.00 39.40           C  
ANISOU 1229  C   LYS A 174     3451   6833   4684    828   -499     32       C  
ATOM   1230  O   LYS A 174      28.698  -7.269  12.743  1.00 38.31           O  
ANISOU 1230  O   LYS A 174     3381   6667   4506    951   -633     77       O  
ATOM   1231  CB  LYS A 174      30.175  -7.504  10.195  1.00 55.61           C  
ANISOU 1231  CB  LYS A 174     5230   9023   6877   1218   -246     88       C  
ATOM   1232  CG  LYS A 174      30.881  -7.331   8.859  1.00 62.76           C  
ANISOU 1232  CG  LYS A 174     5963  10032   7851   1308    -12     93       C  
ATOM   1233  CD  LYS A 174      32.075  -8.278   8.736  1.00 71.44           C  
ANISOU 1233  CD  LYS A 174     6841  11260   9044   1626     38    169       C  
ATOM   1234  CE  LYS A 174      31.848  -9.618   9.451  1.00 74.90           C  
ANISOU 1234  CE  LYS A 174     7470  11554   9432   1863    -88    186       C  
ATOM   1235  NZ  LYS A 174      30.915 -10.542   8.737  1.00 76.25           N  
ANISOU 1235  NZ  LYS A 174     8023  11458   9491   1998     27    106       N  
ATOM   1236  N   PRO A 175      27.560  -5.714  11.582  1.00 36.46           N  
ANISOU 1236  N   PRO A 175     3266   6339   4247    641   -441    -35       N  
ATOM   1237  CA  PRO A 175      26.360  -5.974  12.382  1.00 29.62           C  
ANISOU 1237  CA  PRO A 175     2670   5312   3273    587   -518    -56       C  
ATOM   1238  C   PRO A 175      25.743  -7.324  11.995  1.00 33.91           C  
ANISOU 1238  C   PRO A 175     3416   5685   3781    772   -458    -49       C  
ATOM   1239  O   PRO A 175      26.179  -7.946  11.021  1.00 36.38           O  
ANISOU 1239  O   PRO A 175     3698   5991   4136    936   -350    -54       O  
ATOM   1240  CB  PRO A 175      25.434  -4.821  11.998  1.00 31.57           C  
ANISOU 1240  CB  PRO A 175     3014   5489   3491    372   -444   -120       C  
ATOM   1241  CG  PRO A 175      25.860  -4.458  10.601  1.00 32.55           C  
ANISOU 1241  CG  PRO A 175     3025   5661   3683    382   -283   -135       C  
ATOM   1242  CD  PRO A 175      27.340  -4.674  10.560  1.00 33.23           C  
ANISOU 1242  CD  PRO A 175     2832   5932   3863    489   -296    -79       C  
ATOM   1243  N   ASP A 176      24.746  -7.764  12.753  1.00 28.48           N  
ANISOU 1243  N   ASP A 176     2947   4859   3015    739   -520    -38       N  
ATOM   1244  CA  ASP A 176      24.135  -9.077  12.561  1.00 31.94           C  
ANISOU 1244  CA  ASP A 176     3594   5112   3429    876   -493    -20       C  
ATOM   1245  C   ASP A 176      22.995  -9.055  11.548  1.00 31.41           C  
ANISOU 1245  C   ASP A 176     3687   4896   3353    794   -383    -85       C  
ATOM   1246  O   ASP A 176      22.763 -10.032  10.822  1.00 31.64           O  
ANISOU 1246  O   ASP A 176     3852   4786   3385    909   -334   -103       O  
ATOM   1247  CB  ASP A 176      23.617  -9.579  13.908  1.00 30.36           C  
ANISOU 1247  CB  ASP A 176     3543   4839   3153    862   -607     48       C  
ATOM   1248  CG  ASP A 176      24.693  -9.606  14.953  1.00 34.14           C  
ANISOU 1248  CG  ASP A 176     3890   5467   3615    942   -754    116       C  
ATOM   1249  OD1 ASP A 176      25.486 -10.569  14.931  1.00 36.16           O  
ANISOU 1249  OD1 ASP A 176     4105   5728   3907   1161   -790    173       O  
ATOM   1250  OD2 ASP A 176      24.765  -8.667  15.782  1.00 33.82           O  
ANISOU 1250  OD2 ASP A 176     3792   5536   3521    798   -841    110       O  
ATOM   1251  N   PHE A 177      22.282  -7.935  11.518  1.00 25.46           N  
ANISOU 1251  N   PHE A 177     2927   4162   2583    598   -358   -121       N  
ATOM   1252  CA  PHE A 177      21.162  -7.733  10.614  1.00 25.54           C  
ANISOU 1252  CA  PHE A 177     3057   4060   2588    506   -281   -171       C  
ATOM   1253  C   PHE A 177      21.413  -6.438   9.864  1.00 28.30           C  
ANISOU 1253  C   PHE A 177     3283   4515   2955    408   -209   -214       C  
ATOM   1254  O   PHE A 177      21.668  -5.410  10.484  1.00 31.47           O  
ANISOU 1254  O   PHE A 177     3584   5013   3361    298   -238   -209       O  
ATOM   1255  CB  PHE A 177      19.862  -7.625  11.414  1.00 23.23           C  
ANISOU 1255  CB  PHE A 177     2887   3676   2265    374   -314   -145       C  
ATOM   1256  CG  PHE A 177      19.611  -8.805  12.325  1.00 25.63           C  
ANISOU 1256  CG  PHE A 177     3317   3879   2545    440   -375    -75       C  
ATOM   1257  CD1 PHE A 177      19.111  -9.996  11.811  1.00 26.99           C  
ANISOU 1257  CD1 PHE A 177     3641   3879   2736    499   -370    -68       C  
ATOM   1258  CD2 PHE A 177      19.882  -8.720  13.691  1.00 26.22           C  
ANISOU 1258  CD2 PHE A 177     3382   4016   2565    437   -445    -14       C  
ATOM   1259  CE1 PHE A 177      18.888 -11.093  12.655  1.00 31.56           C  
ANISOU 1259  CE1 PHE A 177     4354   4338   3299    549   -420     14       C  
ATOM   1260  CE2 PHE A 177      19.658  -9.801  14.534  1.00 30.87           C  
ANISOU 1260  CE2 PHE A 177     4107   4506   3116    502   -493     71       C  
ATOM   1261  CZ  PHE A 177      19.159 -10.992  14.004  1.00 32.94           C  
ANISOU 1261  CZ  PHE A 177     4514   4585   3417    555   -473     92       C  
ATOM   1262  N   VAL A 178      21.369  -6.495   8.533  1.00 23.98           N  
ANISOU 1262  N   VAL A 178     2769   3936   2406    448   -120   -255       N  
ATOM   1263  CA  VAL A 178      21.648  -5.323   7.714  1.00 23.58           C  
ANISOU 1263  CA  VAL A 178     2624   3975   2363    367    -34   -276       C  
ATOM   1264  C   VAL A 178      20.530  -5.061   6.710  1.00 24.30           C  
ANISOU 1264  C   VAL A 178     2859   3963   2412    302      7   -312       C  
ATOM   1265  O   VAL A 178      20.153  -5.952   5.935  1.00 22.50           O  
ANISOU 1265  O   VAL A 178     2771   3635   2145    386     15   -343       O  
ATOM   1266  CB  VAL A 178      22.961  -5.497   6.930  1.00 29.74           C  
ANISOU 1266  CB  VAL A 178     3270   4866   3163    500     63   -272       C  
ATOM   1267  CG1 VAL A 178      23.193  -4.319   5.980  1.00 30.18           C  
ANISOU 1267  CG1 VAL A 178     3252   4997   3217    404    176   -275       C  
ATOM   1268  CG2 VAL A 178      24.124  -5.650   7.890  1.00 32.28           C  
ANISOU 1268  CG2 VAL A 178     3396   5321   3547    560      1   -223       C  
ATOM   1269  N   GLY A 179      20.014  -3.836   6.683  1.00 22.89           N  
ANISOU 1269  N   GLY A 179     2659   3801   2237    159     20   -308       N  
ATOM   1270  CA  GLY A 179      19.026  -3.507   5.667  1.00 22.95           C  
ANISOU 1270  CA  GLY A 179     2782   3732   2206    115     44   -326       C  
ATOM   1271  C   GLY A 179      19.638  -3.391   4.284  1.00 22.82           C  
ANISOU 1271  C   GLY A 179     2781   3755   2136    181    146   -342       C  
ATOM   1272  O   GLY A 179      19.316  -4.160   3.364  1.00 25.21           O  
ANISOU 1272  O   GLY A 179     3224   3984   2370    263    149   -378       O  
ATOM   1273  N   PHE A 180      20.549  -2.428   4.124  1.00 21.68           N  
ANISOU 1273  N   PHE A 180     2504   3721   2013    139    233   -313       N  
ATOM   1274  CA  PHE A 180      21.103  -2.123   2.814  1.00 23.52           C  
ANISOU 1274  CA  PHE A 180     2747   4003   2185    184    365   -304       C  
ATOM   1275  C   PHE A 180      22.586  -1.859   2.969  1.00 24.33           C  
ANISOU 1275  C   PHE A 180     2636   4257   2351    204    462   -263       C  
ATOM   1276  O   PHE A 180      22.994  -1.205   3.929  1.00 26.24           O  
ANISOU 1276  O   PHE A 180     2729   4558   2681     93    413   -236       O  
ATOM   1277  CB  PHE A 180      20.434  -0.864   2.247  1.00 24.14           C  
ANISOU 1277  CB  PHE A 180     2888   4049   2235     60    389   -275       C  
ATOM   1278  CG  PHE A 180      18.950  -1.002   2.075  1.00 25.08           C  
ANISOU 1278  CG  PHE A 180     3170   4047   2314     37    282   -297       C  
ATOM   1279  CD1 PHE A 180      18.083  -0.808   3.146  1.00 24.49           C  
ANISOU 1279  CD1 PHE A 180     3078   3918   2308    -40    182   -294       C  
ATOM   1280  CD2 PHE A 180      18.426  -1.346   0.835  1.00 26.45           C  
ANISOU 1280  CD2 PHE A 180     3507   4168   2375     97    282   -316       C  
ATOM   1281  CE1 PHE A 180      16.711  -0.964   2.978  1.00 19.50           C  
ANISOU 1281  CE1 PHE A 180     2547   3195   1665    -60     92   -297       C  
ATOM   1282  CE2 PHE A 180      17.061  -1.500   0.662  1.00 28.30           C  
ANISOU 1282  CE2 PHE A 180     3856   4306   2590     63    156   -328       C  
ATOM   1283  CZ  PHE A 180      16.211  -1.316   1.733  1.00 20.07           C  
ANISOU 1283  CZ  PHE A 180     2752   3225   1649    -16     66   -311       C  
ATOM   1284  N   GLU A 181      23.378  -2.332   2.017  1.00 25.63           N  
ANISOU 1284  N   GLU A 181     2785   4486   2468    342    599   -259       N  
ATOM   1285  CA  GLU A 181      24.801  -2.016   1.996  1.00 29.81           C  
ANISOU 1285  CA  GLU A 181     3069   5184   3074    360    722   -198       C  
ATOM   1286  C   GLU A 181      25.012  -0.991   0.885  1.00 33.15           C  
ANISOU 1286  C   GLU A 181     3499   5650   3447    281    886   -145       C  
ATOM   1287  O   GLU A 181      24.702  -1.253  -0.284  1.00 30.28           O  
ANISOU 1287  O   GLU A 181     3318   5243   2946    378    986   -162       O  
ATOM   1288  CB  GLU A 181      25.644  -3.265   1.733  1.00 29.07           C  
ANISOU 1288  CB  GLU A 181     2925   5150   2971    603    802   -211       C  
ATOM   1289  CG  GLU A 181      27.141  -3.011   1.858  1.00 36.13           C  
ANISOU 1289  CG  GLU A 181     3498   6248   3980    634    917   -132       C  
ATOM   1290  CD  GLU A 181      27.981  -4.135   1.291  1.00 40.25           C  
ANISOU 1290  CD  GLU A 181     3979   6835   4479    918   1060   -135       C  
ATOM   1291  OE1 GLU A 181      28.121  -4.196   0.053  1.00 39.74           O  
ANISOU 1291  OE1 GLU A 181     4018   6779   4303   1022   1257   -139       O  
ATOM   1292  OE2 GLU A 181      28.493  -4.949   2.087  1.00 41.33           O  
ANISOU 1292  OE2 GLU A 181     3997   7010   4697   1051    980   -129       O  
ATOM   1293  N   ILE A 182      25.537   0.177   1.247  1.00 30.53           N  
ANISOU 1293  N   ILE A 182     2992   5393   3216     98    907    -78       N  
ATOM   1294  CA  ILE A 182      25.526   1.320   0.341  1.00 29.29           C  
ANISOU 1294  CA  ILE A 182     2881   5231   3019    -24   1038    -11       C  
ATOM   1295  C   ILE A 182      26.936   1.797   0.010  1.00 31.78           C  
ANISOU 1295  C   ILE A 182     2936   5717   3422    -72   1218     88       C  
ATOM   1296  O   ILE A 182      27.881   1.521   0.754  1.00 34.33           O  
ANISOU 1296  O   ILE A 182     2997   6168   3878    -68   1189    107       O  
ATOM   1297  CB  ILE A 182      24.677   2.482   0.925  1.00 27.83           C  
ANISOU 1297  CB  ILE A 182     2779   4926   2870   -231    913    -10       C  
ATOM   1298  CG1 ILE A 182      25.302   3.032   2.206  1.00 29.10           C  
ANISOU 1298  CG1 ILE A 182     2734   5139   3184   -391    811     -2       C  
ATOM   1299  CG2 ILE A 182      23.243   2.040   1.189  1.00 26.19           C  
ANISOU 1299  CG2 ILE A 182     2790   4571   2589   -180    762    -86       C  
ATOM   1300  CD1 ILE A 182      24.749   4.398   2.624  1.00 31.72           C  
ANISOU 1300  CD1 ILE A 182     3152   5351   3550   -602    745      7       C  
ATOM   1301  N   PRO A 183      27.100   2.499  -1.128  1.00 33.06           N  
ANISOU 1301  N   PRO A 183     3158   5892   3510   -115   1408    167       N  
ATOM   1302  CA  PRO A 183      28.432   3.033  -1.416  1.00 35.74           C  
ANISOU 1302  CA  PRO A 183     3223   6400   3957   -195   1599    285       C  
ATOM   1303  C   PRO A 183      28.793   4.180  -0.477  1.00 35.98           C  
ANISOU 1303  C   PRO A 183     3069   6433   4168   -483   1491    333       C  
ATOM   1304  O   PRO A 183      27.956   4.616   0.329  1.00 34.02           O  
ANISOU 1304  O   PRO A 183     2951   6043   3935   -598   1290    268       O  
ATOM   1305  CB  PRO A 183      28.314   3.537  -2.867  1.00 36.99           C  
ANISOU 1305  CB  PRO A 183     3560   6537   3957   -179   1826    365       C  
ATOM   1306  CG  PRO A 183      26.861   3.719  -3.104  1.00 34.75           C  
ANISOU 1306  CG  PRO A 183     3621   6055   3527   -180   1687    299       C  
ATOM   1307  CD  PRO A 183      26.151   2.719  -2.238  1.00 33.50           C  
ANISOU 1307  CD  PRO A 183     3523   5828   3377    -73   1463    165       C  
ATOM   1308  N   ASP A 184      30.032   4.655  -0.582  1.00 39.18           N  
ANISOU 1308  N   ASP A 184     3178   6998   4712   -598   1627    445       N  
ATOM   1309  CA  ASP A 184      30.516   5.756   0.250  1.00 46.78           C  
ANISOU 1309  CA  ASP A 184     3957   7961   5855   -903   1517    491       C  
ATOM   1310  C   ASP A 184      29.966   7.098  -0.245  1.00 46.05           C  
ANISOU 1310  C   ASP A 184     4078   7696   5723  -1117   1569    548       C  
ATOM   1311  O   ASP A 184      30.694   7.894  -0.833  1.00 45.03           O  
ANISOU 1311  O   ASP A 184     3829   7618   5663  -1280   1745    681       O  
ATOM   1312  CB  ASP A 184      32.051   5.787   0.250  1.00 51.42           C  
ANISOU 1312  CB  ASP A 184     4120   8789   6628   -974   1640    608       C  
ATOM   1313  CG  ASP A 184      32.628   6.638   1.380  1.00 57.53           C  
ANISOU 1313  CG  ASP A 184     4686   9563   7609  -1273   1433    618       C  
ATOM   1314  OD1 ASP A 184      31.856   7.351   2.056  1.00 58.07           O  
ANISOU 1314  OD1 ASP A 184     4951   9458   7654  -1450   1248    546       O  
ATOM   1315  OD2 ASP A 184      33.862   6.593   1.582  1.00 62.45           O  
ANISOU 1315  OD2 ASP A 184     5009  10297   8420  -1302   1436    677       O  
ATOM   1316  N   LYS A 185      28.677   7.328  -0.015  1.00 41.29           N  
ANISOU 1316  N   LYS A 185     3786   6888   5013  -1106   1426    460       N  
ATOM   1317  CA  LYS A 185      28.019   8.577  -0.400  1.00 43.00           C  
ANISOU 1317  CA  LYS A 185     4237   6913   5189  -1268   1448    509       C  
ATOM   1318  C   LYS A 185      27.292   9.055   0.834  1.00 35.18           C  
ANISOU 1318  C   LYS A 185     3355   5763   4249  -1379   1201    402       C  
ATOM   1319  O   LYS A 185      26.854   8.237   1.628  1.00 33.38           O  
ANISOU 1319  O   LYS A 185     3134   5547   4000  -1255   1045    290       O  
ATOM   1320  CB  LYS A 185      26.952   8.323  -1.470  1.00 40.46           C  
ANISOU 1320  CB  LYS A 185     4226   6494   4655  -1078   1522    507       C  
ATOM   1321  CG  LYS A 185      27.452   7.909  -2.834  1.00 51.80           C  
ANISOU 1321  CG  LYS A 185     5664   8048   5968   -941   1778    600       C  
ATOM   1322  CD  LYS A 185      26.258   7.556  -3.722  1.00 54.33           C  
ANISOU 1322  CD  LYS A 185     6324   8261   6058   -752   1768    564       C  
ATOM   1323  CE  LYS A 185      26.280   8.326  -5.028  1.00 56.44           C  
ANISOU 1323  CE  LYS A 185     6764   8492   6189   -781   1973    707       C  
ATOM   1324  NZ  LYS A 185      27.507   8.034  -5.800  1.00 57.55           N  
ANISOU 1324  NZ  LYS A 185     6735   8823   6310   -736   2254    808       N  
ATOM   1325  N   PHE A 186      27.130  10.364   0.994  1.00 35.93           N  
ANISOU 1325  N   PHE A 186     3563   5693   4397  -1600   1177    438       N  
ATOM   1326  CA  PHE A 186      26.379  10.858   2.154  1.00 34.58           C  
ANISOU 1326  CA  PHE A 186     3539   5352   4247  -1677    965    325       C  
ATOM   1327  C   PHE A 186      24.881  10.810   1.888  1.00 34.20           C  
ANISOU 1327  C   PHE A 186     3792   5146   4058  -1502    933    278       C  
ATOM   1328  O   PHE A 186      24.404  11.370   0.893  1.00 38.75           O  
ANISOU 1328  O   PHE A 186     4544   5620   4557  -1479   1044    362       O  
ATOM   1329  CB  PHE A 186      26.800  12.283   2.516  1.00 40.20           C  
ANISOU 1329  CB  PHE A 186     4280   5919   5076  -1980    938    364       C  
ATOM   1330  CG  PHE A 186      26.398  12.684   3.902  1.00 44.06           C  
ANISOU 1330  CG  PHE A 186     4870   6276   5596  -2071    717    228       C  
ATOM   1331  CD1 PHE A 186      25.172  13.290   4.134  1.00 46.58           C  
ANISOU 1331  CD1 PHE A 186     5500   6363   5835  -2016    665    168       C  
ATOM   1332  CD2 PHE A 186      27.242  12.437   4.977  1.00 49.37           C  
ANISOU 1332  CD2 PHE A 186     5328   7063   6366  -2193    560    163       C  
ATOM   1333  CE1 PHE A 186      24.789  13.650   5.424  1.00 51.71           C  
ANISOU 1333  CE1 PHE A 186     6268   6890   6489  -2075    490     37       C  
ATOM   1334  CE2 PHE A 186      26.872  12.789   6.270  1.00 53.33           C  
ANISOU 1334  CE2 PHE A 186     5962   7443   6857  -2268    355     30       C  
ATOM   1335  CZ  PHE A 186      25.644  13.401   6.493  1.00 53.47           C  
ANISOU 1335  CZ  PHE A 186     6312   7222   6782  -2206    335    -38       C  
ATOM   1336  N   VAL A 187      24.143  10.133   2.766  1.00 30.30           N  
ANISOU 1336  N   VAL A 187     3343   4639   3529  -1379    780    160       N  
ATOM   1337  CA  VAL A 187      22.707   9.994   2.588  1.00 29.57           C  
ANISOU 1337  CA  VAL A 187     3479   4426   3329  -1215    739    122       C  
ATOM   1338  C   VAL A 187      21.943  10.568   3.771  1.00 33.30           C  
ANISOU 1338  C   VAL A 187     4078   4747   3825  -1259    603     32       C  
ATOM   1339  O   VAL A 187      22.462  10.632   4.892  1.00 28.59           O  
ANISOU 1339  O   VAL A 187     3398   4171   3292  -1366    502    -38       O  
ATOM   1340  CB  VAL A 187      22.281   8.520   2.372  1.00 29.53           C  
ANISOU 1340  CB  VAL A 187     3442   4535   3241   -993    714     76       C  
ATOM   1341  CG1 VAL A 187      22.867   7.975   1.080  1.00 27.75           C  
ANISOU 1341  CG1 VAL A 187     3165   4429   2950   -907    868    151       C  
ATOM   1342  CG2 VAL A 187      22.685   7.667   3.559  1.00 32.33           C  
ANISOU 1342  CG2 VAL A 187     3645   4991   3650   -975    596     -9       C  
ATOM   1343  N   VAL A 188      20.707  10.985   3.514  1.00 26.83           N  
ANISOU 1343  N   VAL A 188     3466   3782   2948  -1162    600     38       N  
ATOM   1344  CA  VAL A 188      19.864  11.582   4.547  1.00 26.41           C  
ANISOU 1344  CA  VAL A 188     3554   3575   2905  -1161    512    -39       C  
ATOM   1345  C   VAL A 188      18.463  11.030   4.386  1.00 26.00           C  
ANISOU 1345  C   VAL A 188     3586   3505   2788   -951    485    -49       C  
ATOM   1346  O   VAL A 188      18.184  10.353   3.408  1.00 25.74           O  
ANISOU 1346  O   VAL A 188     3531   3548   2699   -842    515      2       O  
ATOM   1347  CB  VAL A 188      19.831  13.127   4.429  1.00 29.19           C  
ANISOU 1347  CB  VAL A 188     4084   3713   3294  -1291    555      1       C  
ATOM   1348  CG1 VAL A 188      21.189  13.741   4.769  1.00 30.08           C  
ANISOU 1348  CG1 VAL A 188     4107   3824   3496  -1550    552      3       C  
ATOM   1349  CG2 VAL A 188      19.367  13.546   3.023  1.00 28.52           C  
ANISOU 1349  CG2 VAL A 188     4114   3563   3160  -1217    660    130       C  
ATOM   1350  N   GLY A 189      17.582  11.318   5.340  1.00 27.04           N  
ANISOU 1350  N   GLY A 189     3814   3537   2923   -898    431   -115       N  
ATOM   1351  CA  GLY A 189      16.218  10.833   5.251  1.00 23.20           C  
ANISOU 1351  CA  GLY A 189     3366   3045   2404   -714    409   -109       C  
ATOM   1352  C   GLY A 189      15.965   9.611   6.109  1.00 23.91           C  
ANISOU 1352  C   GLY A 189     3351   3251   2483   -647    344   -176       C  
ATOM   1353  O   GLY A 189      16.911   8.978   6.607  1.00 26.16           O  
ANISOU 1353  O   GLY A 189     3528   3640   2770   -716    310   -220       O  
ATOM   1354  N   TYR A 190      14.687   9.283   6.288  1.00 23.12           N  
ANISOU 1354  N   TYR A 190     3271   3134   2378   -513    327   -171       N  
ATOM   1355  CA  TYR A 190      14.277   8.205   7.191  1.00 23.21           C  
ANISOU 1355  CA  TYR A 190     3207   3228   2384   -456    282   -217       C  
ATOM   1356  C   TYR A 190      14.968   8.355   8.551  1.00 25.77           C  
ANISOU 1356  C   TYR A 190     3549   3551   2691   -538    263   -300       C  
ATOM   1357  O   TYR A 190      15.516   7.390   9.094  1.00 24.90           O  
ANISOU 1357  O   TYR A 190     3354   3547   2562   -555    212   -330       O  
ATOM   1358  CB  TYR A 190      14.577   6.846   6.532  1.00 20.79           C  
ANISOU 1358  CB  TYR A 190     2792   3048   2061   -431    240   -199       C  
ATOM   1359  CG  TYR A 190      13.847   5.672   7.170  1.00 24.09           C  
ANISOU 1359  CG  TYR A 190     3153   3518   2482   -362    194   -213       C  
ATOM   1360  CD1 TYR A 190      12.460   5.557   7.087  1.00 25.57           C  
ANISOU 1360  CD1 TYR A 190     3339   3677   2701   -280    187   -172       C  
ATOM   1361  CD2 TYR A 190      14.546   4.685   7.855  1.00 21.10           C  
ANISOU 1361  CD2 TYR A 190     2713   3217   2087   -382    157   -251       C  
ATOM   1362  CE1 TYR A 190      11.782   4.482   7.685  1.00 26.04           C  
ANISOU 1362  CE1 TYR A 190     3335   3778   2779   -246    156   -166       C  
ATOM   1363  CE2 TYR A 190      13.883   3.607   8.446  1.00 23.74           C  
ANISOU 1363  CE2 TYR A 190     3018   3577   2424   -331    124   -246       C  
ATOM   1364  CZ  TYR A 190      12.504   3.511   8.360  1.00 26.20           C  
ANISOU 1364  CZ  TYR A 190     3328   3854   2772   -277    130   -203       C  
ATOM   1365  OH  TYR A 190      11.855   2.428   8.952  1.00 25.94           O  
ANISOU 1365  OH  TYR A 190     3256   3843   2758   -254    108   -182       O  
ATOM   1366  N   ALA A 191      14.927   9.586   9.080  1.00 25.25           N  
ANISOU 1366  N   ALA A 191     3618   3353   2623   -582    293   -337       N  
ATOM   1367  CA  ALA A 191      15.532  10.001  10.355  1.00 26.20           C  
ANISOU 1367  CA  ALA A 191     3815   3436   2703   -674    256   -432       C  
ATOM   1368  C   ALA A 191      17.036  10.290  10.313  1.00 26.44           C  
ANISOU 1368  C   ALA A 191     3794   3499   2753   -863    193   -457       C  
ATOM   1369  O   ALA A 191      17.565  10.863  11.253  1.00 28.80           O  
ANISOU 1369  O   ALA A 191     4178   3742   3022   -972    135   -537       O  
ATOM   1370  CB  ALA A 191      15.181   9.043  11.531  1.00 23.22           C  
ANISOU 1370  CB  ALA A 191     3414   3145   2263   -605    225   -475       C  
ATOM   1371  N   LEU A 192      17.716   9.917   9.228  1.00 28.65           N  
ANISOU 1371  N   LEU A 192     3936   3870   3080   -903    206   -387       N  
ATOM   1372  CA  LEU A 192      19.131  10.273   9.082  1.00 30.24           C  
ANISOU 1372  CA  LEU A 192     4048   4115   3329  -1085    174   -384       C  
ATOM   1373  C   LEU A 192      19.285  11.756   8.746  1.00 28.22           C  
ANISOU 1373  C   LEU A 192     3931   3679   3111  -1218    219   -369       C  
ATOM   1374  O   LEU A 192      18.588  12.282   7.878  1.00 28.14           O  
ANISOU 1374  O   LEU A 192     4021   3565   3105  -1150    305   -304       O  
ATOM   1375  CB  LEU A 192      19.821   9.407   8.020  1.00 30.48           C  
ANISOU 1375  CB  LEU A 192     3888   4304   3390  -1063    213   -306       C  
ATOM   1376  CG  LEU A 192      20.159   7.971   8.435  1.00 33.74           C  
ANISOU 1376  CG  LEU A 192     4151   4885   3784   -975    151   -325       C  
ATOM   1377  CD1 LEU A 192      18.968   7.040   8.312  1.00 31.86           C  
ANISOU 1377  CD1 LEU A 192     3962   4647   3496   -795    162   -320       C  
ATOM   1378  CD2 LEU A 192      21.327   7.437   7.610  1.00 37.07           C  
ANISOU 1378  CD2 LEU A 192     4378   5454   4252   -997    192   -267       C  
ATOM   1379  N   ASP A 193      20.200  12.443   9.416  1.00 27.87           N  
ANISOU 1379  N   ASP A 193     3905   3589   3096  -1416    146   -425       N  
ATOM   1380  CA  ASP A 193      20.266  13.883   9.259  1.00 29.67           C  
ANISOU 1380  CA  ASP A 193     4315   3598   3360  -1556    176   -424       C  
ATOM   1381  C   ASP A 193      21.532  14.400   8.586  1.00 37.88           C  
ANISOU 1381  C   ASP A 193     5234   4656   4500  -1791    192   -350       C  
ATOM   1382  O   ASP A 193      22.554  13.711   8.504  1.00 36.08           O  
ANISOU 1382  O   ASP A 193     4757   4630   4321  -1868    156   -321       O  
ATOM   1383  CB  ASP A 193      20.174  14.564  10.619  1.00 30.97           C  
ANISOU 1383  CB  ASP A 193     4677   3617   3474  -1632     78   -562       C  
ATOM   1384  CG  ASP A 193      21.463  14.454  11.398  1.00 32.45           C  
ANISOU 1384  CG  ASP A 193     4744   3904   3684  -1849    -78   -625       C  
ATOM   1385  OD1 ASP A 193      21.968  13.326  11.547  1.00 37.53           O  
ANISOU 1385  OD1 ASP A 193     5157   4776   4327  -1810   -137   -608       O  
ATOM   1386  OD2 ASP A 193      21.966  15.495  11.844  1.00 35.67           O  
ANISOU 1386  OD2 ASP A 193     5288   4152   4114  -2058   -153   -688       O  
ATOM   1387  N   TYR A 194      21.436  15.638   8.123  1.00 32.99           N  
ANISOU 1387  N   TYR A 194     4796   3820   3918  -1895    255   -308       N  
ATOM   1388  CA  TYR A 194      22.597  16.457   7.833  1.00 35.49           C  
ANISOU 1388  CA  TYR A 194     5063   4082   4340  -2183    254   -256       C  
ATOM   1389  C   TYR A 194      22.475  17.688   8.702  1.00 37.50           C  
ANISOU 1389  C   TYR A 194     5597   4057   4596  -2332    171   -362       C  
ATOM   1390  O   TYR A 194      21.656  18.574   8.433  1.00 39.52           O  
ANISOU 1390  O   TYR A 194     6122   4065   4828  -2261    247   -348       O  
ATOM   1391  CB  TYR A 194      22.627  16.839   6.365  1.00 35.95           C  
ANISOU 1391  CB  TYR A 194     5122   4103   4433  -2185    423    -88       C  
ATOM   1392  CG  TYR A 194      23.852  17.618   5.983  1.00 43.18           C  
ANISOU 1392  CG  TYR A 194     5954   4981   5471  -2496    455     -2       C  
ATOM   1393  CD1 TYR A 194      25.099  17.008   5.948  1.00 47.77           C  
ANISOU 1393  CD1 TYR A 194     6203   5808   6139  -2638    436     38       C  
ATOM   1394  CD2 TYR A 194      23.765  18.954   5.649  1.00 52.49           C  
ANISOU 1394  CD2 TYR A 194     7375   5877   6691  -2644    510     54       C  
ATOM   1395  CE1 TYR A 194      26.227  17.711   5.589  1.00 54.96           C  
ANISOU 1395  CE1 TYR A 194     6993   6705   7185  -2939    477    136       C  
ATOM   1396  CE2 TYR A 194      24.887  19.675   5.293  1.00 57.72           C  
ANISOU 1396  CE2 TYR A 194     7954   6495   7481  -2960    547    150       C  
ATOM   1397  CZ  TYR A 194      26.114  19.045   5.265  1.00 61.08           C  
ANISOU 1397  CZ  TYR A 194     8016   7190   8002  -3115    532    193       C  
ATOM   1398  OH  TYR A 194      27.235  19.748   4.905  1.00 72.43           O  
ANISOU 1398  OH  TYR A 194     9325   8608   9589  -3415    575    306       O  
ATOM   1399  N   ASN A 195      23.279  17.738   9.760  1.00 46.34           N  
ANISOU 1399  N   ASN A 195     6666   5208   5733  -2526      3   -471       N  
ATOM   1400  CA  ASN A 195      23.187  18.798  10.755  1.00 44.37           C  
ANISOU 1400  CA  ASN A 195     6716   4693   5451  -2667   -108   -611       C  
ATOM   1401  C   ASN A 195      21.750  19.094  11.220  1.00 40.11           C  
ANISOU 1401  C   ASN A 195     6500   3958   4781  -2402    -49   -701       C  
ATOM   1402  O   ASN A 195      21.299  20.246  11.225  1.00 41.75           O  
ANISOU 1402  O   ASN A 195     7018   3862   4985  -2425     -6   -731       O  
ATOM   1403  CB  ASN A 195      23.926  20.045  10.279  1.00 56.36           C  
ANISOU 1403  CB  ASN A 195     8322   5998   7094  -2979    -99   -551       C  
ATOM   1404  CG  ASN A 195      25.413  19.791  10.110  1.00 66.95           C  
ANISOU 1404  CG  ASN A 195     9316   7547   8576  -3271   -180   -480       C  
ATOM   1405  OD1 ASN A 195      26.001  18.982  10.831  1.00 69.37           O  
ANISOU 1405  OD1 ASN A 195     9397   8086   8873  -3287   -329   -542       O  
ATOM   1406  ND2 ASN A 195      26.025  20.466   9.151  1.00 73.26           N  
ANISOU 1406  ND2 ASN A 195    10041   8288   9509  -3428    -74   -328       N  
ATOM   1407  N   GLU A 196      21.065  18.011  11.592  1.00 37.65           N  
ANISOU 1407  N   GLU A 196     6101   3829   4376  -2149    -39   -730       N  
ATOM   1408  CA  GLU A 196      19.711  17.997  12.169  1.00 43.39           C  
ANISOU 1408  CA  GLU A 196     7046   4456   4983  -1875     24   -805       C  
ATOM   1409  C   GLU A 196      18.577  18.153  11.156  1.00 43.14           C  
ANISOU 1409  C   GLU A 196     7069   4350   4974  -1640    196   -690       C  
ATOM   1410  O   GLU A 196      17.414  17.906  11.485  1.00 40.74           O  
ANISOU 1410  O   GLU A 196     6847   4034   4600  -1387    263   -715       O  
ATOM   1411  CB  GLU A 196      19.564  18.969  13.350  1.00 39.03           C  
ANISOU 1411  CB  GLU A 196     6839   3650   4339  -1939    -49   -976       C  
ATOM   1412  CG  GLU A 196      20.406  18.591  14.568  1.00 43.83           C  
ANISOU 1412  CG  GLU A 196     7417   4369   4867  -2101   -250  -1110       C  
ATOM   1413  CD  GLU A 196      20.157  17.170  15.077  1.00 47.98           C  
ANISOU 1413  CD  GLU A 196     7744   5180   5305  -1919   -273  -1109       C  
ATOM   1414  OE1 GLU A 196      19.007  16.677  15.022  1.00 42.37           O  
ANISOU 1414  OE1 GLU A 196     7056   4505   4540  -1643   -136  -1077       O  
ATOM   1415  OE2 GLU A 196      21.125  16.540  15.547  1.00 54.64           O  
ANISOU 1415  OE2 GLU A 196     8405   6213   6143  -2058   -435  -1130       O  
ATOM   1416  N   TYR A 197      18.920  18.516   9.920  1.00 37.68           N  
ANISOU 1416  N   TYR A 197     6313   3627   4376  -1723    266   -551       N  
ATOM   1417  CA  TYR A 197      17.928  18.568   8.845  1.00 37.17           C  
ANISOU 1417  CA  TYR A 197     6276   3527   4319  -1504    397   -423       C  
ATOM   1418  C   TYR A 197      17.761  17.230   8.142  1.00 33.80           C  
ANISOU 1418  C   TYR A 197     5572   3387   3884  -1370    420   -336       C  
ATOM   1419  O   TYR A 197      18.627  16.360   8.244  1.00 31.51           O  
ANISOU 1419  O   TYR A 197     5059   3309   3605  -1470    362   -345       O  
ATOM   1420  CB  TYR A 197      18.284  19.643   7.824  1.00 43.64           C  
ANISOU 1420  CB  TYR A 197     7217   4154   5212  -1636    467   -303       C  
ATOM   1421  CG  TYR A 197      18.072  21.022   8.370  1.00 53.64           C  
ANISOU 1421  CG  TYR A 197     8828   5069   6482  -1695    466   -377       C  
ATOM   1422  CD1 TYR A 197      16.813  21.604   8.353  1.00 55.73           C  
ANISOU 1422  CD1 TYR A 197     9324   5137   6712  -1436    546   -371       C  
ATOM   1423  CD2 TYR A 197      19.118  21.727   8.941  1.00 60.92           C  
ANISOU 1423  CD2 TYR A 197     9846   5852   7448  -2006    377   -457       C  
ATOM   1424  CE1 TYR A 197      16.605  22.859   8.870  1.00 62.99           C  
ANISOU 1424  CE1 TYR A 197    10593   5711   7629  -1459    558   -448       C  
ATOM   1425  CE2 TYR A 197      18.925  22.987   9.455  1.00 67.00           C  
ANISOU 1425  CE2 TYR A 197    10976   6266   8213  -2067    367   -542       C  
ATOM   1426  CZ  TYR A 197      17.666  23.549   9.420  1.00 69.14           C  
ANISOU 1426  CZ  TYR A 197    11505   6328   8438  -1780    468   -541       C  
ATOM   1427  OH  TYR A 197      17.471  24.808   9.938  1.00 75.64           O  
ANISOU 1427  OH  TYR A 197    12719   6770   9249  -1813    470   -634       O  
ATOM   1428  N   PHE A 198      16.639  17.098   7.430  1.00 31.21           N  
ANISOU 1428  N   PHE A 198     5270   3052   3538  -1140    494   -252       N  
ATOM   1429  CA  PHE A 198      16.292  15.921   6.634  1.00 29.21           C  
ANISOU 1429  CA  PHE A 198     4810   3022   3264  -1004    507   -171       C  
ATOM   1430  C   PHE A 198      15.816  14.709   7.431  1.00 27.99           C  
ANISOU 1430  C   PHE A 198     4519   3044   3070   -881    455   -247       C  
ATOM   1431  O   PHE A 198      15.629  13.633   6.855  1.00 28.06           O  
ANISOU 1431  O   PHE A 198     4365   3230   3067   -797    446   -197       O  
ATOM   1432  CB  PHE A 198      17.433  15.511   5.699  1.00 29.22           C  
ANISOU 1432  CB  PHE A 198     4647   3168   3288  -1152    523    -89       C  
ATOM   1433  CG  PHE A 198      17.914  16.616   4.802  1.00 34.54           C  
ANISOU 1433  CG  PHE A 198     5441   3686   3996  -1283    599     19       C  
ATOM   1434  CD1 PHE A 198      17.143  17.048   3.729  1.00 35.09           C  
ANISOU 1434  CD1 PHE A 198     5634   3664   4035  -1146    666    143       C  
ATOM   1435  CD2 PHE A 198      19.148  17.208   5.017  1.00 40.17           C  
ANISOU 1435  CD2 PHE A 198     6138   4349   4776  -1552    596     12       C  
ATOM   1436  CE1 PHE A 198      17.593  18.071   2.885  1.00 33.49           C  
ANISOU 1436  CE1 PHE A 198     5567   3306   3852  -1266    748    265       C  
ATOM   1437  CE2 PHE A 198      19.610  18.223   4.184  1.00 40.65           C  
ANISOU 1437  CE2 PHE A 198     6309   4257   4878  -1697    682    132       C  
ATOM   1438  CZ  PHE A 198      18.829  18.655   3.117  1.00 41.88           C  
ANISOU 1438  CZ  PHE A 198     6617   4307   4987  -1548    767    262       C  
ATOM   1439  N   ARG A 199      15.616  14.857   8.740  1.00 28.06           N  
ANISOU 1439  N   ARG A 199     4616   2996   3048   -872    424   -365       N  
ATOM   1440  CA  ARG A 199      15.050  13.732   9.492  1.00 28.52           C  
ANISOU 1440  CA  ARG A 199     4567   3208   3060   -745    398   -411       C  
ATOM   1441  C   ARG A 199      13.576  13.518   9.148  1.00 35.23           C  
ANISOU 1441  C   ARG A 199     5408   4057   3920   -513    462   -346       C  
ATOM   1442  O   ARG A 199      13.079  12.381   9.154  1.00 34.38           O  
ANISOU 1442  O   ARG A 199     5147   4108   3808   -423    445   -321       O  
ATOM   1443  CB  ARG A 199      15.233  13.916  11.000  1.00 27.19           C  
ANISOU 1443  CB  ARG A 199     4514   2992   2823   -789    357   -546       C  
ATOM   1444  CG  ARG A 199      16.699  14.002  11.461  1.00 28.33           C  
ANISOU 1444  CG  ARG A 199     4630   3171   2963  -1031    245   -614       C  
ATOM   1445  CD  ARG A 199      16.819  13.709  12.968  1.00 29.79           C  
ANISOU 1445  CD  ARG A 199     4890   3387   3042  -1042    165   -739       C  
ATOM   1446  NE  ARG A 199      18.091  14.125  13.563  1.00 32.29           N  
ANISOU 1446  NE  ARG A 199     5237   3686   3346  -1281     27   -822       N  
ATOM   1447  CZ  ARG A 199      19.192  13.373  13.635  1.00 30.18           C  
ANISOU 1447  CZ  ARG A 199     4755   3608   3105  -1406    -90   -809       C  
ATOM   1448  NH1 ARG A 199      19.206  12.143  13.128  1.00 28.33           N  
ANISOU 1448  NH1 ARG A 199     4289   3575   2900  -1304    -71   -724       N  
ATOM   1449  NH2 ARG A 199      20.287  13.871  14.209  1.00 32.20           N  
ANISOU 1449  NH2 ARG A 199     5030   3842   3362  -1633   -235   -881       N  
ATOM   1450  N   ASP A 200      12.901  14.620   8.823  1.00 29.39           N  
ANISOU 1450  N   ASP A 200     4829   3134   3206   -423    527   -308       N  
ATOM   1451  CA  ASP A 200      11.468  14.645   8.540  1.00 29.16           C  
ANISOU 1451  CA  ASP A 200     4785   3091   3206   -191    582   -236       C  
ATOM   1452  C   ASP A 200      11.229  14.365   7.067  1.00 31.15           C  
ANISOU 1452  C   ASP A 200     4933   3412   3491   -152    551   -103       C  
ATOM   1453  O   ASP A 200      10.627  15.165   6.352  1.00 37.29           O  
ANISOU 1453  O   ASP A 200     5801   4071   4295    -46    578    -15       O  
ATOM   1454  CB  ASP A 200      10.881  16.024   8.902  1.00 31.52           C  
ANISOU 1454  CB  ASP A 200     5320   3142   3512    -81    666   -256       C  
ATOM   1455  CG  ASP A 200      11.604  17.172   8.210  1.00 35.96           C  
ANISOU 1455  CG  ASP A 200     6064   3507   4093   -206    666   -223       C  
ATOM   1456  OD1 ASP A 200      12.811  17.033   7.911  1.00 33.25           O  
ANISOU 1456  OD1 ASP A 200     5681   3208   3746   -431    613   -231       O  
ATOM   1457  OD2 ASP A 200      10.960  18.213   7.961  1.00 38.62           O  
ANISOU 1457  OD2 ASP A 200     6575   3641   4457    -75    728   -177       O  
ATOM   1458  N   LEU A 201      11.724  13.217   6.631  1.00 29.67           N  
ANISOU 1458  N   LEU A 201     4578   3410   3287   -227    489    -90       N  
ATOM   1459  CA  LEU A 201      11.702  12.789   5.238  1.00 28.76           C  
ANISOU 1459  CA  LEU A 201     4390   3377   3162   -213    449     12       C  
ATOM   1460  C   LEU A 201      11.626  11.270   5.280  1.00 26.56           C  
ANISOU 1460  C   LEU A 201     3929   3292   2869   -206    385    -10       C  
ATOM   1461  O   LEU A 201      12.407  10.640   5.993  1.00 27.52           O  
ANISOU 1461  O   LEU A 201     3991   3489   2975   -300    374    -87       O  
ATOM   1462  CB  LEU A 201      12.988  13.246   4.547  1.00 32.38           C  
ANISOU 1462  CB  LEU A 201     4908   3800   3593   -379    471     37       C  
ATOM   1463  CG  LEU A 201      13.338  12.771   3.134  1.00 32.66           C  
ANISOU 1463  CG  LEU A 201     4898   3934   3578   -392    460    128       C  
ATOM   1464  CD1 LEU A 201      12.336  13.291   2.122  1.00 33.85           C  
ANISOU 1464  CD1 LEU A 201     5141   4014   3707   -250    444    244       C  
ATOM   1465  CD2 LEU A 201      14.764  13.221   2.761  1.00 28.81           C  
ANISOU 1465  CD2 LEU A 201     4437   3430   3080   -579    524    146       C  
ATOM   1466  N   ASN A 202      10.685  10.682   4.538  1.00 30.34           N  
ANISOU 1466  N   ASN A 202     4330   3842   3356    -98    328     59       N  
ATOM   1467  CA AASN A 202      10.434   9.236   4.569  0.58 31.00           C  
ANISOU 1467  CA AASN A 202     4269   4074   3438    -94    256     41       C  
ATOM   1468  CA BASN A 202      10.467   9.234   4.606  0.42 30.36           C  
ANISOU 1468  CA BASN A 202     4188   3992   3356    -97    258     37       C  
ATOM   1469  C   ASN A 202      11.419   8.409   3.732  1.00 28.06           C  
ANISOU 1469  C   ASN A 202     3874   3791   2997   -176    219     30       C  
ATOM   1470  O   ASN A 202      11.682   7.250   4.032  1.00 29.29           O  
ANISOU 1470  O   ASN A 202     3946   4038   3145   -202    182    -18       O  
ATOM   1471  CB AASN A 202       9.012   8.947   4.074  0.58 33.61           C  
ANISOU 1471  CB AASN A 202     4520   4437   3814     30    185    118       C  
ATOM   1472  CB BASN A 202       8.995   8.857   4.330  0.42 33.20           C  
ANISOU 1472  CB BASN A 202     4454   4391   3771     27    193    105       C  
ATOM   1473  CG AASN A 202       8.089   8.456   5.173  0.58 38.22           C  
ANISOU 1473  CG AASN A 202     4985   5062   4474     86    203    104       C  
ATOM   1474  CG BASN A 202       8.554   9.166   2.898  0.42 34.37           C  
ANISOU 1474  CG BASN A 202     4642   4528   3889     86    116    200       C  
ATOM   1475  OD1AASN A 202       8.435   8.477   6.362  0.58 36.32           O  
ANISOU 1475  OD1AASN A 202     4763   4807   4230     57    281     35       O  
ATOM   1476  OD1BASN A 202       9.159   9.994   2.218  0.42 38.68           O  
ANISOU 1476  OD1BASN A 202     5319   5000   4378     66    151    233       O  
ATOM   1477  ND2AASN A 202       6.896   8.008   4.777  0.58 42.53           N  
ANISOU 1477  ND2AASN A 202     5407   5667   5086    161    127    178       N  
ATOM   1478  ND2BASN A 202       7.484   8.506   2.442  0.42 27.81           N  
ANISOU 1478  ND2BASN A 202     3701   3771   3093    150      3    253       N  
ATOM   1479  N   HIS A 203      11.943   9.008   2.668  1.00 24.12           N  
ANISOU 1479  N   HIS A 203     3464   3257   2443   -200    242     83       N  
ATOM   1480  CA  HIS A 203      12.860   8.306   1.758  1.00 23.55           C  
ANISOU 1480  CA  HIS A 203     3387   3273   2290   -248    243     82       C  
ATOM   1481  C   HIS A 203      14.308   8.534   2.193  1.00 28.48           C  
ANISOU 1481  C   HIS A 203     3986   3913   2921   -373    330     42       C  
ATOM   1482  O   HIS A 203      14.613   9.552   2.800  1.00 29.88           O  
ANISOU 1482  O   HIS A 203     4208   4000   3146   -444    379     36       O  
ATOM   1483  CB  HIS A 203      12.722   8.843   0.328  1.00 24.44           C  
ANISOU 1483  CB  HIS A 203     3617   3353   2315   -209    245    178       C  
ATOM   1484  CG  HIS A 203      11.322   8.838  -0.202  1.00 26.39           C  
ANISOU 1484  CG  HIS A 203     3886   3584   2557    -91    132    238       C  
ATOM   1485  ND1 HIS A 203      10.617   7.678  -0.444  1.00 27.62           N  
ANISOU 1485  ND1 HIS A 203     3972   3823   2698    -47      7    214       N  
ATOM   1486  CD2 HIS A 203      10.498   9.859  -0.551  1.00 27.39           C  
ANISOU 1486  CD2 HIS A 203     4089   3619   2700     -8    111    330       C  
ATOM   1487  CE1 HIS A 203       9.424   7.984  -0.923  1.00 30.69           C  
ANISOU 1487  CE1 HIS A 203     4368   4192   3102     43    -98    289       C  
ATOM   1488  NE2 HIS A 203       9.324   9.299  -0.988  1.00 27.96           N  
ANISOU 1488  NE2 HIS A 203     4104   3745   2773     86    -34    364       N  
ATOM   1489  N   VAL A 204      15.206   7.608   1.861  1.00 26.81           N  
ANISOU 1489  N   VAL A 204     3706   3812   2667   -397    346     15       N  
ATOM   1490  CA  VAL A 204      16.634   7.890   1.992  1.00 27.41           C  
ANISOU 1490  CA  VAL A 204     3724   3930   2761   -510    432     10       C  
ATOM   1491  C   VAL A 204      17.092   8.532   0.690  1.00 30.83           C  
ANISOU 1491  C   VAL A 204     4240   4349   3127   -534    530    104       C  
ATOM   1492  O   VAL A 204      16.791   8.030  -0.393  1.00 30.05           O  
ANISOU 1492  O   VAL A 204     4206   4288   2925   -443    529    138       O  
ATOM   1493  CB  VAL A 204      17.467   6.635   2.335  1.00 25.15           C  
ANISOU 1493  CB  VAL A 204     3302   3777   2475   -500    422    -50       C  
ATOM   1494  CG1 VAL A 204      18.972   6.909   2.149  1.00 27.71           C  
ANISOU 1494  CG1 VAL A 204     3526   4178   2824   -600    521    -24       C  
ATOM   1495  CG2 VAL A 204      17.195   6.202   3.763  1.00 24.36           C  
ANISOU 1495  CG2 VAL A 204     3140   3679   2435   -503    339   -123       C  
ATOM   1496  N   CYS A 205      17.794   9.659   0.793  1.00 27.55           N  
ANISOU 1496  N   CYS A 205     3842   3866   2759   -665    610    148       N  
ATOM   1497  CA  CYS A 205      18.139  10.426  -0.389  1.00 29.68           C  
ANISOU 1497  CA  CYS A 205     4214   4095   2968   -702    720    264       C  
ATOM   1498  C   CYS A 205      19.585  10.902  -0.354  1.00 29.44           C  
ANISOU 1498  C   CYS A 205     4082   4105   3000   -877    840    303       C  
ATOM   1499  O   CYS A 205      20.216  10.966   0.703  1.00 28.21           O  
ANISOU 1499  O   CYS A 205     3800   3968   2951   -993    805    239       O  
ATOM   1500  CB  CYS A 205      17.191  11.613  -0.551  1.00 30.02           C  
ANISOU 1500  CB  CYS A 205     4439   3955   3014   -681    699    329       C  
ATOM   1501  N   VAL A 206      20.102  11.237  -1.519  1.00 29.13           N  
ANISOU 1501  N   VAL A 206     4095   4085   2889   -901    978    417       N  
ATOM   1502  CA  VAL A 206      21.401  11.882  -1.609  1.00 32.67           C  
ANISOU 1502  CA  VAL A 206     4442   4558   3413  -1093   1114    493       C  
ATOM   1503  C   VAL A 206      21.166  13.389  -1.682  1.00 37.50           C  
ANISOU 1503  C   VAL A 206     5230   4953   4065  -1223   1141    580       C  
ATOM   1504  O   VAL A 206      20.229  13.859  -2.334  1.00 41.21           O  
ANISOU 1504  O   VAL A 206     5913   5300   4444  -1121   1131    645       O  
ATOM   1505  CB  VAL A 206      22.219  11.369  -2.821  1.00 41.24           C  
ANISOU 1505  CB  VAL A 206     5472   5799   4397  -1048   1295    584       C  
ATOM   1506  CG1 VAL A 206      23.452  12.220  -3.042  1.00 46.05           C  
ANISOU 1506  CG1 VAL A 206     5976   6424   5098  -1264   1464    703       C  
ATOM   1507  CG2 VAL A 206      22.636   9.925  -2.601  1.00 41.62           C  
ANISOU 1507  CG2 VAL A 206     5341   6038   4433   -926   1278    488       C  
ATOM   1508  N   ILE A 207      22.017  14.143  -1.002  1.00 40.04           N  
ANISOU 1508  N   ILE A 207     5469   5218   4527  -1449   1159    583       N  
ATOM   1509  CA  ILE A 207      21.818  15.573  -0.833  1.00 42.59           C  
ANISOU 1509  CA  ILE A 207     5981   5291   4910  -1592   1161    637       C  
ATOM   1510  C   ILE A 207      22.460  16.352  -1.972  1.00 52.15           C  
ANISOU 1510  C   ILE A 207     7263   6453   6099  -1717   1347    824       C  
ATOM   1511  O   ILE A 207      23.563  16.024  -2.406  1.00 57.74           O  
ANISOU 1511  O   ILE A 207     7779   7330   6831  -1817   1479    893       O  
ATOM   1512  CB  ILE A 207      22.345  15.996   0.565  1.00 70.88           C  
ANISOU 1512  CB  ILE A 207     9478   8809   8645  -1792   1052    524       C  
ATOM   1513  CG1 ILE A 207      22.405  17.512   0.737  1.00 73.04           C  
ANISOU 1513  CG1 ILE A 207     9955   8802   8994  -1990   1065    574       C  
ATOM   1514  CG2 ILE A 207      23.698  15.353   0.846  1.00 70.08           C  
ANISOU 1514  CG2 ILE A 207     9063   8932   8631  -1932   1074    511       C  
ATOM   1515  CD1 ILE A 207      22.622  17.916   2.195  1.00 72.83           C  
ANISOU 1515  CD1 ILE A 207     9929   8672   9072  -2146    914    423       C  
ATOM   1516  N   SER A 208      21.763  17.366  -2.480  1.00 53.98           N  
ANISOU 1516  N   SER A 208     7768   6458   6282  -1696   1370    921       N  
ATOM   1517  CA  SER A 208      22.286  18.149  -3.593  1.00 56.09           C  
ANISOU 1517  CA  SER A 208     8147   6655   6508  -1808   1554   1123       C  
ATOM   1518  C   SER A 208      23.466  18.999  -3.139  1.00 61.53           C  
ANISOU 1518  C   SER A 208     8740   7262   7376  -2147   1624   1170       C  
ATOM   1519  O   SER A 208      23.766  19.077  -1.942  1.00 62.26           O  
ANISOU 1519  O   SER A 208     8720   7326   7611  -2285   1495   1034       O  
ATOM   1520  CB  SER A 208      21.206  19.034  -4.224  1.00 56.07           C  
ANISOU 1520  CB  SER A 208     8483   6413   6407  -1683   1543   1228       C  
ATOM   1521  OG  SER A 208      20.877  20.135  -3.399  1.00 59.74           O  
ANISOU 1521  OG  SER A 208     9109   6597   6995  -1784   1462   1191       O  
ATOM   1522  N   GLU A 209      24.141  19.624  -4.097  1.00 59.98           N  
ANISOU 1522  N   GLU A 209     8590   7031   7168  -2293   1821   1369       N  
ATOM   1523  CA  GLU A 209      25.239  20.519  -3.768  1.00 67.32           C  
ANISOU 1523  CA  GLU A 209     9403   7877   8299  -2597   1854   1427       C  
ATOM   1524  C   GLU A 209      24.720  21.734  -3.015  1.00 69.00           C  
ANISOU 1524  C   GLU A 209     9873   7737   8604  -2713   1719   1375       C  
ATOM   1525  O   GLU A 209      25.397  22.252  -2.125  1.00 73.77           O  
ANISOU 1525  O   GLU A 209    10377   8262   9388  -2946   1623   1300       O  
ATOM   1526  CB  GLU A 209      26.008  20.947  -5.026  1.00 77.33           C  
ANISOU 1526  CB  GLU A 209    10626   9199   9555  -2630   2054   1652       C  
ATOM   1527  CG  GLU A 209      26.824  19.827  -5.654  1.00 83.61           C  
ANISOU 1527  CG  GLU A 209    11126  10343  10298  -2539   2207   1699       C  
ATOM   1528  CD  GLU A 209      27.611  19.033  -4.620  1.00 88.42           C  
ANISOU 1528  CD  GLU A 209    11378  11152  11065  -2635   2130   1555       C  
ATOM   1529  OE1 GLU A 209      27.541  17.785  -4.644  1.00 87.67           O  
ANISOU 1529  OE1 GLU A 209    11149  11291  10872  -2456   2146   1470       O  
ATOM   1530  OE2 GLU A 209      28.298  19.656  -3.780  1.00 92.35           O  
ANISOU 1530  OE2 GLU A 209    11737  11569  11782  -2882   2037   1524       O  
ATOM   1531  N   THR A 210      23.513  22.175  -3.363  1.00 65.96           N  
ANISOU 1531  N   THR A 210     9826   7142   8094  -2528   1699   1409       N  
ATOM   1532  CA  THR A 210      22.930  23.365  -2.751  1.00 68.66           C  
ANISOU 1532  CA  THR A 210    10452   7126   8509  -2573   1593   1366       C  
ATOM   1533  C   THR A 210      22.465  23.095  -1.314  1.00 66.57           C  
ANISOU 1533  C   THR A 210    10187   6807   8298  -2561   1412   1130       C  
ATOM   1534  O   THR A 210      22.565  23.970  -0.455  1.00 70.49           O  
ANISOU 1534  O   THR A 210    10819   7058   8904  -2721   1322   1044       O  
ATOM   1535  CB  THR A 210      21.778  23.967  -3.612  1.00 79.80           C  
ANISOU 1535  CB  THR A 210    12205   8336   9782  -2329   1622   1494       C  
ATOM   1536  OG1 THR A 210      21.760  25.393  -3.470  1.00 84.73           O  
ANISOU 1536  OG1 THR A 210    13057   8629  10508  -2429   1596   1540       O  
ATOM   1537  CG2 THR A 210      20.420  23.404  -3.211  1.00 74.21           C  
ANISOU 1537  CG2 THR A 210    11597   7626   8975  -2025   1496   1374       C  
ATOM   1538  N   GLY A 211      21.987  21.879  -1.055  1.00 57.27           N  
ANISOU 1538  N   GLY A 211     8833   5883   7043  -2326   1332   1009       N  
ATOM   1539  CA  GLY A 211      21.515  21.515   0.268  1.00 53.08           C  
ANISOU 1539  CA  GLY A 211     8266   5355   6547  -2249   1158    788       C  
ATOM   1540  C   GLY A 211      22.683  21.246   1.197  1.00 57.04           C  
ANISOU 1540  C   GLY A 211     8522   5978   7172  -2515   1087    680       C  
ATOM   1541  O   GLY A 211      22.605  21.514   2.394  1.00 58.67           O  
ANISOU 1541  O   GLY A 211     8789   6073   7431  -2586    946    519       O  
ATOM   1542  N   LYS A 212      23.769  20.713   0.640  1.00 57.66           N  
ANISOU 1542  N   LYS A 212     8325   6296   7289  -2649   1184    774       N  
ATOM   1543  CA  LYS A 212      24.980  20.439   1.412  1.00 59.20           C  
ANISOU 1543  CA  LYS A 212     8232   6642   7620  -2903   1113    704       C  
ATOM   1544  C   LYS A 212      25.609  21.729   1.929  1.00 59.82           C  
ANISOU 1544  C   LYS A 212     8418   6467   7845  -3230   1053    704       C  
ATOM   1545  O   LYS A 212      25.969  21.829   3.103  1.00 59.30           O  
ANISOU 1545  O   LYS A 212     8296   6377   7857  -3361    869    548       O  
ATOM   1546  CB  LYS A 212      25.996  19.643   0.582  1.00 64.27           C  
ANISOU 1546  CB  LYS A 212     8541   7597   8281  -2940   1265    832       C  
ATOM   1547  CG  LYS A 212      25.967  18.142   0.841  1.00 67.10           C  
ANISOU 1547  CG  LYS A 212     8653   8264   8578  -2712   1211    730       C  
ATOM   1548  CD  LYS A 212      27.154  17.426   0.211  1.00 72.34           C  
ANISOU 1548  CD  LYS A 212     8971   9224   9291  -2764   1360    838       C  
ATOM   1549  CE  LYS A 212      26.898  17.073  -1.244  1.00 74.01           C  
ANISOU 1549  CE  LYS A 212     9253   9517   9349  -2567   1581    983       C  
ATOM   1550  NZ  LYS A 212      28.099  16.462  -1.882  1.00 77.00           N  
ANISOU 1550  NZ  LYS A 212     9312  10173   9773  -2599   1766   1094       N  
ATOM   1551  N   ALA A 213      25.734  22.714   1.047  1.00 62.71           N  
ANISOU 1551  N   ALA A 213     8927   6657   8243  -3282   1172    868       N  
ATOM   1552  CA  ALA A 213      26.310  24.006   1.412  1.00 63.81           C  
ANISOU 1552  CA  ALA A 213     9163   6548   8532  -3517   1101    873       C  
ATOM   1553  C   ALA A 213      25.364  24.796   2.315  1.00 68.60           C  
ANISOU 1553  C   ALA A 213    10144   6821   9101  -3471    960    715       C  
ATOM   1554  O   ALA A 213      25.805  25.570   3.167  1.00 73.58           O  
ANISOU 1554  O   ALA A 213    10838   7284   9835  -3655    820    612       O  
ATOM   1555  CB  ALA A 213      26.656  24.813   0.161  1.00 63.70           C  
ANISOU 1555  CB  ALA A 213     9209   6437   8557  -3572   1284   1110       C  
ATOM   1556  N   LYS A 214      24.064  24.596   2.121  1.00 67.16           N  
ANISOU 1556  N   LYS A 214    10209   6542   8768  -3205   1001    698       N  
ATOM   1557  CA  LYS A 214      23.046  25.341   2.860  1.00 74.94           C  
ANISOU 1557  CA  LYS A 214    11560   7204   9708  -3086    911    569       C  
ATOM   1558  C   LYS A 214      22.935  24.899   4.325  1.00 78.07           C  
ANISOU 1558  C   LYS A 214    11938   7635  10092  -3098    733    321       C  
ATOM   1559  O   LYS A 214      22.488  25.667   5.181  1.00 77.91           O  
ANISOU 1559  O   LYS A 214    12187   7356  10061  -3069    637    182       O  
ATOM   1560  CB  LYS A 214      21.679  25.198   2.178  1.00 74.44           C  
ANISOU 1560  CB  LYS A 214    11727   7050   9506  -2762   1012    648       C  
ATOM   1561  CG  LYS A 214      20.762  26.401   2.343  1.00 77.99           C  
ANISOU 1561  CG  LYS A 214    12569   7120   9943  -2614    996    632       C  
ATOM   1562  CD  LYS A 214      19.284  26.019   2.221  1.00 73.45           C  
ANISOU 1562  CD  LYS A 214    12133   6525   9248  -2220   1014    625       C  
ATOM   1563  CE  LYS A 214      18.904  25.620   0.804  1.00 68.91           C  
ANISOU 1563  CE  LYS A 214    11491   6104   8586  -2033   1121    837       C  
ATOM   1564  NZ  LYS A 214      17.460  25.255   0.687  1.00 61.68           N  
ANISOU 1564  NZ  LYS A 214    10628   5230   7577  -1626   1086    826       N  
ATOM   1565  N   TYR A 215      23.346  23.665   4.610  1.00 78.81           N  
ANISOU 1565  N   TYR A 215    11723   8052  10171  -3122    693    268       N  
ATOM   1566  CA  TYR A 215      23.140  23.089   5.935  1.00 79.54           C  
ANISOU 1566  CA  TYR A 215    11774   8232  10216  -3049    521     48       C  
ATOM   1567  C   TYR A 215      24.413  22.600   6.644  1.00 81.66           C  
ANISOU 1567  C   TYR A 215    11732   8726  10570  -3306    378    -25       C  
ATOM   1568  O   TYR A 215      24.321  22.006   7.719  1.00 78.74           O  
ANISOU 1568  O   TYR A 215    11317   8457  10142  -3259    230   -192       O  
ATOM   1569  CB  TYR A 215      22.120  21.941   5.872  1.00 78.90           C  
ANISOU 1569  CB  TYR A 215    11597   8371  10011  -2662    547     17       C  
ATOM   1570  CG  TYR A 215      20.731  22.308   5.377  1.00 79.68           C  
ANISOU 1570  CG  TYR A 215    11954   8294  10026  -2356    638     66       C  
ATOM   1571  CD1 TYR A 215      19.922  23.187   6.090  1.00 82.47           C  
ANISOU 1571  CD1 TYR A 215    12641   8342  10350  -2263    606    -39       C  
ATOM   1572  CD2 TYR A 215      20.219  21.746   4.214  1.00 76.75           C  
ANISOU 1572  CD2 TYR A 215    11490   8070   9600  -2144    748    214       C  
ATOM   1573  CE1 TYR A 215      18.648  23.508   5.645  1.00 80.57           C  
ANISOU 1573  CE1 TYR A 215    12597   7962  10053  -1958    687     21       C  
ATOM   1574  CE2 TYR A 215      18.953  22.063   3.760  1.00 75.26           C  
ANISOU 1574  CE2 TYR A 215    11505   7744   9345  -1865    799    269       C  
ATOM   1575  CZ  TYR A 215      18.171  22.941   4.479  1.00 76.09           C  
ANISOU 1575  CZ  TYR A 215    11901   7563   9448  -1767    771    181       C  
ATOM   1576  OH  TYR A 215      16.910  23.249   4.026  1.00 74.45           O  
ANISOU 1576  OH  TYR A 215    11858   7237   9193  -1467    821    251       O  
ATOM   1577  N   LYS A 216      25.589  22.828   6.059  1.00 87.18           N  
ANISOU 1577  N   LYS A 216    12185   9533  11406  -3506    413    109       N  
ATOM   1578  CA  LYS A 216      26.839  22.416   6.713  1.00 90.63           C  
ANISOU 1578  CA  LYS A 216    12282  10201  11952  -3689    264     60       C  
ATOM   1579  C   LYS A 216      27.074  23.162   8.024  1.00 91.29           C  
ANISOU 1579  C   LYS A 216    12524  10103  12057  -3822     36   -121       C  
ATOM   1580  O   LYS A 216      27.251  24.378   8.032  1.00 93.74           O  
ANISOU 1580  O   LYS A 216    13033  10146  12440  -3964     19   -112       O  
ATOM   1581  CB  LYS A 216      28.059  22.592   5.801  1.00 96.07           C  
ANISOU 1581  CB  LYS A 216    12669  11023  12809  -3865    372    252       C  
ATOM   1582  CG  LYS A 216      29.382  22.317   6.514  1.00 99.39           C  
ANISOU 1582  CG  LYS A 216    12739  11646  13378  -4051    206    209       C  
ATOM   1583  CD  LYS A 216      30.558  22.275   5.549  1.00102.24           C  
ANISOU 1583  CD  LYS A 216    12747  12185  13914  -4175    357    411       C  
ATOM   1584  CE  LYS A 216      30.464  21.088   4.597  1.00 99.28           C  
ANISOU 1584  CE  LYS A 216    12154  12101  13468  -3962    557    530       C  
ATOM   1585  NZ  LYS A 216      31.698  20.931   3.772  1.00101.80           N  
ANISOU 1585  NZ  LYS A 216    12102  12623  13953  -4047    715    712       N  
TER    1586      LYS A 216                                                      
ATOM   1587  N   SER B   4       4.774  12.235 -18.959  1.00 73.09           N  
ANISOU 1587  N   SER B   4     9298   8729   9745   -849     92   2826       N  
ATOM   1588  CA  SER B   4       5.720  11.466 -18.152  1.00 70.21           C  
ANISOU 1588  CA  SER B   4     8940   8481   9258   -874    219   2478       C  
ATOM   1589  C   SER B   4       5.600   9.958 -18.381  1.00 63.04           C  
ANISOU 1589  C   SER B   4     7957   7913   8081   -816    236   2287       C  
ATOM   1590  O   SER B   4       4.499   9.398 -18.341  1.00 61.71           O  
ANISOU 1590  O   SER B   4     7751   7750   7944   -665    181   2266       O  
ATOM   1591  CB  SER B   4       5.551  11.789 -16.668  1.00 70.21           C  
ANISOU 1591  CB  SER B   4     9010   8142   9526   -740    293   2246       C  
ATOM   1592  OG  SER B   4       6.314  10.905 -15.865  1.00 70.46           O  
ANISOU 1592  OG  SER B   4     9033   8310   9427   -749    384   1929       O  
ATOM   1593  N   PRO B   5       6.747   9.294 -18.612  1.00 57.72           N  
ANISOU 1593  N   PRO B   5     7254   7516   7161   -937    314   2148       N  
ATOM   1594  CA  PRO B   5       6.781   7.858 -18.901  1.00 54.58           C  
ANISOU 1594  CA  PRO B   5     6802   7423   6511   -891    340   1952       C  
ATOM   1595  C   PRO B   5       6.747   7.024 -17.629  1.00 47.99           C  
ANISOU 1595  C   PRO B   5     5964   6506   5766   -742    402   1634       C  
ATOM   1596  O   PRO B   5       6.649   5.796 -17.709  1.00 50.63           O  
ANISOU 1596  O   PRO B   5     6264   7027   5948   -678    413   1461       O  
ATOM   1597  CB  PRO B   5       8.121   7.677 -19.626  1.00 58.54           C  
ANISOU 1597  CB  PRO B   5     7264   8216   6761  -1070    426   1950       C  
ATOM   1598  CG  PRO B   5       8.966   8.880 -19.237  1.00 58.45           C  
ANISOU 1598  CG  PRO B   5     7272   8024   6912  -1205    461   2060       C  
ATOM   1599  CD  PRO B   5       8.101   9.861 -18.487  1.00 57.34           C  
ANISOU 1599  CD  PRO B   5     7213   7476   7097  -1115    389   2147       C  
ATOM   1600  N   GLY B   6       6.809   7.675 -16.469  1.00 35.78           N  
ANISOU 1600  N   GLY B   6     4465   4675   4456   -697    435   1559       N  
ATOM   1601  CA  GLY B   6       6.798   6.945 -15.213  1.00 29.93           C  
ANISOU 1601  CA  GLY B   6     3731   3866   3776   -578    489   1280       C  
ATOM   1602  C   GLY B   6       8.204   6.578 -14.776  1.00 29.30           C  
ANISOU 1602  C   GLY B   6     3623   3911   3601   -674    560   1111       C  
ATOM   1603  O   GLY B   6       9.180   7.070 -15.339  1.00 30.66           O  
ANISOU 1603  O   GLY B   6     3767   4183   3701   -834    583   1212       O  
ATOM   1604  N   VAL B   7       8.310   5.720 -13.762  1.00 27.81           N  
ANISOU 1604  N   VAL B   7     3427   3722   3418   -582    591    877       N  
ATOM   1605  CA  VAL B   7       9.614   5.255 -13.301  1.00 28.52           C  
ANISOU 1605  CA  VAL B   7     3461   3942   3434   -653    637    728       C  
ATOM   1606  C   VAL B   7      10.172   4.301 -14.344  1.00 27.97           C  
ANISOU 1606  C   VAL B   7     3290   4186   3153   -670    669    714       C  
ATOM   1607  O   VAL B   7       9.600   3.239 -14.586  1.00 28.08           O  
ANISOU 1607  O   VAL B   7     3290   4296   3082   -557    657    625       O  
ATOM   1608  CB  VAL B   7       9.516   4.501 -11.979  1.00 29.40           C  
ANISOU 1608  CB  VAL B   7     3591   3984   3596   -547    641    511       C  
ATOM   1609  CG1 VAL B   7      10.882   3.930 -11.597  1.00 29.24           C  
ANISOU 1609  CG1 VAL B   7     3481   4123   3505   -613    664    391       C  
ATOM   1610  CG2 VAL B   7       8.995   5.423 -10.871  1.00 32.18           C  
ANISOU 1610  CG2 VAL B   7     4063   4040   4126   -530    639    482       C  
ATOM   1611  N   VAL B   8      11.296   4.667 -14.943  1.00 29.40           N  
ANISOU 1611  N   VAL B   8     3398   4523   3250   -816    719    791       N  
ATOM   1612  CA  VAL B   8      11.890   3.824 -15.973  1.00 37.66           C  
ANISOU 1612  CA  VAL B   8     4346   5880   4082   -828    788    761       C  
ATOM   1613  C   VAL B   8      12.774   2.725 -15.364  1.00 38.07           C  
ANISOU 1613  C   VAL B   8     4295   6050   4118   -751    844    541       C  
ATOM   1614  O   VAL B   8      13.825   2.993 -14.788  1.00 37.29           O  
ANISOU 1614  O   VAL B   8     4112   5968   4089   -828    869    521       O  
ATOM   1615  CB  VAL B   8      12.644   4.669 -17.021  1.00 38.87           C  
ANISOU 1615  CB  VAL B   8     4448   6190   4131  -1018    841    966       C  
ATOM   1616  CG1 VAL B   8      13.337   3.785 -18.064  1.00 36.46           C  
ANISOU 1616  CG1 VAL B   8     4039   6234   3579  -1025    954    905       C  
ATOM   1617  CG2 VAL B   8      11.674   5.623 -17.710  1.00 43.32           C  
ANISOU 1617  CG2 VAL B   8     5114   6637   4708  -1076    762   1211       C  
ATOM   1618  N   ILE B   9      12.314   1.484 -15.476  1.00 31.22           N  
ANISOU 1618  N   ILE B   9     3432   5250   3178   -604    845    389       N  
ATOM   1619  CA  ILE B   9      13.104   0.329 -15.072  1.00 31.59           C  
ANISOU 1619  CA  ILE B   9     3379   5405   3219   -507    895    197       C  
ATOM   1620  C   ILE B   9      13.837  -0.184 -16.303  1.00 35.38           C  
ANISOU 1620  C   ILE B   9     3765   6169   3508   -521   1017    166       C  
ATOM   1621  O   ILE B   9      13.209  -0.640 -17.268  1.00 37.29           O  
ANISOU 1621  O   ILE B   9     4074   6504   3589   -492   1029    146       O  
ATOM   1622  CB  ILE B   9      12.211  -0.764 -14.469  1.00 34.12           C  
ANISOU 1622  CB  ILE B   9     3767   5610   3587   -344    828     48       C  
ATOM   1623  CG1 ILE B   9      11.561  -0.260 -13.185  1.00 38.68           C  
ANISOU 1623  CG1 ILE B   9     4426   5939   4332   -332    742     67       C  
ATOM   1624  CG2 ILE B   9      13.006  -2.020 -14.183  1.00 35.95           C  
ANISOU 1624  CG2 ILE B   9     3900   5934   3824   -232    872   -131       C  
ATOM   1625  CD1 ILE B   9      10.686  -1.279 -12.529  1.00 40.40           C  
ANISOU 1625  CD1 ILE B   9     4697   6055   4597   -196    684    -48       C  
ATOM   1626  N   SER B  10      15.162  -0.080 -16.290  1.00 35.08           N  
ANISOU 1626  N   SER B  10     3569   6282   3480   -576   1112    165       N  
ATOM   1627  CA  SER B  10      15.942  -0.352 -17.500  1.00 41.28           C  
ANISOU 1627  CA  SER B  10     4246   7362   4075   -608   1269    157       C  
ATOM   1628  C   SER B  10      15.867  -1.817 -17.902  1.00 41.46           C  
ANISOU 1628  C   SER B  10     4268   7481   4005   -425   1338    -74       C  
ATOM   1629  O   SER B  10      15.547  -2.686 -17.080  1.00 37.27           O  
ANISOU 1629  O   SER B  10     3765   6795   3600   -276   1266   -220       O  
ATOM   1630  CB  SER B  10      17.401   0.062 -17.329  1.00 48.32           C  
ANISOU 1630  CB  SER B  10     4927   8404   5028   -703   1364    217       C  
ATOM   1631  OG  SER B  10      18.055  -0.764 -16.394  1.00 53.73           O  
ANISOU 1631  OG  SER B  10     5486   9062   5866   -571   1358     68       O  
ATOM   1632  N   ASP B  11      16.150  -2.078 -19.173  1.00 40.47           N  
ANISOU 1632  N   ASP B  11     4162   7512   3703   -429   1432   -102       N  
ATOM   1633  CA  ASP B  11      16.164  -3.433 -19.698  1.00 45.20           C  
ANISOU 1633  CA  ASP B  11     4805   8137   4234   -264   1488   -331       C  
ATOM   1634  C   ASP B  11      17.116  -4.353 -18.916  1.00 47.40           C  
ANISOU 1634  C   ASP B  11     4938   8365   4707    -96   1536   -485       C  
ATOM   1635  O   ASP B  11      16.836  -5.539 -18.753  1.00 50.21           O  
ANISOU 1635  O   ASP B  11     5347   8625   5107     66   1521   -673       O  
ATOM   1636  CB  ASP B  11      16.532  -3.423 -21.190  1.00 44.91           C  
ANISOU 1636  CB  ASP B  11     4804   8285   3975   -320   1602   -326       C  
ATOM   1637  CG  ASP B  11      15.473  -2.745 -22.061  1.00 46.41           C  
ANISOU 1637  CG  ASP B  11     5154   8527   3953   -469   1524   -180       C  
ATOM   1638  OD1 ASP B  11      14.281  -2.774 -21.695  1.00 42.08           O  
ANISOU 1638  OD1 ASP B  11     4716   7867   3407   -470   1390   -161       O  
ATOM   1639  OD2 ASP B  11      15.838  -2.196 -23.125  1.00 51.77           O  
ANISOU 1639  OD2 ASP B  11     5839   9367   4465   -586   1592    -69       O  
ATOM   1640  N   ASP B  12      18.224  -3.803 -18.421  1.00 44.45           N  
ANISOU 1640  N   ASP B  12     4378   8048   4462   -145   1578   -389       N  
ATOM   1641  CA  ASP B  12      19.231  -4.600 -17.714  1.00 48.83           C  
ANISOU 1641  CA  ASP B  12     4760   8584   5211      3   1613   -490       C  
ATOM   1642  C   ASP B  12      19.040  -4.669 -16.187  1.00 50.12           C  
ANISOU 1642  C   ASP B  12     4870   8603   5571     39   1473   -485       C  
ATOM   1643  O   ASP B  12      19.905  -5.184 -15.475  1.00 48.78           O  
ANISOU 1643  O   ASP B  12     4532   8427   5575    135   1469   -521       O  
ATOM   1644  CB  ASP B  12      20.652  -4.121 -18.045  1.00 55.80           C  
ANISOU 1644  CB  ASP B  12     5434   9635   6132    -62   1735   -393       C  
ATOM   1645  CG  ASP B  12      20.878  -2.649 -17.713  1.00 59.74           C  
ANISOU 1645  CG  ASP B  12     5872  10177   6650   -297   1677   -163       C  
ATOM   1646  OD1 ASP B  12      20.031  -2.045 -17.020  1.00 56.74           O  
ANISOU 1646  OD1 ASP B  12     5592   9676   6292   -388   1547    -90       O  
ATOM   1647  OD2 ASP B  12      21.914  -2.094 -18.141  1.00 63.33           O  
ANISOU 1647  OD2 ASP B  12     6180  10775   7107   -395   1767    -55       O  
ATOM   1648  N   GLU B  13      17.915  -4.150 -15.697  1.00 46.31           N  
ANISOU 1648  N   GLU B  13     4522   8015   5058    -41   1363   -433       N  
ATOM   1649  CA  GLU B  13      17.582  -4.196 -14.268  1.00 48.97           C  
ANISOU 1649  CA  GLU B  13     4893   8137   5576    -17   1197   -421       C  
ATOM   1650  C   GLU B  13      17.582  -5.630 -13.727  1.00 42.70           C  
ANISOU 1650  C   GLU B  13     4079   7250   4896    196   1162   -587       C  
ATOM   1651  O   GLU B  13      16.816  -6.476 -14.180  1.00 40.46           O  
ANISOU 1651  O   GLU B  13     3922   6900   4550    303   1166   -713       O  
ATOM   1652  CB  GLU B  13      16.221  -3.541 -14.019  1.00 53.62           C  
ANISOU 1652  CB  GLU B  13     5706   8531   6134    -98   1074   -343       C  
ATOM   1653  CG  GLU B  13      15.598  -3.866 -12.662  1.00 59.04           C  
ANISOU 1653  CG  GLU B  13     6480   8989   6965    -39    924   -374       C  
ATOM   1654  CD  GLU B  13      16.327  -3.202 -11.512  1.00 64.89           C  
ANISOU 1654  CD  GLU B  13     7142   9685   7829   -135    851   -295       C  
ATOM   1655  OE1 GLU B  13      16.526  -3.871 -10.472  1.00 66.45           O  
ANISOU 1655  OE1 GLU B  13     7306   9808   8133    -59    766   -347       O  
ATOM   1656  OE2 GLU B  13      16.695  -2.013 -11.651  1.00 66.92           O  
ANISOU 1656  OE2 GLU B  13     7379   9977   8070   -303    866   -174       O  
ATOM   1657  N   PRO B  14      18.455  -5.907 -12.753  1.00 46.99           N  
ANISOU 1657  N   PRO B  14     4461   7779   5613    244   1109   -572       N  
ATOM   1658  CA  PRO B  14      18.590  -7.275 -12.242  1.00 46.79           C  
ANISOU 1658  CA  PRO B  14     4392   7661   5725    450   1069   -696       C  
ATOM   1659  C   PRO B  14      17.513  -7.658 -11.228  1.00 40.95           C  
ANISOU 1659  C   PRO B  14     3836   6675   5047    473    892   -697       C  
ATOM   1660  O   PRO B  14      17.355  -8.846 -10.955  1.00 43.54           O  
ANISOU 1660  O   PRO B  14     4182   6893   5470    632    851   -793       O  
ATOM   1661  CB  PRO B  14      19.962  -7.254 -11.566  1.00 49.99           C  
ANISOU 1661  CB  PRO B  14     4531   8169   6294    462   1055   -621       C  
ATOM   1662  CG  PRO B  14      20.107  -5.838 -11.093  1.00 52.62           C  
ANISOU 1662  CG  PRO B  14     4866   8532   6597    219    981   -453       C  
ATOM   1663  CD  PRO B  14      19.435  -4.987 -12.150  1.00 51.51           C  
ANISOU 1663  CD  PRO B  14     4869   8434   6266     98   1075   -427       C  
ATOM   1664  N   GLY B  15      16.783  -6.688 -10.685  1.00 33.46           N  
ANISOU 1664  N   GLY B  15     3022   5637   4055    320    799   -593       N  
ATOM   1665  CA  GLY B  15      15.821  -6.985  -9.634  1.00 33.35           C  
ANISOU 1665  CA  GLY B  15     3157   5421   4093    332    657   -584       C  
ATOM   1666  C   GLY B  15      16.541  -7.396  -8.354  1.00 36.70           C  
ANISOU 1666  C   GLY B  15     3478   5811   4657    360    543   -543       C  
ATOM   1667  O   GLY B  15      17.753  -7.212  -8.244  1.00 39.26           O  
ANISOU 1667  O   GLY B  15     3609   6264   5043    340    557   -499       O  
ATOM   1668  N   TYR B  16      15.806  -7.956  -7.394  1.00 29.04           N  
ANISOU 1668  N   TYR B  16     2621   4683   3730    394    424   -538       N  
ATOM   1669  CA  TYR B  16      16.388  -8.315  -6.092  1.00 31.79           C  
ANISOU 1669  CA  TYR B  16     2897   5003   4178    393    288   -469       C  
ATOM   1670  C   TYR B  16      16.286  -9.798  -5.760  1.00 32.43           C  
ANISOU 1670  C   TYR B  16     2966   4978   4379    563    218   -501       C  
ATOM   1671  O   TYR B  16      15.330 -10.463  -6.172  1.00 30.18           O  
ANISOU 1671  O   TYR B  16     2809   4578   4081    638    238   -574       O  
ATOM   1672  CB  TYR B  16      15.665  -7.548  -5.001  1.00 30.60           C  
ANISOU 1672  CB  TYR B  16     2905   4765   3955    245    198   -405       C  
ATOM   1673  CG  TYR B  16      15.703  -6.054  -5.164  1.00 30.58           C  
ANISOU 1673  CG  TYR B  16     2947   4806   3866     75    247   -373       C  
ATOM   1674  CD1 TYR B  16      16.765  -5.323  -4.674  1.00 33.60           C  
ANISOU 1674  CD1 TYR B  16     3225   5280   4262    -59    195   -310       C  
ATOM   1675  CD2 TYR B  16      14.677  -5.380  -5.803  1.00 27.51           C  
ANISOU 1675  CD2 TYR B  16     2700   4353   3400     41    328   -392       C  
ATOM   1676  CE1 TYR B  16      16.814  -3.959  -4.805  1.00 32.78           C  
ANISOU 1676  CE1 TYR B  16     3177   5178   4098   -229    228   -281       C  
ATOM   1677  CE2 TYR B  16      14.712  -3.995  -5.941  1.00 30.97           C  
ANISOU 1677  CE2 TYR B  16     3187   4792   3790   -109    365   -348       C  
ATOM   1678  CZ  TYR B  16      15.790  -3.300  -5.437  1.00 32.60           C  
ANISOU 1678  CZ  TYR B  16     3307   5066   4014   -246    317   -300       C  
ATOM   1679  OH  TYR B  16      15.859  -1.935  -5.562  1.00 36.23           O  
ANISOU 1679  OH  TYR B  16     3827   5493   4445   -409    343   -257       O  
ATOM   1680  N   ASP B  17      17.261 -10.309  -5.002  1.00 35.39           N  
ANISOU 1680  N   ASP B  17     3184   5382   4881    612    118   -430       N  
ATOM   1681  CA  ASP B  17      17.229 -11.701  -4.524  1.00 35.39           C  
ANISOU 1681  CA  ASP B  17     3168   5251   5027    768     21   -419       C  
ATOM   1682  C   ASP B  17      15.969 -11.889  -3.678  1.00 28.89           C  
ANISOU 1682  C   ASP B  17     2564   4279   4135    696    -79   -374       C  
ATOM   1683  O   ASP B  17      15.658 -11.051  -2.835  1.00 27.24           O  
ANISOU 1683  O   ASP B  17     2440   4098   3813    534   -136   -300       O  
ATOM   1684  CB  ASP B  17      18.492 -12.026  -3.698  1.00 39.53           C  
ANISOU 1684  CB  ASP B  17     3474   5846   5700    804   -105   -294       C  
ATOM   1685  CG  ASP B  17      18.628 -13.522  -3.364  1.00 49.10           C  
ANISOU 1685  CG  ASP B  17     4635   6907   7112   1001   -200   -266       C  
ATOM   1686  OD1 ASP B  17      17.641 -14.140  -2.908  1.00 48.92           O  
ANISOU 1686  OD1 ASP B  17     4793   6714   7078   1003   -278   -250       O  
ATOM   1687  OD2 ASP B  17      19.733 -14.083  -3.553  1.00 57.87           O  
ANISOU 1687  OD2 ASP B  17     5513   8064   8413   1156   -195   -247       O  
ATOM   1688  N   LEU B  18      15.247 -12.981  -3.901  1.00 26.73           N  
ANISOU 1688  N   LEU B  18     2380   3847   3928    809    -92   -424       N  
ATOM   1689  CA  LEU B  18      14.010 -13.266  -3.157  1.00 26.80           C  
ANISOU 1689  CA  LEU B  18     2571   3726   3885    738   -174   -366       C  
ATOM   1690  C   LEU B  18      14.274 -13.354  -1.649  1.00 27.19           C  
ANISOU 1690  C   LEU B  18     2613   3781   3938    659   -335   -200       C  
ATOM   1691  O   LEU B  18      13.393 -13.066  -0.834  1.00 29.54           O  
ANISOU 1691  O   LEU B  18     3050   4053   4119    538   -373   -136       O  
ATOM   1692  CB  LEU B  18      13.428 -14.599  -3.619  1.00 27.44           C  
ANISOU 1692  CB  LEU B  18     2717   3626   4082    868   -191   -429       C  
ATOM   1693  CG  LEU B  18      13.071 -14.749  -5.088  1.00 32.26           C  
ANISOU 1693  CG  LEU B  18     3371   4218   4667    937    -59   -607       C  
ATOM   1694  CD1 LEU B  18      12.716 -16.187  -5.385  1.00 35.76           C  
ANISOU 1694  CD1 LEU B  18     3878   4455   5254   1060   -107   -677       C  
ATOM   1695  CD2 LEU B  18      11.914 -13.858  -5.422  1.00 32.46           C  
ANISOU 1695  CD2 LEU B  18     3529   4284   4521    800     -1   -619       C  
ATOM   1696  N   ASP B  19      15.480 -13.780  -1.291  1.00 26.52           N  
ANISOU 1696  N   ASP B  19     2354   3739   3982    730   -426   -124       N  
ATOM   1697  CA  ASP B  19      15.816 -14.068   0.102  1.00 27.59           C  
ANISOU 1697  CA  ASP B  19     2470   3885   4129    662   -615     58       C  
ATOM   1698  C   ASP B  19      15.988 -12.804   0.937  1.00 31.67           C  
ANISOU 1698  C   ASP B  19     3026   4556   4452    447   -653    113       C  
ATOM   1699  O   ASP B  19      16.163 -12.875   2.157  1.00 31.24           O  
ANISOU 1699  O   ASP B  19     2994   4540   4335    341   -811    255       O  
ATOM   1700  CB  ASP B  19      17.091 -14.917   0.178  1.00 37.67           C  
ANISOU 1700  CB  ASP B  19     3517   5161   5633    816   -719    143       C  
ATOM   1701  CG  ASP B  19      16.934 -16.269  -0.509  1.00 50.95           C  
ANISOU 1701  CG  ASP B  19     5187   6641   7531   1041   -692     78       C  
ATOM   1702  OD1 ASP B  19      15.896 -16.931  -0.271  1.00 51.72           O  
ANISOU 1702  OD1 ASP B  19     5457   6571   7622   1029   -734     96       O  
ATOM   1703  OD2 ASP B  19      17.839 -16.655  -1.292  1.00 55.36           O  
ANISOU 1703  OD2 ASP B  19     5565   7206   8265   1222   -620      1       O  
ATOM   1704  N   LEU B  20      15.940 -11.650   0.282  1.00 26.05           N  
ANISOU 1704  N   LEU B  20     2335   3925   3638    371   -516      1       N  
ATOM   1705  CA  LEU B  20      16.081 -10.387   0.999  1.00 25.90           C  
ANISOU 1705  CA  LEU B  20     2380   4013   3448    162   -542     22       C  
ATOM   1706  C   LEU B  20      14.715  -9.818   1.365  1.00 26.67           C  
ANISOU 1706  C   LEU B  20     2717   4040   3377     63   -466    -29       C  
ATOM   1707  O   LEU B  20      14.625  -8.836   2.108  1.00 24.42           O  
ANISOU 1707  O   LEU B  20     2537   3804   2938   -104   -477    -35       O  
ATOM   1708  CB  LEU B  20      16.898  -9.390   0.173  1.00 26.26           C  
ANISOU 1708  CB  LEU B  20     2303   4171   3502    118   -451    -42       C  
ATOM   1709  CG  LEU B  20      18.344  -9.829  -0.011  1.00 28.11           C  
ANISOU 1709  CG  LEU B  20     2263   4517   3900    195   -522     29       C  
ATOM   1710  CD1 LEU B  20      19.057  -9.009  -1.085  1.00 40.05           C  
ANISOU 1710  CD1 LEU B  20     3634   6148   5436    175   -387    -34       C  
ATOM   1711  CD2 LEU B  20      19.081  -9.715   1.301  1.00 34.54           C  
ANISOU 1711  CD2 LEU B  20     3018   5422   4682     53   -735    176       C  
ATOM   1712  N   PHE B  21      13.660 -10.461   0.863  1.00 25.34           N  
ANISOU 1712  N   PHE B  21     2628   3754   3246    166   -391    -69       N  
ATOM   1713  CA  PHE B  21      12.281 -10.023   1.094  1.00 25.78           C  
ANISOU 1713  CA  PHE B  21     2867   3748   3180    103   -302   -104       C  
ATOM   1714  C   PHE B  21      11.421 -11.112   1.695  1.00 24.45           C  
ANISOU 1714  C   PHE B  21     2771   3492   3026    133   -360    -21       C  
ATOM   1715  O   PHE B  21      11.851 -12.274   1.809  1.00 24.22           O  
ANISOU 1715  O   PHE B  21     2666   3414   3121    217   -474     59       O  
ATOM   1716  CB  PHE B  21      11.663  -9.545  -0.229  1.00 27.39           C  
ANISOU 1716  CB  PHE B  21     3086   3913   3406    161   -149   -213       C  
ATOM   1717  CG  PHE B  21      12.360  -8.357  -0.795  1.00 28.60           C  
ANISOU 1717  CG  PHE B  21     3191   4147   3529    101    -82   -269       C  
ATOM   1718  CD1 PHE B  21      11.959  -7.076  -0.444  1.00 32.57           C  
ANISOU 1718  CD1 PHE B  21     3806   4646   3924    -21    -19   -297       C  
ATOM   1719  CD2 PHE B  21      13.466  -8.512  -1.611  1.00 31.44           C  
ANISOU 1719  CD2 PHE B  21     3387   4581   3977    162    -78   -286       C  
ATOM   1720  CE1 PHE B  21      12.622  -5.968  -0.935  1.00 37.49           C  
ANISOU 1720  CE1 PHE B  21     4393   5317   4535    -98     27   -329       C  
ATOM   1721  CE2 PHE B  21      14.135  -7.412  -2.097  1.00 38.21           C  
ANISOU 1721  CE2 PHE B  21     4189   5524   4806     80    -20   -309       C  
ATOM   1722  CZ  PHE B  21      13.713  -6.139  -1.771  1.00 39.59           C  
ANISOU 1722  CZ  PHE B  21     4489   5675   4881    -59     22   -323       C  
ATOM   1723  N   CYS B  22      10.212 -10.731   2.110  1.00 23.98           N  
ANISOU 1723  N   CYS B  22     2850   3408   2855     65   -279    -27       N  
ATOM   1724  CA  CYS B  22       9.232 -11.697   2.593  1.00 26.88           C  
ANISOU 1724  CA  CYS B  22     3278   3702   3232     72   -308     63       C  
ATOM   1725  C   CYS B  22       8.403 -12.131   1.402  1.00 27.60           C  
ANISOU 1725  C   CYS B  22     3357   3693   3438    169   -235      2       C  
ATOM   1726  O   CYS B  22       7.807 -11.302   0.716  1.00 26.51           O  
ANISOU 1726  O   CYS B  22     3243   3563   3268    169   -112    -83       O  
ATOM   1727  CB  CYS B  22       8.338 -11.089   3.682  1.00 26.00           C  
ANISOU 1727  CB  CYS B  22     3300   3643   2936    -54   -238     91       C  
ATOM   1728  N   ILE B  23       8.370 -13.436   1.162  1.00 24.77           N  
ANISOU 1728  N   ILE B  23     2967   3229   3216    245   -326     52       N  
ATOM   1729  CA  ILE B  23       7.694 -14.016   0.002  1.00 25.62           C  
ANISOU 1729  CA  ILE B  23     3074   3231   3431    321   -292    -19       C  
ATOM   1730  C   ILE B  23       6.943 -15.252   0.490  1.00 27.20           C  
ANISOU 1730  C   ILE B  23     3319   3309   3709    301   -385     98       C  
ATOM   1731  O   ILE B  23       7.476 -15.997   1.308  1.00 29.03           O  
ANISOU 1731  O   ILE B  23     3539   3501   3990    301   -506    215       O  
ATOM   1732  CB  ILE B  23       8.746 -14.438  -1.062  1.00 35.58           C  
ANISOU 1732  CB  ILE B  23     4246   4459   4815    453   -308   -127       C  
ATOM   1733  CG1 ILE B  23       9.092 -13.262  -1.971  1.00 36.40           C  
ANISOU 1733  CG1 ILE B  23     4313   4675   4842    457   -185   -245       C  
ATOM   1734  CG2 ILE B  23       8.269 -15.596  -1.911  1.00 33.84           C  
ANISOU 1734  CG2 ILE B  23     4051   4083   4724    531   -340   -183       C  
ATOM   1735  CD1 ILE B  23      10.360 -12.600  -1.593  1.00 43.77           C  
ANISOU 1735  CD1 ILE B  23     5160   5722   5749    443   -195   -236       C  
ATOM   1736  N   PRO B  24       5.722 -15.493  -0.022  1.00 28.54           N  
ANISOU 1736  N   PRO B  24     3528   3416   3900    273   -345     88       N  
ATOM   1737  CA  PRO B  24       4.986 -16.703   0.392  1.00 29.21           C  
ANISOU 1737  CA  PRO B  24     3651   3373   4076    228   -443    213       C  
ATOM   1738  C   PRO B  24       5.790 -17.958   0.082  1.00 30.46           C  
ANISOU 1738  C   PRO B  24     3797   3360   4418    328   -577    203       C  
ATOM   1739  O   PRO B  24       6.249 -18.081  -1.062  1.00 28.91           O  
ANISOU 1739  O   PRO B  24     3579   3111   4296    434   -554     39       O  
ATOM   1740  CB  PRO B  24       3.753 -16.697  -0.517  1.00 32.72           C  
ANISOU 1740  CB  PRO B  24     4109   3781   4542    194   -390    162       C  
ATOM   1741  CG  PRO B  24       3.644 -15.329  -1.073  1.00 30.28           C  
ANISOU 1741  CG  PRO B  24     3776   3607   4123    205   -254     61       C  
ATOM   1742  CD  PRO B  24       5.006 -14.713  -1.048  1.00 27.95           C  
ANISOU 1742  CD  PRO B  24     3454   3382   3783    272   -233    -16       C  
ATOM   1743  N   ASN B  25       5.936 -18.879   1.039  1.00 30.03           N  
ANISOU 1743  N   ASN B  25     3758   3215   4438    300   -706    373       N  
ATOM   1744  CA  ASN B  25       6.733 -20.081   0.797  1.00 38.07           C  
ANISOU 1744  CA  ASN B  25     4758   4034   5672    420   -837    375       C  
ATOM   1745  C   ASN B  25       6.239 -20.899  -0.396  1.00 33.57           C  
ANISOU 1745  C   ASN B  25     4240   3264   5250    473   -848    233       C  
ATOM   1746  O   ASN B  25       7.037 -21.553  -1.063  1.00 32.98           O  
ANISOU 1746  O   ASN B  25     4149   3046   5335    623   -881    113       O  
ATOM   1747  CB  ASN B  25       6.859 -20.963   2.054  1.00 43.35           C  
ANISOU 1747  CB  ASN B  25     5443   4619   6409    366   -997    627       C  
ATOM   1748  CG  ASN B  25       7.614 -22.270   1.782  1.00 56.05           C  
ANISOU 1748  CG  ASN B  25     7033   5969   8295    513  -1140    642       C  
ATOM   1749  OD1 ASN B  25       7.012 -23.347   1.713  1.00 61.77           O  
ANISOU 1749  OD1 ASN B  25     7829   6466   9173    486  -1233    707       O  
ATOM   1750  ND2 ASN B  25       8.934 -22.174   1.615  1.00 52.48           N  
ANISOU 1750  ND2 ASN B  25     6475   5539   7924    670  -1155    582       N  
ATOM   1751  N   HIS B  26       4.940 -20.845  -0.690  1.00 33.29           N  
ANISOU 1751  N   HIS B  26     4262   3225   5160    351   -815    236       N  
ATOM   1752  CA  HIS B  26       4.402 -21.653  -1.789  1.00 33.65           C  
ANISOU 1752  CA  HIS B  26     4374   3084   5326    359   -856    105       C  
ATOM   1753  C   HIS B  26       4.876 -21.186  -3.171  1.00 32.45           C  
ANISOU 1753  C   HIS B  26     4216   2981   5131    469   -757   -157       C  
ATOM   1754  O   HIS B  26       4.717 -21.896  -4.163  1.00 39.71           O  
ANISOU 1754  O   HIS B  26     5208   3747   6134    499   -789   -314       O  
ATOM   1755  CB  HIS B  26       2.865 -21.787  -1.732  1.00 32.62           C  
ANISOU 1755  CB  HIS B  26     4283   2948   5165    176   -876    206       C  
ATOM   1756  CG  HIS B  26       2.121 -20.496  -1.880  1.00 32.42           C  
ANISOU 1756  CG  HIS B  26     4205   3160   4953    104   -739    198       C  
ATOM   1757  ND1 HIS B  26       1.798 -19.690  -0.808  1.00 34.77           N  
ANISOU 1757  ND1 HIS B  26     4455   3636   5121     35   -658    348       N  
ATOM   1758  CD2 HIS B  26       1.577 -19.899  -2.971  1.00 33.25           C  
ANISOU 1758  CD2 HIS B  26     4302   3343   4989     89   -675     68       C  
ATOM   1759  CE1 HIS B  26       1.130 -18.634  -1.237  1.00 33.57           C  
ANISOU 1759  CE1 HIS B  26     4260   3637   4857      7   -538    299       C  
ATOM   1760  NE2 HIS B  26       0.979 -18.738  -2.543  1.00 36.09           N  
ANISOU 1760  NE2 HIS B  26     4595   3904   5214     35   -557    149       N  
ATOM   1761  N   TYR B  27       5.470 -20.003  -3.231  1.00 27.55           N  
ANISOU 1761  N   TYR B  27     3522   2576   4371    513   -638   -206       N  
ATOM   1762  CA  TYR B  27       6.057 -19.519  -4.481  1.00 27.72           C  
ANISOU 1762  CA  TYR B  27     3524   2673   4336    609   -535   -423       C  
ATOM   1763  C   TYR B  27       7.594 -19.467  -4.444  1.00 32.26           C  
ANISOU 1763  C   TYR B  27     4006   3281   4969    769   -499   -485       C  
ATOM   1764  O   TYR B  27       8.213 -18.881  -5.331  1.00 32.86           O  
ANISOU 1764  O   TYR B  27     4036   3475   4974    839   -387   -634       O  
ATOM   1765  CB  TYR B  27       5.518 -18.131  -4.821  1.00 23.31           C  
ANISOU 1765  CB  TYR B  27     2942   2332   3585    526   -421   -431       C  
ATOM   1766  CG  TYR B  27       4.058 -18.081  -5.221  1.00 24.33           C  
ANISOU 1766  CG  TYR B  27     3122   2456   3666    395   -440   -400       C  
ATOM   1767  CD1 TYR B  27       3.485 -19.083  -5.989  1.00 25.36           C  
ANISOU 1767  CD1 TYR B  27     3333   2433   3870    362   -527   -481       C  
ATOM   1768  CD2 TYR B  27       3.263 -17.021  -4.827  1.00 24.06           C  
ANISOU 1768  CD2 TYR B  27     3049   2569   3524    306   -374   -290       C  
ATOM   1769  CE1 TYR B  27       2.141 -19.025  -6.352  1.00 24.26           C  
ANISOU 1769  CE1 TYR B  27     3215   2310   3694    221   -568   -429       C  
ATOM   1770  CE2 TYR B  27       1.927 -16.949  -5.185  1.00 23.85           C  
ANISOU 1770  CE2 TYR B  27     3028   2555   3480    198   -392   -235       C  
ATOM   1771  CZ  TYR B  27       1.373 -17.956  -5.944  1.00 24.06           C  
ANISOU 1771  CZ  TYR B  27     3115   2451   3577    146   -500   -293       C  
ATOM   1772  OH  TYR B  27       0.035 -17.885  -6.304  1.00 25.02           O  
ANISOU 1772  OH  TYR B  27     3217   2603   3688     19   -543   -218       O  
ATOM   1773  N   ALA B  28       8.207 -20.080  -3.436  1.00 32.20           N  
ANISOU 1773  N   ALA B  28     3956   3186   5094    820   -598   -349       N  
ATOM   1774  CA  ALA B  28       9.664 -19.981  -3.253  1.00 37.43           C  
ANISOU 1774  CA  ALA B  28     4487   3905   5829    963   -585   -359       C  
ATOM   1775  C   ALA B  28      10.496 -20.414  -4.469  1.00 39.73           C  
ANISOU 1775  C   ALA B  28     4735   4136   6223   1146   -499   -586       C  
ATOM   1776  O   ALA B  28      11.576 -19.871  -4.715  1.00 41.19           O  
ANISOU 1776  O   ALA B  28     4785   4467   6396   1239   -412   -640       O  
ATOM   1777  CB  ALA B  28      10.105 -20.764  -2.019  1.00 38.29           C  
ANISOU 1777  CB  ALA B  28     4558   3901   6090    988   -744   -149       C  
ATOM   1778  N   GLU B  29      10.006 -21.404  -5.211  1.00 35.94           N  
ANISOU 1778  N   GLU B  29     4370   3443   5842   1190   -518   -722       N  
ATOM   1779  CA  GLU B  29      10.760 -21.966  -6.335  1.00 40.82           C  
ANISOU 1779  CA  GLU B  29     4977   3978   6557   1375   -423   -969       C  
ATOM   1780  C   GLU B  29      10.231 -21.465  -7.680  1.00 39.91           C  
ANISOU 1780  C   GLU B  29     4952   3975   6236   1312   -294  -1186       C  
ATOM   1781  O   GLU B  29      10.793 -21.757  -8.736  1.00 42.71           O  
ANISOU 1781  O   GLU B  29     5314   4318   6595   1439   -178  -1418       O  
ATOM   1782  CB  GLU B  29      10.729 -23.497  -6.288  1.00 48.79           C  
ANISOU 1782  CB  GLU B  29     6073   4635   7830   1484   -534  -1009       C  
ATOM   1783  CG  GLU B  29      11.745 -24.135  -5.330  1.00 59.92           C  
ANISOU 1783  CG  GLU B  29     7349   5921   9497   1643   -631   -847       C  
ATOM   1784  CD  GLU B  29      11.168 -24.480  -3.960  1.00 69.21           C  
ANISOU 1784  CD  GLU B  29     8560   7000  10736   1508   -831   -540       C  
ATOM   1785  OE1 GLU B  29      10.044 -25.028  -3.893  1.00 72.64           O  
ANISOU 1785  OE1 GLU B  29     9154   7269  11178   1371   -920   -502       O  
ATOM   1786  OE2 GLU B  29      11.851 -24.212  -2.948  1.00 70.59           O  
ANISOU 1786  OE2 GLU B  29     8600   7279  10944   1524   -903   -327       O  
ATOM   1787  N   ASP B  30       9.159 -20.687  -7.623  1.00 36.58           N  
ANISOU 1787  N   ASP B  30     4591   3676   5631   1118   -311  -1099       N  
ATOM   1788  CA  ASP B  30       8.426 -20.272  -8.813  1.00 36.02           C  
ANISOU 1788  CA  ASP B  30     4617   3699   5370   1023   -243  -1246       C  
ATOM   1789  C   ASP B  30       8.783 -18.867  -9.286  1.00 37.09           C  
ANISOU 1789  C   ASP B  30     4665   4126   5300    991   -104  -1252       C  
ATOM   1790  O   ASP B  30       8.342 -18.439 -10.355  1.00 36.65           O  
ANISOU 1790  O   ASP B  30     4673   4179   5072    921    -42  -1359       O  
ATOM   1791  CB  ASP B  30       6.929 -20.359  -8.528  1.00 34.44           C  
ANISOU 1791  CB  ASP B  30     4519   3435   5132    833   -364  -1126       C  
ATOM   1792  CG  ASP B  30       6.518 -21.732  -8.032  1.00 41.97           C  
ANISOU 1792  CG  ASP B  30     5562   4093   6292    828   -515  -1088       C  
ATOM   1793  OD1 ASP B  30       7.111 -22.720  -8.504  1.00 44.41           O  
ANISOU 1793  OD1 ASP B  30     5928   4208   6740    961   -519  -1259       O  
ATOM   1794  OD2 ASP B  30       5.614 -21.820  -7.171  1.00 43.35           O  
ANISOU 1794  OD2 ASP B  30     5750   4225   6497    693   -619   -886       O  
ATOM   1795  N   LEU B  31       9.571 -18.150  -8.481  1.00 34.07           N  
ANISOU 1795  N   LEU B  31     4143   3867   4934   1021    -71  -1122       N  
ATOM   1796  CA  LEU B  31       9.985 -16.782  -8.809  1.00 33.14           C  
ANISOU 1796  CA  LEU B  31     3940   3999   4651    974     48  -1104       C  
ATOM   1797  C   LEU B  31      11.497 -16.726  -8.986  1.00 36.06           C  
ANISOU 1797  C   LEU B  31     4155   4463   5082   1118    149  -1169       C  
ATOM   1798  O   LEU B  31      12.229 -17.490  -8.358  1.00 39.99           O  
ANISOU 1798  O   LEU B  31     4573   4852   5769   1242     97  -1143       O  
ATOM   1799  CB  LEU B  31       9.557 -15.798  -7.720  1.00 29.34           C  
ANISOU 1799  CB  LEU B  31     3432   3597   4118    849      3   -899       C  
ATOM   1800  CG  LEU B  31       8.077 -15.812  -7.380  1.00 29.67           C  
ANISOU 1800  CG  LEU B  31     3582   3567   4125    721    -76   -805       C  
ATOM   1801  CD1 LEU B  31       7.776 -14.842  -6.250  1.00 27.15           C  
ANISOU 1801  CD1 LEU B  31     3235   3327   3755    627    -81   -635       C  
ATOM   1802  CD2 LEU B  31       7.289 -15.473  -8.636  1.00 29.68           C  
ANISOU 1802  CD2 LEU B  31     3654   3629   3994    655    -33   -894       C  
ATOM   1803  N   GLU B  32      11.959 -15.836  -9.858  1.00 35.89           N  
ANISOU 1803  N   GLU B  32     4078   4647   4912   1097    289  -1235       N  
ATOM   1804  CA  GLU B  32      13.384 -15.716 -10.120  1.00 38.01           C  
ANISOU 1804  CA  GLU B  32     4170   5043   5230   1218    408  -1289       C  
ATOM   1805  C   GLU B  32      13.954 -14.578  -9.276  1.00 35.23           C  
ANISOU 1805  C   GLU B  32     3682   4840   4862   1129    392  -1105       C  
ATOM   1806  O   GLU B  32      14.986 -14.733  -8.620  1.00 39.65           O  
ANISOU 1806  O   GLU B  32     4079   5423   5561   1208    368  -1039       O  
ATOM   1807  CB  GLU B  32      13.634 -15.449 -11.606  1.00 39.54           C  
ANISOU 1807  CB  GLU B  32     4374   5395   5254   1231    586  -1463       C  
ATOM   1808  CG  GLU B  32      15.078 -15.618 -12.034  1.00 45.32           C  
ANISOU 1808  CG  GLU B  32     4918   6246   6056   1385    742  -1552       C  
ATOM   1809  CD  GLU B  32      15.560 -17.055 -11.934  1.00 55.76           C  
ANISOU 1809  CD  GLU B  32     6242   7352   7593   1568    728  -1634       C  
ATOM   1810  OE1 GLU B  32      14.714 -17.974 -11.962  1.00 58.10           O  
ANISOU 1810  OE1 GLU B  32     6712   7427   7938   1589    638  -1723       O  
ATOM   1811  OE2 GLU B  32      16.787 -17.267 -11.833  1.00 61.45           O  
ANISOU 1811  OE2 GLU B  32     6785   8117   8447   1689    806  -1599       O  
ATOM   1812  N   ARG B  33      13.273 -13.437  -9.306  1.00 30.91           N  
ANISOU 1812  N   ARG B  33     3205   4385   4153    961    396  -1023       N  
ATOM   1813  CA  ARG B  33      13.726 -12.222  -8.620  1.00 31.71           C  
ANISOU 1813  CA  ARG B  33     3221   4611   4218    848    389   -879       C  
ATOM   1814  C   ARG B  33      12.528 -11.387  -8.214  1.00 29.55           C  
ANISOU 1814  C   ARG B  33     3085   4300   3841    698    337   -785       C  
ATOM   1815  O   ARG B  33      11.485 -11.437  -8.869  1.00 32.15           O  
ANISOU 1815  O   ARG B  33     3534   4590   4092    666    347   -824       O  
ATOM   1816  CB  ARG B  33      14.573 -11.368  -9.573  1.00 33.79           C  
ANISOU 1816  CB  ARG B  33     3372   5083   4384    819    537   -911       C  
ATOM   1817  CG  ARG B  33      15.711 -12.081 -10.265  1.00 41.51           C  
ANISOU 1817  CG  ARG B  33     4195   6140   5435    977    653  -1030       C  
ATOM   1818  CD  ARG B  33      16.838 -12.359  -9.300  1.00 46.91           C  
ANISOU 1818  CD  ARG B  33     4681   6834   6308   1054    591   -945       C  
ATOM   1819  NE  ARG B  33      17.565 -11.141  -8.957  1.00 47.46           N  
ANISOU 1819  NE  ARG B  33     4619   7075   6338    913    597   -813       N  
ATOM   1820  CZ  ARG B  33      18.613 -11.105  -8.144  1.00 50.45           C  
ANISOU 1820  CZ  ARG B  33     4803   7515   6850    922    527   -708       C  
ATOM   1821  NH1 ARG B  33      19.055 -12.226  -7.590  1.00 53.13           N  
ANISOU 1821  NH1 ARG B  33     5048   7758   7382   1087    446   -703       N  
ATOM   1822  NH2 ARG B  33      19.218  -9.951  -7.891  1.00 48.89           N  
ANISOU 1822  NH2 ARG B  33     4506   7467   6605    758    522   -596       N  
ATOM   1823  N   VAL B  34      12.665 -10.592  -7.156  1.00 24.70           N  
ANISOU 1823  N   VAL B  34     2454   3705   3227    602    284   -665       N  
ATOM   1824  CA  VAL B  34      11.712  -9.496  -6.946  1.00 23.27           C  
ANISOU 1824  CA  VAL B  34     2381   3514   2945    472    291   -597       C  
ATOM   1825  C   VAL B  34      12.082  -8.389  -7.944  1.00 25.92           C  
ANISOU 1825  C   VAL B  34     2680   3980   3187    405    397   -601       C  
ATOM   1826  O   VAL B  34      13.258  -8.048  -8.074  1.00 25.92           O  
ANISOU 1826  O   VAL B  34     2553   4094   3199    392    439   -595       O  
ATOM   1827  CB  VAL B  34      11.786  -8.944  -5.533  1.00 25.11           C  
ANISOU 1827  CB  VAL B  34     2633   3722   3185    384    220   -503       C  
ATOM   1828  CG1 VAL B  34      10.873  -7.724  -5.397  1.00 26.94           C  
ANISOU 1828  CG1 VAL B  34     2974   3928   3332    276    262   -462       C  
ATOM   1829  CG2 VAL B  34      11.383 -10.014  -4.550  1.00 27.19           C  
ANISOU 1829  CG2 VAL B  34     2938   3878   3515    428    114   -467       C  
ATOM   1830  N   PHE B  35      11.092  -7.843  -8.654  1.00 25.73           N  
ANISOU 1830  N   PHE B  35     2752   3946   3079    354    433   -586       N  
ATOM   1831  CA  PHE B  35      11.359  -6.883  -9.724  1.00 27.87           C  
ANISOU 1831  CA  PHE B  35     2999   4337   3253    285    522   -562       C  
ATOM   1832  C   PHE B  35      10.979  -5.475  -9.274  1.00 29.01           C  
ANISOU 1832  C   PHE B  35     3197   4438   3388    167    520   -450       C  
ATOM   1833  O   PHE B  35      11.754  -4.525  -9.415  1.00 29.12           O  
ANISOU 1833  O   PHE B  35     3158   4522   3385     80    563   -398       O  
ATOM   1834  CB  PHE B  35      10.588  -7.289 -10.988  1.00 29.53           C  
ANISOU 1834  CB  PHE B  35     3276   4577   3367    308    547   -611       C  
ATOM   1835  CG  PHE B  35      11.120  -6.675 -12.256  1.00 31.87           C  
ANISOU 1835  CG  PHE B  35     3533   5044   3533    253    647   -603       C  
ATOM   1836  CD1 PHE B  35      12.412  -6.938 -12.679  1.00 32.26           C  
ANISOU 1836  CD1 PHE B  35     3460   5235   3564    292    744   -673       C  
ATOM   1837  CD2 PHE B  35      10.306  -5.865 -13.043  1.00 36.14           C  
ANISOU 1837  CD2 PHE B  35     4147   5614   3970    163    647   -509       C  
ATOM   1838  CE1 PHE B  35      12.908  -6.383 -13.864  1.00 37.45           C  
ANISOU 1838  CE1 PHE B  35     4075   6078   4076    227    857   -656       C  
ATOM   1839  CE2 PHE B  35      10.783  -5.304 -14.223  1.00 35.31           C  
ANISOU 1839  CE2 PHE B  35     4014   5682   3720     92    732   -473       C  
ATOM   1840  CZ  PHE B  35      12.088  -5.562 -14.634  1.00 39.83           C  
ANISOU 1840  CZ  PHE B  35     4473   6413   4249    117    847   -551       C  
ATOM   1841  N   ILE B  36       9.778  -5.346  -8.723  1.00 24.48           N  
ANISOU 1841  N   ILE B  36     2725   3738   2840    165    476   -413       N  
ATOM   1842  CA  ILE B  36       9.322  -4.082  -8.141  1.00 25.32           C  
ANISOU 1842  CA  ILE B  36     2896   3759   2966     86    488   -334       C  
ATOM   1843  C   ILE B  36       8.748  -4.366  -6.773  1.00 27.19           C  
ANISOU 1843  C   ILE B  36     3194   3886   3251    106    446   -347       C  
ATOM   1844  O   ILE B  36       7.647  -4.922  -6.660  1.00 25.26           O  
ANISOU 1844  O   ILE B  36     2989   3582   3026    158    428   -338       O  
ATOM   1845  CB  ILE B  36       8.232  -3.414  -8.996  1.00 24.09           C  
ANISOU 1845  CB  ILE B  36     2792   3569   2791     72    510   -253       C  
ATOM   1846  CG1 ILE B  36       8.646  -3.381 -10.463  1.00 28.11           C  
ANISOU 1846  CG1 ILE B  36     3258   4219   3205     47    541   -234       C  
ATOM   1847  CG2 ILE B  36       7.910  -1.999  -8.474  1.00 24.04           C  
ANISOU 1847  CG2 ILE B  36     2848   3446   2840     10    540   -177       C  
ATOM   1848  CD1 ILE B  36       7.561  -2.838 -11.406  1.00 27.78           C  
ANISOU 1848  CD1 ILE B  36     3259   4168   3127     24    527   -124       C  
ATOM   1849  N   PRO B  37       9.495  -4.002  -5.714  1.00 27.00           N  
ANISOU 1849  N   PRO B  37     3175   3851   3234     46    427   -360       N  
ATOM   1850  CA  PRO B  37       8.998  -4.286  -4.370  1.00 21.64           C  
ANISOU 1850  CA  PRO B  37     2567   3098   2558     47    394   -371       C  
ATOM   1851  C   PRO B  37       7.668  -3.589  -4.114  1.00 22.23           C  
ANISOU 1851  C   PRO B  37     2738   3064   2643     53    459   -347       C  
ATOM   1852  O   PRO B  37       7.466  -2.454  -4.564  1.00 21.25           O  
ANISOU 1852  O   PRO B  37     2646   2888   2540     22    516   -322       O  
ATOM   1853  CB  PRO B  37      10.071  -3.672  -3.465  1.00 23.15           C  
ANISOU 1853  CB  PRO B  37     2764   3313   2721    -60    359   -387       C  
ATOM   1854  CG  PRO B  37      11.341  -3.790  -4.267  1.00 24.13           C  
ANISOU 1854  CG  PRO B  37     2749   3555   2862    -73    342   -380       C  
ATOM   1855  CD  PRO B  37      10.888  -3.518  -5.705  1.00 26.27           C  
ANISOU 1855  CD  PRO B  37     3005   3843   3134    -34    420   -361       C  
ATOM   1856  N   HIS B  38       6.797  -4.257  -3.368  1.00 24.77           N  
ANISOU 1856  N   HIS B  38     3967   3332   2111    323   -687   -261       N  
ATOM   1857  CA  HIS B  38       5.488  -3.712  -3.015  1.00 26.09           C  
ANISOU 1857  CA  HIS B  38     4063   3420   2429    122   -721   -114       C  
ATOM   1858  C   HIS B  38       5.541  -2.261  -2.541  1.00 20.45           C  
ANISOU 1858  C   HIS B  38     3049   2851   1871     92   -499   -149       C  
ATOM   1859  O   HIS B  38       4.764  -1.416  -2.996  1.00 21.01           O  
ANISOU 1859  O   HIS B  38     2971   2891   2121    -33   -457    -42       O  
ATOM   1860  CB  HIS B  38       4.849  -4.532  -1.899  1.00 27.22           C  
ANISOU 1860  CB  HIS B  38     4287   3463   2594     67   -738     12       C  
ATOM   1861  CG  HIS B  38       3.534  -3.978  -1.447  1.00 28.37           C  
ANISOU 1861  CG  HIS B  38     4183   3599   2996   -114   -623    257       C  
ATOM   1862  ND1 HIS B  38       3.383  -3.290  -0.260  1.00 28.88           N  
ANISOU 1862  ND1 HIS B  38     4083   3803   3089    -12   -376    277       N  
ATOM   1863  CD2 HIS B  38       2.316  -3.982  -2.041  1.00 26.09           C  
ANISOU 1863  CD2 HIS B  38     3777   3206   2931   -339   -730    504       C  
ATOM   1864  CE1 HIS B  38       2.124  -2.918  -0.131  1.00 32.98           C  
ANISOU 1864  CE1 HIS B  38     4385   4337   3810   -127   -286    548       C  
ATOM   1865  NE2 HIS B  38       1.454  -3.322  -1.196  1.00 29.84           N  
ANISOU 1865  NE2 HIS B  38     3970   3806   3563   -355   -500    700       N  
ATOM   1866  N   GLY B  39       6.445  -1.989  -1.606  1.00 22.31           N  
ANISOU 1866  N   GLY B  39     3238   3212   2027    226   -406   -308       N  
ATOM   1867  CA  GLY B  39       6.566  -0.663  -1.019  1.00 22.10           C  
ANISOU 1867  CA  GLY B  39     3027   3247   2124    217   -290   -374       C  
ATOM   1868  C   GLY B  39       6.923   0.399  -2.056  1.00 22.95           C  
ANISOU 1868  C   GLY B  39     2984   3383   2353    111   -273   -376       C  
ATOM   1869  O   GLY B  39       6.502   1.556  -1.939  1.00 23.52           O  
ANISOU 1869  O   GLY B  39     2961   3400   2576     39   -219   -353       O  
ATOM   1870  N   LEU B  40       7.701   0.015  -3.061  1.00 21.25           N  
ANISOU 1870  N   LEU B  40     2778   3254   2043    145   -309   -383       N  
ATOM   1871  CA  LEU B  40       8.060   0.937  -4.131  1.00 23.76           C  
ANISOU 1871  CA  LEU B  40     2955   3621   2452     65   -252   -315       C  
ATOM   1872  C   LEU B  40       6.828   1.235  -4.991  1.00 24.08           C  
ANISOU 1872  C   LEU B  40     3053   3512   2584    -33   -263   -173       C  
ATOM   1873  O   LEU B  40       6.633   2.365  -5.456  1.00 19.69           O  
ANISOU 1873  O   LEU B  40     2395   2916   2169   -134   -200   -107       O  
ATOM   1874  CB  LEU B  40       9.223   0.376  -4.967  1.00 22.11           C  
ANISOU 1874  CB  LEU B  40     2736   3609   2057    226   -234   -308       C  
ATOM   1875  CG  LEU B  40       9.597   1.153  -6.233  1.00 30.80           C  
ANISOU 1875  CG  LEU B  40     3705   4799   3198    198   -124   -157       C  
ATOM   1876  CD1 LEU B  40       9.784   2.648  -5.949  1.00 29.12           C  
ANISOU 1876  CD1 LEU B  40     3243   4551   3270    -45    -63   -110       C  
ATOM   1877  CD2 LEU B  40      10.852   0.577  -6.885  1.00 30.93           C  
ANISOU 1877  CD2 LEU B  40     3665   5101   2986    451    -46   -106       C  
ATOM   1878  N   ILE B  41       5.978   0.231  -5.194  1.00 20.13           N  
ANISOU 1878  N   ILE B  41     2726   2906   2018    -18   -383   -113       N  
ATOM   1879  CA  ILE B  41       4.711   0.464  -5.896  1.00 21.13           C  
ANISOU 1879  CA  ILE B  41     2866   2895   2268   -128   -456     33       C  
ATOM   1880  C   ILE B  41       3.866   1.489  -5.135  1.00 22.31           C  
ANISOU 1880  C   ILE B  41     2834   3024   2619   -214   -343     94       C  
ATOM   1881  O   ILE B  41       3.255   2.382  -5.739  1.00 20.89           O  
ANISOU 1881  O   ILE B  41     2588   2798   2551   -262   -321    176       O  
ATOM   1882  CB  ILE B  41       3.917  -0.842  -6.067  1.00 23.71           C  
ANISOU 1882  CB  ILE B  41     3382   3076   2553   -162   -684    115       C  
ATOM   1883  CG1 ILE B  41       4.705  -1.809  -6.954  1.00 24.57           C  
ANISOU 1883  CG1 ILE B  41     3790   3156   2391     15   -844     30       C  
ATOM   1884  CG2 ILE B  41       2.561  -0.568  -6.695  1.00 21.33           C  
ANISOU 1884  CG2 ILE B  41     3018   2652   2435   -308   -809    288       C  
ATOM   1885  CD1 ILE B  41       4.111  -3.225  -7.024  1.00 29.83           C  
ANISOU 1885  CD1 ILE B  41     4725   3593   3016    -17  -1124     72       C  
ATOM   1886  N  AMET B  42       3.838   1.364  -3.814  0.29 19.85           N  
ANISOU 1886  N  AMET B  42     2486   2750   2307   -168   -271     54       N  
ATOM   1887  N  BMET B  42       3.830   1.361  -3.814  0.71 19.67           N  
ANISOU 1887  N  BMET B  42     2463   2726   2284   -168   -271     56       N  
ATOM   1888  CA AMET B  42       3.065   2.278  -2.978  0.29 19.81           C  
ANISOU 1888  CA AMET B  42     2375   2747   2407   -126   -151    110       C  
ATOM   1889  CA BMET B  42       3.064   2.296  -2.981  0.71 19.31           C  
ANISOU 1889  CA BMET B  42     2310   2683   2344   -126   -150    109       C  
ATOM   1890  C  AMET B  42       3.578   3.703  -3.081  0.29 20.72           C  
ANISOU 1890  C  AMET B  42     2471   2827   2573   -112   -103      2       C  
ATOM   1891  C  BMET B  42       3.579   3.712  -3.095  0.71 21.41           C  
ANISOU 1891  C  BMET B  42     2559   2914   2661   -113   -103      2       C  
ATOM   1892  O  AMET B  42       2.795   4.645  -3.225  0.29 21.11           O  
ANISOU 1892  O  AMET B  42     2489   2822   2710    -89    -60     78       O  
ATOM   1893  O  BMET B  42       2.801   4.665  -3.259  0.71 20.73           O  
ANISOU 1893  O  BMET B  42     2441   2772   2664    -92    -61     78       O  
ATOM   1894  CB AMET B  42       3.081   1.808  -1.522  0.29 20.54           C  
ANISOU 1894  CB AMET B  42     2502   2894   2408     10    -74     82       C  
ATOM   1895  CB BMET B  42       3.072   1.848  -1.511  0.71 19.74           C  
ANISOU 1895  CB BMET B  42     2399   2793   2309     13    -71     82       C  
ATOM   1896  CG AMET B  42       2.595   0.387  -1.369  0.29 22.66           C  
ANISOU 1896  CG AMET B  42     2806   3155   2647    -44   -132    236       C  
ATOM   1897  CG BMET B  42       2.444   0.486  -1.247  0.71 24.43           C  
ANISOU 1897  CG BMET B  42     3010   3387   2884    -32   -108    259       C  
ATOM   1898  SD AMET B  42       1.019   0.161  -2.200  0.29 37.14           S  
ANISOU 1898  SD AMET B  42     4476   4939   4696   -234   -216    560       S  
ATOM   1899  SD BMET B  42       0.692   0.413  -1.660  0.71 29.67           S  
ANISOU 1899  SD BMET B  42     3458   4049   3766   -168   -112    622       S  
ATOM   1900  CE AMET B  42      -0.100   0.576  -0.857  0.29 30.48           C  
ANISOU 1900  CE AMET B  42     3420   4250   3909    -75     43    808       C  
ATOM   1901  CE BMET B  42       0.826  -0.216  -3.341  0.71 40.65           C  
ANISOU 1901  CE BMET B  42     4966   5283   5197   -378   -415    602       C  
ATOM   1902  N   ASP B  43       4.895   3.856  -3.022  1.00 19.86           N  
ANISOU 1902  N   ASP B  43     2380   2745   2421   -132   -134   -152       N  
ATOM   1903  CA  ASP B  43       5.512   5.178  -3.100  1.00 20.09           C  
ANISOU 1903  CA  ASP B  43     2386   2697   2551   -198   -150   -218       C  
ATOM   1904  C   ASP B  43       5.201   5.843  -4.433  1.00 22.69           C  
ANISOU 1904  C   ASP B  43     2687   2964   2969   -305   -123    -81       C  
ATOM   1905  O   ASP B  43       4.925   7.046  -4.487  1.00 20.99           O  
ANISOU 1905  O   ASP B  43     2515   2610   2852   -335   -128    -64       O  
ATOM   1906  CB  ASP B  43       7.027   5.075  -2.969  1.00 22.09           C  
ANISOU 1906  CB  ASP B  43     2563   3037   2795   -257   -212   -328       C  
ATOM   1907  CG  ASP B  43       7.485   4.756  -1.548  1.00 30.44           C  
ANISOU 1907  CG  ASP B  43     3682   4116   3769   -131   -290   -507       C  
ATOM   1908  OD1 ASP B  43       6.766   5.087  -0.576  1.00 28.70           O  
ANISOU 1908  OD1 ASP B  43     3599   3796   3508     12   -293   -562       O  
ATOM   1909  OD2 ASP B  43       8.583   4.179  -1.423  1.00 29.88           O  
ANISOU 1909  OD2 ASP B  43     3528   4182   3643   -124   -344   -582       O  
ATOM   1910  N   ARG B  44       5.279   5.071  -5.510  1.00 18.05           N  
ANISOU 1910  N   ARG B  44     2090   2457   2312   -322   -117      7       N  
ATOM   1911  CA  ARG B  44       5.011   5.635  -6.833  1.00 18.67           C  
ANISOU 1911  CA  ARG B  44     2188   2484   2422   -364    -93    140       C  
ATOM   1912  C   ARG B  44       3.517   5.964  -6.959  1.00 21.26           C  
ANISOU 1912  C   ARG B  44     2555   2709   2816   -331   -123    223       C  
ATOM   1913  O   ARG B  44       3.141   7.024  -7.470  1.00 22.18           O  
ANISOU 1913  O   ARG B  44     2701   2724   3002   -343    -99    290       O  
ATOM   1914  CB  ARG B  44       5.440   4.658  -7.929  1.00 18.42           C  
ANISOU 1914  CB  ARG B  44     2219   2556   2222   -286   -109    196       C  
ATOM   1915  CG  ARG B  44       5.094   5.130  -9.340  1.00 21.68           C  
ANISOU 1915  CG  ARG B  44     2718   2917   2603   -253    -92    337       C  
ATOM   1916  CD  ARG B  44       5.686   6.511  -9.641  1.00 20.43           C  
ANISOU 1916  CD  ARG B  44     2470   2728   2565   -359     42    433       C  
ATOM   1917  NE  ARG B  44       5.392   6.922 -11.022  1.00 22.80           N  
ANISOU 1917  NE  ARG B  44     2887   2986   2791   -283     86    592       N  
ATOM   1918  CZ  ARG B  44       5.280   8.187 -11.417  1.00 28.74           C  
ANISOU 1918  CZ  ARG B  44     3651   3612   3656   -369    157    710       C  
ATOM   1919  NH1 ARG B  44       5.468   9.166 -10.533  1.00 27.79           N  
ANISOU 1919  NH1 ARG B  44     3455   3366   3736   -547    152    672       N  
ATOM   1920  NH2 ARG B  44       4.998   8.479 -12.695  1.00 26.75           N  
ANISOU 1920  NH2 ARG B  44     3543   3327   3294   -252    203    860       N  
ATOM   1921  N   THR B  45       2.681   5.065  -6.440  1.00 20.88           N  
ANISOU 1921  N   THR B  45     2484   2696   2754   -289   -177    249       N  
ATOM   1922  CA  THR B  45       1.226   5.246  -6.452  1.00 21.15           C  
ANISOU 1922  CA  THR B  45     2448   2706   2880   -256   -203    389       C  
ATOM   1923  C   THR B  45       0.796   6.478  -5.662  1.00 22.83           C  
ANISOU 1923  C   THR B  45     2640   2890   3143   -138    -92    379       C  
ATOM   1924  O   THR B  45      -0.123   7.204  -6.073  1.00 22.44           O  
ANISOU 1924  O   THR B  45     2565   2810   3149    -65    -87    484       O  
ATOM   1925  CB  THR B  45       0.497   3.969  -5.978  1.00 25.19           C  
ANISOU 1925  CB  THR B  45     2881   3277   3413   -287   -284    495       C  
ATOM   1926  OG1 THR B  45       0.863   2.883  -6.840  1.00 24.16           O  
ANISOU 1926  OG1 THR B  45     2883   3095   3203   -360   -467    480       O  
ATOM   1927  CG2 THR B  45      -1.034   4.132  -6.040  1.00 21.86           C  
ANISOU 1927  CG2 THR B  45     2274   2892   3140   -280   -316    721       C  
ATOM   1928  N   GLU B  46       1.471   6.746  -4.552  1.00 19.62           N  
ANISOU 1928  N   GLU B  46     2291   2476   2687    -72    -36    239       N  
ATOM   1929  CA  GLU B  46       1.192   7.971  -3.812  1.00 23.03           C  
ANISOU 1929  CA  GLU B  46     2828   2815   3106    103      6    185       C  
ATOM   1930  C   GLU B  46       1.371   9.200  -4.690  1.00 23.47           C  
ANISOU 1930  C   GLU B  46     3000   2692   3225     38    -43    181       C  
ATOM   1931  O   GLU B  46       0.544  10.115  -4.661  1.00 21.14           O  
ANISOU 1931  O   GLU B  46     2793   2320   2920    211    -27    228       O  
ATOM   1932  CB  GLU B  46       2.111   8.105  -2.598  1.00 18.88           C  
ANISOU 1932  CB  GLU B  46     2429   2242   2501    175    -26    -12       C  
ATOM   1933  CG  GLU B  46       1.803   9.348  -1.774  1.00 24.79           C  
ANISOU 1933  CG  GLU B  46     3403   2836   3180    427    -54   -102       C  
ATOM   1934  CD  GLU B  46       2.705   9.472  -0.553  1.00 30.85           C  
ANISOU 1934  CD  GLU B  46     4360   3513   3850    526   -171   -326       C  
ATOM   1935  OE1 GLU B  46       2.514  10.415   0.226  1.00 30.47           O  
ANISOU 1935  OE1 GLU B  46     4590   3296   3691    790   -255   -438       O  
ATOM   1936  OE2 GLU B  46       3.591   8.616  -0.372  1.00 33.64           O  
ANISOU 1936  OE2 GLU B  46     4617   3953   4211    382   -209   -400       O  
ATOM   1937  N   ARG B  47       2.457   9.240  -5.461  1.00 22.42           N  
ANISOU 1937  N   ARG B  47     2872   2505   3141   -179    -86    156       N  
ATOM   1938  CA  ARG B  47       2.693  10.398  -6.327  1.00 22.64           C  
ANISOU 1938  CA  ARG B  47     3009   2353   3241   -272   -111    214       C  
ATOM   1939  C   ARG B  47       1.680  10.422  -7.462  1.00 23.15           C  
ANISOU 1939  C   ARG B  47     3065   2440   3289   -204    -81    368       C  
ATOM   1940  O   ARG B  47       1.242  11.489  -7.895  1.00 26.52           O  
ANISOU 1940  O   ARG B  47     3630   2711   3735   -144    -93    423       O  
ATOM   1941  CB  ARG B  47       4.128  10.396  -6.880  1.00 24.24           C  
ANISOU 1941  CB  ARG B  47     3143   2558   3508   -510   -114    239       C  
ATOM   1942  CG  ARG B  47       4.417  11.504  -7.913  1.00 26.47           C  
ANISOU 1942  CG  ARG B  47     3507   2672   3877   -642    -99    392       C  
ATOM   1943  CD  ARG B  47       4.158  12.908  -7.363  1.00 29.19           C  
ANISOU 1943  CD  ARG B  47     4089   2699   4302   -636   -226    340       C  
ATOM   1944  NE  ARG B  47       4.267  13.936  -8.410  1.00 30.90           N  
ANISOU 1944  NE  ARG B  47     4427   2720   4595   -757   -213    523       N  
ATOM   1945  CZ  ARG B  47       5.298  14.769  -8.547  1.00 38.01           C  
ANISOU 1945  CZ  ARG B  47     5350   3425   5669  -1041   -290    629       C  
ATOM   1946  NH1 ARG B  47       6.325  14.720  -7.707  1.00 40.40           N  
ANISOU 1946  NH1 ARG B  47     5539   3706   6106  -1240   -429    548       N  
ATOM   1947  NH2 ARG B  47       5.303  15.668  -9.523  1.00 39.80           N  
ANISOU 1947  NH2 ARG B  47     5703   3466   5953  -1141   -252    843       N  
ATOM   1948  N   LEU B  48       1.298   9.251  -7.954  1.00 20.59           N  
ANISOU 1948  N   LEU B  48     2621   2279   2925   -204    -90    431       N  
ATOM   1949  CA  LEU B  48       0.304   9.222  -9.034  1.00 24.66           C  
ANISOU 1949  CA  LEU B  48     3141   2797   3434   -138   -147    562       C  
ATOM   1950  C   LEU B  48      -1.020   9.789  -8.567  1.00 24.91           C  
ANISOU 1950  C   LEU B  48     3119   2838   3506     42   -147    627       C  
ATOM   1951  O   LEU B  48      -1.693  10.473  -9.331  1.00 26.83           O  
ANISOU 1951  O   LEU B  48     3424   3019   3751    138   -183    710       O  
ATOM   1952  CB  LEU B  48       0.091   7.811  -9.601  1.00 22.92           C  
ANISOU 1952  CB  LEU B  48     2858   2682   3168   -177   -264    605       C  
ATOM   1953  CG  LEU B  48       1.217   7.263 -10.483  1.00 28.61           C  
ANISOU 1953  CG  LEU B  48     3694   3417   3759   -218   -267    580       C  
ATOM   1954  CD1 LEU B  48       0.926   5.845 -10.915  1.00 30.39           C  
ANISOU 1954  CD1 LEU B  48     3971   3678   3896   -196   -458    584       C  
ATOM   1955  CD2 LEU B  48       1.445   8.136 -11.694  1.00 32.47           C  
ANISOU 1955  CD2 LEU B  48     4324   3825   4188   -167   -214    672       C  
ATOM   1956  N   ALA B  49      -1.399   9.516  -7.317  1.00 21.19           N  
ANISOU 1956  N   ALA B  49     2536   2473   3041    142    -89    610       N  
ATOM   1957  CA  ALA B  49      -2.678  10.038  -6.804  1.00 22.15           C  
ANISOU 1957  CA  ALA B  49     2567   2685   3164    404    -34    725       C  
ATOM   1958  C   ALA B  49      -2.670  11.549  -6.851  1.00 25.94           C  
ANISOU 1958  C   ALA B  49     3308   2970   3576    585    -18    656       C  
ATOM   1959  O   ALA B  49      -3.673  12.200  -7.201  1.00 25.32           O  
ANISOU 1959  O   ALA B  49     3227   2915   3479    804    -18    764       O  
ATOM   1960  CB  ALA B  49      -2.925   9.549  -5.372  1.00 23.29           C  
ANISOU 1960  CB  ALA B  49     2588   2993   3266    549     85    745       C  
ATOM   1961  N   ARG B  50      -1.536  12.126  -6.473  1.00 24.79           N  
ANISOU 1961  N   ARG B  50     3402   2617   3402    497    -39    486       N  
ATOM   1962  CA  ARG B  50      -1.434  13.577  -6.497  1.00 28.34           C  
ANISOU 1962  CA  ARG B  50     4175   2788   3804    618    -97    422       C  
ATOM   1963  C   ARG B  50      -1.492  14.102  -7.925  1.00 29.91           C  
ANISOU 1963  C   ARG B  50     4455   2862   4048    509   -134    529       C  
ATOM   1964  O   ARG B  50      -2.117  15.127  -8.180  1.00 31.29           O  
ANISOU 1964  O   ARG B  50     4836   2891   4161    720   -165    563       O  
ATOM   1965  CB  ARG B  50      -0.180  14.068  -5.775  1.00 33.01           C  
ANISOU 1965  CB  ARG B  50     4994   3139   4412    477   -199    242       C  
ATOM   1966  CG  ARG B  50      -0.288  15.527  -5.339  1.00 48.99           C  
ANISOU 1966  CG  ARG B  50     7437   4822   6355    686   -336    149       C  
ATOM   1967  CD  ARG B  50       0.951  15.962  -4.587  1.00 57.12           C  
ANISOU 1967  CD  ARG B  50     8690   5570   7442    499   -542    -29       C  
ATOM   1968  NE  ARG B  50       2.087  16.140  -5.486  1.00 63.99           N  
ANISOU 1968  NE  ARG B  50     9488   6298   8528     30   -610     59       N  
ATOM   1969  CZ  ARG B  50       3.361  16.039  -5.121  1.00 66.17           C  
ANISOU 1969  CZ  ARG B  50     9704   6489   8950   -283   -748     -4       C  
ATOM   1970  NH1 ARG B  50       3.679  15.744  -3.869  1.00 65.25           N  
ANISOU 1970  NH1 ARG B  50     9646   6375   8770   -174   -873   -206       N  
ATOM   1971  NH2 ARG B  50       4.320  16.226  -6.014  1.00 66.02           N  
ANISOU 1971  NH2 ARG B  50     9545   6408   9131   -678   -754    164       N  
ATOM   1972  N   ASP B  51      -0.867  13.398  -8.868  1.00 27.52           N  
ANISOU 1972  N   ASP B  51     4032   2620   3806    246   -127    588       N  
ATOM   1973  CA  ASP B  51      -0.943  13.816 -10.278  1.00 27.47           C  
ANISOU 1973  CA  ASP B  51     4130   2521   3787    210   -139    713       C  
ATOM   1974  C   ASP B  51      -2.375  13.739 -10.816  1.00 26.16           C  
ANISOU 1974  C   ASP B  51     3890   2473   3577    452   -188    810       C  
ATOM   1975  O   ASP B  51      -2.811  14.599 -11.579  1.00 30.98           O  
ANISOU 1975  O   ASP B  51     4684   2951   4137    584   -218    880       O  
ATOM   1976  CB  ASP B  51      -0.042  12.941 -11.163  1.00 32.95           C  
ANISOU 1976  CB  ASP B  51     4732   3311   4478     -1   -104    770       C  
ATOM   1977  CG  ASP B  51       1.435  13.053 -10.813  1.00 36.27           C  
ANISOU 1977  CG  ASP B  51     5143   3672   4965   -243    -47    741       C  
ATOM   1978  OD1 ASP B  51       1.838  14.048 -10.177  1.00 38.90           O  
ANISOU 1978  OD1 ASP B  51     5611   3789   5380   -319    -89    697       O  
ATOM   1979  OD2 ASP B  51       2.190  12.124 -11.183  1.00 37.95           O  
ANISOU 1979  OD2 ASP B  51     5224   4052   5144   -340      7    768       O  
ATOM   1980  N   VAL B  52      -3.103  12.693 -10.434  1.00 27.27           N  
ANISOU 1980  N   VAL B  52     3745   2862   3755    496   -217    841       N  
ATOM   1981  CA  VAL B  52      -4.497  12.551 -10.875  1.00 30.10           C  
ANISOU 1981  CA  VAL B  52     3931   3370   4136    681   -311    979       C  
ATOM   1982  C   VAL B  52      -5.336  13.707 -10.370  1.00 30.95           C  
ANISOU 1982  C   VAL B  52     4113   3465   4181   1021   -251   1011       C  
ATOM   1983  O   VAL B  52      -6.105  14.329 -11.122  1.00 33.42           O  
ANISOU 1983  O   VAL B  52     4488   3755   4453   1217   -321   1093       O  
ATOM   1984  CB  VAL B  52      -5.101  11.221 -10.364  1.00 32.56           C  
ANISOU 1984  CB  VAL B  52     3874   3939   4560    601   -368   1069       C  
ATOM   1985  CG1 VAL B  52      -6.616  11.218 -10.516  1.00 28.57           C  
ANISOU 1985  CG1 VAL B  52     3082   3631   4140    786   -462   1272       C  
ATOM   1986  CG2 VAL B  52      -4.477  10.043 -11.093  1.00 36.27           C  
ANISOU 1986  CG2 VAL B  52     4356   4381   5045    341   -511   1038       C  
ATOM   1987  N  AMET B  53      -5.173  13.998  -9.084  0.48 31.13           N  
ANISOU 1987  N  AMET B  53     4175   3497   4155   1152   -136    934       N  
ATOM   1988  N  BMET B  53      -5.199  14.025  -9.092  0.52 31.35           N  
ANISOU 1988  N  BMET B  53     4205   3524   4181   1160   -136    936       N  
ATOM   1989  CA AMET B  53      -5.864  15.116  -8.438  0.48 37.00           C  
ANISOU 1989  CA AMET B  53     5089   4209   4759   1578    -78    933       C  
ATOM   1990  CA BMET B  53      -5.983  15.131  -8.546  0.52 36.59           C  
ANISOU 1990  CA BMET B  53     5021   4172   4709   1595    -84    951       C  
ATOM   1991  C  AMET B  53      -5.572  16.446  -9.123  0.48 37.86           C  
ANISOU 1991  C  AMET B  53     5648   3959   4776   1652   -159    862       C  
ATOM   1992  C  BMET B  53      -5.580  16.491  -9.119  0.52 37.93           C  
ANISOU 1992  C  BMET B  53     5670   3961   4781   1663   -160    861       C  
ATOM   1993  O  AMET B  53      -6.466  17.270  -9.323  0.48 39.64           O  
ANISOU 1993  O  AMET B  53     5997   4177   4889   2018   -175    924       O  
ATOM   1994  O  BMET B  53      -6.420  17.381  -9.255  0.52 39.82           O  
ANISOU 1994  O  BMET B  53     6065   4169   4897   2036   -175    909       O  
ATOM   1995  CB AMET B  53      -5.458  15.201  -6.962  0.48 39.68           C  
ANISOU 1995  CB AMET B  53     5538   4539   5000   1723     16    810       C  
ATOM   1996  CB BMET B  53      -5.968  15.125  -7.014  0.52 38.59           C  
ANISOU 1996  CB BMET B  53     5283   4518   4860   1828     41    889       C  
ATOM   1997  CG AMET B  53      -5.883  16.492  -6.275  0.48 46.98           C  
ANISOU 1997  CG AMET B  53     6836   5318   5698   2220     26    740       C  
ATOM   1998  CG BMET B  53      -6.761  13.967  -6.406  0.52 37.79           C  
ANISOU 1998  CG BMET B  53     4684   4839   4834   1881    163   1089       C  
ATOM   1999  SD AMET B  53      -7.613  16.507  -5.768  0.48 45.73           S  
ANISOU 1999  SD AMET B  53     6355   5618   5402   2836    207    992       S  
ATOM   2000  SD BMET B  53      -8.491  13.876  -6.948  0.52 43.35           S  
ANISOU 2000  SD BMET B  53     4934   5920   5618   2145    175   1427       S  
ATOM   2001  CE AMET B  53      -7.514  15.668  -4.188  0.48 38.40           C  
ANISOU 2001  CE AMET B  53     5237   4961   4392   2933    401    999       C  
ATOM   2002  CE BMET B  53      -9.216  15.237  -6.046  0.52 62.25           C  
ANISOU 2002  CE BMET B  53     7584   8369   7698   2781    341   1395       C  
ATOM   2003  N   LYS B  54      -4.309  16.651  -9.475  1.00 36.31           N  
ANISOU 2003  N   LYS B  54     5684   3476   4634   1310   -206    768       N  
ATOM   2004  CA  LYS B  54      -3.879  17.893 -10.129  1.00 39.15           C  
ANISOU 2004  CA  LYS B  54     6475   3451   4951   1286   -284    759       C  
ATOM   2005  C   LYS B  54      -4.577  18.052 -11.475  1.00 42.41           C  
ANISOU 2005  C   LYS B  54     6886   3900   5328   1384   -307    904       C  
ATOM   2006  O   LYS B  54      -4.918  19.156 -11.885  1.00 42.57           O  
ANISOU 2006  O   LYS B  54     7245   3686   5242   1597   -361    932       O  
ATOM   2007  CB  LYS B  54      -2.355  17.919 -10.326  1.00 39.27           C  
ANISOU 2007  CB  LYS B  54     6596   3233   5091    834   -306    730       C  
ATOM   2008  CG  LYS B  54      -1.813  19.129 -11.114  1.00 50.72           C  
ANISOU 2008  CG  LYS B  54     8437   4280   6556    707   -374    817       C  
ATOM   2009  CD  LYS B  54      -1.216  20.186 -10.193  1.00 59.46           C  
ANISOU 2009  CD  LYS B  54     9931   4974   7688    659   -547    700       C  
ATOM   2010  CE  LYS B  54      -0.028  20.914 -10.831  1.00 65.70           C  
ANISOU 2010  CE  LYS B  54    10888   5426   8647    223   -611    842       C  
ATOM   2011  NZ  LYS B  54      -0.390  21.708 -12.034  1.00 70.36           N  
ANISOU 2011  NZ  LYS B  54    11620   5936   9178    283   -553   1002       N  
ATOM   2012  N   GLU B  55      -4.829  16.936 -12.146  1.00 40.19           N  
ANISOU 2012  N   GLU B  55     6270   3887   5113   1263   -307    985       N  
ATOM   2013  CA AGLU B  55      -5.354  16.978 -13.503  0.51 44.42           C  
ANISOU 2013  CA AGLU B  55     6847   4432   5599   1343   -387   1098       C  
ATOM   2014  CA BGLU B  55      -5.355  16.969 -13.509  0.49 44.40           C  
ANISOU 2014  CA BGLU B  55     6842   4431   5597   1342   -388   1099       C  
ATOM   2015  C   GLU B  55      -6.874  16.791 -13.589  1.00 45.27           C  
ANISOU 2015  C   GLU B  55     6696   4807   5696   1668   -486   1184       C  
ATOM   2016  O   GLU B  55      -7.534  17.408 -14.428  1.00 47.22           O  
ANISOU 2016  O   GLU B  55     7092   4999   5851   1904   -576   1251       O  
ATOM   2017  CB AGLU B  55      -4.629  15.936 -14.356  0.51 44.31           C  
ANISOU 2017  CB AGLU B  55     6731   4485   5622   1055   -403   1130       C  
ATOM   2018  CB BGLU B  55      -4.647  15.914 -14.370  0.49 44.33           C  
ANISOU 2018  CB BGLU B  55     6727   4492   5624   1057   -406   1131       C  
ATOM   2019  CG AGLU B  55      -4.882  16.052 -15.845  0.51 49.27           C  
ANISOU 2019  CG AGLU B  55     7536   5051   6134   1161   -492   1229       C  
ATOM   2020  CG BGLU B  55      -5.244  15.720 -15.760  0.49 47.97           C  
ANISOU 2020  CG BGLU B  55     7250   4982   5994   1192   -547   1224       C  
ATOM   2021  CD AGLU B  55      -3.838  15.316 -16.668  0.51 53.07           C  
ANISOU 2021  CD AGLU B  55     8078   5530   6556    962   -448   1265       C  
ATOM   2022  CD BGLU B  55      -5.079  16.938 -16.652  0.49 50.01           C  
ANISOU 2022  CD BGLU B  55     7920   4970   6111   1330   -504   1302       C  
ATOM   2023  OE1AGLU B  55      -2.747  15.031 -16.130  0.51 49.67           O  
ANISOU 2023  OE1AGLU B  55     7583   5101   6189    718   -309   1234       O  
ATOM   2024  OE1BGLU B  55      -3.962  17.496 -16.694  0.49 48.96           O  
ANISOU 2024  OE1BGLU B  55     8007   4622   5973   1140   -353   1341       O  
ATOM   2025  OE2AGLU B  55      -4.108  15.032 -17.855  0.51 59.46           O  
ANISOU 2025  OE2AGLU B  55     9016   6347   7229   1101   -560   1325       O  
ATOM   2026  OE2BGLU B  55      -6.065  17.334 -17.314  0.49 53.65           O  
ANISOU 2026  OE2BGLU B  55     8442   5452   6489   1593   -628   1336       O  
ATOM   2027  N   MET B  56      -7.432  15.958 -12.714  1.00 43.11           N  
ANISOU 2027  N   MET B  56     6015   4838   5525   1684   -469   1217       N  
ATOM   2028  CA  MET B  56      -8.850  15.591 -12.811  1.00 48.45           C  
ANISOU 2028  CA  MET B  56     6301   5838   6269   1909   -575   1383       C  
ATOM   2029  C   MET B  56      -9.778  16.099 -11.708  1.00 55.58           C  
ANISOU 2029  C   MET B  56     7022   6977   7120   2320   -437   1474       C  
ATOM   2030  O   MET B  56     -10.991  15.888 -11.775  1.00 61.17           O  
ANISOU 2030  O   MET B  56     7344   7995   7904   2456   -491   1625       O  
ATOM   2031  CB  MET B  56      -8.996  14.070 -12.898  1.00 47.64           C  
ANISOU 2031  CB  MET B  56     5785   5950   6365   1597   -709   1466       C  
ATOM   2032  CG  MET B  56      -8.129  13.412 -13.939  1.00 46.63           C  
ANISOU 2032  CG  MET B  56     5860   5632   6227   1294   -854   1377       C  
ATOM   2033  SD  MET B  56      -8.517  11.668 -14.032  1.00 44.96           S  
ANISOU 2033  SD  MET B  56     5259   5604   6221   1001  -1121   1470       S  
ATOM   2034  CE  MET B  56     -10.153  11.728 -14.776  1.00 46.19           C  
ANISOU 2034  CE  MET B  56     5117   5933   6500   1191  -1449   1674       C  
ATOM   2035  N   GLY B  57      -9.223  16.749 -10.693  1.00 59.09           N  
ANISOU 2035  N   GLY B  57     9238   5007   8205    227   -904   1087       N  
ATOM   2036  CA  GLY B  57     -10.034  17.286  -9.614  1.00 66.33           C  
ANISOU 2036  CA  GLY B  57    10101   5758   9343    451   -851    949       C  
ATOM   2037  C   GLY B  57      -9.962  18.800  -9.542  1.00 75.36           C  
ANISOU 2037  C   GLY B  57    11523   6606  10504    458   -796    964       C  
ATOM   2038  O   GLY B  57      -8.872  19.375  -9.565  1.00 80.02           O  
ANISOU 2038  O   GLY B  57    12327   7119  10957    177   -704    981       O  
ATOM   2039  N   GLY B  58     -11.117  19.448  -9.414  1.00 78.08           N  
ANISOU 2039  N   GLY B  58    11842   6799  11027    771   -842    945       N  
ATOM   2040  CA  GLY B  58     -12.351  18.737  -9.149  1.00 73.74           C  
ANISOU 2040  CA  GLY B  58    10977   6394  10648   1066   -904    871       C  
ATOM   2041  C   GLY B  58     -13.558  18.960 -10.048  1.00 71.13           C  
ANISOU 2041  C   GLY B  58    10561   6077  10387   1359  -1075    975       C  
ATOM   2042  O   GLY B  58     -14.225  20.002  -9.996  1.00 70.21           O  
ANISOU 2042  O   GLY B  58    10538   5754  10383   1569  -1084    984       O  
ATOM   2043  N   HIS B  59     -13.807  17.969 -10.900  1.00 63.82           N  
ANISOU 2043  N   HIS B  59     9462   5400   9387   1360  -1217   1051       N  
ATOM   2044  CA  HIS B  59     -15.155  17.598 -11.281  1.00 64.21           C  
ANISOU 2044  CA  HIS B  59     9241   5602   9554   1637  -1355   1043       C  
ATOM   2045  C   HIS B  59     -15.303  16.197 -10.691  1.00 56.47           C  
ANISOU 2045  C   HIS B  59     7923   4897   8637   1584  -1306    906       C  
ATOM   2046  O   HIS B  59     -14.332  15.629 -10.194  1.00 52.40           O  
ANISOU 2046  O   HIS B  59     7432   4423   8057   1357  -1200    863       O  
ATOM   2047  CB  HIS B  59     -15.352  17.575 -12.798  1.00 77.68           C  
ANISOU 2047  CB  HIS B  59    11025   7380  11111   1653  -1565   1229       C  
ATOM   2048  CG  HIS B  59     -16.765  17.295 -13.219  1.00 90.88           C  
ANISOU 2048  CG  HIS B  59    12421   9210  12899   1929  -1723   1217       C  
ATOM   2049  ND1 HIS B  59     -17.857  17.783 -12.528  1.00 96.89           N  
ANISOU 2049  ND1 HIS B  59    13011   9922  13883   2212  -1692   1113       N  
ATOM   2050  CD2 HIS B  59     -17.267  16.575 -14.250  1.00 94.74           C  
ANISOU 2050  CD2 HIS B  59    12766   9924  13308   1953  -1906   1281       C  
ATOM   2051  CE1 HIS B  59     -18.968  17.376 -13.118  1.00 99.83           C  
ANISOU 2051  CE1 HIS B  59    13128  10492  14311   2392  -1854   1120       C  
ATOM   2052  NE2 HIS B  59     -18.639  16.645 -14.166  1.00 98.76           N  
ANISOU 2052  NE2 HIS B  59    13010  10520  13994   2236  -1992   1219       N  
ATOM   2053  N   HIS B  60     -16.511  15.657 -10.716  1.00 53.49           N  
ANISOU 2053  N   HIS B  60     7226   4706   8391   1780  -1375    836       N  
ATOM   2054  CA  HIS B  60     -16.760  14.300 -10.267  1.00 50.20           C  
ANISOU 2054  CA  HIS B  60     6477   4557   8039   1713  -1328    714       C  
ATOM   2055  C   HIS B  60     -15.969  13.330 -11.146  1.00 37.34           C  
ANISOU 2055  C   HIS B  60     4884   3078   6225   1482  -1419    816       C  
ATOM   2056  O   HIS B  60     -15.945  13.479 -12.366  1.00 51.42           O  
ANISOU 2056  O   HIS B  60     6797   4878   7864   1470  -1582    958       O  
ATOM   2057  CB  HIS B  60     -18.261  14.020 -10.384  1.00 57.94           C  
ANISOU 2057  CB  HIS B  60     7129   5717   9168   1936  -1404    639       C  
ATOM   2058  CG  HIS B  60     -18.664  12.653  -9.936  1.00 61.38           C  
ANISOU 2058  CG  HIS B  60     7218   6424   9679   1848  -1335    506       C  
ATOM   2059  ND1 HIS B  60     -18.265  11.504 -10.586  1.00 60.61           N  
ANISOU 2059  ND1 HIS B  60     7057   6504   9468   1657  -1410    551       N  
ATOM   2060  CD2 HIS B  60     -19.448  12.247  -8.906  1.00 63.78           C  
ANISOU 2060  CD2 HIS B  60     7233   6849  10151   1910  -1180    328       C  
ATOM   2061  CE1 HIS B  60     -18.771  10.452  -9.969  1.00 56.28           C  
ANISOU 2061  CE1 HIS B  60     6207   6153   9023   1600  -1306    412       C  
ATOM   2062  NE2 HIS B  60     -19.491  10.875  -8.949  1.00 60.98           N  
ANISOU 2062  NE2 HIS B  60     6659   6725   9784   1740  -1160    279       N  
ATOM   2063  N  AILE B  61     -15.298  12.359 -10.545  0.36 34.25           N  
ANISOU 2063  N  AILE B  61     4395   2794   5825   1303  -1306    748       N  
ATOM   2064  N  BILE B  61     -15.345  12.333 -10.513  0.64 34.25           N  
ANISOU 2064  N  BILE B  61     4380   2801   5834   1308  -1303    741       N  
ATOM   2065  CA AILE B  61     -14.674  11.345 -11.373  0.36 32.60           C  
ANISOU 2065  CA AILE B  61     4187   2751   5450   1114  -1386    831       C  
ATOM   2066  CA BILE B  61     -14.572  11.299 -11.200  0.64 33.75           C  
ANISOU 2066  CA BILE B  61     4327   2892   5604   1098  -1359    818       C  
ATOM   2067  C  AILE B  61     -15.293   9.982 -11.122  0.36 35.42           C  
ANISOU 2067  C  AILE B  61     4203   3359   5896   1099  -1360    717       C  
ATOM   2068  C  BILE B  61     -15.264   9.942 -11.082  0.64 36.52           C  
ANISOU 2068  C  BILE B  61     4338   3504   6033   1091  -1350    712       C  
ATOM   2069  O  AILE B  61     -15.713   9.655 -10.008  0.36 35.83           O  
ANISOU 2069  O  AILE B  61     4055   3465   6093   1130  -1193    567       O  
ATOM   2070  O  BILE B  61     -15.688   9.559  -9.989  0.64 35.81           O  
ANISOU 2070  O  BILE B  61     4043   3478   6085   1116  -1184    562       O  
ATOM   2071  CB AILE B  61     -13.125  11.301 -11.253  0.36 37.56           C  
ANISOU 2071  CB AILE B  61     5040   3364   5868    838  -1245    870       C  
ATOM   2072  CB BILE B  61     -13.151  11.164 -10.589  0.64 35.54           C  
ANISOU 2072  CB BILE B  61     4705   3128   5670    837  -1146    788       C  
ATOM   2073  CG1AILE B  61     -12.668  10.151 -10.354  0.36 34.08           C  
ANISOU 2073  CG1AILE B  61     4412   3131   5403    688  -1044    730       C  
ATOM   2074  CG1BILE B  61     -12.318  12.416 -10.870  0.64 42.56           C  
ANISOU 2074  CG1BILE B  61     5947   3776   6447    761  -1154    900       C  
ATOM   2075  CG2AILE B  61     -12.566  12.663 -10.809  0.36 43.41           C  
ANISOU 2075  CG2AILE B  61     6062   3829   6605    825  -1174    899       C  
ATOM   2076  CG2BILE B  61     -12.431   9.945 -11.133  0.64 34.27           C  
ANISOU 2076  CG2BILE B  61     4495   3203   5323    631  -1127    806       C  
ATOM   2077  CD1AILE B  61     -11.172   9.915 -10.373  0.36 32.74           C  
ANISOU 2077  CD1AILE B  61     4396   3030   5014    434   -928    753       C  
ATOM   2078  CD1BILE B  61     -11.055  12.512 -10.028  0.64 41.25           C  
ANISOU 2078  CD1BILE B  61     5886   3616   6172    526   -940    827       C  
ATOM   2079  N   VAL B  62     -15.381   9.210 -12.193  1.00 35.18           N  
ANISOU 2079  N   VAL B  62     4132   3491   5745   1027  -1502    775       N  
ATOM   2080  CA  VAL B  62     -15.786   7.810 -12.115  1.00 29.59           C  
ANISOU 2080  CA  VAL B  62     3159   3009   5073    947  -1474    675       C  
ATOM   2081  C   VAL B  62     -14.521   7.015 -12.343  1.00 28.62           C  
ANISOU 2081  C   VAL B  62     3180   2977   4719    702  -1369    697       C  
ATOM   2082  O   VAL B  62     -13.870   7.164 -13.373  1.00 31.09           O  
ANISOU 2082  O   VAL B  62     3693   3284   4837    621  -1472    814       O  
ATOM   2083  CB  VAL B  62     -16.842   7.444 -13.171  1.00 31.59           C  
ANISOU 2083  CB  VAL B  62     3279   3414   5311   1007  -1660    673       C  
ATOM   2084  CG1 VAL B  62     -17.212   5.961 -13.061  1.00 36.97           C  
ANISOU 2084  CG1 VAL B  62     3716   4301   6030    880  -1619    557       C  
ATOM   2085  CG2 VAL B  62     -18.075   8.313 -12.988  1.00 36.27           C  
ANISOU 2085  CG2 VAL B  62     3746   3970   6066   1239  -1706    630       C  
ATOM   2086  N   ALA B  63     -14.144   6.198 -11.369  1.00 25.55           N  
ANISOU 2086  N   ALA B  63     2700   2670   4340    592  -1157    587       N  
ATOM   2087  CA  ALA B  63     -12.943   5.408 -11.498  1.00 24.20           C  
ANISOU 2087  CA  ALA B  63     2638   2588   3967    403  -1057    593       C  
ATOM   2088  C   ALA B  63     -13.362   4.038 -11.956  1.00 33.94           C  
ANISOU 2088  C   ALA B  63     3732   3978   5184    340  -1095    537       C  
ATOM   2089  O   ALA B  63     -14.202   3.389 -11.324  1.00 31.02           O  
ANISOU 2089  O   ALA B  63     3163   3661   4963    360  -1034    436       O  
ATOM   2090  CB  ALA B  63     -12.193   5.321 -10.194  1.00 25.49           C  
ANISOU 2090  CB  ALA B  63     2820   2739   4124    337   -832    518       C  
ATOM   2091  N   LEU B  64     -12.765   3.607 -13.064  1.00 26.55           N  
ANISOU 2091  N   LEU B  64     2919   3113   4057    245  -1182    594       N  
ATOM   2092  CA ALEU B  64     -13.133   2.355 -13.693  0.65 26.32           C  
ANISOU 2092  CA ALEU B  64     2804   3211   3987    175  -1241    535       C  
ATOM   2093  CA BLEU B  64     -13.114   2.344 -13.708  0.35 26.89           C  
ANISOU 2093  CA BLEU B  64     2879   3284   4055    173  -1241    536       C  
ATOM   2094  C   LEU B  64     -12.012   1.339 -13.486  1.00 25.73           C  
ANISOU 2094  C   LEU B  64     2811   3199   3767     49  -1078    487       C  
ATOM   2095  O   LEU B  64     -10.901   1.516 -13.981  1.00 26.95           O  
ANISOU 2095  O   LEU B  64     3128   3374   3739    -13  -1052    539       O  
ATOM   2096  CB ALEU B  64     -13.400   2.621 -15.180  0.65 30.41           C  
ANISOU 2096  CB ALEU B  64     3409   3763   4381    185  -1480    622       C  
ATOM   2097  CB BLEU B  64     -13.261   2.530 -15.217  0.35 30.53           C  
ANISOU 2097  CB BLEU B  64     3441   3787   4372    167  -1467    621       C  
ATOM   2098  CG ALEU B  64     -13.967   1.565 -16.114  0.65 33.03           C  
ANISOU 2098  CG ALEU B  64     3672   4224   4654    119  -1615    564       C  
ATOM   2099  CG BLEU B  64     -14.491   3.159 -15.850  0.35 32.84           C  
ANISOU 2099  CG BLEU B  64     3645   4069   4765    303  -1715    669       C  
ATOM   2100  CD1ALEU B  64     -15.052   0.782 -15.410  0.65 32.63           C  
ANISOU 2100  CD1ALEU B  64     3358   4221   4819    121  -1579    432       C  
ATOM   2101  CD1BLEU B  64     -14.638   2.639 -17.275  0.35 36.66           C  
ANISOU 2101  CD1BLEU B  64     4200   4665   5066    236  -1910    694       C  
ATOM   2102  CD2ALEU B  64     -14.532   2.249 -17.355  0.65 37.64           C  
ANISOU 2102  CD2ALEU B  64     4320   4822   5158    190  -1894    667       C  
ATOM   2103  CD2BLEU B  64     -15.725   2.859 -15.034  0.35 33.80           C  
ANISOU 2103  CD2BLEU B  64     3468   4222   5152    384  -1700    553       C  
ATOM   2104  N   CYS B  65     -12.308   0.275 -12.747  1.00 25.64           N  
ANISOU 2104  N   CYS B  65     2687   3216   3837     14   -962    385       N  
ATOM   2105  CA  CYS B  65     -11.306  -0.753 -12.474  1.00 27.57           C  
ANISOU 2105  CA  CYS B  65     3017   3498   3961    -62   -819    339       C  
ATOM   2106  C   CYS B  65     -11.305  -1.856 -13.534  1.00 29.12           C  
ANISOU 2106  C   CYS B  65     3259   3760   4044   -138   -890    293       C  
ATOM   2107  O   CYS B  65     -12.324  -2.518 -13.752  1.00 27.12           O  
ANISOU 2107  O   CYS B  65     2906   3519   3879   -175   -955    229       O  
ATOM   2108  CB  CYS B  65     -11.558  -1.383 -11.108  1.00 27.07           C  
ANISOU 2108  CB  CYS B  65     2873   3400   4012    -62   -652    268       C  
ATOM   2109  SG  CYS B  65     -10.352  -2.674 -10.721  1.00 27.87           S  
ANISOU 2109  SG  CYS B  65     3101   3520   3967   -103   -505    227       S  
ATOM   2110  N   VAL B  66     -10.174  -2.053 -14.209  1.00 27.16           N  
ANISOU 2110  N   VAL B  66     3155   3563   3599   -172   -870    309       N  
ATOM   2111  CA  VAL B  66     -10.106  -3.149 -15.169  1.00 24.80           C  
ANISOU 2111  CA  VAL B  66     2925   3318   3182   -237   -911    240       C  
ATOM   2112  C   VAL B  66      -9.673  -4.426 -14.458  1.00 24.80           C  
ANISOU 2112  C   VAL B  66     2949   3283   3189   -242   -754    149       C  
ATOM   2113  O   VAL B  66      -8.496  -4.580 -14.093  1.00 24.35           O  
ANISOU 2113  O   VAL B  66     2961   3248   3042   -200   -634    149       O  
ATOM   2114  CB  VAL B  66      -9.176  -2.856 -16.355  1.00 31.59           C  
ANISOU 2114  CB  VAL B  66     3931   4260   3810   -271   -953    279       C  
ATOM   2115  CG1 VAL B  66      -9.308  -3.966 -17.373  1.00 30.33           C  
ANISOU 2115  CG1 VAL B  66     3844   4149   3531   -335  -1006    185       C  
ATOM   2116  CG2 VAL B  66      -9.533  -1.516 -17.003  1.00 30.36           C  
ANISOU 2116  CG2 VAL B  66     3807   4103   3625   -263  -1107    401       C  
ATOM   2117  N   LEU B  67     -10.640  -5.326 -14.259  1.00 24.25           N  
ANISOU 2117  N   LEU B  67     2824   3161   3229   -294   -760     73       N  
ATOM   2118  CA  LEU B  67     -10.440  -6.588 -13.542  1.00 25.13           C  
ANISOU 2118  CA  LEU B  67     2997   3190   3361   -308   -616      0       C  
ATOM   2119  C   LEU B  67      -9.775  -7.612 -14.468  1.00 28.79           C  
ANISOU 2119  C   LEU B  67     3618   3657   3663   -328   -614    -79       C  
ATOM   2120  O   LEU B  67      -9.836  -7.452 -15.689  1.00 27.39           O  
ANISOU 2120  O   LEU B  67     3475   3557   3377   -373   -734    -98       O  
ATOM   2121  CB  LEU B  67     -11.789  -7.108 -13.036  1.00 21.10           C  
ANISOU 2121  CB  LEU B  67     2378   2612   3025   -401   -610    -54       C  
ATOM   2122  CG  LEU B  67     -12.481  -6.285 -11.945  1.00 26.60           C  
ANISOU 2122  CG  LEU B  67     2913   3300   3893   -372   -561     -9       C  
ATOM   2123  CD1 LEU B  67     -13.867  -6.835 -11.664  1.00 28.30           C  
ANISOU 2123  CD1 LEU B  67     2986   3494   4275   -493   -551    -86       C  
ATOM   2124  CD2 LEU B  67     -11.646  -6.258 -10.666  1.00 27.32           C  
ANISOU 2124  CD2 LEU B  67     3079   3337   3964   -296   -389     33       C  
ATOM   2125  N   LYS B  68      -9.128  -8.646 -13.920  1.00 24.05           N  
ANISOU 2125  N   LYS B  68     3134   2973   3032   -281   -480   -127       N  
ATOM   2126  CA  LYS B  68      -8.931  -8.835 -12.482  1.00 26.70           C  
ANISOU 2126  CA  LYS B  68     3470   3225   3450   -216   -348    -88       C  
ATOM   2127  C   LYS B  68      -7.671  -8.140 -12.014  1.00 24.04           C  
ANISOU 2127  C   LYS B  68     3126   2976   3034    -87   -295    -25       C  
ATOM   2128  O   LYS B  68      -7.582  -7.696 -10.870  1.00 25.15           O  
ANISOU 2128  O   LYS B  68     3219   3103   3233    -43   -232     31       O  
ATOM   2129  CB  LYS B  68      -8.774 -10.325 -12.170  1.00 25.18           C  
ANISOU 2129  CB  LYS B  68     3448   2881   3239   -208   -251   -157       C  
ATOM   2130  CG  LYS B  68      -9.941 -11.213 -12.531  1.00 27.53           C  
ANISOU 2130  CG  LYS B  68     3782   3067   3612   -375   -275   -242       C  
ATOM   2131  CD  LYS B  68      -9.768 -12.550 -11.808  1.00 32.88           C  
ANISOU 2131  CD  LYS B  68     4664   3540   4290   -364   -142   -273       C  
ATOM   2132  CE  LYS B  68     -10.414 -13.685 -12.535  1.00 33.59           C  
ANISOU 2132  CE  LYS B  68     4882   3498   4382   -518   -159   -395       C  
ATOM   2133  NZ  LYS B  68     -10.104 -14.982 -11.847  1.00 33.18           N  
ANISOU 2133  NZ  LYS B  68     5090   3201   4314   -484    -24   -412       N  
ATOM   2134  N   GLY B  69      -6.687  -8.069 -12.901  1.00 23.57           N  
ANISOU 2134  N   GLY B  69     3109   3018   2827    -40   -313    -48       N  
ATOM   2135  CA  GLY B  69      -5.360  -7.593 -12.546  1.00 26.89           C  
ANISOU 2135  CA  GLY B  69     3507   3549   3162     64   -253    -19       C  
ATOM   2136  C   GLY B  69      -5.253  -6.174 -12.010  1.00 27.06           C  
ANISOU 2136  C   GLY B  69     3418   3643   3222     42   -268     69       C  
ATOM   2137  O   GLY B  69      -4.309  -5.842 -11.281  1.00 30.11           O  
ANISOU 2137  O   GLY B  69     3767   4099   3573    110   -209     87       O  
ATOM   2138  N   GLY B  70      -6.201  -5.318 -12.366  1.00 24.85           N  
ANISOU 2138  N   GLY B  70     3086   3344   3013    -46   -356    117       N  
ATOM   2139  CA  GLY B  70      -6.100  -3.934 -11.936  1.00 22.35           C  
ANISOU 2139  CA  GLY B  70     2703   3059   2731    -61   -369    193       C  
ATOM   2140  C   GLY B  70      -6.595  -3.714 -10.516  1.00 23.35           C  
ANISOU 2140  C   GLY B  70     2775   3105   2992    -30   -311    210       C  
ATOM   2141  O   GLY B  70      -6.468  -2.605  -9.998  1.00 23.37           O  
ANISOU 2141  O   GLY B  70     2740   3115   3026    -34   -305    253       O  
ATOM   2142  N   TYR B  71      -7.136  -4.751  -9.877  1.00 22.29           N  
ANISOU 2142  N   TYR B  71     2659   2887   2922    -12   -255    173       N  
ATOM   2143  CA  TYR B  71      -7.856  -4.541  -8.611  1.00 21.75           C  
ANISOU 2143  CA  TYR B  71     2545   2745   2976    -12   -187    185       C  
ATOM   2144  C   TYR B  71      -6.977  -3.974  -7.490  1.00 21.30           C  
ANISOU 2144  C   TYR B  71     2496   2728   2868     45   -116    210       C  
ATOM   2145  O   TYR B  71      -7.435  -3.155  -6.688  1.00 22.21           O  
ANISOU 2145  O   TYR B  71     2563   2815   3060     35    -83    222       O  
ATOM   2146  CB  TYR B  71      -8.620  -5.814  -8.159  1.00 25.98           C  
ANISOU 2146  CB  TYR B  71     3125   3175   3571    -45   -118    146       C  
ATOM   2147  CG  TYR B  71      -7.966  -6.603  -7.028  1.00 25.96           C  
ANISOU 2147  CG  TYR B  71     3239   3125   3501     23     -6    156       C  
ATOM   2148  CD1 TYR B  71      -8.144  -6.240  -5.699  1.00 25.04           C  
ANISOU 2148  CD1 TYR B  71     3117   2986   3412     33     83    184       C  
ATOM   2149  CD2 TYR B  71      -7.195  -7.729  -7.301  1.00 25.80           C  
ANISOU 2149  CD2 TYR B  71     3351   3073   3378     91      5    135       C  
ATOM   2150  CE1 TYR B  71      -7.545  -6.966  -4.671  1.00 26.76           C  
ANISOU 2150  CE1 TYR B  71     3468   3162   3536    102    162    209       C  
ATOM   2151  CE2 TYR B  71      -6.591  -8.454  -6.287  1.00 26.53           C  
ANISOU 2151  CE2 TYR B  71     3570   3111   3400    188     80    160       C  
ATOM   2152  CZ  TYR B  71      -6.765  -8.058  -4.975  1.00 27.36           C  
ANISOU 2152  CZ  TYR B  71     3676   3204   3515    189    149    206       C  
ATOM   2153  OH  TYR B  71      -6.176  -8.784  -3.958  1.00 27.76           O  
ANISOU 2153  OH  TYR B  71     3878   3201   3467    291    202    246       O  
ATOM   2154  N   LYS B  72      -5.730  -4.423  -7.397  1.00 20.45           N  
ANISOU 2154  N   LYS B  72     2443   2695   2633    112    -94    201       N  
ATOM   2155  CA  LYS B  72      -4.871  -3.954  -6.302  1.00 23.82           C  
ANISOU 2155  CA  LYS B  72     2864   3188   3000    161    -51    212       C  
ATOM   2156  C   LYS B  72      -4.443  -2.504  -6.523  1.00 23.97           C  
ANISOU 2156  C   LYS B  72     2817   3284   3007     98    -88    225       C  
ATOM   2157  O   LYS B  72      -4.584  -1.651  -5.639  1.00 21.95           O  
ANISOU 2157  O   LYS B  72     2546   3007   2786     74    -61    229       O  
ATOM   2158  CB  LYS B  72      -3.642  -4.849  -6.147  1.00 25.14           C  
ANISOU 2158  CB  LYS B  72     3074   3438   3040    274    -40    191       C  
ATOM   2159  CG  LYS B  72      -3.868  -6.050  -5.265  1.00 35.91           C  
ANISOU 2159  CG  LYS B  72     4556   4694   4393    359     12    202       C  
ATOM   2160  CD  LYS B  72      -4.199  -5.613  -3.859  1.00 41.63           C  
ANISOU 2160  CD  LYS B  72     5302   5388   5128    344     64    232       C  
ATOM   2161  CE  LYS B  72      -2.965  -5.140  -3.130  1.00 44.58           C  
ANISOU 2161  CE  LYS B  72     5640   5913   5384    417     34    228       C  
ATOM   2162  NZ  LYS B  72      -3.312  -4.725  -1.747  1.00 41.71           N  
ANISOU 2162  NZ  LYS B  72     5325   5521   5003    393     85    246       N  
ATOM   2163  N   PHE B  73      -3.918  -2.225  -7.708  1.00 20.94           N  
ANISOU 2163  N   PHE B  73     2417   2977   2562     58   -138    228       N  
ATOM   2164  CA  PHE B  73      -3.519  -0.870  -8.056  1.00 21.91           C  
ANISOU 2164  CA  PHE B  73     2519   3146   2662    -34   -165    254       C  
ATOM   2165  C   PHE B  73      -4.711   0.087  -7.903  1.00 24.16           C  
ANISOU 2165  C   PHE B  73     2813   3286   3079    -69   -196    292       C  
ATOM   2166  O   PHE B  73      -4.580   1.199  -7.380  1.00 20.07           O  
ANISOU 2166  O   PHE B  73     2305   2736   2583   -112   -184    299       O  
ATOM   2167  CB  PHE B  73      -2.976  -0.864  -9.490  1.00 20.29           C  
ANISOU 2167  CB  PHE B  73     2325   3028   2355    -89   -199    261       C  
ATOM   2168  CG  PHE B  73      -2.518   0.474  -9.968  1.00 22.61           C  
ANISOU 2168  CG  PHE B  73     2638   3354   2601   -214   -213    303       C  
ATOM   2169  CD1 PHE B  73      -1.641   1.248  -9.211  1.00 21.49           C  
ANISOU 2169  CD1 PHE B  73     2460   3279   2425   -277   -166    283       C  
ATOM   2170  CD2 PHE B  73      -2.942   0.953 -11.204  1.00 26.22           C  
ANISOU 2170  CD2 PHE B  73     3168   3768   3027   -285   -279    364       C  
ATOM   2171  CE1 PHE B  73      -1.206   2.491  -9.679  1.00 23.55           C  
ANISOU 2171  CE1 PHE B  73     2768   3543   2637   -430   -165    321       C  
ATOM   2172  CE2 PHE B  73      -2.505   2.190 -11.684  1.00 29.85           C  
ANISOU 2172  CE2 PHE B  73     3694   4225   3422   -417   -284    422       C  
ATOM   2173  CZ  PHE B  73      -1.633   2.955 -10.921  1.00 26.12           C  
ANISOU 2173  CZ  PHE B  73     3195   3799   2930   -499   -217    399       C  
ATOM   2174  N   PHE B  74      -5.883  -0.361  -8.330  1.00 20.86           N  
ANISOU 2174  N   PHE B  74     2386   2782   2756    -46   -238    301       N  
ATOM   2175  CA  PHE B  74      -7.098   0.445  -8.221  1.00 21.42           C  
ANISOU 2175  CA  PHE B  74     2426   2739   2974    -40   -278    322       C  
ATOM   2176  C   PHE B  74      -7.403   0.763  -6.749  1.00 20.98           C  
ANISOU 2176  C   PHE B  74     2345   2628   2998     -8   -180    285       C  
ATOM   2177  O   PHE B  74      -7.646   1.914  -6.392  1.00 22.73           O  
ANISOU 2177  O   PHE B  74     2574   2779   3282     -6   -179    289       O  
ATOM   2178  CB  PHE B  74      -8.249  -0.315  -8.894  1.00 19.99           C  
ANISOU 2178  CB  PHE B  74     2195   2524   2877    -28   -343    313       C  
ATOM   2179  CG  PHE B  74      -9.603   0.363  -8.788  1.00 23.04           C  
ANISOU 2179  CG  PHE B  74     2493   2826   3437      8   -394    317       C  
ATOM   2180  CD1 PHE B  74      -9.992   1.319  -9.718  1.00 25.15           C  
ANISOU 2180  CD1 PHE B  74     2770   3058   3729     27   -531    376       C  
ATOM   2181  CD2 PHE B  74     -10.497   0.003  -7.792  1.00 23.02           C  
ANISOU 2181  CD2 PHE B  74     2396   2784   3564     30   -303    260       C  
ATOM   2182  CE1 PHE B  74     -11.249   1.926  -9.639  1.00 26.94           C  
ANISOU 2182  CE1 PHE B  74     2892   3216   4129    105   -597    372       C  
ATOM   2183  CE2 PHE B  74     -11.745   0.609  -7.705  1.00 28.46           C  
ANISOU 2183  CE2 PHE B  74     2961   3426   4427     80   -340    241       C  
ATOM   2184  CZ  PHE B  74     -12.124   1.561  -8.640  1.00 26.71           C  
ANISOU 2184  CZ  PHE B  74     2727   3174   4248    135   -497    294       C  
ATOM   2185  N   ALA B  75      -7.380  -0.252  -5.889  1.00 18.66           N  
ANISOU 2185  N   ALA B  75     2051   2353   2687     17    -93    249       N  
ATOM   2186  CA  ALA B  75      -7.754  -0.042  -4.485  1.00 20.42           C  
ANISOU 2186  CA  ALA B  75     2272   2533   2956     35     13    213       C  
ATOM   2187  C   ALA B  75      -6.762   0.894  -3.801  1.00 21.43           C  
ANISOU 2187  C   ALA B  75     2447   2700   2995     18     33    199       C  
ATOM   2188  O   ALA B  75      -7.148   1.788  -3.048  1.00 22.43           O  
ANISOU 2188  O   ALA B  75     2580   2763   3179     16     82    164       O  
ATOM   2189  CB  ALA B  75      -7.847  -1.374  -3.745  1.00 22.27           C  
ANISOU 2189  CB  ALA B  75     2545   2768   3149     51    101    200       C  
ATOM   2190  N   ASP B  76      -5.484   0.694  -4.080  1.00 19.42           N  
ANISOU 2190  N   ASP B  76     2217   2559   2604      1     -2    209       N  
ATOM   2191  CA  ASP B  76      -4.433   1.493  -3.464  1.00 20.25           C  
ANISOU 2191  CA  ASP B  76     2342   2739   2613    -46      7    179       C  
ATOM   2192  C   ASP B  76      -4.418   2.909  -4.027  1.00 20.66           C  
ANISOU 2192  C   ASP B  76     2416   2725   2708   -132    -31    190       C  
ATOM   2193  O   ASP B  76      -4.289   3.870  -3.274  1.00 22.12           O  
ANISOU 2193  O   ASP B  76     2643   2866   2896   -179      1    147       O  
ATOM   2194  CB  ASP B  76      -3.064   0.832  -3.669  1.00 22.85           C  
ANISOU 2194  CB  ASP B  76     2643   3242   2795    -35    -22    172       C  
ATOM   2195  CG  ASP B  76      -2.902  -0.450  -2.875  1.00 27.00           C  
ANISOU 2195  CG  ASP B  76     3193   3808   3257     76      6    167       C  
ATOM   2196  OD1 ASP B  76      -3.637  -0.633  -1.895  1.00 27.83           O  
ANISOU 2196  OD1 ASP B  76     3353   3828   3393    101     66    164       O  
ATOM   2197  OD2 ASP B  76      -2.013  -1.272  -3.217  1.00 26.04           O  
ANISOU 2197  OD2 ASP B  76     3047   3801   3046    144    -26    165       O  
ATOM   2198  N   LEU B  77      -4.563   3.052  -5.347  1.00 18.48           N  
ANISOU 2198  N   LEU B  77     2142   2427   2451   -157   -100    247       N  
ATOM   2199  CA  LEU B  77      -4.565   4.378  -5.932  1.00 21.66           C  
ANISOU 2199  CA  LEU B  77     2616   2736   2879   -236   -142    283       C  
ATOM   2200  C   LEU B  77      -5.734   5.155  -5.369  1.00 25.16           C  
ANISOU 2200  C   LEU B  77     3086   2998   3475   -171   -130    269       C  
ATOM   2201  O   LEU B  77      -5.584   6.315  -4.969  1.00 23.70           O  
ANISOU 2201  O   LEU B  77     2986   2712   3308   -220   -111    247       O  
ATOM   2202  CB  LEU B  77      -4.649   4.330  -7.459  1.00 21.68           C  
ANISOU 2202  CB  LEU B  77     2645   2740   2853   -263   -226    363       C  
ATOM   2203  CG  LEU B  77      -4.758   5.682  -8.175  1.00 22.41           C  
ANISOU 2203  CG  LEU B  77     2862   2698   2955   -336   -283    435       C  
ATOM   2204  CD1 LEU B  77      -3.463   6.504  -8.086  1.00 21.36           C  
ANISOU 2204  CD1 LEU B  77     2797   2615   2702   -509   -231    423       C  
ATOM   2205  CD2 LEU B  77      -5.109   5.426  -9.628  1.00 24.93           C  
ANISOU 2205  CD2 LEU B  77     3217   3021   3233   -331   -383    521       C  
ATOM   2206  N   LEU B  78      -6.899   4.511  -5.310  1.00 21.83           N  
ANISOU 2206  N   LEU B  78     2590   2536   3169    -66   -130    265       N  
ATOM   2207  CA  LEU B  78      -8.068   5.179  -4.752  1.00 23.63           C  
ANISOU 2207  CA  LEU B  78     2797   2622   3557     19   -102    229       C  
ATOM   2208  C   LEU B  78      -7.880   5.503  -3.261  1.00 25.07           C  
ANISOU 2208  C   LEU B  78     3010   2792   3724     11     25    136       C  
ATOM   2209  O   LEU B  78      -8.361   6.527  -2.782  1.00 20.85           O  
ANISOU 2209  O   LEU B  78     2519   2125   3278     49     60     88       O  
ATOM   2210  CB  LEU B  78      -9.328   4.366  -4.990  1.00 21.32           C  
ANISOU 2210  CB  LEU B  78     2376   2333   3392    104   -117    225       C  
ATOM   2211  CG  LEU B  78     -10.127   4.820  -6.210  1.00 30.47           C  
ANISOU 2211  CG  LEU B  78     3505   3422   4648    166   -264    289       C  
ATOM   2212  CD1 LEU B  78      -9.311   4.792  -7.500  1.00 34.75           C  
ANISOU 2212  CD1 LEU B  78     4141   4011   5050     90   -378    381       C  
ATOM   2213  CD2 LEU B  78     -11.401   4.004  -6.366  1.00 30.01           C  
ANISOU 2213  CD2 LEU B  78     3278   3400   4725    228   -283    257       C  
ATOM   2214  N   ASP B  79      -7.161   4.659  -2.526  1.00 21.62           N  
ANISOU 2214  N   ASP B  79     2569   2484   3161    -28     87    106       N  
ATOM   2215  CA  ASP B  79      -6.915   4.977  -1.113  1.00 21.34           C  
ANISOU 2215  CA  ASP B  79     2586   2454   3068    -46    189     19       C  
ATOM   2216  C   ASP B  79      -6.052   6.225  -0.960  1.00 20.99           C  
ANISOU 2216  C   ASP B  79     2640   2373   2962   -142    169    -18       C  
ATOM   2217  O   ASP B  79      -6.298   7.047  -0.073  1.00 23.37           O  
ANISOU 2217  O   ASP B  79     3011   2583   3287   -147    239   -104       O  
ATOM   2218  CB  ASP B  79      -6.295   3.798  -0.359  1.00 22.86           C  
ANISOU 2218  CB  ASP B  79     2777   2794   3115    -50    231     12       C  
ATOM   2219  CG  ASP B  79      -7.333   2.823   0.130  1.00 29.48           C  
ANISOU 2219  CG  ASP B  79     3579   3610   4010     12    321     10       C  
ATOM   2220  OD1 ASP B  79      -8.521   3.200   0.148  1.00 35.30           O  
ANISOU 2220  OD1 ASP B  79     4262   4247   4902     49    376    -21       O  
ATOM   2221  OD2 ASP B  79      -6.962   1.690   0.498  1.00 32.04           O  
ANISOU 2221  OD2 ASP B  79     3933   4014   4228     24    341     38       O  
ATOM   2222  N   TYR B  80      -5.055   6.368  -1.825  1.00 22.27           N  
ANISOU 2222  N   TYR B  80     2816   2605   3042   -235     88     34       N  
ATOM   2223  CA  TYR B  80      -4.210   7.555  -1.794  1.00 21.32           C  
ANISOU 2223  CA  TYR B  80     2791   2446   2862   -376     75      0       C  
ATOM   2224  C   TYR B  80      -4.976   8.794  -2.223  1.00 22.64           C  
ANISOU 2224  C   TYR B  80     3073   2367   3164   -359     61     18       C  
ATOM   2225  O   TYR B  80      -4.756   9.861  -1.668  1.00 22.70           O  
ANISOU 2225  O   TYR B  80     3200   2255   3168   -435     97    -52       O  
ATOM   2226  CB  TYR B  80      -2.948   7.385  -2.652  1.00 21.64           C  
ANISOU 2226  CB  TYR B  80     2798   2645   2777   -504     17     45       C  
ATOM   2227  CG  TYR B  80      -1.849   6.591  -1.974  1.00 23.05           C  
ANISOU 2227  CG  TYR B  80     2882   3068   2809   -532     23    -12       C  
ATOM   2228  CD1 TYR B  80      -1.185   7.099  -0.865  1.00 24.88           C  
ANISOU 2228  CD1 TYR B  80     3137   3363   2952   -622     44   -115       C  
ATOM   2229  CD2 TYR B  80      -1.476   5.330  -2.449  1.00 26.43           C  
ANISOU 2229  CD2 TYR B  80     3202   3660   3179   -455     -6     30       C  
ATOM   2230  CE1 TYR B  80      -0.173   6.378  -0.236  1.00 26.33           C  
ANISOU 2230  CE1 TYR B  80     3222   3790   2993   -623     16   -163       C  
ATOM   2231  CE2 TYR B  80      -0.462   4.606  -1.831  1.00 23.48           C  
ANISOU 2231  CE2 TYR B  80     2742   3503   2677   -436    -21    -17       C  
ATOM   2232  CZ  TYR B  80       0.184   5.138  -0.730  1.00 26.41           C  
ANISOU 2232  CZ  TYR B  80     3120   3955   2961   -514    -21   -108       C  
ATOM   2233  OH  TYR B  80       1.193   4.432  -0.110  1.00 28.03           O  
ANISOU 2233  OH  TYR B  80     3226   4393   3030   -472    -67   -152       O  
ATOM   2234  N   ILE B  81      -5.867   8.660  -3.208  1.00 20.01           N  
ANISOU 2234  N   ILE B  81     2713   1948   2943   -254     -2    108       N  
ATOM   2235  CA  ILE B  81      -6.729   9.788  -3.592  1.00 20.74           C  
ANISOU 2235  CA  ILE B  81     2910   1795   3176   -176    -40    135       C  
ATOM   2236  C   ILE B  81      -7.675  10.163  -2.441  1.00 21.60           C  
ANISOU 2236  C   ILE B  81     3007   1788   3412    -48     56     20       C  
ATOM   2237  O   ILE B  81      -7.869  11.332  -2.138  1.00 25.43           O  
ANISOU 2237  O   ILE B  81     3629   2071   3961    -30     78    -30       O  
ATOM   2238  CB  ILE B  81      -7.545   9.495  -4.876  1.00 29.93           C  
ANISOU 2238  CB  ILE B  81     4024   2924   4422    -66   -159    253       C  
ATOM   2239  CG1 ILE B  81      -6.620   9.433  -6.091  1.00 24.83           C  
ANISOU 2239  CG1 ILE B  81     3449   2351   3634   -206   -239    362       C  
ATOM   2240  CG2 ILE B  81      -8.595  10.585  -5.111  1.00 31.86           C  
ANISOU 2240  CG2 ILE B  81     4352   2920   4832     82   -216    275       C  
ATOM   2241  CD1 ILE B  81      -7.252   8.740  -7.307  1.00 27.18           C  
ANISOU 2241  CD1 ILE B  81     3679   2699   3950   -123   -356    461       C  
ATOM   2242  N   LYS B  82      -8.279   9.173  -1.805  1.00 22.02           N  
ANISOU 2242  N   LYS B  82     2911   1958   3496     36    126    -29       N  
ATOM   2243  CA  LYS B  82      -9.116   9.468  -0.641  1.00 25.34           C  
ANISOU 2243  CA  LYS B  82     3313   2305   4010    133    254   -155       C  
ATOM   2244  C   LYS B  82      -8.351  10.189   0.472  1.00 27.29           C  
ANISOU 2244  C   LYS B  82     3707   2519   4144     27    343   -271       C  
ATOM   2245  O   LYS B  82      -8.888  11.083   1.104  1.00 26.17           O  
ANISOU 2245  O   LYS B  82     3643   2217   4085     93    422   -375       O  
ATOM   2246  CB  LYS B  82      -9.771   8.183  -0.132  1.00 27.94           C  
ANISOU 2246  CB  LYS B  82     3478   2785   4354    186    338   -179       C  
ATOM   2247  CG  LYS B  82     -10.827   7.667  -1.092  1.00 30.53           C  
ANISOU 2247  CG  LYS B  82     3648   3117   4836    294    263   -111       C  
ATOM   2248  CD  LYS B  82     -10.979   6.154  -0.974  1.00 38.55           C  
ANISOU 2248  CD  LYS B  82     4545   4299   5802    255    307    -92       C  
ATOM   2249  CE  LYS B  82     -11.103   5.727   0.469  1.00 43.21           C  
ANISOU 2249  CE  LYS B  82     5143   4945   6329    229    490   -187       C  
ATOM   2250  NZ  LYS B  82     -11.112   4.241   0.600  1.00 48.43           N  
ANISOU 2250  NZ  LYS B  82     5755   5731   6915    174    533   -147       N  
ATOM   2251  N   ALA B  83      -7.085   9.833   0.681  1.00 26.25           N  
ANISOU 2251  N   ALA B  83     3609   2541   3823   -134    323   -264       N  
ATOM   2252  CA  ALA B  83      -6.266  10.508   1.698  1.00 23.76           C  
ANISOU 2252  CA  ALA B  83     3422   2226   3380   -265    378   -384       C  
ATOM   2253  C   ALA B  83      -6.124  11.989   1.392  1.00 26.99           C  
ANISOU 2253  C   ALA B  83     4009   2397   3848   -330    356   -416       C  
ATOM   2254  O   ALA B  83      -6.163  12.833   2.290  1.00 27.31           O  
ANISOU 2254  O   ALA B  83     4182   2315   3880   -360    436   -553       O  
ATOM   2255  CB  ALA B  83      -4.893   9.858   1.802  1.00 26.59           C  
ANISOU 2255  CB  ALA B  83     3742   2825   3538   -413    322   -366       C  
ATOM   2256  N   LEU B  84      -5.928  12.305   0.115  1.00 25.37           N  
ANISOU 2256  N   LEU B  84     3839   2115   3685   -365    253   -289       N  
ATOM   2257  CA  LEU B  84      -5.836  13.697  -0.313  1.00 27.46           C  
ANISOU 2257  CA  LEU B  84     4319   2111   4004   -429    226   -285       C  
ATOM   2258  C   LEU B  84      -7.177  14.406  -0.115  1.00 30.97           C  
ANISOU 2258  C   LEU B  84     4828   2291   4648   -199    263   -330       C  
ATOM   2259  O   LEU B  84      -7.222  15.580   0.288  1.00 31.89           O  
ANISOU 2259  O   LEU B  84     5150   2162   4807   -215    307   -420       O  
ATOM   2260  CB  LEU B  84      -5.437  13.769  -1.795  1.00 30.26           C  
ANISOU 2260  CB  LEU B  84     4710   2448   4339   -504    111   -113       C  
ATOM   2261  CG  LEU B  84      -4.070  13.251  -2.212  1.00 29.18           C  
ANISOU 2261  CG  LEU B  84     4510   2557   4021   -732     83    -72       C  
ATOM   2262  CD1 LEU B  84      -3.924  13.214  -3.748  1.00 28.38           C  
ANISOU 2262  CD1 LEU B  84     4439   2442   3901   -772     -8    100       C  
ATOM   2263  CD2 LEU B  84      -2.981  14.134  -1.600  1.00 27.27           C  
ANISOU 2263  CD2 LEU B  84     4400   2292   3668   -990    132   -182       C  
ATOM   2264  N   ASN B  85      -8.267  13.704  -0.421  1.00 28.81           N  
ANISOU 2264  N   ASN B  85     4376   2068   4503     14    245   -280       N  
ATOM   2265  CA  ASN B  85      -9.606  14.296  -0.314  1.00 31.84           C  
ANISOU 2265  CA  ASN B  85     4754   2246   5099    266    270   -329       C  
ATOM   2266  C   ASN B  85      -9.998  14.693   1.104  1.00 34.97           C  
ANISOU 2266  C   ASN B  85     5182   2581   5523    323    443   -533       C  
ATOM   2267  O   ASN B  85     -10.838  15.568   1.291  1.00 38.52           O  
ANISOU 2267  O   ASN B  85     5699   2803   6133    507    483   -612       O  
ATOM   2268  CB  ASN B  85     -10.672  13.344  -0.872  1.00 33.44           C  
ANISOU 2268  CB  ASN B  85     4703   2577   5427    449    218   -257       C  
ATOM   2269  CG  ASN B  85     -10.721  13.341  -2.374  1.00 40.29           C  
ANISOU 2269  CG  ASN B  85     5581   3408   6320    478     30    -74       C  
ATOM   2270  OD1 ASN B  85     -10.331  14.308  -3.017  1.00 45.08           O  
ANISOU 2270  OD1 ASN B  85     6406   3813   6909    439    -55      5       O  
ATOM   2271  ND2 ASN B  85     -11.219  12.257  -2.945  1.00 47.93           N  
ANISOU 2271  ND2 ASN B  85     6335   4559   7316    534    -33     -6       N  
ATOM   2272  N   ARG B  86      -9.408  14.047   2.104  1.00 33.64           N  
ANISOU 2272  N   ARG B  86     4973   2618   5192    184    544   -623       N  
ATOM   2273  CA  ARG B  86      -9.775  14.360   3.491  1.00 33.66           C  
ANISOU 2273  CA  ARG B  86     5021   2587   5179    222    720   -823       C  
ATOM   2274  C   ARG B  86      -8.716  15.173   4.242  1.00 38.28           C  
ANISOU 2274  C   ARG B  86     5843   3103   5599     15    755   -945       C  
ATOM   2275  O   ARG B  86      -8.973  15.677   5.339  1.00 37.44           O  
ANISOU 2275  O   ARG B  86     5836   2921   5469     36    894  -1130       O  
ATOM   2276  CB  ARG B  86     -10.152  13.088   4.266  1.00 31.86           C  
ANISOU 2276  CB  ARG B  86     4603   2620   4883    243    831   -857       C  
ATOM   2277  CG  ARG B  86      -8.990  12.147   4.509  1.00 27.44           C  
ANISOU 2277  CG  ARG B  86     4031   2307   4087     47    787   -799       C  
ATOM   2278  CD  ARG B  86      -9.410  10.852   5.184  1.00 34.31           C  
ANISOU 2278  CD  ARG B  86     4760   3389   4888     78    888   -799       C  
ATOM   2279  NE  ARG B  86      -8.234   9.994   5.310  1.00 33.13           N  
ANISOU 2279  NE  ARG B  86     4619   3448   4520    -68    810   -727       N  
ATOM   2280  CZ  ARG B  86      -8.000   8.897   4.598  1.00 31.53           C  
ANISOU 2280  CZ  ARG B  86     4299   3383   4298    -69    722   -585       C  
ATOM   2281  NH1 ARG B  86      -8.884   8.457   3.704  1.00 27.51           N  
ANISOU 2281  NH1 ARG B  86     3652   2839   3960     38    698   -499       N  
ATOM   2282  NH2 ARG B  86      -6.868   8.232   4.792  1.00 29.51           N  
ANISOU 2282  NH2 ARG B  86     4059   3306   3846   -171    651   -542       N  
ATOM   2283  N   ASN B  87      -7.539  15.330   3.638  1.00 37.91           N  
ANISOU 2283  N   ASN B  87     5881   3087   5435   -197    636   -857       N  
ATOM   2284  CA  ASN B  87      -6.449  16.067   4.286  1.00 42.03           C  
ANISOU 2284  CA  ASN B  87     6596   3576   5795   -440    653   -979       C  
ATOM   2285  C   ASN B  87      -6.007  17.343   3.570  1.00 47.68           C  
ANISOU 2285  C   ASN B  87     7553   4004   6560   -563    590   -954       C  
ATOM   2286  O   ASN B  87      -5.392  18.224   4.185  1.00 51.99           O  
ANISOU 2286  O   ASN B  87     8303   4430   7020   -748    631  -1097       O  
ATOM   2287  CB  ASN B  87      -5.240  15.149   4.505  1.00 43.55           C  
ANISOU 2287  CB  ASN B  87     6672   4108   5766   -643    593   -949       C  
ATOM   2288  CG  ASN B  87      -5.455  14.164   5.644  1.00 45.14           C  
ANISOU 2288  CG  ASN B  87     6759   4541   5851   -578    676  -1024       C  
ATOM   2289  OD1 ASN B  87      -5.824  14.557   6.755  1.00 44.50           O  
ANISOU 2289  OD1 ASN B  87     6780   4400   5727   -554    796  -1192       O  
ATOM   2290  ND2 ASN B  87      -5.234  12.880   5.369  1.00 42.56           N  
ANISOU 2290  ND2 ASN B  87     6246   4464   5460   -549    620   -901       N  
ATOM   2291  N   SER B  88      -6.316  17.458   2.283  1.00 76.44           N  
ANISOU 2291  N   SER B  88    11509   5930  11604  -1609  -2172  -1899       N  
ATOM   2292  CA  SER B  88      -5.822  18.607   1.522  1.00 78.38           C  
ANISOU 2292  CA  SER B  88    11796   5840  12144  -1934  -2039  -1787       C  
ATOM   2293  C   SER B  88      -6.876  19.661   1.182  1.00 80.01           C  
ANISOU 2293  C   SER B  88    12394   5554  12452  -1702  -1840  -1705       C  
ATOM   2294  O   SER B  88      -7.960  19.706   1.770  1.00 74.01           O  
ANISOU 2294  O   SER B  88    11853   4714  11554  -1290  -1814  -1852       O  
ATOM   2295  CB  SER B  88      -5.093  18.161   0.247  1.00 73.22           C  
ANISOU 2295  CB  SER B  88    10793   5364  11663  -2215  -1950  -1438       C  
ATOM   2296  OG  SER B  88      -6.008  17.733  -0.743  1.00 68.57           O  
ANISOU 2296  OG  SER B  88    10235   4734  11084  -1950  -1787  -1068       O  
ATOM   2297  N   ASP B  89      -6.524  20.496   0.210  1.00 88.39           N  
ANISOU 2297  N   ASP B  89    13534   6311  13739  -1960  -1688  -1477       N  
ATOM   2298  CA  ASP B  89      -7.279  21.691  -0.137  1.00 96.01           C  
ANISOU 2298  CA  ASP B  89    14907   6750  14824  -1780  -1539  -1407       C  
ATOM   2299  C   ASP B  89      -8.150  21.493  -1.375  1.00 93.13           C  
ANISOU 2299  C   ASP B  89    14583   6326  14477  -1475  -1397   -974       C  
ATOM   2300  O   ASP B  89      -8.626  22.462  -1.965  1.00 95.80           O  
ANISOU 2300  O   ASP B  89    15232   6245  14921  -1343  -1287   -820       O  
ATOM   2301  CB  ASP B  89      -6.302  22.840  -0.388  1.00104.94           C  
ANISOU 2301  CB  ASP B  89    16176   7522  16176  -2280  -1456  -1443       C  
ATOM   2302  CG  ASP B  89      -5.189  22.456  -1.353  1.00108.47           C  
ANISOU 2302  CG  ASP B  89    16293   8197  16724  -2767  -1357  -1189       C  
ATOM   2303  OD1 ASP B  89      -4.822  23.288  -2.212  1.00113.81           O  
ANISOU 2303  OD1 ASP B  89    17119   8538  17586  -3054  -1159   -986       O  
ATOM   2304  OD2 ASP B  89      -4.683  21.316  -1.253  1.00107.22           O  
ANISOU 2304  OD2 ASP B  89    15719   8558  16462  -2844  -1468  -1201       O  
ATOM   2305  N   ARG B  90      -8.351  20.241  -1.772  1.00 86.89           N  
ANISOU 2305  N   ARG B  90    13485   5953  13577  -1349  -1419   -786       N  
ATOM   2306  CA  ARG B  90      -9.145  19.939  -2.960  1.00 83.80           C  
ANISOU 2306  CA  ARG B  90    13085   5585  13171  -1069  -1312   -396       C  
ATOM   2307  C   ARG B  90      -9.911  18.644  -2.769  1.00 74.51           C  
ANISOU 2307  C   ARG B  90    11654   4802  11855   -732  -1371   -404       C  
ATOM   2308  O   ARG B  90      -9.550  17.826  -1.924  1.00 71.68           O  
ANISOU 2308  O   ARG B  90    11090   4764  11382   -812  -1457   -617       O  
ATOM   2309  CB  ARG B  90      -8.252  19.853  -4.188  1.00 86.14           C  
ANISOU 2309  CB  ARG B  90    13256   5949  13525  -1462  -1191    -37       C  
ATOM   2310  N   SER B  91     -10.961  18.451  -3.559  1.00 72.81           N  
ANISOU 2310  N   SER B  91    11440   4608  11614   -351  -1310   -177       N  
ATOM   2311  CA  SER B  91     -11.794  17.260  -3.419  1.00 71.20           C  
ANISOU 2311  CA  SER B  91    10921   4907  11227    -41  -1256   -197       C  
ATOM   2312  C   SER B  91     -12.144  16.563  -4.730  1.00 73.71           C  
ANISOU 2312  C   SER B  91    11026   5494  11488     58  -1186    174       C  
ATOM   2313  O   SER B  91     -12.137  17.174  -5.802  1.00 79.00           O  
ANISOU 2313  O   SER B  91    11884   5885  12249     59  -1200    462       O  
ATOM   2314  CB  SER B  91     -13.090  17.600  -2.678  1.00 70.64           C  
ANISOU 2314  CB  SER B  91    10948   4776  11116    436  -1229   -487       C  
ATOM   2315  OG  SER B  91     -13.008  17.240  -1.309  1.00 68.34           O  
ANISOU 2315  OG  SER B  91    10618   4691  10659    398  -1210   -848       O  
ATOM   2316  N   ILE B  92     -12.448  15.272  -4.619  1.00 69.14           N  
ANISOU 2316  N   ILE B  92    10106   5437  10727    130  -1116    163       N  
ATOM   2317  CA  ILE B  92     -13.169  14.540  -5.654  1.00 63.79           C  
ANISOU 2317  CA  ILE B  92     9216   5054   9965    326  -1062    394       C  
ATOM   2318  C   ILE B  92     -14.639  15.057  -5.606  1.00 61.66           C  
ANISOU 2318  C   ILE B  92     8990   4703   9736    810  -1072    269       C  
ATOM   2319  O   ILE B  92     -14.818  16.262  -5.753  1.00 61.62           O  
ANISOU 2319  O   ILE B  92     9295   4240   9878    977  -1160    274       O  
ATOM   2320  CB  ILE B  92     -13.008  13.068  -5.441  1.00 52.29           C  
ANISOU 2320  CB  ILE B  92     7451   4090   8326    217   -993    372       C  
ATOM   2321  N   PRO B  93     -15.698  14.232  -5.385  1.00 54.91           N  
ANISOU 2321  N   PRO B  93     7836   4257   8769   1041   -985    129       N  
ATOM   2322  CA  PRO B  93     -16.179  12.865  -5.126  1.00 52.30           C  
ANISOU 2322  CA  PRO B  93     7169   4436   8265    995   -853     49       C  
ATOM   2323  C   PRO B  93     -15.846  11.910  -6.246  1.00 43.54           C  
ANISOU 2323  C   PRO B  93     5889   3575   7078    839   -870    333       C  
ATOM   2324  O   PRO B  93     -15.618  12.332  -7.383  1.00 40.69           O  
ANISOU 2324  O   PRO B  93     5613   3075   6774    872   -969    590       O  
ATOM   2325  CB  PRO B  93     -17.705  13.029  -5.069  1.00 56.39           C  
ANISOU 2325  CB  PRO B  93     7485   5124   8818   1400   -799   -156       C  
ATOM   2326  CG  PRO B  93     -17.974  14.249  -5.836  1.00 61.76           C  
ANISOU 2326  CG  PRO B  93     8361   5434   9672   1724   -979    -48       C  
ATOM   2327  CD  PRO B  93     -16.850  15.150  -5.444  1.00 60.64           C  
ANISOU 2327  CD  PRO B  93     8631   4798   9613   1510  -1041     -7       C  
ATOM   2328  N   MET B  94     -15.793  10.635  -5.897  1.00 37.28           N  
ANISOU 2328  N   MET B  94     4919   3119   6129    665   -768    283       N  
ATOM   2329  CA  MET B  94     -15.562   9.588  -6.853  1.00 38.58           C  
ANISOU 2329  CA  MET B  94     4927   3529   6203    542   -774    480       C  
ATOM   2330  C   MET B  94     -16.686   8.584  -6.746  1.00 37.40           C  
ANISOU 2330  C   MET B  94     4532   3725   5955    592   -661    346       C  
ATOM   2331  O   MET B  94     -17.156   8.290  -5.647  1.00 34.86           O  
ANISOU 2331  O   MET B  94     4192   3495   5558    556   -519    128       O  
ATOM   2332  CB  MET B  94     -14.264   8.860  -6.530  1.00 36.37           C  
ANISOU 2332  CB  MET B  94     4706   3281   5834    253   -778    533       C  
ATOM   2333  CG  MET B  94     -13.017   9.706  -6.600  1.00 41.37           C  
ANISOU 2333  CG  MET B  94     5489   3654   6577     98   -866    620       C  
ATOM   2334  SD  MET B  94     -11.600   8.602  -6.514  1.00 49.54           S  
ANISOU 2334  SD  MET B  94     6428   4882   7513   -151   -903    653       S  
ATOM   2335  CE  MET B  94     -12.210   7.329  -7.566  1.00 46.48           C  
ANISOU 2335  CE  MET B  94     5873   4790   6995    -70   -838    780       C  
ATOM   2336  N   THR B  95     -17.112   8.060  -7.887  1.00 33.85           N  
ANISOU 2336  N   THR B  95     3906   3473   5482    639   -710    464       N  
ATOM   2337  CA  THR B  95     -17.875   6.816  -7.904  1.00 33.18           C  
ANISOU 2337  CA  THR B  95     3595   3717   5294    536   -605    353       C  
ATOM   2338  C   THR B  95     -17.010   5.760  -8.575  1.00 30.74           C  
ANISOU 2338  C   THR B  95     3342   3469   4869    329   -640    521       C  
ATOM   2339  O   THR B  95     -15.996   6.087  -9.205  1.00 29.98           O  
ANISOU 2339  O   THR B  95     3368   3241   4781    315   -735    712       O  
ATOM   2340  CB  THR B  95     -19.209   6.968  -8.627  1.00 35.48           C  
ANISOU 2340  CB  THR B  95     3584   4243   5654    768   -661    255       C  
ATOM   2341  OG1 THR B  95     -18.991   7.550  -9.918  1.00 36.06           O  
ANISOU 2341  OG1 THR B  95     3717   4235   5750    958   -877    478       O  
ATOM   2342  CG2 THR B  95     -20.138   7.872  -7.822  1.00 38.55           C  
ANISOU 2342  CG2 THR B  95     3858   4627   6161   1018   -597      6       C  
ATOM   2343  N   VAL B  96     -17.381   4.493  -8.439  1.00 30.10           N  
ANISOU 2343  N   VAL B  96     3185   3575   4677    155   -543    434       N  
ATOM   2344  CA  VAL B  96     -16.539   3.429  -8.981  1.00 30.25           C  
ANISOU 2344  CA  VAL B  96     3301   3607   4584      6   -583    548       C  
ATOM   2345  C   VAL B  96     -17.349   2.445  -9.801  1.00 33.35           C  
ANISOU 2345  C   VAL B  96     3529   4225   4919    -68   -579    482       C  
ATOM   2346  O   VAL B  96     -18.552   2.264  -9.580  1.00 32.66           O  
ANISOU 2346  O   VAL B  96     3241   4308   4860   -114   -493    308       O  
ATOM   2347  CB  VAL B  96     -15.783   2.666  -7.867  1.00 33.94           C  
ANISOU 2347  CB  VAL B  96     4008   3951   4936   -159   -516    519       C  
ATOM   2348  CG1 VAL B  96     -15.032   3.633  -6.969  1.00 38.04           C  
ANISOU 2348  CG1 VAL B  96     4667   4285   5500   -105   -554    521       C  
ATOM   2349  CG2 VAL B  96     -16.742   1.847  -7.039  1.00 34.22           C  
ANISOU 2349  CG2 VAL B  96     4074   4062   4867   -332   -335    368       C  
ATOM   2350  N   ASP B  97     -16.698   1.821 -10.773  1.00 29.65           N  
ANISOU 2350  N   ASP B  97     3113   3782   4369    -89   -667    583       N  
ATOM   2351  CA  ASP B  97     -17.294   0.668 -11.429  1.00 32.38           C  
ANISOU 2351  CA  ASP B  97     3380   4290   4632   -213   -672    480       C  
ATOM   2352  C   ASP B  97     -16.157  -0.256 -11.811  1.00 27.90           C  
ANISOU 2352  C   ASP B  97     3022   3626   3951   -261   -705    548       C  
ATOM   2353  O   ASP B  97     -14.986   0.115 -11.720  1.00 26.71           O  
ANISOU 2353  O   ASP B  97     2979   3365   3803   -175   -733    669       O  
ATOM   2354  CB  ASP B  97     -18.119   1.074 -12.657  1.00 37.82           C  
ANISOU 2354  CB  ASP B  97     3825   5215   5330    -64   -814    459       C  
ATOM   2355  CG  ASP B  97     -19.132  -0.010 -13.085  1.00 46.45           C  
ANISOU 2355  CG  ASP B  97     4744   6526   6380   -244   -821    244       C  
ATOM   2356  OD1 ASP B  97     -19.326  -1.018 -12.360  1.00 41.18           O  
ANISOU 2356  OD1 ASP B  97     4162   5790   5695   -526   -668    119       O  
ATOM   2357  OD2 ASP B  97     -19.743   0.163 -14.161  1.00 54.75           O  
ANISOU 2357  OD2 ASP B  97     5598   7805   7397   -116   -995    197       O  
ATOM   2358  N   PHE B  98     -16.508  -1.460 -12.226  1.00 28.14           N  
ANISOU 2358  N   PHE B  98     3092   3703   3895   -400   -702    432       N  
ATOM   2359  CA  PHE B  98     -15.523  -2.495 -12.452  1.00 27.71           C  
ANISOU 2359  CA  PHE B  98     3274   3519   3736   -407   -731    437       C  
ATOM   2360  C   PHE B  98     -15.895  -3.132 -13.765  1.00 29.12           C  
ANISOU 2360  C   PHE B  98     3382   3857   3824   -419   -812    336       C  
ATOM   2361  O   PHE B  98     -17.054  -3.478 -13.982  1.00 30.80           O  
ANISOU 2361  O   PHE B  98     3466   4190   4047   -579   -814    187       O  
ATOM   2362  CB  PHE B  98     -15.606  -3.549 -11.345  1.00 28.40           C  
ANISOU 2362  CB  PHE B  98     3646   3372   3773   -599   -641    365       C  
ATOM   2363  CG  PHE B  98     -15.301  -3.018  -9.981  1.00 27.81           C  
ANISOU 2363  CG  PHE B  98     3694   3157   3715   -593   -575    439       C  
ATOM   2364  CD1 PHE B  98     -16.298  -2.418  -9.211  1.00 28.51           C  
ANISOU 2364  CD1 PHE B  98     3666   3314   3854   -716   -437    389       C  
ATOM   2365  CD2 PHE B  98     -14.019  -3.120  -9.460  1.00 28.86           C  
ANISOU 2365  CD2 PHE B  98     4037   3126   3803   -441   -665    518       C  
ATOM   2366  CE1 PHE B  98     -16.015  -1.912  -7.939  1.00 29.54           C  
ANISOU 2366  CE1 PHE B  98     3946   3325   3953   -702   -375    427       C  
ATOM   2367  CE2 PHE B  98     -13.720  -2.625  -8.186  1.00 30.00           C  
ANISOU 2367  CE2 PHE B  98     4314   3159   3926   -428   -650    558       C  
ATOM   2368  CZ  PHE B  98     -14.728  -2.021  -7.423  1.00 30.52           C  
ANISOU 2368  CZ  PHE B  98     4322   3269   4006   -568   -497    517       C  
ATOM   2369  N   ILE B  99     -14.928  -3.266 -14.658  1.00 28.72           N  
ANISOU 2369  N   ILE B  99     3385   3849   3676   -259   -873    384       N  
ATOM   2370  CA  ILE B  99     -15.215  -3.954 -15.898  1.00 30.32           C  
ANISOU 2370  CA  ILE B  99     3578   4202   3738   -259   -952    254       C  
ATOM   2371  C   ILE B  99     -14.218  -5.072 -16.098  1.00 30.79           C  
ANISOU 2371  C   ILE B  99     3881   4116   3703   -192   -949    161       C  
ATOM   2372  O   ILE B  99     -13.087  -5.038 -15.602  1.00 30.68           O  
ANISOU 2372  O   ILE B  99     3952   3985   3721    -55   -917    235       O  
ATOM   2373  CB  ILE B  99     -15.244  -3.001 -17.132  1.00 43.70           C  
ANISOU 2373  CB  ILE B  99     5109   6171   5325    -90  -1033    364       C  
ATOM   2374  CG1 ILE B  99     -14.003  -2.129 -17.173  1.00 47.41           C  
ANISOU 2374  CG1 ILE B  99     5598   6623   5793     54   -956    578       C  
ATOM   2375  CG2 ILE B  99     -16.489  -2.123 -17.137  1.00 42.69           C  
ANISOU 2375  CG2 ILE B  99     4759   6190   5271    -86  -1117    383       C  
ATOM   2376  CD1 ILE B  99     -12.856  -2.756 -17.921  1.00 58.22           C  
ANISOU 2376  CD1 ILE B  99     7054   8060   7008    147   -902    530       C  
ATOM   2377  N   ARG B 100     -14.629  -6.090 -16.816  1.00 32.74           N  
ANISOU 2377  N   ARG B 100     4230   4369   3841   -268  -1007    -41       N  
ATOM   2378  CA AARG B 100     -13.702  -7.139 -17.174  0.60 36.31           C  
ANISOU 2378  CA AARG B 100     4927   4680   4190   -131  -1022   -172       C  
ATOM   2379  CA BARG B 100     -13.680  -7.120 -17.187  0.40 36.48           C  
ANISOU 2379  CA BARG B 100     4944   4706   4210   -125  -1022   -169       C  
ATOM   2380  C   ARG B 100     -13.841  -7.449 -18.651  1.00 37.84           C  
ANISOU 2380  C   ARG B 100     5085   5111   4182    -66  -1091   -334       C  
ATOM   2381  O   ARG B 100     -14.947  -7.400 -19.199  1.00 41.23           O  
ANISOU 2381  O   ARG B 100     5401   5704   4560   -225  -1177   -428       O  
ATOM   2382  CB AARG B 100     -13.972  -8.375 -16.334  0.60 38.68           C  
ANISOU 2382  CB AARG B 100     5573   4589   4536   -303  -1024   -299       C  
ATOM   2383  CB BARG B 100     -13.828  -8.376 -16.335  0.40 39.15           C  
ANISOU 2383  CB BARG B 100     5642   4643   4592   -269  -1025   -293       C  
ATOM   2384  CG AARG B 100     -12.923  -9.440 -16.471  0.60 42.47           C  
ANISOU 2384  CG AARG B 100     6371   4826   4940    -70  -1073   -427       C  
ATOM   2385  CG BARG B 100     -12.622  -9.302 -16.440  0.40 42.50           C  
ANISOU 2385  CG BARG B 100     6346   4854   4947      9  -1071   -398       C  
ATOM   2386  CD AARG B 100     -13.221 -10.607 -15.573  0.60 42.98           C  
ANISOU 2386  CD AARG B 100     6894   4409   5027   -242  -1088   -497       C  
ATOM   2387  CD BARG B 100     -13.004 -10.751 -16.222  0.40 44.51           C  
ANISOU 2387  CD BARG B 100     7053   4692   5167   -137  -1120   -588       C  
ATOM   2388  NE AARG B 100     -12.367 -11.734 -15.911  0.60 46.37           N  
ANISOU 2388  NE AARG B 100     7677   4568   5374     30  -1184   -674       N  
ATOM   2389  NE BARG B 100     -13.753 -10.916 -14.986  0.40 44.13           N  
ANISOU 2389  NE BARG B 100     7203   4362   5200   -459  -1054   -481       N  
ATOM   2390  CZ AARG B 100     -12.542 -12.963 -15.446  0.60 49.88           C  
ANISOU 2390  CZ AARG B 100     8650   4510   5794    -70  -1231   -774       C  
ATOM   2391  CZ BARG B 100     -13.909 -12.073 -14.354  0.40 46.65           C  
ANISOU 2391  CZ BARG B 100     8035   4201   5490   -612  -1059   -539       C  
ATOM   2392  NH1AARG B 100     -13.542 -13.220 -14.615  0.60 50.71           N  
ANISOU 2392  NH1AARG B 100     8971   4362   5934   -510  -1147   -697       N  
ATOM   2393  NH1BARG B 100     -13.360 -13.177 -14.839  0.40 50.60           N  
ANISOU 2393  NH1BARG B 100     8907   4406   5913   -423  -1167   -722       N  
ATOM   2394  NH2AARG B 100     -11.716 -13.932 -15.812  0.60 51.79           N  
ANISOU 2394  NH2AARG B 100     9221   4490   5966    266  -1347   -958       N  
ATOM   2395  NH2BARG B 100     -14.607 -12.124 -13.230  0.40 45.64           N  
ANISOU 2395  NH2BARG B 100     8086   3866   5389   -951   -939   -414       N  
ATOM   2396  N   LEU B 101     -12.723  -7.749 -19.290  1.00 42.82           N  
ANISOU 2396  N   LEU B 101     7214   4006   5050   -566  -3073   -353       N  
ATOM   2397  CA  LEU B 101     -12.746  -8.114 -20.697  1.00 53.55           C  
ANISOU 2397  CA  LEU B 101     8465   5410   6471   -490  -3165   -465       C  
ATOM   2398  C   LEU B 101     -12.469  -9.600 -20.829  1.00 61.18           C  
ANISOU 2398  C   LEU B 101     9746   6068   7432   -522  -3342   -528       C  
ATOM   2399  O   LEU B 101     -11.401 -10.078 -20.435  1.00 63.83           O  
ANISOU 2399  O   LEU B 101    10375   6342   7536   -328  -3223   -515       O  
ATOM   2400  CB  LEU B 101     -11.719  -7.300 -21.475  1.00 57.18           C  
ANISOU 2400  CB  LEU B 101     8816   6188   6720   -185  -2870   -513       C  
ATOM   2401  CG  LEU B 101     -12.171  -5.958 -22.055  1.00 60.71           C  
ANISOU 2401  CG  LEU B 101     8932   6917   7217   -163  -2776   -496       C  
ATOM   2402  CD1 LEU B 101     -13.061  -5.178 -21.104  1.00 63.78           C  
ANISOU 2402  CD1 LEU B 101     9176   7309   7750   -319  -2822   -396       C  
ATOM   2403  CD2 LEU B 101     -10.953  -5.148 -22.402  1.00 56.42           C  
ANISOU 2403  CD2 LEU B 101     8349   6592   6496     61  -2466   -496       C  
ATOM   2404  N   LYS B 102     -13.443 -10.325 -21.368  1.00 67.90           N  
ANISOU 2404  N   LYS B 102    10509   6723   8566   -772  -3617   -598       N  
ATOM   2405  CA  LYS B 102     -13.359 -11.778 -21.472  1.00 74.46           C  
ANISOU 2405  CA  LYS B 102    11626   7198   9467   -866  -3800   -681       C  
ATOM   2406  C   LYS B 102     -13.856 -12.266 -22.825  1.00 79.25           C  
ANISOU 2406  C   LYS B 102    12098   7816  10198   -908  -4017   -871       C  
ATOM   2407  O   LYS B 102     -13.647 -13.420 -23.189  1.00 87.37           O  
ANISOU 2407  O   LYS B 102    13366   8594  11237   -920  -4167   -998       O  
ATOM   2408  CB  LYS B 102     -14.151 -12.433 -20.347  1.00 77.82           C  
ANISOU 2408  CB  LYS B 102    12112   7208  10246  -1269  -3841   -563       C  
ATOM   2409  N   VAL B 115     -17.576  -8.235 -22.326  1.00 69.72           N  
ANISOU 2409  N   VAL B 115     9285   7368   9837  -1460  -3937   -450       N  
ATOM   2410  CA  VAL B 115     -17.431  -7.178 -21.326  1.00 68.85           C  
ANISOU 2410  CA  VAL B 115     9092   7364   9704  -1419  -3734   -267       C  
ATOM   2411  C   VAL B 115     -18.389  -7.415 -20.166  1.00 72.29           C  
ANISOU 2411  C   VAL B 115     9275   7543  10649  -1842  -3701    -33       C  
ATOM   2412  O   VAL B 115     -19.535  -6.968 -20.210  1.00 74.91           O  
ANISOU 2412  O   VAL B 115     9107   7975  11382  -2029  -3702    119       O  
ATOM   2413  CB  VAL B 115     -17.726  -5.774 -21.923  1.00 60.23           C  
ANISOU 2413  CB  VAL B 115     7683   6654   8548  -1223  -3659   -227       C  
ATOM   2414  CG1 VAL B 115     -17.489  -4.683 -20.878  1.00 57.20           C  
ANISOU 2414  CG1 VAL B 115     7239   6361   8133  -1159  -3462    -67       C  
ATOM   2415  CG2 VAL B 115     -16.862  -5.517 -23.131  1.00 56.27           C  
ANISOU 2415  CG2 VAL B 115     7360   6380   7640   -880  -3579   -393       C  
ATOM   2416  N   ILE B 116     -17.943  -8.120 -19.131  1.00 69.60           N  
ANISOU 2416  N   ILE B 116     9251   6907  10286  -1923  -3496     64       N  
ATOM   2417  CA  ILE B 116     -18.841  -8.383 -18.007  1.00 73.92           C  
ANISOU 2417  CA  ILE B 116     9559   7290  11235  -2148  -3079    402       C  
ATOM   2418  C   ILE B 116     -18.875  -7.204 -17.046  1.00 70.96           C  
ANISOU 2418  C   ILE B 116     9043   7200  10719  -1916  -2583    621       C  
ATOM   2419  O   ILE B 116     -17.871  -6.504 -16.863  1.00 62.31           O  
ANISOU 2419  O   ILE B 116     8217   6304   9155  -1591  -2483    514       O  
ATOM   2420  CB  ILE B 116     -18.526  -9.712 -17.259  1.00 79.00           C  
ANISOU 2420  CB  ILE B 116    10577   7508  11933  -2276  -2923    500       C  
ATOM   2421  CG1 ILE B 116     -18.460  -9.492 -15.741  1.00 80.70           C  
ANISOU 2421  CG1 ILE B 116    10857   7756  12047  -2139  -2307    839       C  
ATOM   2422  CG2 ILE B 116     -17.267 -10.368 -17.809  1.00 76.51           C  
ANISOU 2422  CG2 ILE B 116    10815   7059  11195  -2090  -3226    201       C  
ATOM   2423  CD1 ILE B 116     -17.097  -9.169 -15.178  1.00 78.21           C  
ANISOU 2423  CD1 ILE B 116    11009   7606  11102  -1735  -2139    759       C  
ATOM   2424  N   GLY B 117     -20.030  -6.989 -16.429  1.00 75.63           N  
ANISOU 2424  N   GLY B 117     9204   7805  11727  -2082  -2270    919       N  
ATOM   2425  CA  GLY B 117     -20.164  -5.893 -15.500  1.00 74.42           C  
ANISOU 2425  CA  GLY B 117     8922   7898  11455  -1848  -1783   1111       C  
ATOM   2426  C   GLY B 117     -20.198  -4.598 -16.270  1.00 76.14           C  
ANISOU 2426  C   GLY B 117     8913   8436  11580  -1653  -1930    979       C  
ATOM   2427  O   GLY B 117     -20.598  -4.564 -17.435  1.00 78.29           O  
ANISOU 2427  O   GLY B 117     8941   8775  12031  -1761  -2350    862       O  
ATOM   2428  N   GLY B 118     -19.755  -3.526 -15.629  1.00 74.23           N  
ANISOU 2428  N   GLY B 118     8768   8389  11047  -1351  -1590    991       N  
ATOM   2429  CA  GLY B 118     -20.081  -2.207 -16.117  1.00 76.21           C  
ANISOU 2429  CA  GLY B 118     8723   8891  11342  -1177  -1578    978       C  
ATOM   2430  C   GLY B 118     -21.496  -1.933 -15.642  1.00 81.67           C  
ANISOU 2430  C   GLY B 118     8899   9633  12497  -1280  -1266   1292       C  
ATOM   2431  O   GLY B 118     -22.226  -2.854 -15.267  1.00 84.58           O  
ANISOU 2431  O   GLY B 118     9094   9845  13197  -1549  -1190   1490       O  
ATOM   2432  N   ASP B 119     -21.886  -0.666 -15.641  1.00 82.25           N  
ANISOU 2432  N   ASP B 119     8720   9911  12620  -1060  -1058   1361       N  
ATOM   2433  CA  ASP B 119     -23.212  -0.281 -15.174  1.00 86.09           C  
ANISOU 2433  CA  ASP B 119     8698  10486  13524  -1085   -717   1676       C  
ATOM   2434  C   ASP B 119     -24.055   0.171 -16.349  1.00 85.55           C  
ANISOU 2434  C   ASP B 119     8125  10595  13786  -1123  -1038   1730       C  
ATOM   2435  O   ASP B 119     -25.241   0.470 -16.191  1.00 90.35           O  
ANISOU 2435  O   ASP B 119     8216  11318  14793  -1151   -839   2003       O  
ATOM   2436  CB  ASP B 119     -23.104   0.880 -14.181  1.00 88.30           C  
ANISOU 2436  CB  ASP B 119     9069  10866  13615   -744   -178   1727       C  
ATOM   2437  CG  ASP B 119     -22.841   0.421 -12.756  1.00 90.71           C  
ANISOU 2437  CG  ASP B 119     9674  11077  13716   -706    263   1811       C  
ATOM   2438  OD1 ASP B 119     -23.141  -0.751 -12.433  1.00 93.31           O  
ANISOU 2438  OD1 ASP B 119     9983  11265  14206   -957    271   1975       O  
ATOM   2439  OD2 ASP B 119     -22.349   1.248 -11.957  1.00 88.75           O  
ANISOU 2439  OD2 ASP B 119     9680  10893  13148   -415    606   1715       O  
ATOM   2440  N   ASP B 120     -23.423   0.168 -17.523  1.00 81.49           N  
ANISOU 2440  N   ASP B 120     7759  10124  13078  -1102  -1535   1483       N  
ATOM   2441  CA  ASP B 120     -23.783   1.007 -18.669  1.00 78.92           C  
ANISOU 2441  CA  ASP B 120     7118  10034  12834   -950  -1808   1480       C  
ATOM   2442  C   ASP B 120     -23.436   2.458 -18.359  1.00 73.23           C  
ANISOU 2442  C   ASP B 120     6486   9406  11931   -562  -1437   1508       C  
ATOM   2443  O   ASP B 120     -22.271   2.788 -18.136  1.00 71.52           O  
ANISOU 2443  O   ASP B 120     6735   9109  11329   -405  -1359   1309       O  
ATOM   2444  CB  ASP B 120     -25.255   0.862 -19.069  1.00 85.72           C  
ANISOU 2444  CB  ASP B 120     7309  11046  14214  -1128  -1931   1720       C  
ATOM   2445  N   THR B 123     -23.758   5.863 -17.505  1.00 55.59           N  
ANISOU 2445  N   THR B 123     4092   7293   9737    263   -438   1737       N  
ATOM   2446  CA  THR B 123     -23.279   6.493 -16.273  1.00 63.62           C  
ANISOU 2446  CA  THR B 123     5438   8165  10569    440     69   1643       C  
ATOM   2447  C   THR B 123     -22.110   7.437 -16.527  1.00 60.69           C  
ANISOU 2447  C   THR B 123     5452   7698   9911    647     69   1401       C  
ATOM   2448  O   THR B 123     -21.860   8.359 -15.750  1.00 63.26           O  
ANISOU 2448  O   THR B 123     5960   7911  10165    856    471   1316       O  
ATOM   2449  CB  THR B 123     -22.783   5.456 -15.243  1.00 66.73           C  
ANISOU 2449  CB  THR B 123     6170   8444  10739    241    169   1528       C  
ATOM   2450  OG1 THR B 123     -23.075   4.128 -15.697  1.00 74.33           O  
ANISOU 2450  OG1 THR B 123     6998   9417  11828    -87   -199   1592       O  
ATOM   2451  CG2 THR B 123     -23.430   5.701 -13.889  1.00 66.14           C  
ANISOU 2451  CG2 THR B 123     6032   8357  10743    358    745   1680       C  
ATOM   2452  N   LEU B 124     -21.387   7.194 -17.613  1.00 58.22           N  
ANISOU 2452  N   LEU B 124     5258   7422   9440    587   -378   1284       N  
ATOM   2453  CA  LEU B 124     -20.127   7.886 -17.857  1.00 53.28           C  
ANISOU 2453  CA  LEU B 124     5005   6701   8538    723   -403   1063       C  
ATOM   2454  C   LEU B 124     -20.285   9.265 -18.510  1.00 56.23           C  
ANISOU 2454  C   LEU B 124     5222   7068   9077   1010   -275   1185       C  
ATOM   2455  O   LEU B 124     -19.357  10.076 -18.492  1.00 54.58           O  
ANISOU 2455  O   LEU B 124     5285   6717   8734   1133   -156   1033       O  
ATOM   2456  CB  LEU B 124     -19.210   7.001 -18.695  1.00 48.57           C  
ANISOU 2456  CB  LEU B 124     4629   6155   7671    571   -887    905       C  
ATOM   2457  CG  LEU B 124     -18.959   5.620 -18.092  1.00 45.29           C  
ANISOU 2457  CG  LEU B 124     4418   5696   7095    312  -1010    791       C  
ATOM   2458  CD1 LEU B 124     -17.896   4.871 -18.877  1.00 40.55           C  
ANISOU 2458  CD1 LEU B 124     4101   5115   6190    232  -1440    603       C  
ATOM   2459  CD2 LEU B 124     -18.561   5.752 -16.627  1.00 44.80           C  
ANISOU 2459  CD2 LEU B 124     4634   5514   6876    337   -600    676       C  
ATOM   2460  N   THR B 125     -21.463   9.523 -19.072  1.00 55.63           N  
ANISOU 2460  N   THR B 125     4688   7138   9312   1115   -293   1473       N  
ATOM   2461  CA  THR B 125     -21.715  10.748 -19.828  1.00 51.16           C  
ANISOU 2461  CA  THR B 125     3935   6589   8915   1425   -199   1661       C  
ATOM   2462  C   THR B 125     -21.510  12.031 -19.021  1.00 53.75           C  
ANISOU 2462  C   THR B 125     4440   6656   9326   1661    329   1609       C  
ATOM   2463  O   THR B 125     -22.097  12.211 -17.952  1.00 52.98           O  
ANISOU 2463  O   THR B 125     4299   6481   9350   1707    714   1617       O  
ATOM   2464  CB  THR B 125     -23.122  10.736 -20.442  1.00 56.26           C  
ANISOU 2464  CB  THR B 125     4010   7484   9880   1515   -302   1999       C  
ATOM   2465  OG1 THR B 125     -23.285   9.543 -21.220  1.00 55.75           O  
ANISOU 2465  OG1 THR B 125     3799   7640   9744   1268   -839   1983       O  
ATOM   2466  CG2 THR B 125     -23.332  11.953 -21.346  1.00 55.81           C  
ANISOU 2466  CG2 THR B 125     3795   7472   9937   1869   -239   2218       C  
ATOM   2467  N   GLY B 126     -20.671  12.921 -19.545  1.00 51.32           N  
ANISOU 2467  N   GLY B 126     4337   6202   8961   1814    355   1553       N  
ATOM   2468  CA  GLY B 126     -20.433  14.204 -18.912  1.00 52.30           C  
ANISOU 2468  CA  GLY B 126     4641   6019   9213   2023    823   1476       C  
ATOM   2469  C   GLY B 126     -19.627  14.100 -17.636  1.00 53.55           C  
ANISOU 2469  C   GLY B 126     5211   5978   9157   1871   1025   1090       C  
ATOM   2470  O   GLY B 126     -19.570  15.053 -16.854  1.00 59.03           O  
ANISOU 2470  O   GLY B 126     6065   6415   9949   2019   1430    955       O  
ATOM   2471  N   LYS B 127     -19.007  12.938 -17.426  1.00 49.15           N  
ANISOU 2471  N   LYS B 127     4835   5543   8296   1597    734    903       N  
ATOM   2472  CA  LYS B 127     -18.197  12.695 -16.239  1.00 49.95           C  
ANISOU 2472  CA  LYS B 127     5318   5532   8127   1464    863    551       C  
ATOM   2473  C   LYS B 127     -16.722  12.635 -16.613  1.00 45.51           C  
ANISOU 2473  C   LYS B 127     5061   4918   7312   1338    608    309       C  
ATOM   2474  O   LYS B 127     -16.379  12.369 -17.765  1.00 44.23           O  
ANISOU 2474  O   LYS B 127     4823   4866   7118   1308    280    430       O  
ATOM   2475  CB  LYS B 127     -18.599  11.368 -15.592  1.00 51.18           C  
ANISOU 2475  CB  LYS B 127     5453   5867   8127   1277    772    559       C  
ATOM   2476  CG  LYS B 127     -20.008  11.342 -15.025  1.00 56.80           C  
ANISOU 2476  CG  LYS B 127     5852   6645   9085   1375   1077    801       C  
ATOM   2477  CD  LYS B 127     -20.050  11.899 -13.605  1.00 64.10           C  
ANISOU 2477  CD  LYS B 127     6996   7436   9924   1517   1559    618       C  
ATOM   2478  CE  LYS B 127     -21.482  11.965 -13.074  1.00 70.36           C  
ANISOU 2478  CE  LYS B 127     7447   8313  10974   1671   1922    903       C  
ATOM   2479  NZ  LYS B 127     -22.175  10.649 -13.177  1.00 72.23           N  
ANISOU 2479  NZ  LYS B 127     7403   8768  11274   1449   1731   1152       N  
ATOM   2480  N   ASN B 128     -15.853  12.889 -15.640  1.00 39.13           N  
ANISOU 2480  N   ASN B 128     5047   3532   6288   1074  -1037    668       N  
ATOM   2481  CA  ASN B 128     -14.429  12.641 -15.813  1.00 37.97           C  
ANISOU 2481  CA  ASN B 128     5038   3392   5998    859  -1021    581       C  
ATOM   2482  C   ASN B 128     -14.145  11.193 -15.491  1.00 36.58           C  
ANISOU 2482  C   ASN B 128     4729   3469   5701    785   -969    631       C  
ATOM   2483  O   ASN B 128     -14.282  10.782 -14.347  1.00 39.43           O  
ANISOU 2483  O   ASN B 128     4943   4032   6005    907   -843    587       O  
ATOM   2484  CB  ASN B 128     -13.609  13.521 -14.872  1.00 43.20           C  
ANISOU 2484  CB  ASN B 128     5775   4008   6630    885   -936    312       C  
ATOM   2485  CG  ASN B 128     -13.722  14.992 -15.200  1.00 51.07           C  
ANISOU 2485  CG  ASN B 128     6915   4665   7826    929   -980    245       C  
ATOM   2486  OD1 ASN B 128     -14.451  15.384 -16.111  1.00 49.34           O  
ANISOU 2486  OD1 ASN B 128     6743   4270   7733    974  -1056    443       O  
ATOM   2487  ND2 ASN B 128     -12.998  15.818 -14.451  1.00 58.16           N  
ANISOU 2487  ND2 ASN B 128     7868   5460   8772    930   -942    -43       N  
ATOM   2488  N   VAL B 129     -13.725  10.419 -16.485  1.00 31.47           N  
ANISOU 2488  N   VAL B 129     4131   2817   5008    614  -1055    729       N  
ATOM   2489  CA  VAL B 129     -13.523   8.989 -16.291  1.00 27.24           C  
ANISOU 2489  CA  VAL B 129     3468   2455   4426    549  -1019    785       C  
ATOM   2490  C   VAL B 129     -12.042   8.659 -16.203  1.00 26.16           C  
ANISOU 2490  C   VAL B 129     3439   2400   4101    410   -960    688       C  
ATOM   2491  O   VAL B 129     -11.261   9.094 -17.052  1.00 28.10           O  
ANISOU 2491  O   VAL B 129     3853   2548   4274    284  -1020    659       O  
ATOM   2492  CB  VAL B 129     -14.147   8.184 -17.444  1.00 27.75           C  
ANISOU 2492  CB  VAL B 129     3478   2468   4595    481  -1183    905       C  
ATOM   2493  CG1 VAL B 129     -13.945   6.689 -17.236  1.00 25.35           C  
ANISOU 2493  CG1 VAL B 129     3035   2267   4330    408  -1147    945       C  
ATOM   2494  CG2 VAL B 129     -15.633   8.525 -17.578  1.00 32.79           C  
ANISOU 2494  CG2 VAL B 129     3972   3049   5438    618  -1265    997       C  
ATOM   2495  N   LEU B 130     -11.666   7.916 -15.161  1.00 24.59           N  
ANISOU 2495  N   LEU B 130     3122   2402   3820    459   -828    668       N  
ATOM   2496  CA  LEU B 130     -10.312   7.407 -14.992  1.00 23.23           C  
ANISOU 2496  CA  LEU B 130     3003   2356   3469    360   -772    593       C  
ATOM   2497  C   LEU B 130     -10.327   5.890 -15.143  1.00 26.45           C  
ANISOU 2497  C   LEU B 130     3301   2835   3914    330   -752    734       C  
ATOM   2498  O   LEU B 130     -10.836   5.170 -14.278  1.00 30.58           O  
ANISOU 2498  O   LEU B 130     3642   3474   4503    451   -636    853       O  
ATOM   2499  CB  LEU B 130      -9.754   7.765 -13.605  1.00 23.87           C  
ANISOU 2499  CB  LEU B 130     3028   2647   3395    485   -646    442       C  
ATOM   2500  CG  LEU B 130      -8.338   7.266 -13.331  1.00 33.52           C  
ANISOU 2500  CG  LEU B 130     4267   4047   4423    411   -598    354       C  
ATOM   2501  CD1 LEU B 130      -7.335   7.902 -14.290  1.00 26.07           C  
ANISOU 2501  CD1 LEU B 130     3487   2953   3466    198   -684    250       C  
ATOM   2502  CD2 LEU B 130      -7.936   7.508 -11.880  1.00 29.90           C  
ANISOU 2502  CD2 LEU B 130     3711   3873   3778    595   -500    193       C  
ATOM   2503  N   ILE B 131      -9.744   5.408 -16.233  1.00 25.12           N  
ANISOU 2503  N   ILE B 131     3236   2594   3714    187   -849    728       N  
ATOM   2504  CA  ILE B 131      -9.568   3.979 -16.437  1.00 21.83           C  
ANISOU 2504  CA  ILE B 131     2739   2201   3354    155   -845    800       C  
ATOM   2505  C   ILE B 131      -8.299   3.533 -15.729  1.00 22.17           C  
ANISOU 2505  C   ILE B 131     2784   2433   3208    167   -710    765       C  
ATOM   2506  O   ILE B 131      -7.235   4.110 -15.928  1.00 25.00           O  
ANISOU 2506  O   ILE B 131     3265   2854   3378     95   -712    644       O  
ATOM   2507  CB  ILE B 131      -9.458   3.635 -17.937  1.00 26.02           C  
ANISOU 2507  CB  ILE B 131     3383   2612   3891     47  -1024    755       C  
ATOM   2508  CG1 ILE B 131     -10.760   3.989 -18.658  1.00 31.35           C  
ANISOU 2508  CG1 ILE B 131     4026   3147   4737     68  -1190    785       C  
ATOM   2509  CG2 ILE B 131      -9.096   2.153 -18.122  1.00 24.99           C  
ANISOU 2509  CG2 ILE B 131     3186   2479   3832     23  -1026    762       C  
ATOM   2510  CD1 ILE B 131     -10.626   4.132 -20.172  1.00 33.06           C  
ANISOU 2510  CD1 ILE B 131     4395   3323   4844     23  -1383    720       C  
ATOM   2511  N   VAL B 132      -8.421   2.506 -14.895  1.00 23.51           N  
ANISOU 2511  N   VAL B 132     2792   2696   3446    266   -584    897       N  
ATOM   2512  CA  VAL B 132      -7.301   2.053 -14.071  1.00 20.76           C  
ANISOU 2512  CA  VAL B 132     2414   2577   2898    339   -447    897       C  
ATOM   2513  C   VAL B 132      -6.893   0.646 -14.479  1.00 25.71           C  
ANISOU 2513  C   VAL B 132     3006   3140   3624    312   -434    990       C  
ATOM   2514  O   VAL B 132      -7.662  -0.310 -14.291  1.00 24.44           O  
ANISOU 2514  O   VAL B 132     2696   2861   3729    360   -383   1173       O  
ATOM   2515  CB  VAL B 132      -7.670   2.073 -12.582  1.00 21.94           C  
ANISOU 2515  CB  VAL B 132     2397   2953   2985    557   -271   1012       C  
ATOM   2516  CG1 VAL B 132      -6.489   1.602 -11.734  1.00 23.13           C  
ANISOU 2516  CG1 VAL B 132     2507   3399   2883    675   -150   1014       C  
ATOM   2517  CG2 VAL B 132      -8.127   3.478 -12.169  1.00 23.32           C  
ANISOU 2517  CG2 VAL B 132     2607   3173   3079    617   -299    863       C  
ATOM   2518  N  AGLU B 133      -5.674   0.519 -14.997  0.46 25.22           N  
ANISOU 2518  N  AGLU B 133     3060   3143   3380    243   -466    870       N  
ATOM   2519  N  BGLU B 133      -5.670   0.526 -14.990  0.08 25.28           N  
ANISOU 2519  N  BGLU B 133     3068   3152   3387    243   -465    870       N  
ATOM   2520  N  CGLU B 133      -5.695   0.514 -15.047  0.46 25.27           N  
ANISOU 2520  N  CGLU B 133     3069   3138   3393    237   -472    868       N  
ATOM   2521  CA AGLU B 133      -5.208  -0.730 -15.592  0.46 25.69           C  
ANISOU 2521  CA AGLU B 133     3123   3115   3524    226   -481    897       C  
ATOM   2522  CA BGLU B 133      -5.177  -0.709 -15.585  0.08 25.84           C  
ANISOU 2522  CA BGLU B 133     3144   3140   3534    226   -480    893       C  
ATOM   2523  CA CGLU B 133      -5.220  -0.765 -15.577  0.46 25.29           C  
ANISOU 2523  CA CGLU B 133     3067   3062   3479    229   -479    902       C  
ATOM   2524  C  AGLU B 133      -3.907  -1.228 -14.964  0.46 24.86           C  
ANISOU 2524  C  AGLU B 133     2990   3244   3210    319   -352    914       C  
ATOM   2525  C  BGLU B 133      -3.937  -1.235 -14.870  0.08 25.18           C  
ANISOU 2525  C  BGLU B 133     3020   3294   3253    329   -342    926       C  
ATOM   2526  C  CGLU B 133      -3.957  -1.240 -14.884  0.46 24.97           C  
ANISOU 2526  C  CGLU B 133     2994   3263   3232    328   -344    926       C  
ATOM   2527  O  AGLU B 133      -3.084  -0.439 -14.510  0.46 25.60           O  
ANISOU 2527  O  AGLU B 133     3109   3573   3046    327   -318    813       O  
ATOM   2528  O  BGLU B 133      -3.183  -0.470 -14.272  0.08 25.38           O  
ANISOU 2528  O  BGLU B 133     3053   3566   3023    357   -295    841       O  
ATOM   2529  O  CGLU B 133      -3.199  -0.447 -14.337  0.46 26.00           O  
ANISOU 2529  O  CGLU B 133     3139   3633   3106    348   -303    835       O  
ATOM   2530  CB AGLU B 133      -5.022  -0.539 -17.106  0.46 27.51           C  
ANISOU 2530  CB AGLU B 133     3518   3214   3721     92   -663    731       C  
ATOM   2531  CB BGLU B 133      -4.850  -0.461 -17.058  0.08 26.81           C  
ANISOU 2531  CB BGLU B 133     3438   3157   3591     92   -650    722       C  
ATOM   2532  CB CGLU B 133      -4.915  -0.648 -17.075  0.46 27.30           C  
ANISOU 2532  CB CGLU B 133     3487   3197   3687     99   -652    733       C  
ATOM   2533  CG AGLU B 133      -4.536  -1.767 -17.864  0.46 28.95           C  
ANISOU 2533  CG AGLU B 133     3725   3308   3966    101   -712    677       C  
ATOM   2534  CG BGLU B 133      -5.933  -0.882 -18.032  0.08 29.23           C  
ANISOU 2534  CG BGLU B 133     3746   3212   4149     45   -821    694       C  
ATOM   2535  CG CGLU B 133      -6.094  -0.798 -18.005  0.46 29.90           C  
ANISOU 2535  CG CGLU B 133     3823   3284   4254     43   -827    702       C  
ATOM   2536  CD AGLU B 133      -5.571  -2.870 -17.905  0.46 31.52           C  
ANISOU 2536  CD AGLU B 133     3918   3371   4686    123   -761    749       C  
ATOM   2537  CD BGLU B 133      -5.624  -2.215 -18.689  0.08 31.48           C  
ANISOU 2537  CD BGLU B 133     4027   3378   4557     61   -883    627       C  
ATOM   2538  CD CGLU B 133      -5.690  -0.660 -19.463  0.46 30.68           C  
ANISOU 2538  CD CGLU B 133     4090   3363   4203    -17   -992    534       C  
ATOM   2539  OE1AGLU B 133      -5.835  -3.478 -16.848  0.46 35.94           O  
ANISOU 2539  OE1AGLU B 133     4315   3911   5430    206   -604    952       O  
ATOM   2540  OE1BGLU B 133      -5.594  -3.236 -17.974  0.08 33.19           O  
ANISOU 2540  OE1BGLU B 133     4110   3530   4970    131   -768    749       O  
ATOM   2541  OE1CGLU B 133      -5.231  -1.658 -20.061  0.46 30.31           O  
ANISOU 2541  OE1CGLU B 133     4065   3279   4171      9  -1042    444       O  
ATOM   2542  OE2AGLU B 133      -6.130  -3.122 -18.992  0.46 35.00           O  
ANISOU 2542  OE2AGLU B 133     4399   3632   5265     66   -958    606       O  
ATOM   2543  OE2BGLU B 133      -5.395  -2.237 -19.917  0.08 31.97           O  
ANISOU 2543  OE2BGLU B 133     4216   3415   4514     30  -1039    455       O  
ATOM   2544  OE2CGLU B 133      -5.824   0.454 -20.001  0.46 34.35           O  
ANISOU 2544  OE2CGLU B 133     4662   3859   4530    -63  -1059    505       O  
ATOM   2545  N   ASP B 134      -3.718  -2.542 -14.941  1.00 22.86           N  
ANISOU 2545  N   ASP B 134     2669   2916   3102    394   -291   1030       N  
ATOM   2546  CA  ASP B 134      -2.513  -3.123 -14.362  1.00 22.99           C  
ANISOU 2546  CA  ASP B 134     2644   3160   2933    522   -167   1078       C  
ATOM   2547  C   ASP B 134      -1.311  -2.981 -15.297  1.00 26.91           C  
ANISOU 2547  C   ASP B 134     3272   3733   3219    436   -247    873       C  
ATOM   2548  O   ASP B 134      -0.221  -2.578 -14.869  1.00 28.13           O  
ANISOU 2548  O   ASP B 134     3410   4174   3105    471   -192    810       O  
ATOM   2549  CB  ASP B 134      -2.736  -4.588 -13.943  1.00 30.78           C  
ANISOU 2549  CB  ASP B 134     3499   4007   4190    663    -43   1324       C  
ATOM   2550  CG  ASP B 134      -3.235  -5.474 -15.087  1.00 31.66           C  
ANISOU 2550  CG  ASP B 134     3649   3721   4658    560   -172   1254       C  
ATOM   2551  OD1 ASP B 134      -3.650  -4.944 -16.140  1.00 31.82           O  
ANISOU 2551  OD1 ASP B 134     3783   3610   4695    408   -362   1045       O  
ATOM   2552  OD2 ASP B 134      -3.217  -6.712 -14.917  1.00 41.44           O  
ANISOU 2552  OD2 ASP B 134     4795   4780   6171    654    -89   1405       O  
ATOM   2553  N   ILE B 135      -1.508  -3.290 -16.574  1.00 27.17           N  
ANISOU 2553  N   ILE B 135     3414   3542   3366    340   -379    759       N  
ATOM   2554  CA  ILE B 135      -0.391  -3.311 -17.508  1.00 24.11           C  
ANISOU 2554  CA  ILE B 135     3135   3257   2770    308   -422    603       C  
ATOM   2555  C   ILE B 135      -0.815  -3.075 -18.945  1.00 31.77           C  
ANISOU 2555  C   ILE B 135     4247   4069   3754    210   -593    453       C  
ATOM   2556  O   ILE B 135      -1.860  -3.561 -19.387  1.00 31.10           O  
ANISOU 2556  O   ILE B 135     4162   3733   3920    203   -711    428       O  
ATOM   2557  CB  ILE B 135       0.414  -4.643 -17.384  1.00 35.70           C  
ANISOU 2557  CB  ILE B 135     4550   4746   4269    463   -337    644       C  
ATOM   2558  CG1 ILE B 135       1.654  -4.624 -18.285  1.00 34.41           C  
ANISOU 2558  CG1 ILE B 135     4473   4752   3848    464   -353    488       C  
ATOM   2559  CG2 ILE B 135      -0.466  -5.849 -17.708  1.00 38.80           C  
ANISOU 2559  CG2 ILE B 135     4915   4780   5046    509   -393    676       C  
ATOM   2560  CD1 ILE B 135       2.618  -5.774 -18.008  1.00 35.41           C  
ANISOU 2560  CD1 ILE B 135     4533   4963   3957    648   -247    529       C  
ATOM   2561  N   ILE B 136      -0.008  -2.288 -19.655  1.00 29.79           N  
ANISOU 2561  N   ILE B 136     4095   3988   3237    145   -604    366       N  
ATOM   2562  CA AILE B 136      -0.177  -2.057 -21.083  0.49 30.20           C  
ANISOU 2562  CA AILE B 136     4286   3994   3196    114   -737    257       C  
ATOM   2563  CA BILE B 136      -0.200  -2.088 -21.083  0.51 30.38           C  
ANISOU 2563  CA BILE B 136     4307   4010   3225    116   -739    256       C  
ATOM   2564  C   ILE B 136       0.936  -2.793 -21.816  1.00 32.80           C  
ANISOU 2564  C   ILE B 136     4657   4467   3338    216   -706    159       C  
ATOM   2565  O   ILE B 136       2.112  -2.550 -21.549  1.00 32.56           O  
ANISOU 2565  O   ILE B 136     4583   4667   3120    216   -570    196       O  
ATOM   2566  CB AILE B 136      -0.057  -0.566 -21.432  0.49 28.88           C  
ANISOU 2566  CB AILE B 136     4189   3920   2865     -9   -728    299       C  
ATOM   2567  CB BILE B 136      -0.251  -0.592 -21.456  0.51 29.31           C  
ANISOU 2567  CB BILE B 136     4246   3942   2948     -7   -748    297       C  
ATOM   2568  CG1AILE B 136      -1.093   0.246 -20.655  0.49 26.70           C  
ANISOU 2568  CG1AILE B 136     3872   3509   2762    -81   -750    371       C  
ATOM   2569  CG1BILE B 136      -1.515   0.046 -20.870  0.51 26.43           C  
ANISOU 2569  CG1BILE B 136     3851   3404   2786    -65   -805    361       C  
ATOM   2570  CG2AILE B 136      -0.223  -0.363 -22.944  0.49 31.05           C  
ANISOU 2570  CG2AILE B 136     4604   4206   2989     18   -843    245       C  
ATOM   2571  CG2BILE B 136      -0.233  -0.404 -22.977  0.51 31.28           C  
ANISOU 2571  CG2BILE B 136     4635   4233   3017     23   -848    240       C  
ATOM   2572  CD1AILE B 136      -2.520  -0.128 -21.008  0.49 25.71           C  
ANISOU 2572  CD1AILE B 136     3754   3159   2853    -51   -905    358       C  
ATOM   2573  CD1BILE B 136      -1.562   1.564 -20.961  0.51 24.47           C  
ANISOU 2573  CD1BILE B 136     3658   3168   2470   -173   -790    414       C  
ATOM   2574  N   ASP B 137       0.569  -3.693 -22.720  1.00 31.01           N  
ANISOU 2574  N   ASP B 137     4493   4114   3174    316   -841      8       N  
ATOM   2575  CA  ASP B 137       1.545  -4.444 -23.490  1.00 33.07           C  
ANISOU 2575  CA  ASP B 137     4804   4512   3250    463   -824   -127       C  
ATOM   2576  C   ASP B 137       1.276  -4.177 -24.969  1.00 35.90           C  
ANISOU 2576  C   ASP B 137     5302   4942   3395    523   -978   -277       C  
ATOM   2577  O   ASP B 137       1.900  -3.290 -25.561  1.00 37.05           O  
ANISOU 2577  O   ASP B 137     5507   5341   3229    510   -900   -196       O  
ATOM   2578  CB  ASP B 137       1.450  -5.931 -23.140  1.00 34.72           C  
ANISOU 2578  CB  ASP B 137     4947   4502   3742    590   -845   -214       C  
ATOM   2579  CG  ASP B 137       2.381  -6.797 -23.974  1.00 39.36           C  
ANISOU 2579  CG  ASP B 137     5593   5195   4166    782   -848   -406       C  
ATOM   2580  OD1 ASP B 137       3.378  -6.266 -24.505  1.00 41.79           O  
ANISOU 2580  OD1 ASP B 137     5946   5827   4106    822   -756   -398       O  
ATOM   2581  OD2 ASP B 137       2.106  -8.011 -24.091  1.00 38.10           O  
ANISOU 2581  OD2 ASP B 137     5419   4781   4278    899   -935   -562       O  
ATOM   2582  N   THR B 138       0.332  -4.906 -25.567  1.00 36.27           N  
ANISOU 2582  N   THR B 138     5382   4782   3618    598  -1198   -485       N  
ATOM   2583  CA  THR B 138      -0.056  -4.597 -26.952  1.00 38.97           C  
ANISOU 2583  CA  THR B 138     5848   5247   3713    696  -1382   -645       C  
ATOM   2584  C   THR B 138      -0.884  -3.316 -27.041  1.00 39.79           C  
ANISOU 2584  C   THR B 138     5981   5360   3777    571  -1430   -476       C  
ATOM   2585  O   THR B 138      -1.022  -2.739 -28.114  1.00 44.30           O  
ANISOU 2585  O   THR B 138     6655   6119   4057    661  -1517   -493       O  
ATOM   2586  CB  THR B 138      -0.872  -5.722 -27.627  1.00 41.37           C  
ANISOU 2586  CB  THR B 138     6155   5339   4225    823  -1663   -995       C  
ATOM   2587  OG1 THR B 138      -2.131  -5.884 -26.955  1.00 44.08           O  
ANISOU 2587  OG1 THR B 138     6380   5337   5030    678  -1780   -971       O  
ATOM   2588  CG2 THR B 138      -0.097  -7.025 -27.627  1.00 45.55           C  
ANISOU 2588  CG2 THR B 138     6667   5801   4838    976  -1632  -1194       C  
ATOM   2589  N   GLY B 139      -1.460  -2.888 -25.924  1.00 34.32           N  
ANISOU 2589  N   GLY B 139     5195   4480   3366    401  -1370   -306       N  
ATOM   2590  CA  GLY B 139      -2.332  -1.725 -25.930  1.00 34.75           C  
ANISOU 2590  CA  GLY B 139     5268   4497   3439    303  -1421   -164       C  
ATOM   2591  C   GLY B 139      -3.760  -2.057 -26.344  1.00 40.54           C  
ANISOU 2591  C   GLY B 139     5967   5039   4397    333  -1689   -311       C  
ATOM   2592  O   GLY B 139      -4.607  -1.173 -26.413  1.00 41.62           O  
ANISOU 2592  O   GLY B 139     6108   5143   4565    286  -1759   -208       O  
ATOM   2593  N   LYS B 140      -4.041  -3.338 -26.590  1.00 39.88           N  
ANISOU 2593  N   LYS B 140     5828   4810   4516    409  -1846   -563       N  
ATOM   2594  CA  LYS B 140      -5.352  -3.739 -27.093  1.00 40.37           C  
ANISOU 2594  CA  LYS B 140     5818   4694   4829    431  -2141   -766       C  
ATOM   2595  C   LYS B 140      -6.512  -3.647 -26.087  1.00 44.28           C  
ANISOU 2595  C   LYS B 140     6132   4912   5780    277  -2145   -623       C  
ATOM   2596  O   LYS B 140      -7.594  -3.179 -26.451  1.00 44.34           O  
ANISOU 2596  O   LYS B 140     6093   4887   5869    267  -2329   -647       O  
ATOM   2597  CB  LYS B 140      -5.279  -5.083 -27.837  1.00 48.32           C  
ANISOU 2597  CB  LYS B 140     6813   5615   5932    568  -2348  -1149       C  
ATOM   2598  CG  LYS B 140      -4.493  -4.943 -29.150  1.00 60.15           C  
ANISOU 2598  CG  LYS B 140     8482   7474   6898    784  -2382  -1306       C  
ATOM   2599  CD  LYS B 140      -4.188  -6.260 -29.855  1.00 70.33           C  
ANISOU 2599  CD  LYS B 140     9762   8715   8246    957  -2498  -1683       C  
ATOM   2600  CE  LYS B 140      -3.336  -6.004 -31.101  1.00 75.37           C  
ANISOU 2600  CE  LYS B 140    10521   9766   8351   1174  -2387  -1716       C  
ATOM   2601  NZ  LYS B 140      -2.764  -7.248 -31.684  1.00 80.84           N  
ANISOU 2601  NZ  LYS B 140    11220  10452   9045   1377  -2457  -2061       N  
ATOM   2602  N   THR B 141      -6.321  -4.066 -24.836  1.00 45.04           N  
ANISOU 2602  N   THR B 141     6113   4849   6151    189  -1937   -453       N  
ATOM   2603  CA ATHR B 141      -7.424  -3.854 -23.898  0.35 44.40           C  
ANISOU 2603  CA ATHR B 141     5854   4578   6439     82  -1903   -271       C  
ATOM   2604  CA BTHR B 141      -7.302  -3.866 -23.775  0.65 43.16           C  
ANISOU 2604  CA BTHR B 141     5698   4427   6272     80  -1868   -248       C  
ATOM   2605  C   THR B 141      -7.611  -2.371 -23.627  1.00 45.33           C  
ANISOU 2605  C   THR B 141     6038   4856   6329     44  -1815    -71       C  
ATOM   2606  O   THR B 141      -8.749  -1.950 -23.394  1.00 46.25           O  
ANISOU 2606  O   THR B 141     6045   4874   6654      6  -1888      2       O  
ATOM   2607  CB ATHR B 141      -7.381  -4.658 -22.553  0.35 41.22           C  
ANISOU 2607  CB ATHR B 141     5277   3988   6398     39  -1688    -80       C  
ATOM   2608  CB BTHR B 141      -6.751  -4.413 -22.432  0.65 39.89           C  
ANISOU 2608  CB BTHR B 141     5183   3945   6029     59  -1593    -38       C  
ATOM   2609  OG1ATHR B 141      -7.072  -3.781 -21.462  0.35 39.76           O  
ANISOU 2609  OG1ATHR B 141     5094   3962   6052     17  -1442    188       O  
ATOM   2610  OG1BTHR B 141      -6.493  -5.817 -22.556  0.65 40.36           O  
ANISOU 2610  OG1BTHR B 141     5178   3804   6355    106  -1628   -170       O  
ATOM   2611  CG2ATHR B 141      -6.412  -5.809 -22.597  0.35 40.98           C  
ANISOU 2611  CG2ATHR B 141     5269   3897   6404    112  -1626   -178       C  
ATOM   2612  CG2BTHR B 141      -7.725  -4.176 -21.294  0.65 39.91           C  
ANISOU 2612  CG2BTHR B 141     4997   3830   6338     -3  -1481    208       C  
ATOM   2613  N   MET B 142      -6.550  -1.566 -23.726  1.00 38.18           N  
ANISOU 2613  N   MET B 142     5294   4176   5037     57  -1674      5       N  
ATOM   2614  CA AMET B 142      -6.701  -0.120 -23.523  0.72 34.21           C  
ANISOU 2614  CA AMET B 142     4854   3761   4384     15  -1599    173       C  
ATOM   2615  CA BMET B 142      -6.672  -0.125 -23.560  0.28 33.03           C  
ANISOU 2615  CA BMET B 142     4709   3617   4224     17  -1601    169       C  
ATOM   2616  C   MET B 142      -7.497   0.535 -24.658  1.00 35.08           C  
ANISOU 2616  C   MET B 142     5036   3903   4388     73  -1812    131       C  
ATOM   2617  O   MET B 142      -8.386   1.344 -24.393  1.00 35.02           O  
ANISOU 2617  O   MET B 142     4986   3827   4493     56  -1839    241       O  
ATOM   2618  CB AMET B 142      -5.352   0.596 -23.297  0.72 27.64           C  
ANISOU 2618  CB AMET B 142     4130   3115   3259    -18  -1392    268       C  
ATOM   2619  CB BMET B 142      -5.298   0.539 -23.473  0.28 28.47           C  
ANISOU 2619  CB BMET B 142     4249   3232   3335     -8  -1408    251       C  
ATOM   2620  CG AMET B 142      -5.489   2.099 -23.048  0.72 28.23           C  
ANISOU 2620  CG AMET B 142     4256   3201   3270    -77  -1318    416       C  
ATOM   2621  CG BMET B 142      -5.336   1.796 -22.657  0.28 27.61           C  
ANISOU 2621  CG BMET B 142     4135   3119   3235    -85  -1275    406       C  
ATOM   2622  SD AMET B 142      -3.912   2.998 -23.064  0.72 40.15           S  
ANISOU 2622  SD AMET B 142     5857   4884   4515   -151  -1117    499       S  
ATOM   2623  SD BMET B 142      -6.204   1.425 -21.130  0.28 44.71           S  
ANISOU 2623  SD BMET B 142     6108   5151   5729    -92  -1204    467       S  
ATOM   2624  CE AMET B 142      -3.236   2.437 -24.631  0.72 40.95           C  
ANISOU 2624  CE AMET B 142     6075   5171   4312    -46  -1183    442       C  
ATOM   2625  CE BMET B 142      -7.763   2.246 -21.400  0.28 21.74           C  
ANISOU 2625  CE BMET B 142     3171   2103   2988    -76  -1351    518       C  
ATOM   2626  N   GLN B 143      -7.190   0.188 -25.903  1.00 45.09           N  
ANISOU 2626  N   GLN B 143     6408   5306   5419    180  -1961    -26       N  
ATOM   2627  CA  GLN B 143      -7.963   0.672 -27.050  1.00 49.11           C  
ANISOU 2627  CA  GLN B 143     6972   5909   5778    296  -2192    -77       C  
ATOM   2628  C   GLN B 143      -9.445   0.314 -26.905  1.00 51.90           C  
ANISOU 2628  C   GLN B 143     7142   6075   6503    282  -2416   -178       C  
ATOM   2629  O   GLN B 143     -10.327   1.117 -27.214  1.00 54.03           O  
ANISOU 2629  O   GLN B 143     7392   6367   6769    325  -2486    -96       O  
ATOM   2630  CB  GLN B 143      -7.424   0.067 -28.349  1.00 60.35           C  
ANISOU 2630  CB  GLN B 143     8483   7549   6900    455  -2275   -288       C  
ATOM   2631  CG  GLN B 143      -8.471  -0.063 -29.457  1.00 71.00           C  
ANISOU 2631  CG  GLN B 143     9776   8972   8230    587  -2488   -466       C  
ATOM   2632  CD  GLN B 143      -8.266  -1.300 -30.323  1.00 79.39           C  
ANISOU 2632  CD  GLN B 143    10822  10100   9242    712  -2620   -812       C  
ATOM   2633  OE1 GLN B 143      -9.117  -2.192 -30.367  1.00 83.49           O  
ANISOU 2633  OE1 GLN B 143    11201  10433  10089    706  -2826  -1065       O  
ATOM   2634  NE2 GLN B 143      -7.134  -1.356 -31.016  1.00 81.22           N  
ANISOU 2634  NE2 GLN B 143    11178  10585   9096    828  -2492   -820       N  
ATOM   2635  N   THR B 144      -9.702  -0.898 -26.420  1.00 51.31           N  
ANISOU 2635  N   THR B 144     6906   5803   6787    217  -2465   -331       N  
ATOM   2636  CA  THR B 144     -11.057  -1.413 -26.237  1.00 51.65           C  
ANISOU 2636  CA  THR B 144     6713   5634   7279    171  -2661   -424       C  
ATOM   2637  C   THR B 144     -11.803  -0.650 -25.147  1.00 49.51           C  
ANISOU 2637  C   THR B 144     6317   5263   7231     89  -2504   -147       C  
ATOM   2638  O   THR B 144     -12.976  -0.295 -25.308  1.00 48.22           O  
ANISOU 2638  O   THR B 144     6021   5060   7241    106  -2665   -138       O  
ATOM   2639  CB  THR B 144     -11.023  -2.917 -25.875  1.00 50.76           C  
ANISOU 2639  CB  THR B 144     6439   5273   7576    103  -2688   -595       C  
ATOM   2640  OG1 THR B 144     -10.498  -3.660 -26.984  1.00 50.51           O  
ANISOU 2640  OG1 THR B 144     6511   5322   7358    222  -2839   -914       O  
ATOM   2641  CG2 THR B 144     -12.417  -3.429 -25.532  1.00 50.40           C  
ANISOU 2641  CG2 THR B 144     6094   4965   8090     17  -2820   -621       C  
ATOM   2642  N   LEU B 145     -11.113  -0.397 -24.042  1.00 41.95           N  
ANISOU 2642  N   LEU B 145     5391   4299   6249     27  -2200     58       N  
ATOM   2643  CA  LEU B 145     -11.692   0.362 -22.947  1.00 42.68           C  
ANISOU 2643  CA  LEU B 145     5385   4347   6485     -4  -2032    288       C  
ATOM   2644  C   LEU B 145     -11.943   1.803 -23.376  1.00 47.33           C  
ANISOU 2644  C   LEU B 145     6107   5042   6832     57  -2067    374       C  
ATOM   2645  O   LEU B 145     -12.931   2.420 -22.955  1.00 46.61           O  
ANISOU 2645  O   LEU B 145     5906   4897   6909     82  -2072    482       O  
ATOM   2646  CB  LEU B 145     -10.771   0.335 -21.738  1.00 44.07           C  
ANISOU 2646  CB  LEU B 145     5580   4559   6607    -38  -1730    431       C  
ATOM   2647  CG  LEU B 145     -11.257  -0.526 -20.584  1.00 48.59           C  
ANISOU 2647  CG  LEU B 145     5911   5003   7549    -58  -1590    560       C  
ATOM   2648  CD1 LEU B 145     -12.646  -0.076 -20.178  1.00 57.22           C  
ANISOU 2648  CD1 LEU B 145     6813   6026   8903    -42  -1617    678       C  
ATOM   2649  CD2 LEU B 145     -11.284  -1.961 -21.014  1.00 45.35           C  
ANISOU 2649  CD2 LEU B 145     5395   4419   7416    -93  -1704    432       C  
ATOM   2650  N   LEU B 146     -11.047   2.329 -24.214  1.00 43.36           N  
ANISOU 2650  N   LEU B 146     5830   4688   5958     98  -2073    352       N  
ATOM   2651  CA  LEU B 146     -11.142   3.718 -24.688  1.00 42.16           C  
ANISOU 2651  CA  LEU B 146     5818   4606   5596    164  -2072    489       C  
ATOM   2652  C   LEU B 146     -12.230   3.976 -25.741  1.00 46.06           C  
ANISOU 2652  C   LEU B 146     6282   5150   6069    289  -2320    448       C  
ATOM   2653  O   LEU B 146     -12.722   5.096 -25.837  1.00 48.63           O  
ANISOU 2653  O   LEU B 146     6644   5473   6359    350  -2277    593       O  
ATOM   2654  CB  LEU B 146      -9.796   4.210 -25.215  1.00 38.62           C  
ANISOU 2654  CB  LEU B 146     5581   4297   4794    163  -1944    548       C  
ATOM   2655  CG  LEU B 146      -8.751   4.610 -24.188  1.00 36.57           C  
ANISOU 2655  CG  LEU B 146     5356   4014   4524     47  -1673    630       C  
ATOM   2656  CD1 LEU B 146      -7.461   4.946 -24.900  1.00 40.03           C  
ANISOU 2656  CD1 LEU B 146     5951   4601   4659     37  -1572    684       C  
ATOM   2657  CD2 LEU B 146      -9.240   5.808 -23.381  1.00 34.05           C  
ANISOU 2657  CD2 LEU B 146     5018   3567   4352     29  -1576    755       C  
ATOM   2658  N   SER B 147     -12.597   2.964 -26.528  1.00 52.44           N  
ANISOU 2658  N   SER B 147     7011   6009   6905    330  -2521    218       N  
ATOM   2659  CA  SER B 147     -13.702   3.091 -27.497  1.00 55.33           C  
ANISOU 2659  CA  SER B 147     7301   6464   7257    450  -2716    120       C  
ATOM   2660  C   SER B 147     -15.037   2.853 -26.799  1.00 54.49           C  
ANISOU 2660  C   SER B 147     6933   6181   7590    392  -2800    109       C  
ATOM   2661  O   SER B 147     -16.046   3.517 -27.063  1.00 58.23           O  
ANISOU 2661  O   SER B 147     7331   6696   8097    474  -2871    167       O  
ATOM   2662  CB  SER B 147     -13.513   2.129 -28.658  1.00 62.39           C  
ANISOU 2662  CB  SER B 147     8211   7505   7989    535  -2884   -164       C  
ATOM   2663  OG  SER B 147     -12.300   2.420 -29.327  1.00 69.73           O  
ANISOU 2663  OG  SER B 147     9354   8647   8491    615  -2765   -111       O  
ATOM   2664  N   LEU B 148     -15.019   1.904 -25.878  1.00 55.49           N  
ANISOU 2664  N   LEU B 148     6899   6122   8062    260  -2765     70       N  
ATOM   2665  CA  LEU B 148     -15.950   1.914 -24.769  1.00 62.47           C  
ANISOU 2665  CA  LEU B 148     7538   6845   9352    192  -2689    209       C  
ATOM   2666  C   LEU B 148     -15.649   3.222 -24.023  1.00 68.14           C  
ANISOU 2666  C   LEU B 148     8384   7602   9904    230  -2461    458       C  
ATOM   2667  O   LEU B 148     -14.696   3.927 -24.354  1.00 70.16           O  
ANISOU 2667  O   LEU B 148     8889   7950   9819    265  -2382    510       O  
ATOM   2668  CB  LEU B 148     -15.681   0.709 -23.874  1.00 65.39           C  
ANISOU 2668  CB  LEU B 148     7729   7038  10078     67  -2614    207       C  
ATOM   2669  CG  LEU B 148     -16.868   0.003 -23.236  1.00 68.30           C  
ANISOU 2669  CG  LEU B 148     7749   7220  10983    -11  -2607    252       C  
ATOM   2670  CD1 LEU B 148     -17.877  -0.297 -24.305  1.00 72.65           C  
ANISOU 2670  CD1 LEU B 148     8208   7756  11641     13  -2862     19       C  
ATOM   2671  CD2 LEU B 148     -16.421  -1.281 -22.547  1.00 68.97           C  
ANISOU 2671  CD2 LEU B 148     7675   7117  11414   -121  -2509    275       C  
ATOM   2672  N   VAL B 149     -16.439   3.560 -23.016  1.00 65.43           N  
ANISOU 2672  N   VAL B 149     7868   7186   9807    229  -2326    601       N  
ATOM   2673  CA  VAL B 149     -16.316   4.873 -22.384  1.00 56.55           C  
ANISOU 2673  CA  VAL B 149     6861   6089   8535    296  -2122    758       C  
ATOM   2674  C   VAL B 149     -16.579   6.032 -23.365  1.00 50.05           C  
ANISOU 2674  C   VAL B 149     6197   5337   7482    410  -2209    782       C  
ATOM   2675  O   VAL B 149     -17.472   6.833 -23.125  1.00 51.02           O  
ANISOU 2675  O   VAL B 149     6248   5447   7688    501  -2173    863       O  
ATOM   2676  CB  VAL B 149     -14.955   5.107 -21.701  1.00 51.36           C  
ANISOU 2676  CB  VAL B 149     6384   5437   7692    251  -1918    809       C  
ATOM   2677  CG1 VAL B 149     -14.980   6.437 -21.001  1.00 48.78           C  
ANISOU 2677  CG1 VAL B 149     6137   5096   7300    321  -1744    902       C  
ATOM   2678  CG2 VAL B 149     -14.621   3.981 -20.719  1.00 50.86           C  
ANISOU 2678  CG2 VAL B 149     6174   5348   7800    177  -1780    820       C  
ATOM   2679  N   ARG B 150     -15.808   6.124 -24.452  1.00 43.75           N  
ANISOU 2679  N   ARG B 150     5604   4631   6389    433  -2298    737       N  
ATOM   2680  CA  ARG B 150     -15.949   7.238 -25.396  1.00 50.57           C  
ANISOU 2680  CA  ARG B 150     6613   5582   7019    569  -2328    834       C  
ATOM   2681  C   ARG B 150     -17.293   7.230 -26.106  1.00 51.94           C  
ANISOU 2681  C   ARG B 150     6631   5843   7261    694  -2530    788       C  
ATOM   2682  O   ARG B 150     -17.748   8.260 -26.619  1.00 47.15           O  
ANISOU 2682  O   ARG B 150     6079   5295   6539    844  -2531    921       O  
ATOM   2683  CB  ARG B 150     -14.798   7.279 -26.407  1.00 52.80           C  
ANISOU 2683  CB  ARG B 150     7117   5998   6948    592  -2328    844       C  
ATOM   2684  CG  ARG B 150     -13.643   8.138 -25.924  1.00 52.89           C  
ANISOU 2684  CG  ARG B 150     7312   5923   6863    525  -2089   1002       C  
ATOM   2685  CD  ARG B 150     -12.451   8.143 -26.846  1.00 53.79           C  
ANISOU 2685  CD  ARG B 150     7606   6180   6653    535  -2043   1054       C  
ATOM   2686  NE  ARG B 150     -11.368   8.899 -26.227  1.00 55.88           N  
ANISOU 2686  NE  ARG B 150     7993   6318   6921    422  -1816   1189       N  
ATOM   2687  CZ  ARG B 150     -10.081   8.734 -26.500  1.00 55.87           C  
ANISOU 2687  CZ  ARG B 150     8106   6396   6726    350  -1715   1225       C  
ATOM   2688  NH1 ARG B 150      -9.701   7.831 -27.396  1.00 54.46           N  
ANISOU 2688  NH1 ARG B 150     7950   6444   6299    410  -1804   1128       N  
ATOM   2689  NH2 ARG B 150      -9.175   9.474 -25.872  1.00 54.24           N  
ANISOU 2689  NH2 ARG B 150     7973   6048   6588    222  -1525   1334       N  
ATOM   2690  N   GLN B 151     -17.936   6.068 -26.112  1.00 52.68           N  
ANISOU 2690  N   GLN B 151     6510   5931   7575    632  -2697    607       N  
ATOM   2691  CA  GLN B 151     -19.255   5.940 -26.716  1.00 55.77           C  
ANISOU 2691  CA  GLN B 151     6704   6404   8082    724  -2905    522       C  
ATOM   2692  C   GLN B 151     -20.318   6.575 -25.825  1.00 53.36           C  
ANISOU 2692  C   GLN B 151     6221   6013   8039    757  -2807    665       C  
ATOM   2693  O   GLN B 151     -21.414   6.886 -26.289  1.00 58.96           O  
ANISOU 2693  O   GLN B 151     6792   6814   8796    875  -2938    666       O  
ATOM   2694  CB  GLN B 151     -19.595   4.465 -26.972  1.00 62.41           C  
ANISOU 2694  CB  GLN B 151     7349   7210   9154    620  -3101    256       C  
ATOM   2695  CG  GLN B 151     -20.196   3.739 -25.765  1.00 65.48           C  
ANISOU 2695  CG  GLN B 151     7462   7385  10034    466  -3020    278       C  
ATOM   2696  CD  GLN B 151     -20.465   2.260 -26.031  1.00 70.74           C  
ANISOU 2696  CD  GLN B 151     7935   7937  11007    348  -3186     30       C  
ATOM   2697  OE1 GLN B 151     -19.631   1.562 -26.611  1.00 72.51           O  
ANISOU 2697  OE1 GLN B 151     8290   8170  11090    328  -3264   -156       O  
ATOM   2698  NE2 GLN B 151     -21.632   1.779 -25.606  1.00 71.18           N  
ANISOU 2698  NE2 GLN B 151     7674   7870  11500    279  -3221     28       N  
ATOM   2699  N   TYR B 152     -19.998   6.758 -24.547  1.00 49.88           N  
ANISOU 2699  N   TYR B 152     5774   5436   7744    678  -2569    777       N  
ATOM   2700  CA  TYR B 152     -20.941   7.367 -23.618  1.00 53.56           C  
ANISOU 2700  CA  TYR B 152     6078   5857   8415    744  -2433    900       C  
ATOM   2701  C   TYR B 152     -20.677   8.856 -23.433  1.00 51.73           C  
ANISOU 2701  C   TYR B 152     6057   5604   7996    882  -2273   1041       C  
ATOM   2702  O   TYR B 152     -21.212   9.463 -22.516  1.00 53.59           O  
ANISOU 2702  O   TYR B 152     6213   5792   8357    959  -2120   1117       O  
ATOM   2703  CB  TYR B 152     -20.941   6.634 -22.268  1.00 54.27           C  
ANISOU 2703  CB  TYR B 152     5984   5857   8779    628  -2248    934       C  
ATOM   2704  CG  TYR B 152     -21.515   5.237 -22.373  1.00 62.63           C  
ANISOU 2704  CG  TYR B 152     6765   6868  10162    498  -2382    841       C  
ATOM   2705  CD1 TYR B 152     -22.889   5.038 -22.457  1.00 65.17           C  
ANISOU 2705  CD1 TYR B 152     6801   7202  10760    521  -2479    840       C  
ATOM   2706  CD2 TYR B 152     -20.685   4.121 -22.413  1.00 64.36           C  
ANISOU 2706  CD2 TYR B 152     7003   7008  10444    355  -2413    749       C  
ATOM   2707  CE1 TYR B 152     -23.422   3.769 -22.571  1.00 68.29           C  
ANISOU 2707  CE1 TYR B 152     6931   7497  11518    380  -2596    744       C  
ATOM   2708  CE2 TYR B 152     -21.208   2.843 -22.526  1.00 66.70           C  
ANISOU 2708  CE2 TYR B 152     7047   7191  11107    233  -2531    650       C  
ATOM   2709  CZ  TYR B 152     -22.582   2.675 -22.607  1.00 70.74           C  
ANISOU 2709  CZ  TYR B 152     7275   7682  11921    235  -2619    646       C  
ATOM   2710  OH  TYR B 152     -23.130   1.413 -22.723  1.00 72.28           O  
ANISOU 2710  OH  TYR B 152     7215   7712  12537    100  -2723    541       O  
ATOM   2711  N   ASN B 153     -19.858   9.433 -24.310  1.00 48.32           N  
ANISOU 2711  N   ASN B 153     5881   5198   7281    923  -2298   1078       N  
ATOM   2712  CA  ASN B 153     -19.530  10.863 -24.256  1.00 48.67           C  
ANISOU 2712  CA  ASN B 153     6125   5158   7209   1036  -2143   1228       C  
ATOM   2713  C   ASN B 153     -19.172  11.410 -22.871  1.00 48.26           C  
ANISOU 2713  C   ASN B 153     6105   4947   7284   1002  -1910   1237       C  
ATOM   2714  O   ASN B 153     -19.887  12.245 -22.318  1.00 51.21           O  
ANISOU 2714  O   ASN B 153     6431   5253   7773   1138  -1828   1286       O  
ATOM   2715  CB  ASN B 153     -20.662  11.693 -24.855  1.00 53.03           C  
ANISOU 2715  CB  ASN B 153     6620   5769   7761   1253  -2223   1335       C  
ATOM   2716  CG  ASN B 153     -20.958  11.316 -26.291  1.00 58.72           C  
ANISOU 2716  CG  ASN B 153     7319   6703   8288   1341  -2459   1324       C  
ATOM   2717  OD1 ASN B 153     -20.105  11.456 -27.171  1.00 61.18           O  
ANISOU 2717  OD1 ASN B 153     7818   7092   8336   1364  -2469   1387       O  
ATOM   2718  ND2 ASN B 153     -22.181  10.854 -26.543  1.00 63.02           N  
ANISOU 2718  ND2 ASN B 153     7616   7373   8954   1408  -2646   1246       N  
ATOM   2719  N   PRO B 154     -18.058  10.939 -22.308  1.00 42.72           N  
ANISOU 2719  N   PRO B 154     5482   4205   6547    850  -1814   1173       N  
ATOM   2720  CA  PRO B 154     -17.580  11.480 -21.031  1.00 41.75           C  
ANISOU 2720  CA  PRO B 154     5399   3963   6500    846  -1623   1149       C  
ATOM   2721  C   PRO B 154     -17.057  12.894 -21.241  1.00 42.02           C  
ANISOU 2721  C   PRO B 154     5651   3822   6493    900  -1542   1212       C  
ATOM   2722  O   PRO B 154     -16.805  13.283 -22.386  1.00 41.52           O  
ANISOU 2722  O   PRO B 154     5717   3756   6302    910  -1591   1320       O  
ATOM   2723  CB  PRO B 154     -16.425  10.550 -20.679  1.00 39.06           C  
ANISOU 2723  CB  PRO B 154     5096   3659   6087    677  -1583   1076       C  
ATOM   2724  CG  PRO B 154     -15.943  10.075 -22.015  1.00 39.56           C  
ANISOU 2724  CG  PRO B 154     5262   3794   5973    603  -1720   1087       C  
ATOM   2725  CD  PRO B 154     -17.143   9.929 -22.865  1.00 40.93           C  
ANISOU 2725  CD  PRO B 154     5317   4052   6184    706  -1893   1108       C  
ATOM   2726  N   LYS B 155     -16.907  13.659 -20.165  1.00 45.90           N  
ANISOU 2726  N   LYS B 155     6170   4161   7108    956  -1419   1150       N  
ATOM   2727  CA  LYS B 155     -16.326  14.992 -20.280  1.00 49.04           C  
ANISOU 2727  CA  LYS B 155     6760   4314   7558    973  -1340   1177       C  
ATOM   2728  C   LYS B 155     -14.840  14.874 -20.630  1.00 44.06           C  
ANISOU 2728  C   LYS B 155     6284   3630   6826    769  -1303   1178       C  
ATOM   2729  O   LYS B 155     -14.321  15.639 -21.454  1.00 42.44           O  
ANISOU 2729  O   LYS B 155     6222   3303   6602    735  -1255   1310       O  
ATOM   2730  CB  LYS B 155     -16.529  15.794 -18.992  1.00 52.49           C  
ANISOU 2730  CB  LYS B 155     7177   4578   8190   1100  -1255   1029       C  
ATOM   2731  CG  LYS B 155     -16.100  17.246 -19.095  1.00 57.32           C  
ANISOU 2731  CG  LYS B 155     7961   4870   8949   1121  -1179   1020       C  
ATOM   2732  CD  LYS B 155     -16.617  18.063 -17.928  1.00 64.12           C  
ANISOU 2732  CD  LYS B 155     8781   5571  10011   1319  -1129    824       C  
ATOM   2733  CE  LYS B 155     -15.600  18.147 -16.812  1.00 66.95           C  
ANISOU 2733  CE  LYS B 155     9172   5814  10453   1257  -1103    525       C  
ATOM   2734  NZ  LYS B 155     -16.011  19.153 -15.786  1.00 74.42           N  
ANISOU 2734  NZ  LYS B 155    10103   6586  11586   1482  -1059    257       N  
ATOM   2735  N   MET B 156     -14.172  13.914 -19.998  1.00 38.72           N  
ANISOU 2735  N   MET B 156     5563   3056   6092    651  -1307   1064       N  
ATOM   2736  CA  MET B 156     -12.781  13.590 -20.301  1.00 41.49           C  
ANISOU 2736  CA  MET B 156     6030   3410   6323    458  -1280   1062       C  
ATOM   2737  C   MET B 156     -12.487  12.131 -19.924  1.00 39.14           C  
ANISOU 2737  C   MET B 156     5619   3366   5886    376  -1288    967       C  
ATOM   2738  O   MET B 156     -13.150  11.556 -19.044  1.00 36.10           O  
ANISOU 2738  O   MET B 156     5070   3089   5559    453  -1270    891       O  
ATOM   2739  CB  MET B 156     -11.815  14.549 -19.571  1.00 48.68           C  
ANISOU 2739  CB  MET B 156     7019   4119   7358    367  -1155    922       C  
ATOM   2740  CG  MET B 156     -11.597  14.235 -18.080  1.00 53.22           C  
ANISOU 2740  CG  MET B 156     7475   4824   7925    377  -1078    639       C  
ATOM   2741  SD  MET B 156     -10.185  15.045 -17.244  1.00 53.77           S  
ANISOU 2741  SD  MET B 156     7584   4769   8077    230   -981    359       S  
ATOM   2742  CE  MET B 156     -10.449  16.763 -17.645  1.00 46.10           C  
ANISOU 2742  CE  MET B 156     6737   3324   7456    268   -984    406       C  
ATOM   2743  N   VAL B 157     -11.523  11.516 -20.614  1.00 35.27           N  
ANISOU 2743  N   VAL B 157     5202   2979   5221    240  -1293    995       N  
ATOM   2744  CA AVAL B 157     -11.039  10.186 -20.243  0.69 35.14           C  
ANISOU 2744  CA AVAL B 157     5094   3164   5093    160  -1271    896       C  
ATOM   2745  CA BVAL B 157     -11.037  10.193 -20.250  0.31 35.34           C  
ANISOU 2745  CA BVAL B 157     5121   3189   5119    160  -1271    897       C  
ATOM   2746  C   VAL B 157      -9.536  10.221 -20.055  1.00 35.58           C  
ANISOU 2746  C   VAL B 157     5223   3266   5029     10  -1152    822       C  
ATOM   2747  O   VAL B 157      -8.811  10.809 -20.863  1.00 36.50           O  
ANISOU 2747  O   VAL B 157     5466   3316   5088    -67  -1129    912       O  
ATOM   2748  CB AVAL B 157     -11.322   9.105 -21.310  0.69 36.62           C  
ANISOU 2748  CB AVAL B 157     5262   3472   5179    164  -1422    948       C  
ATOM   2749  CB BVAL B 157     -11.382   9.135 -21.313  0.31 36.16           C  
ANISOU 2749  CB BVAL B 157     5202   3409   5128    170  -1426    952       C  
ATOM   2750  CG1AVAL B 157     -11.333   7.731 -20.667  0.69 28.89           C  
ANISOU 2750  CG1AVAL B 157     4128   2612   4236    131  -1405    855       C  
ATOM   2751  CG1BVAL B 157     -12.843   8.982 -21.392  0.31 38.11           C  
ANISOU 2751  CG1BVAL B 157     5312   3635   5533    296  -1558    988       C  
ATOM   2752  CG2AVAL B 157     -12.621   9.364 -22.000  0.69 40.94           C  
ANISOU 2752  CG2AVAL B 157     5764   3986   5806    297  -1575   1029       C  
ATOM   2753  CG2BVAL B 157     -10.843   9.535 -22.681  0.31 36.19           C  
ANISOU 2753  CG2BVAL B 157     5377   3426   4948    162  -1482   1069       C  
ATOM   2754  N   LYS B 158      -9.080   9.598 -18.977  1.00 29.38           N  
ANISOU 2754  N   LYS B 158     4336   2614   4212    -14  -1065    684       N  
ATOM   2755  CA  LYS B 158      -7.662   9.499 -18.707  1.00 34.54           C  
ANISOU 2755  CA  LYS B 158     5012   3362   4748   -140   -970    591       C  
ATOM   2756  C   LYS B 158      -7.412   8.043 -18.391  1.00 32.52           C  
ANISOU 2756  C   LYS B 158     4658   3317   4381   -128   -950    568       C  
ATOM   2757  O   LYS B 158      -8.324   7.335 -17.942  1.00 30.39           O  
ANISOU 2757  O   LYS B 158     4273   3085   4187    -27   -968    599       O  
ATOM   2758  CB  LYS B 158      -7.265  10.368 -17.511  1.00 36.13           C  
ANISOU 2758  CB  LYS B 158     5171   3533   5026   -139   -890    405       C  
ATOM   2759  CG  LYS B 158      -7.535  11.854 -17.684  1.00 43.70           C  
ANISOU 2759  CG  LYS B 158     6214   4207   6184   -143   -904    395       C  
ATOM   2760  CD  LYS B 158      -6.586  12.481 -18.685  1.00 46.36           C  
ANISOU 2760  CD  LYS B 158     6658   4398   6559   -314   -874    508       C  
ATOM   2761  CE  LYS B 158      -6.898  13.962 -18.891  1.00 50.64           C  
ANISOU 2761  CE  LYS B 158     7278   4588   7373   -313   -870    552       C  
ATOM   2762  NZ  LYS B 158      -5.784  14.622 -19.612  1.00 50.49           N  
ANISOU 2762  NZ  LYS B 158     7313   4416   7457   -504   -788    673       N  
ATOM   2763  N   VAL B 159      -6.183   7.589 -18.623  1.00 26.05           N  
ANISOU 2763  N   VAL B 159     3865   2618   3415   -224   -900    537       N  
ATOM   2764  CA  VAL B 159      -5.825   6.210 -18.309  1.00 23.41           C  
ANISOU 2764  CA  VAL B 159     3443   2456   2993   -195   -867    522       C  
ATOM   2765  C   VAL B 159      -4.661   6.214 -17.330  1.00 27.20           C  
ANISOU 2765  C   VAL B 159     3856   3113   3366   -219   -753    407       C  
ATOM   2766  O   VAL B 159      -3.682   6.935 -17.530  1.00 28.12           O  
ANISOU 2766  O   VAL B 159     4015   3236   3433   -332   -724    343       O  
ATOM   2767  CB  VAL B 159      -5.421   5.436 -19.573  1.00 25.07           C  
ANISOU 2767  CB  VAL B 159     3732   2698   3096   -233   -932    569       C  
ATOM   2768  CG1 VAL B 159      -5.007   4.016 -19.225  1.00 23.82           C  
ANISOU 2768  CG1 VAL B 159     3486   2663   2901   -192   -894    540       C  
ATOM   2769  CG2 VAL B 159      -6.567   5.429 -20.590  1.00 30.38           C  
ANISOU 2769  CG2 VAL B 159     4454   3248   3839   -181  -1090    636       C  
ATOM   2770  N   ALA B 160      -4.783   5.430 -16.261  1.00 20.02           N  
ANISOU 2770  N   ALA B 160     2817   2358   2433   -101   -687    398       N  
ATOM   2771  CA  ALA B 160      -3.678   5.208 -15.336  1.00 21.80           C  
ANISOU 2771  CA  ALA B 160     2956   2826   2503    -71   -597    298       C  
ATOM   2772  C   ALA B 160      -3.318   3.743 -15.482  1.00 29.12           C  
ANISOU 2772  C   ALA B 160     3836   3857   3373    -20   -554    405       C  
ATOM   2773  O   ALA B 160      -4.196   2.890 -15.402  1.00 30.42           O  
ANISOU 2773  O   ALA B 160     3944   3954   3661     67   -546    536       O  
ATOM   2774  CB  ALA B 160      -4.105   5.478 -13.915  1.00 22.56           C  
ANISOU 2774  CB  ALA B 160     2933   3068   2570     98   -539    229       C  
ATOM   2775  N   SER B 161      -2.036   3.446 -15.672  1.00 25.22           N  
ANISOU 2775  N   SER B 161     3341   3509   2732    -70   -521    352       N  
ATOM   2776  CA  SER B 161      -1.604   2.061 -15.756  1.00 22.46           C  
ANISOU 2776  CA  SER B 161     2948   3249   2339      9   -471    438       C  
ATOM   2777  C   SER B 161      -0.394   1.877 -14.857  1.00 24.34           C  
ANISOU 2777  C   SER B 161     3074   3788   2387     82   -384    375       C  
ATOM   2778  O   SER B 161       0.568   2.657 -14.938  1.00 25.57           O  
ANISOU 2778  O   SER B 161     3224   4051   2442    -25   -397    235       O  
ATOM   2779  CB  SER B 161      -1.303   1.670 -17.219  1.00 26.19           C  
ANISOU 2779  CB  SER B 161     3540   3607   2803    -81   -539    441       C  
ATOM   2780  OG  SER B 161      -0.997   0.288 -17.315  1.00 26.60           O  
ANISOU 2780  OG  SER B 161     3554   3688   2863     17   -507    488       O  
ATOM   2781  N   LEU B 162      -0.459   0.900 -13.952  1.00 22.23           N  
ANISOU 2781  N   LEU B 162     2691   3665   2092    272   -293    492       N  
ATOM   2782  CA  LEU B 162       0.693   0.603 -13.100  1.00 24.36           C  
ANISOU 2782  CA  LEU B 162     2839   4273   2145    395   -220    453       C  
ATOM   2783  C   LEU B 162       1.948   0.360 -13.932  1.00 24.69           C  
ANISOU 2783  C   LEU B 162     2908   4375   2097    297   -232    383       C  
ATOM   2784  O   LEU B 162       3.018   0.913 -13.651  1.00 26.80           O  
ANISOU 2784  O   LEU B 162     3096   4873   2215    255   -240    235       O  
ATOM   2785  CB  LEU B 162       0.444  -0.626 -12.214  1.00 25.27           C  
ANISOU 2785  CB  LEU B 162     2835   4508   2257    648    -91    684       C  
ATOM   2786  CG  LEU B 162       1.619  -0.892 -11.276  1.00 29.84           C  
ANISOU 2786  CG  LEU B 162     3277   5497   2565    829    -26    658       C  
ATOM   2787  CD1 LEU B 162       1.770   0.245 -10.258  1.00 30.11           C  
ANISOU 2787  CD1 LEU B 162     3224   5822   2393    890    -72    447       C  
ATOM   2788  CD2 LEU B 162       1.464  -2.219 -10.543  1.00 33.65           C  
ANISOU 2788  CD2 LEU B 162     3651   6077   3058   1104    131    965       C  
ATOM   2789  N   LEU B 163       1.818  -0.483 -14.946  1.00 23.75           N  
ANISOU 2789  N   LEU B 163     2881   4065   2079    275   -239    469       N  
ATOM   2790  CA  LEU B 163       2.964  -0.860 -15.773  1.00 24.70           C  
ANISOU 2790  CA  LEU B 163     3024   4269   2090    239   -228    418       C  
ATOM   2791  C   LEU B 163       2.705  -0.618 -17.251  1.00 22.85           C  
ANISOU 2791  C   LEU B 163     2950   3824   1908    100   -306    381       C  
ATOM   2792  O   LEU B 163       1.583  -0.793 -17.739  1.00 25.89           O  
ANISOU 2792  O   LEU B 163     3426   3961   2450     88   -383    416       O  
ATOM   2793  CB  LEU B 163       3.298  -2.334 -15.582  1.00 26.73           C  
ANISOU 2793  CB  LEU B 163     3227   4568   2360    438   -151    532       C  
ATOM   2794  CG  LEU B 163       3.431  -2.858 -14.161  1.00 31.13           C  
ANISOU 2794  CG  LEU B 163     3626   5343   2859    655    -48    662       C  
ATOM   2795  CD1 LEU B 163       3.677  -4.374 -14.174  1.00 32.44           C  
ANISOU 2795  CD1 LEU B 163     3760   5447   3119    851     40    825       C  
ATOM   2796  CD2 LEU B 163       4.545  -2.138 -13.397  1.00 27.96           C  
ANISOU 2796  CD2 LEU B 163     3090   5338   2194    677    -40    535       C  
ATOM   2797  N   VAL B 164       3.755  -0.221 -17.961  1.00 23.15           N  
ANISOU 2797  N   VAL B 164     2999   3994   1803     14   -284    321       N  
ATOM   2798  CA  VAL B 164       3.732  -0.122 -19.410  1.00 24.85           C  
ANISOU 2798  CA  VAL B 164     3353   4113   1976    -45   -324    318       C  
ATOM   2799  C   VAL B 164       4.978  -0.834 -19.896  1.00 27.01           C  
ANISOU 2799  C   VAL B 164     3583   4598   2079     43   -244    297       C  
ATOM   2800  O   VAL B 164       6.073  -0.492 -19.468  1.00 25.56           O  
ANISOU 2800  O   VAL B 164     3262   4649   1799      5   -159    285       O  
ATOM   2801  CB  VAL B 164       3.796   1.340 -19.884  1.00 27.11           C  
ANISOU 2801  CB  VAL B 164     3678   4367   2257   -235   -328    332       C  
ATOM   2802  CG1 VAL B 164       3.907   1.393 -21.422  1.00 32.15           C  
ANISOU 2802  CG1 VAL B 164     4446   4995   2773   -235   -335    386       C  
ATOM   2803  CG2 VAL B 164       2.556   2.085 -19.453  1.00 25.73           C  
ANISOU 2803  CG2 VAL B 164     3551   3973   2252   -294   -408    341       C  
ATOM   2804  N   LYS B 165       4.820  -1.830 -20.765  1.00 25.55           N  
ANISOU 2804  N   LYS B 165     3496   4340   1870    174   -282    264       N  
ATOM   2805  CA  LYS B 165       5.979  -2.558 -21.305  1.00 28.28           C  
ANISOU 2805  CA  LYS B 165     3811   4893   2042    305   -202    224       C  
ATOM   2806  C   LYS B 165       6.591  -1.815 -22.487  1.00 27.58           C  
ANISOU 2806  C   LYS B 165     3771   4963   1746    241   -153    245       C  
ATOM   2807  O   LYS B 165       5.868  -1.262 -23.308  1.00 30.59           O  
ANISOU 2807  O   LYS B 165     4283   5231   2109    188   -227    265       O  
ATOM   2808  CB  LYS B 165       5.571  -3.957 -21.772  1.00 31.15           C  
ANISOU 2808  CB  LYS B 165     4257   5092   2486    502   -273    132       C  
ATOM   2809  CG  LYS B 165       5.379  -4.961 -20.654  1.00 33.44           C  
ANISOU 2809  CG  LYS B 165     4454   5267   2986    620   -244    182       C  
ATOM   2810  CD  LYS B 165       5.405  -6.396 -21.213  1.00 36.50           C  
ANISOU 2810  CD  LYS B 165     4893   5495   3481    825   -282     74       C  
ATOM   2811  CE  LYS B 165       5.449  -7.391 -20.071  1.00 34.31           C  
ANISOU 2811  CE  LYS B 165     4496   5120   3420    966   -195    204       C  
ATOM   2812  NZ  LYS B 165       5.377  -8.787 -20.552  1.00 27.66           N  
ANISOU 2812  NZ  LYS B 165     3695   4020   2793   1154   -235     98       N  
ATOM   2813  N   ARG B 166       7.919  -1.818 -22.591  1.00 28.88           N  
ANISOU 2813  N   ARG B 166     3911   4311   2749   -304    -42     69       N  
ATOM   2814  CA  ARG B 166       8.569  -1.302 -23.798  1.00 27.52           C  
ANISOU 2814  CA  ARG B 166     3671   4199   2588   -448    -42    102       C  
ATOM   2815  C   ARG B 166       8.510  -2.375 -24.868  1.00 35.26           C  
ANISOU 2815  C   ARG B 166     4696   5228   3472   -473     21    134       C  
ATOM   2816  O   ARG B 166       9.372  -3.260 -24.943  1.00 35.52           O  
ANISOU 2816  O   ARG B 166     4722   5343   3430   -417     73     84       O  
ATOM   2817  CB  ARG B 166      10.018  -0.866 -23.531  1.00 26.56           C  
ANISOU 2817  CB  ARG B 166     3431   4161   2498   -453    -52      5       C  
ATOM   2818  CG  ARG B 166      10.123   0.514 -22.875  1.00 30.83           C  
ANISOU 2818  CG  ARG B 166     3905   4643   3168   -499   -111    -39       C  
ATOM   2819  CD  ARG B 166      11.566   1.001 -22.724  1.00 33.61           C  
ANISOU 2819  CD  ARG B 166     4093   5077   3602   -541   -114   -181       C  
ATOM   2820  NE  ARG B 166      12.372   0.062 -21.946  1.00 35.90           N  
ANISOU 2820  NE  ARG B 166     4330   5502   3810   -366   -160   -319       N  
ATOM   2821  CZ  ARG B 166      12.366  -0.017 -20.619  1.00 37.15           C  
ANISOU 2821  CZ  ARG B 166     4499   5684   3932   -184   -255   -429       C  
ATOM   2822  NH1 ARG B 166      11.600   0.802 -19.901  1.00 31.22           N  
ANISOU 2822  NH1 ARG B 166     3801   4823   3238   -178   -310   -418       N  
ATOM   2823  NH2 ARG B 166      13.131  -0.918 -20.008  1.00 37.84           N  
ANISOU 2823  NH2 ARG B 166     4563   5907   3906     20   -291   -546       N  
ATOM   2824  N   THR B 167       7.470  -2.295 -25.686  1.00 32.83           N  
ANISOU 2824  N   THR B 167     4434   4876   3163   -539      6    202       N  
ATOM   2825  CA  THR B 167       7.186  -3.319 -26.678  1.00 36.92           C  
ANISOU 2825  CA  THR B 167     4999   5434   3595   -557     43    202       C  
ATOM   2826  C   THR B 167       6.412  -2.664 -27.834  1.00 41.35           C  
ANISOU 2826  C   THR B 167     5580   5991   4140   -628    -20    271       C  
ATOM   2827  O   THR B 167       5.703  -1.669 -27.617  1.00 42.74           O  
ANISOU 2827  O   THR B 167     5748   6109   4383   -637    -82    316       O  
ATOM   2828  CB  THR B 167       6.382  -4.457 -26.019  1.00 39.25           C  
ANISOU 2828  CB  THR B 167     5341   5669   3904   -487     96    141       C  
ATOM   2829  OG1 THR B 167       6.238  -5.552 -26.930  1.00 46.99           O  
ANISOU 2829  OG1 THR B 167     6360   6680   4814   -514    148    104       O  
ATOM   2830  CG2 THR B 167       5.020  -3.955 -25.592  1.00 32.65           C  
ANISOU 2830  CG2 THR B 167     4494   4735   3175   -497     50    150       C  
ATOM   2831  N   PRO B 168       6.565  -3.193 -29.068  1.00 40.15           N  
ANISOU 2831  N   PRO B 168     5470   5906   3878   -650     -5    278       N  
ATOM   2832  CA  PRO B 168       5.899  -2.540 -30.202  1.00 39.88           C  
ANISOU 2832  CA  PRO B 168     5483   5888   3783   -660    -78    339       C  
ATOM   2833  C   PRO B 168       4.392  -2.421 -29.995  1.00 40.78           C  
ANISOU 2833  C   PRO B 168     5569   5967   3960   -636   -182    301       C  
ATOM   2834  O   PRO B 168       3.762  -3.377 -29.545  1.00 38.81           O  
ANISOU 2834  O   PRO B 168     5280   5698   3770   -636   -173    198       O  
ATOM   2835  CB  PRO B 168       6.191  -3.487 -31.371  1.00 40.36           C  
ANISOU 2835  CB  PRO B 168     5604   6032   3701   -654    -53    309       C  
ATOM   2836  CG  PRO B 168       7.469  -4.165 -31.003  1.00 37.53           C  
ANISOU 2836  CG  PRO B 168     5229   5697   3332   -663     64    288       C  
ATOM   2837  CD  PRO B 168       7.372  -4.352 -29.497  1.00 38.30           C  
ANISOU 2837  CD  PRO B 168     5263   5738   3550   -638     76    233       C  
ATOM   2838  N   ARG B 169       3.824  -1.267 -30.339  1.00 42.66           N  
ANISOU 2838  N   ARG B 169     5828   6188   4193   -610   -257    379       N  
ATOM   2839  CA  ARG B 169       2.428  -0.996 -30.021  1.00 52.65           C  
ANISOU 2839  CA  ARG B 169     7040   7425   5540   -573   -359    342       C  
ATOM   2840  C   ARG B 169       1.726  -0.238 -31.155  1.00 60.95           C  
ANISOU 2840  C   ARG B 169     8144   8535   6479   -489   -474    393       C  
ATOM   2841  O   ARG B 169       1.909   0.971 -31.313  1.00 65.24           O  
ANISOU 2841  O   ARG B 169     8764   9036   6987   -450   -462    522       O  
ATOM   2842  CB  ARG B 169       2.357  -0.213 -28.705  1.00 55.52           C  
ANISOU 2842  CB  ARG B 169     7372   7681   6042   -580   -330    385       C  
ATOM   2843  CG  ARG B 169       1.123  -0.484 -27.861  1.00 55.70           C  
ANISOU 2843  CG  ARG B 169     7316   7645   6201   -560   -362    310       C  
ATOM   2844  CD  ARG B 169       1.272   0.091 -26.459  1.00 52.27           C  
ANISOU 2844  CD  ARG B 169     6882   7101   5876   -549   -308    346       C  
ATOM   2845  NE  ARG B 169       2.123  -0.747 -25.622  1.00 57.82           N  
ANISOU 2845  NE  ARG B 169     7599   7783   6588   -549   -206    296       N  
ATOM   2846  CZ  ARG B 169       3.236  -0.335 -25.025  1.00 53.00           C  
ANISOU 2846  CZ  ARG B 169     7010   7164   5963   -542   -173    319       C  
ATOM   2847  NH1 ARG B 169       3.641   0.918 -25.155  1.00 50.81           N  
ANISOU 2847  NH1 ARG B 169     6740   6871   5695   -572   -205    388       N  
ATOM   2848  NH2 ARG B 169       3.936  -1.179 -24.287  1.00 55.78           N  
ANISOU 2848  NH2 ARG B 169     7377   7522   6296   -493   -100    258       N  
ATOM   2849  N   SER B 170       0.922  -0.955 -31.936  1.00 64.47           N  
ANISOU 2849  N   SER B 170     8555   9076   6865   -446   -580    276       N  
ATOM   2850  CA  SER B 170       0.235  -0.364 -33.086  1.00 73.04           C  
ANISOU 2850  CA  SER B 170     9698  10255   7800   -311   -722    294       C  
ATOM   2851  C   SER B 170      -0.759   0.719 -32.664  1.00 77.30           C  
ANISOU 2851  C   SER B 170    10200  10759   8411   -230   -807    342       C  
ATOM   2852  O   SER B 170      -0.451   1.911 -32.705  1.00 79.34           O  
ANISOU 2852  O   SER B 170    10575  10955   8616   -173   -763    507       O  
ATOM   2853  CB  SER B 170      -0.480  -1.444 -33.909  1.00 73.89           C  
ANISOU 2853  CB  SER B 170     9735  10489   7849   -278   -849     97       C  
ATOM   2854  OG  SER B 170      -1.573  -1.989 -33.196  1.00 74.96           O  
ANISOU 2854  OG  SER B 170     9684  10607   8189   -331   -900    -74       O  
ATOM   2855  N   TYR B 173      -2.807   5.660 -28.378  1.00 56.17           N  
ANISOU 2855  N   TYR B 173     7515   7558   6269   -125   -713    739       N  
ATOM   2856  CA  TYR B 173      -2.956   6.376 -27.112  1.00 57.31           C  
ANISOU 2856  CA  TYR B 173     7659   7559   6558   -150   -649    786       C  
ATOM   2857  C   TYR B 173      -1.842   6.021 -26.131  1.00 57.01           C  
ANISOU 2857  C   TYR B 173     7623   7437   6601   -285   -531    758       C  
ATOM   2858  O   TYR B 173      -1.600   4.846 -25.854  1.00 57.55           O  
ANISOU 2858  O   TYR B 173     7616   7546   6704   -344   -513    654       O  
ATOM   2859  CB  TYR B 173      -4.314   6.058 -26.479  1.00 58.66           C  
ANISOU 2859  CB  TYR B 173     7685   7735   6869   -100   -718    694       C  
ATOM   2860  CG  TYR B 173      -4.727   6.999 -25.366  1.00 58.77           C  
ANISOU 2860  CG  TYR B 173     7726   7606   6996    -69   -668    765       C  
ATOM   2861  CD1 TYR B 173      -5.375   8.196 -25.657  1.00 62.61           C  
ANISOU 2861  CD1 TYR B 173     8282   8071   7437     62   -714    871       C  
ATOM   2862  CD2 TYR B 173      -4.487   6.689 -24.029  1.00 56.87           C  
ANISOU 2862  CD2 TYR B 173     7467   7254   6888   -140   -572    727       C  
ATOM   2863  CE1 TYR B 173      -5.769   9.066 -24.656  1.00 61.14           C  
ANISOU 2863  CE1 TYR B 173     8132   7747   7351     96   -662    936       C  
ATOM   2864  CE2 TYR B 173      -4.880   7.558 -23.012  1.00 58.02           C  
ANISOU 2864  CE2 TYR B 173     7654   7267   7122    -95   -529    786       C  
ATOM   2865  CZ  TYR B 173      -5.522   8.746 -23.337  1.00 58.25           C  
ANISOU 2865  CZ  TYR B 173     7741   7271   7122     10   -573    889       C  
ATOM   2866  OH  TYR B 173      -5.920   9.628 -22.353  1.00 56.64           O  
ANISOU 2866  OH  TYR B 173     7591   6929   7001     59   -524    949       O  
ATOM   2867  N   LYS B 174      -1.162   7.042 -25.615  1.00 54.72           N  
ANISOU 2867  N   LYS B 174     7420   7030   6340   -318   -449    838       N  
ATOM   2868  CA  LYS B 174      -0.208   6.860 -24.524  1.00 50.58           C  
ANISOU 2868  CA  LYS B 174     6878   6440   5901   -407   -375    778       C  
ATOM   2869  C   LYS B 174      -0.940   7.119 -23.208  1.00 39.28           C  
ANISOU 2869  C   LYS B 174     5427   4912   4587   -359   -380    756       C  
ATOM   2870  O   LYS B 174      -1.697   8.086 -23.100  1.00 37.32           O  
ANISOU 2870  O   LYS B 174     5222   4590   4367   -296   -395    832       O  
ATOM   2871  CB  LYS B 174       0.970   7.812 -24.678  1.00 53.47           C  
ANISOU 2871  CB  LYS B 174     7320   6734   6263   -483   -282    827       C  
ATOM   2872  N   PRO B 175      -0.735   6.253 -22.204  1.00 37.21           N  
ANISOU 2872  N   PRO B 175     5122   4640   4378   -362   -352    662       N  
ATOM   2873  CA  PRO B 175      -1.488   6.464 -20.956  1.00 31.10           C  
ANISOU 2873  CA  PRO B 175     4359   3759   3699   -287   -333    652       C  
ATOM   2874  C   PRO B 175      -1.107   7.767 -20.270  1.00 32.04           C  
ANISOU 2874  C   PRO B 175     4557   3767   3851   -283   -320    689       C  
ATOM   2875  O   PRO B 175       0.034   8.203 -20.368  1.00 32.25           O  
ANISOU 2875  O   PRO B 175     4604   3793   3856   -356   -304    665       O  
ATOM   2876  CB  PRO B 175      -1.098   5.259 -20.088  1.00 36.29           C  
ANISOU 2876  CB  PRO B 175     5004   4421   4362   -261   -274    553       C  
ATOM   2877  CG  PRO B 175       0.143   4.693 -20.724  1.00 40.32           C  
ANISOU 2877  CG  PRO B 175     5499   5038   4784   -332   -277    509       C  
ATOM   2878  CD  PRO B 175       0.063   5.016 -22.186  1.00 39.81           C  
ANISOU 2878  CD  PRO B 175     5414   5046   4665   -397   -322    573       C  
ATOM   2879  N   ASP B 176      -2.056   8.377 -19.573  1.00 32.06           N  
ANISOU 2879  N   ASP B 176     4593   3669   3921   -205   -315    731       N  
ATOM   2880  CA  ASP B 176      -1.819   9.666 -18.932  1.00 33.79           C  
ANISOU 2880  CA  ASP B 176     4899   3764   4175   -198   -298    760       C  
ATOM   2881  C   ASP B 176      -1.030   9.576 -17.630  1.00 32.66           C  
ANISOU 2881  C   ASP B 176     4788   3572   4048   -175   -284    649       C  
ATOM   2882  O   ASP B 176      -0.289  10.492 -17.271  1.00 34.18           O  
ANISOU 2882  O   ASP B 176     5021   3702   4266   -219   -283    607       O  
ATOM   2883  CB  ASP B 176      -3.159  10.338 -18.674  1.00 36.98           C  
ANISOU 2883  CB  ASP B 176     5335   4081   4634   -100   -296    847       C  
ATOM   2884  CG  ASP B 176      -4.008  10.406 -19.920  1.00 35.76           C  
ANISOU 2884  CG  ASP B 176     5137   4006   4446    -71   -343    929       C  
ATOM   2885  OD1 ASP B 176      -4.761   9.446 -20.195  1.00 29.70           O  
ANISOU 2885  OD1 ASP B 176     4260   3325   3700    -40   -375    886       O  
ATOM   2886  OD2 ASP B 176      -3.887  11.411 -20.636  1.00 35.00           O  
ANISOU 2886  OD2 ASP B 176     5118   3881   4297    -68   -340   1021       O  
ATOM   2887  N   PHE B 177      -1.206   8.476 -16.910  1.00 25.26           N  
ANISOU 2887  N   PHE B 177     3841   2660   3098    -91   -266    588       N  
ATOM   2888  CA  PHE B 177      -0.498   8.280 -15.654  1.00 25.81           C  
ANISOU 2888  CA  PHE B 177     3967   2704   3136     -3   -266    478       C  
ATOM   2889  C   PHE B 177       0.124   6.889 -15.659  1.00 29.54           C  
ANISOU 2889  C   PHE B 177     4408   3284   3532     30   -248    402       C  
ATOM   2890  O   PHE B 177      -0.583   5.886 -15.774  1.00 32.14           O  
ANISOU 2890  O   PHE B 177     4732   3615   3865     71   -177    432       O  
ATOM   2891  CB  PHE B 177      -1.472   8.405 -14.476  1.00 26.65           C  
ANISOU 2891  CB  PHE B 177     4171   2682   3274    151   -213    504       C  
ATOM   2892  CG  PHE B 177      -2.324   9.642 -14.522  1.00 30.07           C  
ANISOU 2892  CG  PHE B 177     4637   3004   3782    141   -212    600       C  
ATOM   2893  CD1 PHE B 177      -1.791  10.885 -14.190  1.00 28.63           C  
ANISOU 2893  CD1 PHE B 177     4513   2751   3614    109   -249    572       C  
ATOM   2894  CD2 PHE B 177      -3.663   9.566 -14.893  1.00 27.71           C  
ANISOU 2894  CD2 PHE B 177     4304   2673   3553    167   -169    701       C  
ATOM   2895  CE1 PHE B 177      -2.579  12.030 -14.236  1.00 30.85           C  
ANISOU 2895  CE1 PHE B 177     4851   2914   3955    115   -227    671       C  
ATOM   2896  CE2 PHE B 177      -4.457  10.709 -14.931  1.00 27.53           C  
ANISOU 2896  CE2 PHE B 177     4316   2559   3585    191   -170    794       C  
ATOM   2897  CZ  PHE B 177      -3.914  11.941 -14.606  1.00 28.58           C  
ANISOU 2897  CZ  PHE B 177     4542   2607   3710    170   -191    793       C  
ATOM   2898  N   VAL B 178       1.444   6.819 -15.536  1.00 24.54           N  
ANISOU 2898  N   VAL B 178     3747   2736   2843     12   -300    289       N  
ATOM   2899  CA  VAL B 178       2.133   5.528 -15.605  1.00 23.46           C  
ANISOU 2899  CA  VAL B 178     3586   2712   2617     61   -283    221       C  
ATOM   2900  C   VAL B 178       2.948   5.284 -14.348  1.00 24.40           C  
ANISOU 2900  C   VAL B 178     3765   2859   2645    240   -321     83       C  
ATOM   2901  O   VAL B 178       3.708   6.163 -13.936  1.00 26.68           O  
ANISOU 2901  O   VAL B 178     4021   3166   2952    228   -413    -27       O  
ATOM   2902  CB  VAL B 178       3.087   5.497 -16.810  1.00 31.07           C  
ANISOU 2902  CB  VAL B 178     4437   3795   3574   -102   -315    201       C  
ATOM   2903  CG1 VAL B 178       3.938   4.217 -16.805  1.00 28.41           C  
ANISOU 2903  CG1 VAL B 178     4078   3581   3137    -35   -301    119       C  
ATOM   2904  CG2 VAL B 178       2.315   5.627 -18.096  1.00 31.02           C  
ANISOU 2904  CG2 VAL B 178     4399   3781   3605   -225   -289    329       C  
ATOM   2905  N   GLY B 179       2.797   4.112 -13.723  1.00 21.70           N  
ANISOU 2905  N   GLY B 179     3520   2518   2207    423   -243     74       N  
ATOM   2906  CA  GLY B 179       3.618   3.817 -12.565  1.00 23.39           C  
ANISOU 2906  CA  GLY B 179     3817   2782   2287    654   -290    -59       C  
ATOM   2907  C   GLY B 179       5.061   3.599 -12.996  1.00 30.08           C  
ANISOU 2907  C   GLY B 179     4533   3813   3083    612   -393   -196       C  
ATOM   2908  O   GLY B 179       5.949   4.395 -12.658  1.00 26.87           O  
ANISOU 2908  O   GLY B 179     4041   3475   2692    603   -526   -349       O  
ATOM   2909  N   PHE B 180       5.287   2.520 -13.748  1.00 24.44           N  
ANISOU 2909  N   PHE B 180     3006   3302   2978     40   -295    559       N  
ATOM   2910  CA  PHE B 180       6.631   2.055 -14.082  1.00 22.23           C  
ANISOU 2910  CA  PHE B 180     2715   3183   2549    -86   -193    530       C  
ATOM   2911  C   PHE B 180       6.669   1.637 -15.539  1.00 26.88           C  
ANISOU 2911  C   PHE B 180     3354   3929   2931   -177   -191    611       C  
ATOM   2912  O   PHE B 180       5.755   0.972 -16.011  1.00 25.49           O  
ANISOU 2912  O   PHE B 180     3190   3801   2694   -128   -261    599       O  
ATOM   2913  CB  PHE B 180       6.959   0.827 -13.237  1.00 22.97           C  
ANISOU 2913  CB  PHE B 180     2716   3364   2649    -17   -103    353       C  
ATOM   2914  CG  PHE B 180       6.938   1.083 -11.755  1.00 21.86           C  
ANISOU 2914  CG  PHE B 180     2579   3092   2635     40   -106    264       C  
ATOM   2915  CD1 PHE B 180       5.745   1.018 -11.033  1.00 22.53           C  
ANISOU 2915  CD1 PHE B 180     2680   3071   2808    162   -113    204       C  
ATOM   2916  CD2 PHE B 180       8.113   1.374 -11.088  1.00 22.89           C  
ANISOU 2916  CD2 PHE B 180     2701   3211   2787    -48    -97    240       C  
ATOM   2917  CE1 PHE B 180       5.734   1.245  -9.653  1.00 25.39           C  
ANISOU 2917  CE1 PHE B 180     3105   3317   3226    192    -76    102       C  
ATOM   2918  CE2 PHE B 180       8.113   1.619  -9.718  1.00 24.55           C  
ANISOU 2918  CE2 PHE B 180     2978   3298   3053    -33   -126    153       C  
ATOM   2919  CZ  PHE B 180       6.927   1.554  -9.002  1.00 23.57           C  
ANISOU 2919  CZ  PHE B 180     2925   3068   2962     85    -98     74       C  
ATOM   2920  N   GLU B 181       7.727   2.013 -16.244  1.00 24.64           N  
ANISOU 2920  N   GLU B 181     3111   3726   2527   -332   -103    691       N  
ATOM   2921  CA  GLU B 181       7.935   1.530 -17.603  1.00 26.13           C  
ANISOU 2921  CA  GLU B 181     3391   4084   2455   -444    -32    732       C  
ATOM   2922  C   GLU B 181       8.974   0.417 -17.552  1.00 29.24           C  
ANISOU 2922  C   GLU B 181     3675   4636   2800   -437    197    559       C  
ATOM   2923  O   GLU B 181      10.114   0.633 -17.136  1.00 30.01           O  
ANISOU 2923  O   GLU B 181     3646   4757   2998   -483    322    547       O  
ATOM   2924  CB  GLU B 181       8.405   2.661 -18.497  1.00 28.58           C  
ANISOU 2924  CB  GLU B 181     3831   4382   2647   -635    -36    946       C  
ATOM   2925  CG  GLU B 181       8.337   2.347 -19.982  1.00 35.62           C  
ANISOU 2925  CG  GLU B 181     4908   5426   3200   -780      0   1024       C  
ATOM   2926  CD  GLU B 181       9.092   3.350 -20.780  1.00 39.99           C  
ANISOU 2926  CD  GLU B 181     5588   5997   3611  -1006     73   1229       C  
ATOM   2927  OE1 GLU B 181      10.342   3.345 -20.674  1.00 42.81           O  
ANISOU 2927  OE1 GLU B 181     5831   6444   3990  -1095    322   1182       O  
ATOM   2928  OE2 GLU B 181       8.440   4.150 -21.491  1.00 42.21           O  
ANISOU 2928  OE2 GLU B 181     6064   6191   3781  -1099   -131   1457       O  
ATOM   2929  N   ILE B 182       8.582  -0.779 -17.977  1.00 27.79           N  
ANISOU 2929  N   ILE B 182     3528   4541   2491   -381    239    430       N  
ATOM   2930  CA  ILE B 182       9.392  -1.967 -17.715  1.00 25.21           C  
ANISOU 2930  CA  ILE B 182     3081   4298   2199   -305    436    241       C  
ATOM   2931  C   ILE B 182       9.854  -2.626 -19.007  1.00 27.50           C  
ANISOU 2931  C   ILE B 182     3486   4732   2229   -391    647    167       C  
ATOM   2932  O   ILE B 182       9.310  -2.339 -20.077  1.00 30.12           O  
ANISOU 2932  O   ILE B 182     4038   5108   2298   -519    590    250       O  
ATOM   2933  CB  ILE B 182       8.594  -2.980 -16.884  1.00 23.95           C  
ANISOU 2933  CB  ILE B 182     2877   4068   2154   -146    340    107       C  
ATOM   2934  CG1 ILE B 182       7.372  -3.476 -17.655  1.00 27.52           C  
ANISOU 2934  CG1 ILE B 182     3490   4528   2440   -168    216     94       C  
ATOM   2935  CG2 ILE B 182       8.216  -2.382 -15.520  1.00 25.09           C  
ANISOU 2935  CG2 ILE B 182     2933   4078   2524    -68    199    149       C  
ATOM   2936  CD1 ILE B 182       6.676  -4.663 -16.950  1.00 28.59           C  
ANISOU 2936  CD1 ILE B 182     3578   4603   2682    -49    162    -46       C  
ATOM   2937  N   PRO B 183      10.866  -3.510 -18.920  1.00 28.52           N  
ANISOU 2937  N   PRO B 183     3480   4926   2431   -320    892     10       N  
ATOM   2938  CA  PRO B 183      11.264  -4.222 -20.140  1.00 33.05           C  
ANISOU 2938  CA  PRO B 183     4192   5614   2750   -381   1153   -113       C  
ATOM   2939  C   PRO B 183      10.195  -5.234 -20.539  1.00 31.77           C  
ANISOU 2939  C   PRO B 183     4244   5413   2413   -346   1045   -249       C  
ATOM   2940  O   PRO B 183       9.258  -5.482 -19.785  1.00 34.04           O  
ANISOU 2940  O   PRO B 183     4503   5596   2834   -257    801   -247       O  
ATOM   2941  CB  PRO B 183      12.534  -4.976 -19.723  1.00 38.29           C  
ANISOU 2941  CB  PRO B 183     4594   6306   3650   -250   1426   -257       C  
ATOM   2942  CG  PRO B 183      12.890  -4.483 -18.337  1.00 31.46           C  
ANISOU 2942  CG  PRO B 183     3462   5362   3128   -174   1258   -159       C  
ATOM   2943  CD  PRO B 183      11.653  -3.922 -17.739  1.00 29.87           C  
ANISOU 2943  CD  PRO B 183     3384   5052   2914   -180    933    -60       C  
ATOM   2944  N   ASP B 184      10.365  -5.840 -21.702  1.00 37.58           N  
ANISOU 2944  N   ASP B 184     5198   6229   2851   -430   1247   -379       N  
ATOM   2945  CA  ASP B 184       9.451  -6.867 -22.170  1.00 42.28           C  
ANISOU 2945  CA  ASP B 184     6029   6777   3257   -437   1146   -535       C  
ATOM   2946  C   ASP B 184       9.797  -8.198 -21.503  1.00 38.31           C  
ANISOU 2946  C   ASP B 184     5393   6170   2992   -231   1278   -767       C  
ATOM   2947  O   ASP B 184      10.306  -9.113 -22.145  1.00 45.55           O  
ANISOU 2947  O   ASP B 184     6429   7086   3792   -204   1550   -987       O  
ATOM   2948  CB  ASP B 184       9.545  -6.983 -23.695  1.00 47.16           C  
ANISOU 2948  CB  ASP B 184     6999   7501   3418   -633   1311   -601       C  
ATOM   2949  CG  ASP B 184       8.445  -7.846 -24.296  1.00 54.55           C  
ANISOU 2949  CG  ASP B 184     8219   8359   4151   -690   1090   -708       C  
ATOM   2950  OD1 ASP B 184       7.536  -8.281 -23.557  1.00 55.72           O  
ANISOU 2950  OD1 ASP B 184     8304   8425   4444   -634    838   -731       O  
ATOM   2951  OD2 ASP B 184       8.495  -8.069 -25.526  1.00 61.97           O  
ANISOU 2951  OD2 ASP B 184     9419   9310   4816   -794   1150   -755       O  
ATOM   2952  N   LYS B 185       9.532  -8.274 -20.208  1.00 35.33           N  
ANISOU 2952  N   LYS B 185     4791   5689   2944    -87   1095   -713       N  
ATOM   2953  CA  LYS B 185       9.710  -9.492 -19.425  1.00 39.51           C  
ANISOU 2953  CA  LYS B 185     5208   6085   3717     98   1136   -873       C  
ATOM   2954  C   LYS B 185       8.360  -9.863 -18.833  1.00 35.50           C  
ANISOU 2954  C   LYS B 185     4763   5471   3256     96    828   -844       C  
ATOM   2955  O   LYS B 185       7.558  -8.986 -18.538  1.00 35.42           O  
ANISOU 2955  O   LYS B 185     4730   5482   3248     27    604   -671       O  
ATOM   2956  CB  LYS B 185      10.698  -9.249 -18.280  1.00 42.91           C  
ANISOU 2956  CB  LYS B 185     5311   6494   4499    244   1184   -801       C  
ATOM   2957  CG  LYS B 185      12.155  -9.279 -18.687  1.00 56.46           C  
ANISOU 2957  CG  LYS B 185     6862   8286   6303    296   1518   -864       C  
ATOM   2958  CD  LYS B 185      13.052  -8.972 -17.498  1.00 60.63           C  
ANISOU 2958  CD  LYS B 185     7045   8792   7199    405   1467   -752       C  
ATOM   2959  CE  LYS B 185      14.520  -9.047 -17.902  1.00 68.06           C  
ANISOU 2959  CE  LYS B 185     7741   9813   8304    463   1801   -800       C  
ATOM   2960  NZ  LYS B 185      15.320  -7.930 -17.314  1.00 70.27           N  
ANISOU 2960  NZ  LYS B 185     7746  10175   8777    389   1738   -601       N  
ATOM   2961  N   PHE B 186       8.107 -11.149 -18.619  1.00 37.04           N  
ANISOU 2961  N   PHE B 186     5020   5533   3523    174    831  -1006       N  
ATOM   2962  CA  PHE B 186       6.840 -11.536 -18.001  1.00 34.14           C  
ANISOU 2962  CA  PHE B 186     4678   5066   3228    147    564   -963       C  
ATOM   2963  C   PHE B 186       6.888 -11.376 -16.485  1.00 32.85           C  
ANISOU 2963  C   PHE B 186     4285   4836   3360    269    477   -849       C  
ATOM   2964  O   PHE B 186       7.686 -12.014 -15.808  1.00 31.62           O  
ANISOU 2964  O   PHE B 186     4026   4593   3396    409    571   -903       O  
ATOM   2965  CB  PHE B 186       6.436 -12.961 -18.382  1.00 38.18           C  
ANISOU 2965  CB  PHE B 186     5385   5438   3683    133    571  -1165       C  
ATOM   2966  CG  PHE B 186       4.973 -13.243 -18.170  1.00 39.76           C  
ANISOU 2966  CG  PHE B 186     5645   5579   3883     12    287  -1108       C  
ATOM   2967  CD1 PHE B 186       4.502 -13.648 -16.935  1.00 37.24           C  
ANISOU 2967  CD1 PHE B 186     5183   5149   3819     80    183  -1042       C  
ATOM   2968  CD2 PHE B 186       4.070 -13.106 -19.222  1.00 45.93           C  
ANISOU 2968  CD2 PHE B 186     6623   6421   4405   -191    119  -1106       C  
ATOM   2969  CE1 PHE B 186       3.149 -13.906 -16.739  1.00 38.48           C  
ANISOU 2969  CE1 PHE B 186     5349   5263   4009    -45    -39   -981       C  
ATOM   2970  CE2 PHE B 186       2.722 -13.362 -19.037  1.00 46.72           C  
ANISOU 2970  CE2 PHE B 186     6715   6475   4561   -311   -157  -1034       C  
ATOM   2971  CZ  PHE B 186       2.261 -13.766 -17.791  1.00 40.84           C  
ANISOU 2971  CZ  PHE B 186     5785   5625   4108   -235   -212   -977       C  
ATOM   2972  N   VAL B 187       6.032 -10.518 -15.951  1.00 24.47           N  
ANISOU 2972  N   VAL B 187     3157   3803   2336    215    294   -689       N  
ATOM   2973  CA  VAL B 187       6.052 -10.240 -14.524  1.00 23.23           C  
ANISOU 2973  CA  VAL B 187     2843   3592   2392    300    237   -594       C  
ATOM   2974  C   VAL B 187       4.729 -10.685 -13.905  1.00 26.99           C  
ANISOU 2974  C   VAL B 187     3332   3987   2936    263     93   -565       C  
ATOM   2975  O   VAL B 187       3.714 -10.779 -14.590  1.00 25.75           O  
ANISOU 2975  O   VAL B 187     3243   3846   2694    159    -14   -563       O  
ATOM   2976  CB  VAL B 187       6.301  -8.736 -14.241  1.00 28.50           C  
ANISOU 2976  CB  VAL B 187     3415   4337   3078    281    212   -449       C  
ATOM   2977  CG1 VAL B 187       7.692  -8.321 -14.706  1.00 28.21           C  
ANISOU 2977  CG1 VAL B 187     3322   4379   3019    292    368   -456       C  
ATOM   2978  CG2 VAL B 187       5.247  -7.891 -14.925  1.00 31.05           C  
ANISOU 2978  CG2 VAL B 187     3797   4707   3294    179     86   -353       C  
ATOM   2979  N   VAL B 188       4.745 -10.977 -12.614  1.00 25.71           N  
ANISOU 2979  N   VAL B 188     3103   3742   2924    327     83   -531       N  
ATOM   2980  CA  VAL B 188       3.553 -11.429 -11.914  1.00 25.26           C  
ANISOU 2980  CA  VAL B 188     3045   3613   2940    278      3   -495       C  
ATOM   2981  C   VAL B 188       3.557 -10.765 -10.551  1.00 23.10           C  
ANISOU 2981  C   VAL B 188     2702   3325   2750    317     17   -401       C  
ATOM   2982  O   VAL B 188       4.569 -10.194 -10.152  1.00 25.10           O  
ANISOU 2982  O   VAL B 188     2929   3600   3008    374     47   -377       O  
ATOM   2983  CB  VAL B 188       3.561 -12.958 -11.722  1.00 22.90           C  
ANISOU 2983  CB  VAL B 188     2836   3175   2691    282      8   -581       C  
ATOM   2984  CG1 VAL B 188       3.437 -13.682 -13.062  1.00 24.80           C  
ANISOU 2984  CG1 VAL B 188     3204   3396   2822    220      0   -715       C  
ATOM   2985  CG2 VAL B 188       4.828 -13.406 -10.981  1.00 27.27           C  
ANISOU 2985  CG2 VAL B 188     3377   3649   3334    410     67   -589       C  
ATOM   2986  N   GLY B 189       2.441 -10.829  -9.835  1.00 19.13           N  
ANISOU 2986  N   GLY B 189     2175   2786   2309    269      5   -353       N  
ATOM   2987  CA  GLY B 189       2.405 -10.276  -8.490  1.00 19.35           C  
ANISOU 2987  CA  GLY B 189     2197   2788   2366    288     60   -294       C  
ATOM   2988  C   GLY B 189       1.637  -8.964  -8.468  1.00 21.24           C  
ANISOU 2988  C   GLY B 189     2353   3072   2646    291     90   -248       C  
ATOM   2989  O   GLY B 189       1.380  -8.399  -9.529  1.00 21.35           O  
ANISOU 2989  O   GLY B 189     2305   3141   2666    289     28   -230       O  
ATOM   2990  N   TYR B 190       1.288  -8.482  -7.272  1.00 20.46           N  
ANISOU 2990  N   TYR B 190     2274   2932   2567    296    186   -229       N  
ATOM   2991  CA  TYR B 190       0.429  -7.290  -7.108  1.00 22.77           C  
ANISOU 2991  CA  TYR B 190     2482   3219   2952    329    261   -206       C  
ATOM   2992  C   TYR B 190      -0.817  -7.408  -8.001  1.00 26.08           C  
ANISOU 2992  C   TYR B 190     2723   3669   3517    313    209   -163       C  
ATOM   2993  O   TYR B 190      -1.197  -6.465  -8.712  1.00 22.84           O  
ANISOU 2993  O   TYR B 190     2212   3271   3195    357    145   -113       O  
ATOM   2994  CB  TYR B 190       1.228  -6.008  -7.387  1.00 16.97           C  
ANISOU 2994  CB  TYR B 190     1780   2483   2185    378    223   -199       C  
ATOM   2995  CG  TYR B 190       0.594  -4.728  -6.892  1.00 22.70           C  
ANISOU 2995  CG  TYR B 190     2485   3134   3008    435    322   -199       C  
ATOM   2996  CD1 TYR B 190       0.481  -4.452  -5.527  1.00 20.68           C  
ANISOU 2996  CD1 TYR B 190     2346   2801   2709    434    480   -261       C  
ATOM   2997  CD2 TYR B 190       0.125  -3.787  -7.787  1.00 23.20           C  
ANISOU 2997  CD2 TYR B 190     2439   3181   3195    488    258   -137       C  
ATOM   2998  CE1 TYR B 190      -0.098  -3.270  -5.082  1.00 20.76           C  
ANISOU 2998  CE1 TYR B 190     2361   2710   2819    503    614   -299       C  
ATOM   2999  CE2 TYR B 190      -0.450  -2.599  -7.355  1.00 20.49           C  
ANISOU 2999  CE2 TYR B 190     2071   2722   2992    573    354   -141       C  
ATOM   3000  CZ  TYR B 190      -0.556  -2.348  -6.001  1.00 21.24           C  
ANISOU 3000  CZ  TYR B 190     2279   2729   3060    589    553   -240       C  
ATOM   3001  OH  TYR B 190      -1.126  -1.164  -5.580  1.00 22.23           O  
ANISOU 3001  OH  TYR B 190     2403   2708   3335    690    689   -280       O  
ATOM   3002  N   ALA B 191      -1.431  -8.599  -7.958  1.00 22.12           N  
ANISOU 3002  N   ALA B 191     2189   3166   3050    232    205   -164       N  
ATOM   3003  CA  ALA B 191      -2.660  -8.950  -8.701  1.00 22.07           C  
ANISOU 3003  CA  ALA B 191     2002   3188   3196    166    117   -115       C  
ATOM   3004  C   ALA B 191      -2.480  -9.374 -10.167  1.00 22.19           C  
ANISOU 3004  C   ALA B 191     2048   3250   3134    102   -103   -118       C  
ATOM   3005  O   ALA B 191      -3.430  -9.868 -10.776  1.00 23.13           O  
ANISOU 3005  O   ALA B 191     2058   3385   3346      1   -229    -82       O  
ATOM   3006  CB  ALA B 191      -3.774  -7.862  -8.565  1.00 24.68           C  
ANISOU 3006  CB  ALA B 191     2104   3516   3756    234    179    -46       C  
ATOM   3007  N   LEU B 192      -1.279  -9.193 -10.715  1.00 23.16           N  
ANISOU 3007  N   LEU B 192     2322   3395   3083    140   -140   -164       N  
ATOM   3008  CA  LEU B 192      -0.962  -9.684 -12.060  1.00 26.05           C  
ANISOU 3008  CA  LEU B 192     2787   3802   3309     68   -282   -204       C  
ATOM   3009  C   LEU B 192      -0.706 -11.185 -11.986  1.00 26.30           C  
ANISOU 3009  C   LEU B 192     2940   3765   3288      7   -265   -308       C  
ATOM   3010  O   LEU B 192       0.018 -11.651 -11.093  1.00 23.77           O  
ANISOU 3010  O   LEU B 192     2685   3379   2966     67   -152   -346       O  
ATOM   3011  CB  LEU B 192       0.279  -8.989 -12.629  1.00 23.91           C  
ANISOU 3011  CB  LEU B 192     2621   3581   2882    125   -257   -222       C  
ATOM   3012  CG  LEU B 192       0.120  -7.556 -13.134  1.00 33.81           C  
ANISOU 3012  CG  LEU B 192     3819   4880   4148    148   -326   -109       C  
ATOM   3013  CD1 LEU B 192       0.161  -6.560 -11.986  1.00 31.13           C  
ANISOU 3013  CD1 LEU B 192     3402   4484   3944    252   -215    -68       C  
ATOM   3014  CD2 LEU B 192       1.176  -7.220 -14.185  1.00 40.18           C  
ANISOU 3014  CD2 LEU B 192     4764   5755   4747    117   -333   -120       C  
ATOM   3015  N   ASP B 193      -1.256 -11.934 -12.934  1.00 26.67           N  
ANISOU 3015  N   ASP B 193     3039   3805   3290   -120   -404   -347       N  
ATOM   3016  CA  ASP B 193      -1.239 -13.389 -12.829  1.00 22.36           C  
ANISOU 3016  CA  ASP B 193     2616   3143   2738   -195   -401   -446       C  
ATOM   3017  C   ASP B 193      -0.471 -14.112 -13.933  1.00 25.69           C  
ANISOU 3017  C   ASP B 193     3265   3525   2969   -222   -423   -601       C  
ATOM   3018  O   ASP B 193      -0.162 -13.554 -14.990  1.00 25.56           O  
ANISOU 3018  O   ASP B 193     3325   3602   2785   -239   -466   -627       O  
ATOM   3019  CB  ASP B 193      -2.667 -13.941 -12.824  1.00 24.05           C  
ANISOU 3019  CB  ASP B 193     2719   3327   3092   -365   -529   -390       C  
ATOM   3020  CG  ASP B 193      -3.308 -13.903 -14.198  1.00 30.63           C  
ANISOU 3020  CG  ASP B 193     3578   4219   3842   -515   -768   -392       C  
ATOM   3021  OD1 ASP B 193      -3.293 -12.829 -14.826  1.00 29.75           O  
ANISOU 3021  OD1 ASP B 193     3417   4218   3667   -478   -849   -320       O  
ATOM   3022  OD2 ASP B 193      -3.814 -14.949 -14.655  1.00 29.45           O  
ANISOU 3022  OD2 ASP B 193     3522   3989   3677   -689   -899   -456       O  
ATOM   3023  N   TYR B 194      -0.195 -15.384 -13.669  1.00 24.08           N  
ANISOU 3023  N   TYR B 194     3192   3163   2793   -233   -379   -705       N  
ATOM   3024  CA  TYR B 194       0.192 -16.332 -14.708  1.00 27.17           C  
ANISOU 3024  CA  TYR B 194     3823   3459   3042   -290   -394   -890       C  
ATOM   3025  C   TYR B 194      -0.773 -17.480 -14.514  1.00 28.75           C  
ANISOU 3025  C   TYR B 194     4079   3502   3343   -458   -512   -909       C  
ATOM   3026  O   TYR B 194      -0.709 -18.188 -13.506  1.00 29.28           O  
ANISOU 3026  O   TYR B 194     4137   3424   3562   -423   -449   -878       O  
ATOM   3027  CB  TYR B 194       1.633 -16.797 -14.507  1.00 29.27           C  
ANISOU 3027  CB  TYR B 194     4183   3626   3312   -100   -200  -1005       C  
ATOM   3028  CG  TYR B 194       2.059 -17.891 -15.469  1.00 30.13           C  
ANISOU 3028  CG  TYR B 194     4551   3584   3313   -122   -148  -1234       C  
ATOM   3029  CD1 TYR B 194       2.248 -17.618 -16.812  1.00 32.36           C  
ANISOU 3029  CD1 TYR B 194     4996   3959   3341   -192   -124  -1362       C  
ATOM   3030  CD2 TYR B 194       2.261 -19.194 -15.029  1.00 30.49           C  
ANISOU 3030  CD2 TYR B 194     4712   3373   3500    -80   -114  -1325       C  
ATOM   3031  CE1 TYR B 194       2.634 -18.606 -17.696  1.00 41.41           C  
ANISOU 3031  CE1 TYR B 194     6425   4954   4356   -217    -32  -1610       C  
ATOM   3032  CE2 TYR B 194       2.654 -20.187 -15.902  1.00 35.50           C  
ANISOU 3032  CE2 TYR B 194     5607   3827   4055    -81    -38  -1565       C  
ATOM   3033  CZ  TYR B 194       2.837 -19.890 -17.234  1.00 41.52           C  
ANISOU 3033  CZ  TYR B 194     6539   4692   4544   -149     19  -1725       C  
ATOM   3034  OH  TYR B 194       3.224 -20.882 -18.112  1.00 46.25           O  
ANISOU 3034  OH  TYR B 194     7443   5098   5032   -156    137  -2003       O  
ATOM   3035  N   ASN B 195      -1.699 -17.628 -15.457  1.00 29.57           N  
ANISOU 3035  N   ASN B 195     4242   3634   3360   -669   -711   -934       N  
ATOM   3036  CA AASN B 195      -2.763 -18.626 -15.362  0.59 31.58           C  
ANISOU 3036  CA AASN B 195     4518   3754   3729   -888   -868   -931       C  
ATOM   3037  CA BASN B 195      -2.747 -18.642 -15.356  0.41 31.58           C  
ANISOU 3037  CA BASN B 195     4521   3751   3729   -887   -865   -933       C  
ATOM   3038  C   ASN B 195      -3.486 -18.620 -14.011  1.00 30.68           C  
ANISOU 3038  C   ASN B 195     4147   3628   3881   -902   -824   -747       C  
ATOM   3039  O   ASN B 195      -3.729 -19.668 -13.408  1.00 31.70           O  
ANISOU 3039  O   ASN B 195     4340   3576   4130   -990   -807   -751       O  
ATOM   3040  CB AASN B 195      -2.230 -20.014 -15.716  0.59 38.31           C  
ANISOU 3040  CB AASN B 195     5691   4351   4513   -923   -829  -1149       C  
ATOM   3041  CB BASN B 195      -2.181 -20.038 -15.617  0.41 37.61           C  
ANISOU 3041  CB BASN B 195     5596   4254   4439   -908   -813  -1145       C  
ATOM   3042  CG AASN B 195      -1.780 -20.104 -17.162  0.59 42.10           C  
ANISOU 3042  CG AASN B 195     6462   4839   4696   -975   -859  -1361       C  
ATOM   3043  CG BASN B 195      -3.266 -21.076 -15.779  0.41 42.66           C  
ANISOU 3043  CG BASN B 195     6319   4733   5157  -1191  -1014  -1167       C  
ATOM   3044  OD1AASN B 195      -2.300 -19.400 -18.027  0.59 45.33           O  
ANISOU 3044  OD1AASN B 195     6865   5421   4935  -1111  -1031  -1318       O  
ATOM   3045  OD1BASN B 195      -4.305 -20.806 -16.378  0.41 46.02           O  
ANISOU 3045  OD1BASN B 195     6662   5266   5557  -1415  -1252  -1102       O  
ATOM   3046  ND2AASN B 195      -0.812 -20.971 -17.432  0.59 45.95           N  
ANISOU 3046  ND2AASN B 195     7213   5127   5118   -866   -685  -1586       N  
ATOM   3047  ND2BASN B 195      -3.049 -22.258 -15.213  0.41 45.58           N  
ANISOU 3047  ND2BASN B 195     6837   4833   5650  -1194   -946  -1232       N  
ATOM   3048  N   GLU B 196      -3.815 -17.413 -13.545  1.00 29.11           N  
ANISOU 3048  N   GLU B 196     3684   3611   3766   -819   -785   -589       N  
ATOM   3049  CA  GLU B 196      -4.563 -17.174 -12.297  1.00 28.66           C  
ANISOU 3049  CA  GLU B 196     3375   3579   3934   -827   -685   -426       C  
ATOM   3050  C   GLU B 196      -3.728 -17.251 -11.024  1.00 34.27           C  
ANISOU 3050  C   GLU B 196     4145   4223   4653   -666   -457   -405       C  
ATOM   3051  O   GLU B 196      -4.181 -16.832  -9.962  1.00 32.68           O  
ANISOU 3051  O   GLU B 196     3786   4067   4563   -651   -325   -286       O  
ATOM   3052  CB  GLU B 196      -5.822 -18.042 -12.184  1.00 31.21           C  
ANISOU 3052  CB  GLU B 196     3596   3824   4436  -1084   -799   -365       C  
ATOM   3053  CG  GLU B 196      -6.874 -17.750 -13.246  1.00 39.08           C  
ANISOU 3053  CG  GLU B 196     4437   4923   5488  -1266  -1075   -318       C  
ATOM   3054  CD  GLU B 196      -7.302 -16.289 -13.258  1.00 39.74           C  
ANISOU 3054  CD  GLU B 196     4219   5202   5679  -1143  -1081   -178       C  
ATOM   3055  OE1 GLU B 196      -7.288 -15.652 -12.185  1.00 36.66           O  
ANISOU 3055  OE1 GLU B 196     3661   4855   5413   -990   -843   -100       O  
ATOM   3056  OE2 GLU B 196      -7.655 -15.777 -14.339  1.00 42.92           O  
ANISOU 3056  OE2 GLU B 196     4580   5697   6033  -1206  -1333   -146       O  
ATOM   3057  N   TYR B 197      -2.499 -17.752 -11.130  1.00 26.29           N  
ANISOU 3057  N   TYR B 197     3361   3105   3525   -545   -409   -519       N  
ATOM   3058  CA  TYR B 197      -1.611 -17.787  -9.982  1.00 25.03           C  
ANISOU 3058  CA  TYR B 197     3254   2885   3374   -395   -264   -473       C  
ATOM   3059  C   TYR B 197      -0.806 -16.497  -9.837  1.00 23.42           C  
ANISOU 3059  C   TYR B 197     2971   2834   3094   -214   -184   -454       C  
ATOM   3060  O   TYR B 197      -0.692 -15.714 -10.791  1.00 22.73           O  
ANISOU 3060  O   TYR B 197     2837   2870   2930   -181   -227   -498       O  
ATOM   3061  CB  TYR B 197      -0.680 -19.000 -10.049  1.00 25.98           C  
ANISOU 3061  CB  TYR B 197     3603   2781   3486   -335   -269   -574       C  
ATOM   3062  CG  TYR B 197      -1.396 -20.297  -9.777  1.00 32.75           C  
ANISOU 3062  CG  TYR B 197     4570   3429   4444   -517   -330   -555       C  
ATOM   3063  CD1 TYR B 197      -1.512 -20.785  -8.484  1.00 32.21           C  
ANISOU 3063  CD1 TYR B 197     4534   3249   4453   -556   -274   -408       C  
ATOM   3064  CD2 TYR B 197      -1.979 -21.025 -10.809  1.00 37.69           C  
ANISOU 3064  CD2 TYR B 197     5296   3959   5066   -683   -455   -674       C  
ATOM   3065  CE1 TYR B 197      -2.176 -21.968  -8.224  1.00 39.84           C  
ANISOU 3065  CE1 TYR B 197     5612   4008   5518   -751   -326   -365       C  
ATOM   3066  CE2 TYR B 197      -2.645 -22.218 -10.560  1.00 42.97           C  
ANISOU 3066  CE2 TYR B 197     6074   4409   5844   -882   -525   -652       C  
ATOM   3067  CZ  TYR B 197      -2.743 -22.680  -9.264  1.00 45.07           C  
ANISOU 3067  CZ  TYR B 197     6349   4562   6212   -913   -452   -489       C  
ATOM   3068  OH  TYR B 197      -3.401 -23.855  -9.000  1.00 51.65           O  
ANISOU 3068  OH  TYR B 197     7300   5165   7159  -1135   -516   -442       O  
ATOM   3069  N   PHE B 198      -0.263 -16.302  -8.637  1.00 22.13           N  
ANISOU 3069  N   PHE B 198     2821   2650   2937   -127    -89   -376       N  
ATOM   3070  CA  PHE B 198       0.589 -15.167  -8.270  1.00 20.55           C  
ANISOU 3070  CA  PHE B 198     2576   2558   2675     15    -30   -352       C  
ATOM   3071  C   PHE B 198      -0.159 -13.868  -8.015  1.00 23.18           C  
ANISOU 3071  C   PHE B 198     2757   3031   3019      3     30   -289       C  
ATOM   3072  O   PHE B 198       0.480 -12.836  -7.818  1.00 24.02           O  
ANISOU 3072  O   PHE B 198     2843   3209   3075    100     65   -281       O  
ATOM   3073  CB  PHE B 198       1.692 -14.898  -9.311  1.00 20.09           C  
ANISOU 3073  CB  PHE B 198     2539   2541   2551    130    -54   -453       C  
ATOM   3074  CG  PHE B 198       2.588 -16.069  -9.580  1.00 24.91           C  
ANISOU 3074  CG  PHE B 198     3275   2997   3191    199    -63   -542       C  
ATOM   3075  CD1 PHE B 198       3.602 -16.405  -8.698  1.00 21.28           C  
ANISOU 3075  CD1 PHE B 198     2846   2445   2796    313    -59   -491       C  
ATOM   3076  CD2 PHE B 198       2.443 -16.809 -10.745  1.00 27.29           C  
ANISOU 3076  CD2 PHE B 198     3674   3233   3463    155    -86   -680       C  
ATOM   3077  CE1 PHE B 198       4.437 -17.485  -8.957  1.00 25.95           C  
ANISOU 3077  CE1 PHE B 198     3516   2861   3482    416    -64   -566       C  
ATOM   3078  CE2 PHE B 198       3.275 -17.889 -11.013  1.00 34.75           C  
ANISOU 3078  CE2 PHE B 198     4743   3997   4463    248    -54   -793       C  
ATOM   3079  CZ  PHE B 198       4.280 -18.222 -10.116  1.00 31.39           C  
ANISOU 3079  CZ  PHE B 198     4300   3465   4163    399    -35   -731       C  
ATOM   3080  N   ARG B 199      -1.490 -13.886  -8.051  1.00 20.89           N  
ANISOU 3080  N   ARG B 199     2343   2766   2830   -110     40   -246       N  
ATOM   3081  CA  ARG B 199      -2.212 -12.658  -7.727  1.00 21.56           C  
ANISOU 3081  CA  ARG B 199     2256   2949   2988    -80    129   -189       C  
ATOM   3082  C   ARG B 199      -2.048 -12.364  -6.251  1.00 27.26           C  
ANISOU 3082  C   ARG B 199     3050   3644   3662    -55    309   -154       C  
ATOM   3083  O   ARG B 199      -2.104 -11.201  -5.833  1.00 25.31           O  
ANISOU 3083  O   ARG B 199     2756   3444   3417     21    412   -152       O  
ATOM   3084  CB  ARG B 199      -3.691 -12.737  -8.097  1.00 22.54           C  
ANISOU 3084  CB  ARG B 199     2163   3107   3294   -193    100   -135       C  
ATOM   3085  CG  ARG B 199      -3.961 -12.898  -9.615  1.00 23.17           C  
ANISOU 3085  CG  ARG B 199     2198   3224   3382   -257   -135   -157       C  
ATOM   3086  CD  ARG B 199      -5.399 -12.521  -9.956  1.00 25.11           C  
ANISOU 3086  CD  ARG B 199     2156   3531   3855   -338   -212    -61       C  
ATOM   3087  NE  ARG B 199      -5.880 -13.028 -11.245  1.00 26.64           N  
ANISOU 3087  NE  ARG B 199     2335   3740   4047   -486   -488    -61       N  
ATOM   3088  CZ  ARG B 199      -5.714 -12.397 -12.408  1.00 28.24           C  
ANISOU 3088  CZ  ARG B 199     2565   4011   4155   -468   -685    -52       C  
ATOM   3089  NH1 ARG B 199      -5.070 -11.242 -12.445  1.00 25.38           N  
ANISOU 3089  NH1 ARG B 199     2221   3696   3725   -302   -625    -34       N  
ATOM   3090  NH2 ARG B 199      -6.191 -12.923 -13.532  1.00 29.82           N  
ANISOU 3090  NH2 ARG B 199     2802   4220   4306   -642   -954    -55       N  
ATOM   3091  N   ASP B 200      -1.824 -13.429  -5.481  1.00 22.69           N  
ANISOU 3091  N   ASP B 200     2625   2969   3025   -130    334   -126       N  
ATOM   3092  CA  ASP B 200      -1.678 -13.358  -4.024  1.00 23.98           C  
ANISOU 3092  CA  ASP B 200     2933   3099   3079   -159    481    -73       C  
ATOM   3093  C   ASP B 200      -0.228 -13.128  -3.620  1.00 27.14           C  
ANISOU 3093  C   ASP B 200     3511   3472   3328    -66    388    -81       C  
ATOM   3094  O   ASP B 200       0.311 -13.802  -2.741  1.00 28.86           O  
ANISOU 3094  O   ASP B 200     3918   3605   3444   -110    352    -15       O  
ATOM   3095  CB  ASP B 200      -2.183 -14.648  -3.370  1.00 25.16           C  
ANISOU 3095  CB  ASP B 200     3183   3146   3231   -320    523      7       C  
ATOM   3096  CG  ASP B 200      -1.503 -15.893  -3.916  1.00 26.85           C  
ANISOU 3096  CG  ASP B 200     3515   3225   3460   -326    328      3       C  
ATOM   3097  OD1 ASP B 200      -1.106 -15.895  -5.102  1.00 24.46           O  
ANISOU 3097  OD1 ASP B 200     3150   2934   3211   -243    199    -86       O  
ATOM   3098  OD2 ASP B 200      -1.387 -16.882  -3.154  1.00 29.55           O  
ANISOU 3098  OD2 ASP B 200     4034   3433   3759   -418    317     91       O  
ATOM   3099  N   LEU B 201       0.407 -12.185  -4.295  1.00 27.58           N  
ANISOU 3099  N   LEU B 201     3495   3597   3386     48    326   -139       N  
ATOM   3100  CA  LEU B 201       1.802 -11.836  -4.045  1.00 27.54           C  
ANISOU 3100  CA  LEU B 201     3588   3586   3288    124    225   -140       C  
ATOM   3101  C   LEU B 201       1.853 -10.315  -4.051  1.00 26.34           C  
ANISOU 3101  C   LEU B 201     3387   3510   3112    172    283   -178       C  
ATOM   3102  O   LEU B 201       1.286  -9.693  -4.943  1.00 29.62           O  
ANISOU 3102  O   LEU B 201     3654   3980   3621    209    308   -208       O  
ATOM   3103  CB  LEU B 201       2.681 -12.440  -5.136  1.00 27.16           C  
ANISOU 3103  CB  LEU B 201     3489   3522   3308    203     92   -178       C  
ATOM   3104  CG  LEU B 201       4.141 -12.021  -5.267  1.00 27.30           C  
ANISOU 3104  CG  LEU B 201     3495   3562   3314    297      0   -184       C  
ATOM   3105  CD1 LEU B 201       4.902 -12.429  -4.037  1.00 29.43           C  
ANISOU 3105  CD1 LEU B 201     3895   3752   3536    284    -95    -95       C  
ATOM   3106  CD2 LEU B 201       4.736 -12.681  -6.510  1.00 27.04           C  
ANISOU 3106  CD2 LEU B 201     3389   3518   3368    376    -35   -254       C  
ATOM   3107  N   ASN B 202       2.482  -9.710  -3.044  1.00 22.40           N  
ANISOU 3107  N   ASN B 202     3032   2992   2485    156    282   -168       N  
ATOM   3108  CA  ASN B 202       2.437  -8.247  -2.926  1.00 23.34           C  
ANISOU 3108  CA  ASN B 202     3151   3135   2584    183    353   -220       C  
ATOM   3109  C   ASN B 202       3.464  -7.532  -3.816  1.00 22.55           C  
ANISOU 3109  C   ASN B 202     2964   3074   2529    245    220   -228       C  
ATOM   3110  O   ASN B 202       3.237  -6.399  -4.245  1.00 26.65           O  
ANISOU 3110  O   ASN B 202     3426   3602   3098    279    263   -256       O  
ATOM   3111  CB  ASN B 202       2.520  -7.791  -1.453  1.00 28.22           C  
ANISOU 3111  CB  ASN B 202     4010   3699   3011    101    433   -235       C  
ATOM   3112  CG  ASN B 202       3.876  -8.109  -0.794  1.00 34.59           C  
ANISOU 3112  CG  ASN B 202     4983   4482   3677     43    216   -175       C  
ATOM   3113  OD1 ASN B 202       4.602  -9.002  -1.233  1.00 41.12           O  
ANISOU 3113  OD1 ASN B 202     5732   5313   4580     77     50   -108       O  
ATOM   3114  ND2 ASN B 202       4.207  -7.373   0.277  1.00 33.70           N  
ANISOU 3114  ND2 ASN B 202     5103   4332   3371    -47    211   -202       N  
ATOM   3115  N   HIS B 203       4.577  -8.210  -4.105  1.00 20.73           N  
ANISOU 3115  N   HIS B 203     2713   2857   2306    260     74   -195       N  
ATOM   3116  CA  HIS B 203       5.642  -7.635  -4.931  1.00 20.56           C  
ANISOU 3116  CA  HIS B 203     2586   2888   2338    299    -11   -194       C  
ATOM   3117  C   HIS B 203       5.386  -7.976  -6.392  1.00 25.36           C  
ANISOU 3117  C   HIS B 203     3057   3553   3024    352     19   -220       C  
ATOM   3118  O   HIS B 203       4.747  -8.988  -6.692  1.00 26.59           O  
ANISOU 3118  O   HIS B 203     3208   3691   3206    358     41   -239       O  
ATOM   3119  CB  HIS B 203       7.002  -8.248  -4.532  1.00 19.42           C  
ANISOU 3119  CB  HIS B 203     2438   2729   2212    305   -161   -142       C  
ATOM   3120  CG  HIS B 203       7.317  -8.135  -3.070  1.00 18.53           C  
ANISOU 3120  CG  HIS B 203     2503   2558   1979    218   -262    -92       C  
ATOM   3121  ND1 HIS B 203       7.437  -6.927  -2.429  1.00 23.88           N  
ANISOU 3121  ND1 HIS B 203     3297   3224   2551    134   -276   -112       N  
ATOM   3122  CD2 HIS B 203       7.526  -9.093  -2.136  1.00 19.68           C  
ANISOU 3122  CD2 HIS B 203     2772   2637   2069    185   -369    -17       C  
ATOM   3123  CE1 HIS B 203       7.713  -7.139  -1.148  1.00 24.16           C  
ANISOU 3123  CE1 HIS B 203     3538   3205   2436     36   -388    -66       C  
ATOM   3124  NE2 HIS B 203       7.782  -8.439  -0.952  1.00 22.34           N  
ANISOU 3124  NE2 HIS B 203     3310   2947   2233     65   -457     10       N  
ATOM   3125  N   VAL B 204       5.897  -7.162  -7.314  1.00 20.30           N  
ANISOU 3125  N   VAL B 204     2337   2976   2401    361     13   -219       N  
ATOM   3126  CA  VAL B 204       5.949  -7.591  -8.710  1.00 21.67           C  
ANISOU 3126  CA  VAL B 204     2437   3212   2584    384     35   -247       C  
ATOM   3127  C   VAL B 204       7.265  -8.343  -8.896  1.00 24.39           C  
ANISOU 3127  C   VAL B 204     2724   3568   2975    431     31   -269       C  
ATOM   3128  O   VAL B 204       8.318  -7.857  -8.494  1.00 24.78           O  
ANISOU 3128  O   VAL B 204     2714   3634   3069    427     -8   -227       O  
ATOM   3129  CB  VAL B 204       5.844  -6.414  -9.690  1.00 22.06           C  
ANISOU 3129  CB  VAL B 204     2454   3322   2604    353     45   -213       C  
ATOM   3130  CG1 VAL B 204       6.105  -6.887 -11.127  1.00 23.10           C  
ANISOU 3130  CG1 VAL B 204     2571   3534   2672    343     77   -246       C  
ATOM   3131  CG2 VAL B 204       4.459  -5.770  -9.574  1.00 22.94           C  
ANISOU 3131  CG2 VAL B 204     2577   3395   2744    348     39   -182       C  
ATOM   3132  N   CYS B 205       7.194  -9.536  -9.485  1.00 20.55           N  
ANISOU 3132  N   CYS B 205     2246   3057   2506    475     66   -336       N  
ATOM   3133  CA  CYS B 205       8.349 -10.417  -9.552  1.00 22.24           C  
ANISOU 3133  CA  CYS B 205     2392   3234   2825    564     87   -369       C  
ATOM   3134  C   CYS B 205       8.412 -11.018 -10.935  1.00 28.29           C  
ANISOU 3134  C   CYS B 205     3172   4023   3555    593    211   -487       C  
ATOM   3135  O   CYS B 205       7.416 -11.024 -11.669  1.00 23.31           O  
ANISOU 3135  O   CYS B 205     2641   3415   2800    521    220   -530       O  
ATOM   3136  CB  CYS B 205       8.235 -11.526  -8.511  1.00 26.75           C  
ANISOU 3136  CB  CYS B 205     3025   3666   3472    605      0   -343       C  
ATOM   3137  N   VAL B 206       9.588 -11.527 -11.274  1.00 29.99           N  
ANISOU 3137  N   VAL B 206     3284   4225   3885    692    306   -539       N  
ATOM   3138  CA  VAL B 206       9.785 -12.229 -12.525  1.00 35.05           C  
ANISOU 3138  CA  VAL B 206     3975   4861   4482    733    479   -692       C  
ATOM   3139  C   VAL B 206       9.640 -13.713 -12.244  1.00 36.74           C  
ANISOU 3139  C   VAL B 206     4267   4881   4811    831    461   -777       C  
ATOM   3140  O   VAL B 206      10.254 -14.262 -11.318  1.00 36.90           O  
ANISOU 3140  O   VAL B 206     4194   4786   5039    941    385   -715       O  
ATOM   3141  CB  VAL B 206      11.161 -11.928 -13.145  1.00 38.46           C  
ANISOU 3141  CB  VAL B 206     4232   5381   5000    798    668   -723       C  
ATOM   3142  CG1 VAL B 206      11.420 -12.838 -14.339  1.00 40.61           C  
ANISOU 3142  CG1 VAL B 206     4591   5616   5225    862    905   -923       C  
ATOM   3143  CG2 VAL B 206      11.232 -10.466 -13.564  1.00 40.89           C  
ANISOU 3143  CG2 VAL B 206     4505   5860   5170    661    688   -630       C  
ATOM   3144  N   ILE B 207       8.800 -14.351 -13.047  1.00 36.81           N  
ANISOU 3144  N   ILE B 207     4465   4837   4682    770    498   -904       N  
ATOM   3145  CA  ILE B 207       8.502 -15.763 -12.901  1.00 33.94           C  
ANISOU 3145  CA  ILE B 207     4229   4257   4410    823    476   -998       C  
ATOM   3146  C   ILE B 207       9.683 -16.600 -13.386  1.00 40.04           C  
ANISOU 3146  C   ILE B 207     4955   4909   5349   1010    667  -1145       C  
ATOM   3147  O   ILE B 207      10.361 -16.227 -14.344  1.00 44.93           O  
ANISOU 3147  O   ILE B 207     5529   5639   5902   1037    880  -1248       O  
ATOM   3148  CB  ILE B 207       7.184 -16.084 -13.658  1.00 52.09           C  
ANISOU 3148  CB  ILE B 207     6747   6540   6504    654    424  -1088       C  
ATOM   3149  CG1 ILE B 207       6.684 -17.491 -13.354  1.00 53.03           C  
ANISOU 3149  CG1 ILE B 207     7015   6411   6723    654    357  -1157       C  
ATOM   3150  CG2 ILE B 207       7.332 -15.835 -15.168  1.00 56.32           C  
ANISOU 3150  CG2 ILE B 207     7401   7183   6815    592    574  -1242       C  
ATOM   3151  CD1 ILE B 207       5.309 -17.754 -13.933  1.00 49.87           C  
ANISOU 3151  CD1 ILE B 207     6790   6002   6156    443    246  -1207       C  
ATOM   3152  N   SER B 208       9.952 -17.714 -12.707  1.00 37.28           N  
ANISOU 3152  N   SER B 208     4609   4323   5233   1142    609  -1143       N  
ATOM   3153  CA  SER B 208      11.049 -18.588 -13.079  1.00 46.72           C  
ANISOU 3153  CA  SER B 208     5732   5353   6669   1365    792  -1280       C  
ATOM   3154  C   SER B 208      10.573 -19.633 -14.095  1.00 47.59           C  
ANISOU 3154  C   SER B 208     6124   5280   6676   1352    935  -1541       C  
ATOM   3155  O   SER B 208       9.377 -19.729 -14.382  1.00 42.85           O  
ANISOU 3155  O   SER B 208     5758   4683   5841   1149    828  -1578       O  
ATOM   3156  CB  SER B 208      11.622 -19.293 -11.851  1.00 48.70           C  
ANISOU 3156  CB  SER B 208     5853   5394   7255   1531    621  -1127       C  
ATOM   3157  OG  SER B 208      10.717 -20.257 -11.346  1.00 48.06           O  
ANISOU 3157  OG  SER B 208     6004   5086   7172   1469    460  -1105       O  
ATOM   3158  N   GLU B 209      11.507 -20.406 -14.639  1.00 53.64           N  
ANISOU 3158  N   GLU B 209     6867   5884   7631   1559   1173  -1721       N  
ATOM   3159  CA  GLU B 209      11.153 -21.444 -15.599  1.00 56.01           C  
ANISOU 3159  CA  GLU B 209     7491   6004   7786   1533   1285  -1948       C  
ATOM   3160  C   GLU B 209      10.337 -22.543 -14.931  1.00 55.98           C  
ANISOU 3160  C   GLU B 209     7682   5673   7916   1506   1084  -1958       C  
ATOM   3161  O   GLU B 209       9.330 -23.000 -15.480  1.00 52.29           O  
ANISOU 3161  O   GLU B 209     7520   5110   7238   1317   1040  -2109       O  
ATOM   3162  CB  GLU B 209      12.401 -22.018 -16.275  1.00 67.05           C  
ANISOU 3162  CB  GLU B 209     8821   7356   9299   1752   1523  -2048       C  
ATOM   3163  CG  GLU B 209      13.089 -21.038 -17.217  1.00 72.10           C  
ANISOU 3163  CG  GLU B 209     9338   8306   9749   1718   1759  -2080       C  
ATOM   3164  CD  GLU B 209      12.144 -20.492 -18.272  1.00 76.41           C  
ANISOU 3164  CD  GLU B 209    10174   9019   9842   1449   1792  -2203       C  
ATOM   3165  OE1 GLU B 209      12.259 -19.298 -18.620  1.00 76.72           O  
ANISOU 3165  OE1 GLU B 209    10119   9333   9699   1331   1855  -2116       O  
ATOM   3166  OE2 GLU B 209      11.283 -21.259 -18.754  1.00 79.78           O  
ANISOU 3166  OE2 GLU B 209    10926   9292  10095   1337   1724  -2368       O  
ATOM   3167  N   THR B 210      10.770 -22.956 -13.743  1.00 56.40           N  
ANISOU 3167  N   THR B 210     7566   5555   8307   1665    929  -1770       N  
ATOM   3168  CA  THR B 210      10.045 -23.952 -12.956  1.00 59.63           C  
ANISOU 3168  CA  THR B 210     8156   5662   8840   1615    699  -1693       C  
ATOM   3169  C   THR B 210       8.641 -23.457 -12.571  1.00 52.31           C  
ANISOU 3169  C   THR B 210     7347   4900   7627   1293    478  -1548       C  
ATOM   3170  O   THR B 210       7.695 -24.244 -12.475  1.00 51.79           O  
ANISOU 3170  O   THR B 210     7514   4640   7522   1135    358  -1566       O  
ATOM   3171  CB  THR B 210      10.848 -24.364 -11.701  1.00 65.37           C  
ANISOU 3171  CB  THR B 210     8683   6211   9943   1825    531  -1447       C  
ATOM   3172  OG1 THR B 210       9.966 -24.507 -10.580  1.00 62.12           O  
ANISOU 3172  OG1 THR B 210     8379   5745   9478   1645    237  -1205       O  
ATOM   3173  CG2 THR B 210      11.899 -23.309 -11.375  1.00 68.90           C  
ANISOU 3173  CG2 THR B 210     8766   6938  10477   1940    553  -1291       C  
ATOM   3174  N   GLY B 211       8.508 -22.150 -12.364  1.00 43.44           N  
ANISOU 3174  N   GLY B 211     6050   4119   6335   1195    437  -1406       N  
ATOM   3175  CA  GLY B 211       7.208 -21.545 -12.117  1.00 42.78           C  
ANISOU 3175  CA  GLY B 211     6027   4209   6016    926    283  -1291       C  
ATOM   3176  C   GLY B 211       6.333 -21.580 -13.365  1.00 43.24           C  
ANISOU 3176  C   GLY B 211     6287   4322   5821    735    329  -1486       C  
ATOM   3177  O   GLY B 211       5.125 -21.835 -13.285  1.00 38.40           O  
ANISOU 3177  O   GLY B 211     5793   3677   5119    516    180  -1449       O  
ATOM   3178  N   LYS B 212       6.941 -21.341 -14.527  1.00 44.41           N  
ANISOU 3178  N   LYS B 212     6474   4551   5846    797    531  -1687       N  
ATOM   3179  CA  LYS B 212       6.199 -21.380 -15.782  1.00 46.87           C  
ANISOU 3179  CA  LYS B 212     7032   4913   5862    594    550  -1875       C  
ATOM   3180  C   LYS B 212       5.687 -22.786 -16.058  1.00 48.33           C  
ANISOU 3180  C   LYS B 212     7512   4768   6082    518    503  -2053       C  
ATOM   3181  O   LYS B 212       4.562 -22.965 -16.522  1.00 49.74           O  
ANISOU 3181  O   LYS B 212     7874   4948   6079    256    341  -2093       O  
ATOM   3182  CB  LYS B 212       7.052 -20.884 -16.959  1.00 54.51           C  
ANISOU 3182  CB  LYS B 212     8035   6027   6649    663    817  -2057       C  
ATOM   3183  CG  LYS B 212       7.054 -19.366 -17.145  1.00 56.96           C  
ANISOU 3183  CG  LYS B 212     8175   6689   6779    583    804  -1898       C  
ATOM   3184  CD  LYS B 212       7.843 -18.945 -18.386  1.00 64.41           C  
ANISOU 3184  CD  LYS B 212     9202   7770   7500    600   1087  -2069       C  
ATOM   3185  CE  LYS B 212       7.221 -19.491 -19.668  1.00 68.64           C  
ANISOU 3185  CE  LYS B 212    10122   8257   7702    407   1092  -2286       C  
ATOM   3186  NZ  LYS B 212       7.976 -19.088 -20.899  1.00 73.82           N  
ANISOU 3186  NZ  LYS B 212    10839   9086   8123    415   1308  -2349       N  
ATOM   3187  N   ALA B 213       6.521 -23.781 -15.768  1.00 49.92           N  
ANISOU 3187  N   ALA B 213     7748   4669   6549    744    624  -2150       N  
ATOM   3188  CA  ALA B 213       6.177 -25.176 -16.020  1.00 53.45           C  
ANISOU 3188  CA  ALA B 213     8504   4734   7072    701    601  -2339       C  
ATOM   3189  C   ALA B 213       5.115 -25.688 -15.041  1.00 50.05           C  
ANISOU 3189  C   ALA B 213     8104   4163   6751    513    313  -2130       C  
ATOM   3190  O   ALA B 213       4.191 -26.402 -15.429  1.00 51.63           O  
ANISOU 3190  O   ALA B 213     8560   4194   6864    279    190  -2232       O  
ATOM   3191  CB  ALA B 213       7.428 -26.052 -15.970  1.00 60.22           C  
ANISOU 3191  CB  ALA B 213     9316   5346   8217   1036    764  -2430       C  
ATOM   3192  N   LYS B 214       5.258 -25.325 -13.772  1.00 44.33           N  
ANISOU 3192  N   LYS B 214     7132   3508   6203    593    211  -1837       N  
ATOM   3193  CA  LYS B 214       4.345 -25.784 -12.729  1.00 46.91           C  
ANISOU 3193  CA  LYS B 214     7484   3715   6625    419     -6  -1616       C  
ATOM   3194  C   LYS B 214       2.903 -25.327 -12.966  1.00 43.47           C  
ANISOU 3194  C   LYS B 214     7059   3482   5977     77   -149  -1559       C  
ATOM   3195  O   LYS B 214       1.967 -26.124 -12.869  1.00 43.01           O  
ANISOU 3195  O   LYS B 214     7153   3237   5952   -150   -283  -1546       O  
ATOM   3196  CB  LYS B 214       4.826 -25.312 -11.350  1.00 45.95           C  
ANISOU 3196  CB  LYS B 214     7127   3680   6652    549    -67  -1318       C  
ATOM   3197  CG  LYS B 214       4.087 -25.950 -10.177  1.00 50.30           C  
ANISOU 3197  CG  LYS B 214     7753   4058   7302    391   -241  -1084       C  
ATOM   3198  CD  LYS B 214       4.477 -25.309  -8.837  1.00 50.45           C  
ANISOU 3198  CD  LYS B 214     7590   4218   7359    465   -308   -794       C  
ATOM   3199  CE  LYS B 214       5.902 -25.673  -8.429  1.00 54.09           C  
ANISOU 3199  CE  LYS B 214     7992   4500   8061    776   -317   -746       C  
ATOM   3200  NZ  LYS B 214       6.286 -25.017  -7.136  1.00 55.39           N  
ANISOU 3200  NZ  LYS B 214     8018   4810   8218    804   -437   -461       N  
ATOM   3201  N   TYR B 215       2.730 -24.050 -13.291  1.00 40.42           N  
ANISOU 3201  N   TYR B 215     6493   3459   5405     39   -131  -1513       N  
ATOM   3202  CA  TYR B 215       1.392 -23.472 -13.418  1.00 41.02           C  
ANISOU 3202  CA  TYR B 215     6495   3743   5349   -241   -282  -1412       C  
ATOM   3203  C   TYR B 215       0.920 -23.332 -14.870  1.00 46.66           C  
ANISOU 3203  C   TYR B 215     7361   4544   5822   -411   -335  -1608       C  
ATOM   3204  O   TYR B 215      -0.043 -22.619 -15.148  1.00 50.22           O  
ANISOU 3204  O   TYR B 215     7701   5213   6169   -603   -478  -1512       O  
ATOM   3205  CB  TYR B 215       1.323 -22.122 -12.690  1.00 37.15           C  
ANISOU 3205  CB  TYR B 215     5711   3562   4841   -190   -269  -1192       C  
ATOM   3206  CG  TYR B 215       1.717 -22.212 -11.230  1.00 34.38           C  
ANISOU 3206  CG  TYR B 215     5264   3142   4657    -75   -246   -994       C  
ATOM   3207  CD1 TYR B 215       0.950 -22.937 -10.322  1.00 38.10           C  
ANISOU 3207  CD1 TYR B 215     5781   3459   5237   -229   -325   -851       C  
ATOM   3208  CD2 TYR B 215       2.852 -21.567 -10.757  1.00 36.47           C  
ANISOU 3208  CD2 TYR B 215     5405   3499   4952    153   -160   -935       C  
ATOM   3209  CE1 TYR B 215       1.312 -23.024  -8.979  1.00 39.65           C  
ANISOU 3209  CE1 TYR B 215     5948   3593   5523   -156   -317   -654       C  
ATOM   3210  CE2 TYR B 215       3.220 -21.641  -9.420  1.00 36.07           C  
ANISOU 3210  CE2 TYR B 215     5306   3388   5012    226   -190   -743       C  
ATOM   3211  CZ  TYR B 215       2.453 -22.370  -8.537  1.00 39.12           C  
ANISOU 3211  CZ  TYR B 215     5784   3620   5459     72   -268   -604       C  
ATOM   3212  OH  TYR B 215       2.843 -22.450  -7.215  1.00 36.51           O  
ANISOU 3212  OH  TYR B 215     5462   3230   5180    118   -309   -401       O  
ATOM   3213  N   LYS B 216       1.600 -24.010 -15.790  1.00 49.94           N  
ANISOU 3213  N   LYS B 216     8042   4780   6152   -339   -222  -1879       N  
ATOM   3214  CA  LYS B 216       1.224 -23.957 -17.199  1.00 56.65           C  
ANISOU 3214  CA  LYS B 216     9127   5695   6704   -528   -271  -2087       C  
ATOM   3215  C   LYS B 216      -0.142 -24.601 -17.409  1.00 62.54           C  
ANISOU 3215  C   LYS B 216    10005   6329   7427   -878   -551  -2081       C  
ATOM   3216  O   LYS B 216      -0.441 -25.638 -16.819  1.00 61.34           O  
ANISOU 3216  O   LYS B 216     9937   5892   7478   -942   -610  -2072       O  
ATOM   3217  CB  LYS B 216       2.284 -24.646 -18.070  1.00 65.11           C  
ANISOU 3217  CB  LYS B 216    10494   6562   7683   -371    -25  -2417       C  
ATOM   3218  CG  LYS B 216       1.839 -24.949 -19.496  1.00 71.30           C  
ANISOU 3218  CG  LYS B 216    11509   7401   8181   -576    -94  -2599       C  
ATOM   3219  CD  LYS B 216       3.009 -24.968 -20.474  1.00 75.78           C  
ANISOU 3219  CD  LYS B 216    12161   8023   8610   -367    200  -2806       C  
ATOM   3220  CE  LYS B 216       2.547 -25.361 -21.872  1.00 81.97           C  
ANISOU 3220  CE  LYS B 216    13222   8836   9085   -580    124  -2977       C  
ATOM   3221  NZ  LYS B 216       1.341 -24.589 -22.297  1.00 82.45           N  
ANISOU 3221  NZ  LYS B 216    13285   9136   8907   -901   -189  -2816       N  
ATOM   3222  N   ALA B 217      -0.973 -23.975 -18.239  1.00 70.42           N  
ANISOU 3222  N   ALA B 217    11012   7547   8197  -1120   -748  -2061       N  
ATOM   3223  CA  ALA B 217      -2.298 -24.510 -18.546  1.00 77.12           C  
ANISOU 3223  CA  ALA B 217    11933   8327   9041  -1481  -1058  -2036       C  
ATOM   3224  C   ALA B 217      -2.284 -25.326 -19.834  1.00 85.78           C  
ANISOU 3224  C   ALA B 217    13314   9337   9944  -1565  -1065  -2262       C  
ATOM   3225  O   ALA B 217      -1.439 -25.115 -20.708  1.00 87.22           O  
ANISOU 3225  O   ALA B 217    13650   9592   9899  -1422   -882  -2430       O  
ATOM   3226  CB  ALA B 217      -3.318 -23.386 -18.637  1.00 74.92           C  
ANISOU 3226  CB  ALA B 217    11362   8372   8731  -1653  -1299  -1794       C  
ATOM   3227  OXT ALA B 217      -3.122 -26.207 -20.034  1.00 91.27           O  
ANISOU 3227  OXT ALA B 217    14090   9888  10702  -1791  -1246  -2278       O  
TER    3228      ALA B 217                                                      
ATOM   3229  N   SER C   4     -10.278  20.758  20.620  1.00 70.62           N  
ANISOU 3229  N   SER C   4    10395   8353   8083    905   1012   -910       N  
ATOM   3230  CA  SER C   4     -11.254  19.868  21.243  1.00 70.28           C  
ANISOU 3230  CA  SER C   4    10158   8404   8143    889   1223  -1085       C  
ATOM   3231  C   SER C   4     -10.692  19.225  22.509  1.00 72.47           C  
ANISOU 3231  C   SER C   4    10718   8611   8207    441   1242  -1071       C  
ATOM   3232  O   SER C   4      -9.473  19.119  22.667  1.00 74.64           O  
ANISOU 3232  O   SER C   4    11191   8882   8285    161   1006   -908       O  
ATOM   3233  CB  SER C   4     -11.731  18.792  20.245  1.00 66.17           C  
ANISOU 3233  CB  SER C   4     9033   8223   7888   1102   1085  -1111       C  
ATOM   3234  OG  SER C   4     -10.654  18.105  19.622  1.00 57.40           O  
ANISOU 3234  OG  SER C   4     7774   7279   6757    973    718   -932       O  
ATOM   3235  N   PRO C   5     -11.582  18.802  23.425  1.00 71.80           N  
ANISOU 3235  N   PRO C   5    10644   8496   8142    381   1531  -1234       N  
ATOM   3236  CA  PRO C   5     -11.166  17.954  24.551  1.00 67.57           C  
ANISOU 3236  CA  PRO C   5    10287   7954   7433      0   1558  -1209       C  
ATOM   3237  C   PRO C   5     -10.775  16.569  24.042  1.00 54.93           C  
ANISOU 3237  C   PRO C   5     8329   6597   5943    -75   1318  -1105       C  
ATOM   3238  O   PRO C   5     -10.283  15.737  24.809  1.00 52.63           O  
ANISOU 3238  O   PRO C   5     8157   6330   5512   -363   1293  -1034       O  
ATOM   3239  CB  PRO C   5     -12.437  17.850  25.400  1.00 73.77           C  
ANISOU 3239  CB  PRO C   5    11071   8682   8277     48   1946  -1415       C  
ATOM   3240  CG  PRO C   5     -13.552  18.059  24.428  1.00 75.57           C  
ANISOU 3240  CG  PRO C   5    10897   9028   8789    464   2043  -1541       C  
ATOM   3241  CD  PRO C   5     -13.028  19.083  23.456  1.00 74.63           C  
ANISOU 3241  CD  PRO C   5    10835   8852   8670    680   1856  -1440       C  
ATOM   3242  N   GLY C   6     -11.005  16.338  22.751  1.00 42.40           N  
ANISOU 3242  N   GLY C   6     6316   5194   4599    204   1154  -1097       N  
ATOM   3243  CA  GLY C   6     -10.634  15.095  22.105  1.00 36.14           C  
ANISOU 3243  CA  GLY C   6     5175   4627   3931    174    912  -1015       C  
ATOM   3244  C   GLY C   6     -11.792  14.125  22.014  1.00 32.48           C  
ANISOU 3244  C   GLY C   6     4322   4291   3727    265   1096  -1193       C  
ATOM   3245  O   GLY C   6     -12.941  14.485  22.263  1.00 36.09           O  
ANISOU 3245  O   GLY C   6     4708   4716   4289    409   1390  -1378       O  
ATOM   3246  N   VAL C   7     -11.486  12.883  21.658  1.00 30.81           N  
ANISOU 3246  N   VAL C   7     3861   4232   3615    178    930  -1140       N  
ATOM   3247  CA  VAL C   7     -12.492  11.837  21.672  1.00 32.24           C  
ANISOU 3247  CA  VAL C   7     3708   4511   4032    181   1114  -1311       C  
ATOM   3248  C   VAL C   7     -12.777  11.485  23.123  1.00 35.99           C  
ANISOU 3248  C   VAL C   7     4484   4815   4376   -102   1410  -1342       C  
ATOM   3249  O   VAL C   7     -11.886  11.046  23.854  1.00 32.91           O  
ANISOU 3249  O   VAL C   7     4391   4340   3773   -365   1338  -1178       O  
ATOM   3250  CB  VAL C   7     -12.012  10.589  20.926  1.00 29.61           C  
ANISOU 3250  CB  VAL C   7     3077   4342   3830    146    863  -1245       C  
ATOM   3251  CG1 VAL C   7     -13.048   9.478  21.045  1.00 35.74           C  
ANISOU 3251  CG1 VAL C   7     3552   5180   4848     87   1088  -1437       C  
ATOM   3252  CG2 VAL C   7     -11.725  10.910  19.457  1.00 36.78           C  
ANISOU 3252  CG2 VAL C   7     3661   5455   4859    442    561  -1214       C  
ATOM   3253  N   VAL C   8     -14.018  11.701  23.551  1.00 35.93           N  
ANISOU 3253  N   VAL C   8     4393   4785   4473    -30   1747  -1546       N  
ATOM   3254  CA  VAL C   8     -14.393  11.423  24.927  1.00 41.06           C  
ANISOU 3254  CA  VAL C   8     5309   5291   5000   -275   2055  -1583       C  
ATOM   3255  C   VAL C   8     -14.773   9.957  25.084  1.00 45.04           C  
ANISOU 3255  C   VAL C   8     5585   5859   5670   -446   2154  -1623       C  
ATOM   3256  O   VAL C   8     -15.745   9.481  24.486  1.00 45.74           O  
ANISOU 3256  O   VAL C   8     5250   6094   6034   -329   2256  -1806       O  
ATOM   3257  CB  VAL C   8     -15.554  12.307  25.385  1.00 46.21           C  
ANISOU 3257  CB  VAL C   8     5991   5898   5668   -125   2391  -1779       C  
ATOM   3258  CG1 VAL C   8     -16.025  11.880  26.759  1.00 46.04           C  
ANISOU 3258  CG1 VAL C   8     6183   5770   5540   -371   2718  -1826       C  
ATOM   3259  CG2 VAL C   8     -15.126  13.764  25.407  1.00 40.94           C  
ANISOU 3259  CG2 VAL C   8     5650   5094   4810      8   2336  -1731       C  
ATOM   3260  N   ILE C   9     -13.981   9.233  25.869  1.00 38.43           N  
ANISOU 3260  N   ILE C   9     5026   4920   4656   -722   2124  -1450       N  
ATOM   3261  CA  ILE C   9     -14.321   7.859  26.217  1.00 40.56           C  
ANISOU 3261  CA  ILE C   9     5173   5183   5054   -911   2274  -1463       C  
ATOM   3262  C   ILE C   9     -14.986   7.922  27.586  1.00 41.36           C  
ANISOU 3262  C   ILE C   9     5519   5163   5035  -1079   2660  -1520       C  
ATOM   3263  O   ILE C   9     -14.375   8.364  28.564  1.00 41.77           O  
ANISOU 3263  O   ILE C   9     5992   5099   4780  -1212   2693  -1390       O  
ATOM   3264  CB  ILE C   9     -13.080   6.957  26.204  1.00 38.90           C  
ANISOU 3264  CB  ILE C   9     5108   4949   4722  -1064   2024  -1221       C  
ATOM   3265  CG1 ILE C   9     -12.474   6.932  24.796  1.00 37.20           C  
ANISOU 3265  CG1 ILE C   9     4623   4883   4628   -872   1643  -1179       C  
ATOM   3266  CG2 ILE C   9     -13.425   5.541  26.653  1.00 39.54           C  
ANISOU 3266  CG2 ILE C   9     5130   4970   4925  -1261   2222  -1217       C  
ATOM   3267  CD1 ILE C   9     -11.264   6.056  24.664  1.00 34.40           C  
ANISOU 3267  CD1 ILE C   9     4376   4539   4156   -975   1380   -946       C  
ATOM   3268  N   SER C  10     -16.260   7.546  27.652  1.00 49.43           N  
ANISOU 3268  N   SER C  10     6261   6236   6282  -1069   2955  -1726       N  
ATOM   3269  CA  SER C  10     -17.021   7.750  28.881  1.00 53.27           C  
ANISOU 3269  CA  SER C  10     6939   6634   6668  -1177   3287  -1779       C  
ATOM   3270  C   SER C  10     -16.710   6.680  29.918  1.00 52.71           C  
ANISOU 3270  C   SER C  10     7102   6440   6486  -1475   3436  -1630       C  
ATOM   3271  O   SER C  10     -16.142   5.636  29.592  1.00 48.06           O  
ANISOU 3271  O   SER C  10     6458   5842   5960  -1594   3348  -1525       O  
ATOM   3272  CB  SER C  10     -18.526   7.845  28.603  1.00 58.50           C  
ANISOU 3272  CB  SER C  10     7231   7407   7591  -1020   3376  -1961       C  
ATOM   3273  OG  SER C  10     -18.898   7.035  27.504  1.00 63.79           O  
ANISOU 3273  OG  SER C  10     7473   8214   8551   -963   3232  -2042       O  
ATOM   3274  N   ASP C  11     -17.078   6.959  31.166  1.00 49.89           N  
ANISOU 3274  N   ASP C  11     7007   5985   5965  -1565   3628  -1600       N  
ATOM   3275  CA  ASP C  11     -16.749   6.091  32.297  1.00 55.02           C  
ANISOU 3275  CA  ASP C  11     7925   6514   6466  -1799   3735  -1426       C  
ATOM   3276  C   ASP C  11     -17.328   4.692  32.137  1.00 55.65           C  
ANISOU 3276  C   ASP C  11     7757   6575   6814  -1911   3842  -1449       C  
ATOM   3277  O   ASP C  11     -16.749   3.714  32.607  1.00 57.47           O  
ANISOU 3277  O   ASP C  11     8159   6708   6970  -2058   3830  -1268       O  
ATOM   3278  CB  ASP C  11     -17.250   6.702  33.611  1.00 56.15           C  
ANISOU 3278  CB  ASP C  11     8313   6591   6429  -1830   3924  -1437       C  
ATOM   3279  CG  ASP C  11     -16.368   7.833  34.114  1.00 59.97           C  
ANISOU 3279  CG  ASP C  11     9170   7034   6583  -1804   3793  -1351       C  
ATOM   3280  OD1 ASP C  11     -15.689   8.482  33.296  1.00 59.01           O  
ANISOU 3280  OD1 ASP C  11     9066   6948   6407  -1707   3586  -1349       O  
ATOM   3281  OD2 ASP C  11     -16.366   8.074  35.342  1.00 66.34           O  
ANISOU 3281  OD2 ASP C  11    10242   7776   7186  -1884   3889  -1295       O  
ATOM   3282  N   ASP C  12     -18.473   4.608  31.468  1.00 55.53           N  
ANISOU 3282  N   ASP C  12     7344   6657   7099  -1821   3913  -1667       N  
ATOM   3283  CA  ASP C  12     -19.132   3.330  31.240  1.00 63.27           C  
ANISOU 3283  CA  ASP C  12     8075   7617   8346  -1937   4000  -1731       C  
ATOM   3284  C   ASP C  12     -18.809   2.748  29.862  1.00 61.20           C  
ANISOU 3284  C   ASP C  12     7508   7430   8314  -1881   3781  -1787       C  
ATOM   3285  O   ASP C  12     -19.647   2.094  29.239  1.00 63.89           O  
ANISOU 3285  O   ASP C  12     7514   7832   8929  -1883   3785  -1949       O  
ATOM   3286  CB  ASP C  12     -20.648   3.450  31.454  1.00 70.20           C  
ANISOU 3286  CB  ASP C  12     8708   8579   9385  -1909   4191  -1929       C  
ATOM   3287  CG  ASP C  12     -21.333   4.293  30.394  1.00 73.82           C  
ANISOU 3287  CG  ASP C  12     8810   9248   9993  -1655   4050  -2116       C  
ATOM   3288  OD1 ASP C  12     -20.637   5.033  29.660  1.00 70.21           O  
ANISOU 3288  OD1 ASP C  12     8347   8848   9480  -1479   3833  -2093       O  
ATOM   3289  OD2 ASP C  12     -22.578   4.214  30.300  1.00 78.78           O  
ANISOU 3289  OD2 ASP C  12     9168   9995  10770  -1618   4143  -2269       O  
ATOM   3290  N   GLU C  13     -17.592   2.995  29.388  1.00 56.75           N  
ANISOU 3290  N   GLU C  13     7065   6879   7620  -1831   3571  -1654       N  
ATOM   3291  CA  GLU C  13     -17.127   2.388  28.146  1.00 57.52           C  
ANISOU 3291  CA  GLU C  13     6897   7048   7910  -1779   3345  -1675       C  
ATOM   3292  C   GLU C  13     -16.751   0.931  28.385  1.00 58.04           C  
ANISOU 3292  C   GLU C  13     7068   6953   8031  -1973   3381  -1538       C  
ATOM   3293  O   GLU C  13     -15.837   0.640  29.161  1.00 56.18           O  
ANISOU 3293  O   GLU C  13     7212   6589   7544  -2078   3380  -1281       O  
ATOM   3294  CB  GLU C  13     -15.927   3.153  27.583  1.00 60.42           C  
ANISOU 3294  CB  GLU C  13     7373   7488   8094  -1638   3047  -1546       C  
ATOM   3295  CG  GLU C  13     -15.283   2.516  26.345  1.00 67.17           C  
ANISOU 3295  CG  GLU C  13     7997   8416   9109  -1545   2707  -1511       C  
ATOM   3296  CD  GLU C  13     -16.104   2.695  25.072  1.00 74.83           C  
ANISOU 3296  CD  GLU C  13     8443   9595  10394  -1349   2631  -1788       C  
ATOM   3297  OE1 GLU C  13     -17.184   3.323  25.134  1.00 80.25           O  
ANISOU 3297  OE1 GLU C  13     8994  10351  11146  -1243   2736  -1951       O  
ATOM   3298  OE2 GLU C  13     -15.663   2.212  24.003  1.00 75.97           O  
ANISOU 3298  OE2 GLU C  13     8360   9828  10677  -1254   2356  -1792       O  
ATOM   3299  N   PRO C  14     -17.464   0.003  27.724  1.00 66.67           N  
ANISOU 3299  N   PRO C  14     7851   8052   9428  -1994   3383  -1702       N  
ATOM   3300  CA  PRO C  14     -17.124  -1.417  27.857  1.00 67.63           C  
ANISOU 3300  CA  PRO C  14     8085   7994   9618  -2148   3420  -1587       C  
ATOM   3301  C   PRO C  14     -15.808  -1.759  27.170  1.00 59.78           C  
ANISOU 3301  C   PRO C  14     7147   6994   8572  -2106   3158  -1410       C  
ATOM   3302  O   PRO C  14     -15.208  -2.777  27.501  1.00 65.21           O  
ANISOU 3302  O   PRO C  14     8061   7511   9205  -2203   3171  -1219       O  
ATOM   3303  CB  PRO C  14     -18.284  -2.128  27.146  1.00 70.35           C  
ANISOU 3303  CB  PRO C  14     8059   8381  10292  -2162   3462  -1862       C  
ATOM   3304  CG  PRO C  14     -18.826  -1.119  26.195  1.00 70.12           C  
ANISOU 3304  CG  PRO C  14     7680   8605  10357  -1947   3280  -2070       C  
ATOM   3305  CD  PRO C  14     -18.642   0.216  26.863  1.00 69.70           C  
ANISOU 3305  CD  PRO C  14     7809   8606  10067  -1864   3332  -1987       C  
ATOM   3306  N   GLY C  15     -15.356  -0.925  26.240  1.00 54.32           N  
ANISOU 3306  N   GLY C  15     6258   6496   7887  -1944   2914  -1459       N  
ATOM   3307  CA  GLY C  15     -14.221  -1.303  25.413  1.00 51.71           C  
ANISOU 3307  CA  GLY C  15     5925   6193   7529  -1842   2563  -1313       C  
ATOM   3308  C   GLY C  15     -14.556  -2.585  24.665  1.00 52.04           C  
ANISOU 3308  C   GLY C  15     5703   6179   7892  -1911   2585  -1451       C  
ATOM   3309  O   GLY C  15     -15.731  -2.862  24.406  1.00 55.29           O  
ANISOU 3309  O   GLY C  15     5873   6617   8517  -1899   2687  -1702       O  
ATOM   3310  N   TYR C  16     -13.541  -3.387  24.354  1.00 45.39           N  
ANISOU 3310  N   TYR C  16     4999   5249   7000  -1895   2387  -1261       N  
ATOM   3311  CA  TYR C  16     -13.741  -4.576  23.528  1.00 45.27           C  
ANISOU 3311  CA  TYR C  16     4753   5170   7276  -1930   2364  -1400       C  
ATOM   3312  C   TYR C  16     -13.114  -5.847  24.109  1.00 47.74           C  
ANISOU 3312  C   TYR C  16     5421   5194   7526  -2076   2487  -1164       C  
ATOM   3313  O   TYR C  16     -12.015  -5.807  24.666  1.00 45.36           O  
ANISOU 3313  O   TYR C  16     5494   4835   6906  -2026   2371   -836       O  
ATOM   3314  CB  TYR C  16     -13.173  -4.328  22.129  1.00 39.71           C  
ANISOU 3314  CB  TYR C  16     3749   4694   6646  -1683   1941  -1465       C  
ATOM   3315  CG  TYR C  16     -13.735  -3.107  21.446  1.00 42.36           C  
ANISOU 3315  CG  TYR C  16     3757   5317   7021  -1471   1788  -1662       C  
ATOM   3316  CD1 TYR C  16     -14.902  -3.190  20.696  1.00 50.05           C  
ANISOU 3316  CD1 TYR C  16     4462   6393   8161  -1342   1751  -1928       C  
ATOM   3317  CD2 TYR C  16     -13.110  -1.869  21.562  1.00 37.01           C  
ANISOU 3317  CD2 TYR C  16     3202   4768   6090  -1317   1597  -1510       C  
ATOM   3318  CE1 TYR C  16     -15.427  -2.082  20.074  1.00 50.41           C  
ANISOU 3318  CE1 TYR C  16     4339   6656   8159  -1105   1573  -2025       C  
ATOM   3319  CE2 TYR C  16     -13.632  -0.745  20.941  1.00 42.82           C  
ANISOU 3319  CE2 TYR C  16     3648   5740   6880  -1118   1501  -1681       C  
ATOM   3320  CZ  TYR C  16     -14.791  -0.867  20.196  1.00 46.07           C  
ANISOU 3320  CZ  TYR C  16     3849   6220   7435   -977   1449  -1892       C  
ATOM   3321  OH  TYR C  16     -15.324   0.233  19.574  1.00 46.25           O  
ANISOU 3321  OH  TYR C  16     3760   6415   7400   -737   1286  -1948       O  
ATOM   3322  N   ASP C  17     -13.819  -6.969  23.963  1.00 45.63           N  
ANISOU 3322  N   ASP C  17     5075   4779   7482  -2156   2642  -1314       N  
ATOM   3323  CA  ASP C  17     -13.307  -8.283  24.352  1.00 50.26           C  
ANISOU 3323  CA  ASP C  17     5968   5079   8051  -2254   2760  -1119       C  
ATOM   3324  C   ASP C  17     -12.020  -8.552  23.569  1.00 47.97           C  
ANISOU 3324  C   ASP C  17     5710   4788   7728  -2152   2469   -958       C  
ATOM   3325  O   ASP C  17     -11.966  -8.308  22.366  1.00 42.67           O  
ANISOU 3325  O   ASP C  17     4682   4327   7203  -1993   2173  -1144       O  
ATOM   3326  CB  ASP C  17     -14.353  -9.371  24.054  1.00 55.20           C  
ANISOU 3326  CB  ASP C  17     6425   5582   8968  -2356   2952  -1378       C  
ATOM   3327  CG  ASP C  17     -13.954 -10.755  24.581  1.00 64.66           C  
ANISOU 3327  CG  ASP C  17     7967   6449  10150  -2459   3133  -1181       C  
ATOM   3328  OD1 ASP C  17     -12.780 -11.155  24.425  1.00 64.08           O  
ANISOU 3328  OD1 ASP C  17     8112   6271   9965  -2384   2987   -934       O  
ATOM   3329  OD2 ASP C  17     -14.826 -11.455  25.148  1.00 71.76           O  
ANISOU 3329  OD2 ASP C  17     8927   7195  11144  -2603   3425  -1269       O  
ATOM   3330  N   LEU C  18     -10.997  -9.056  24.262  1.00 37.47           N  
ANISOU 3330  N   LEU C  18     5055   4461   4720  -1712    610    451       N  
ATOM   3331  CA  LEU C  18      -9.696  -9.344  23.656  1.00 35.61           C  
ANISOU 3331  CA  LEU C  18     4957   4011   4564  -1526    447    371       C  
ATOM   3332  C   LEU C  18      -9.836 -10.296  22.470  1.00 32.17           C  
ANISOU 3332  C   LEU C  18     4548   3408   4266  -1529    280    309       C  
ATOM   3333  O   LEU C  18      -9.084 -10.210  21.509  1.00 33.38           O  
ANISOU 3333  O   LEU C  18     4697   3503   4482  -1337    208    164       O  
ATOM   3334  CB  LEU C  18      -8.759  -9.974  24.692  1.00 36.63           C  
ANISOU 3334  CB  LEU C  18     5294   3991   4633  -1564    332    482       C  
ATOM   3335  CG  LEU C  18      -8.378  -9.149  25.921  1.00 38.45           C  
ANISOU 3335  CG  LEU C  18     5541   4373   4694  -1573    461    531       C  
ATOM   3336  CD1 LEU C  18      -7.632  -9.999  26.946  1.00 40.82           C  
ANISOU 3336  CD1 LEU C  18     6049   4533   4927  -1670    303    695       C  
ATOM   3337  CD2 LEU C  18      -7.530  -7.977  25.506  1.00 34.31           C  
ANISOU 3337  CD2 LEU C  18     4953   3917   4168  -1337    526    378       C  
ATOM   3338  N   ASP C  19     -10.816 -11.191  22.544  1.00 32.65           N  
ANISOU 3338  N   ASP C  19     4630   3421   4356  -1771    220    412       N  
ATOM   3339  CA  ASP C  19     -10.961 -12.246  21.538  1.00 37.36           C  
ANISOU 3339  CA  ASP C  19     5304   3812   5079  -1815     29    346       C  
ATOM   3340  C   ASP C  19     -11.410 -11.763  20.165  1.00 32.76           C  
ANISOU 3340  C   ASP C  19     4538   3366   4543  -1725     68    189       C  
ATOM   3341  O   ASP C  19     -11.478 -12.553  19.222  1.00 33.72           O  
ANISOU 3341  O   ASP C  19     4716   3348   4747  -1747    -84     88       O  
ATOM   3342  CB  ASP C  19     -11.928 -13.317  22.029  1.00 43.62           C  
ANISOU 3342  CB  ASP C  19     6184   4512   5878  -2160    -65    525       C  
ATOM   3343  CG  ASP C  19     -11.290 -14.255  23.008  1.00 60.83           C  
ANISOU 3343  CG  ASP C  19     8634   6419   8059  -2255   -237    680       C  
ATOM   3344  OD1 ASP C  19     -10.510 -13.781  23.861  1.00 66.38           O  
ANISOU 3344  OD1 ASP C  19     9379   7165   8678  -2144   -180    729       O  
ATOM   3345  OD2 ASP C  19     -11.556 -15.470  22.916  1.00 72.93           O  
ANISOU 3345  OD2 ASP C  19    10350   7679   9680  -2448   -455    760       O  
ATOM   3346  N   LEU C  20     -11.732 -10.481  20.060  1.00 31.19           N  
ANISOU 3346  N   LEU C  20     4133   3430   4289  -1630    251    167       N  
ATOM   3347  CA  LEU C  20     -12.203  -9.926  18.794  1.00 30.51           C  
ANISOU 3347  CA  LEU C  20     3865   3492   4234  -1558    270     64       C  
ATOM   3348  C   LEU C  20     -11.043  -9.331  18.015  1.00 30.72           C  
ANISOU 3348  C   LEU C  20     3904   3518   4252  -1313    247    -77       C  
ATOM   3349  O   LEU C  20     -11.199  -8.922  16.859  1.00 28.31           O  
ANISOU 3349  O   LEU C  20     3478   3330   3947  -1256    230   -158       O  
ATOM   3350  CB  LEU C  20     -13.275  -8.858  19.039  1.00 36.04           C  
ANISOU 3350  CB  LEU C  20     4327   4462   4905  -1578    446    131       C  
ATOM   3351  CG  LEU C  20     -14.584  -9.376  19.627  1.00 35.52           C  
ANISOU 3351  CG  LEU C  20     4158   4514   4823  -1841    491    256       C  
ATOM   3352  CD1 LEU C  20     -15.457  -8.228  20.109  1.00 41.49           C  
ANISOU 3352  CD1 LEU C  20     4662   5559   5543  -1784    692    282       C  
ATOM   3353  CD2 LEU C  20     -15.346 -10.212  18.624  1.00 36.66           C  
ANISOU 3353  CD2 LEU C  20     4251   4652   5027  -2015    354    247       C  
ATOM   3354  N   PHE C  21      -9.881  -9.297  18.664  1.00 28.01           N  
ANISOU 3354  N   PHE C  21     3692   3074   3879  -1196    239    -88       N  
ATOM   3355  CA  PHE C  21      -8.679  -8.690  18.102  1.00 28.75           C  
ANISOU 3355  CA  PHE C  21     3774   3216   3933   -993    230   -202       C  
ATOM   3356  C   PHE C  21      -7.482  -9.636  18.105  1.00 30.67           C  
ANISOU 3356  C   PHE C  21     4167   3287   4200   -884     89   -300       C  
ATOM   3357  O   PHE C  21      -7.538 -10.718  18.688  1.00 30.35           O  
ANISOU 3357  O   PHE C  21     4278   3030   4222   -955    -20   -255       O  
ATOM   3358  CB  PHE C  21      -8.340  -7.415  18.864  1.00 27.51           C  
ANISOU 3358  CB  PHE C  21     3580   3167   3707   -927    367   -135       C  
ATOM   3359  CG  PHE C  21      -9.387  -6.355  18.730  1.00 35.65           C  
ANISOU 3359  CG  PHE C  21     4455   4351   4742   -952    486    -85       C  
ATOM   3360  CD1 PHE C  21      -9.357  -5.473  17.662  1.00 37.49           C  
ANISOU 3360  CD1 PHE C  21     4573   4699   4971   -873    481   -123       C  
ATOM   3361  CD2 PHE C  21     -10.426  -6.266  19.645  1.00 40.74           C  
ANISOU 3361  CD2 PHE C  21     5052   5039   5388  -1056    591      2       C  
ATOM   3362  CE1 PHE C  21     -10.325  -4.496  17.516  1.00 45.16           C  
ANISOU 3362  CE1 PHE C  21     5405   5775   5978   -860    553    -69       C  
ATOM   3363  CE2 PHE C  21     -11.402  -5.293  19.504  1.00 47.34           C  
ANISOU 3363  CE2 PHE C  21     5715   6023   6251  -1025    692     18       C  
ATOM   3364  CZ  PHE C  21     -11.349  -4.403  18.436  1.00 48.36           C  
ANISOU 3364  CZ  PHE C  21     5749   6212   6413   -910    659    -15       C  
ATOM   3365  N   CYS C  22      -6.413  -9.225  17.420  1.00 28.63           N  
ANISOU 3365  N   CYS C  22     3852   3134   3891   -716     77   -429       N  
ATOM   3366  CA  CYS C  22      -5.175  -9.992  17.401  1.00 32.72           C  
ANISOU 3366  CA  CYS C  22     4454   3550   4429   -554    -45   -554       C  
ATOM   3367  C   CYS C  22      -4.338  -9.454  18.555  1.00 31.66           C  
ANISOU 3367  C   CYS C  22     4358   3430   4241   -503     -2   -445       C  
ATOM   3368  O   CYS C  22      -4.003  -8.277  18.582  1.00 31.66           O  
ANISOU 3368  O   CYS C  22     4263   3620   4147   -491    106   -413       O  
ATOM   3369  CB  CYS C  22      -4.447  -9.815  16.062  1.00 33.74           C  
ANISOU 3369  CB  CYS C  22     4454   3876   4491   -418    -61   -762       C  
ATOM   3370  N   ILE C  23      -4.047 -10.312  19.528  1.00 31.09           N  
ANISOU 3370  N   ILE C  23     4442   3144   4225   -499   -109   -372       N  
ATOM   3371  CA  ILE C  23      -3.347  -9.910  20.748  1.00 34.60           C  
ANISOU 3371  CA  ILE C  23     4940   3604   4603   -489    -90   -245       C  
ATOM   3372  C   ILE C  23      -2.175 -10.857  20.986  1.00 33.89           C  
ANISOU 3372  C   ILE C  23     4933   3367   4575   -310   -280   -300       C  
ATOM   3373  O   ILE C  23      -2.341 -12.068  20.867  1.00 36.92           O  
ANISOU 3373  O   ILE C  23     5443   3496   5088   -280   -445   -332       O  
ATOM   3374  CB  ILE C  23      -4.294 -10.051  21.963  1.00 36.66           C  
ANISOU 3374  CB  ILE C  23     5315   3768   4844   -706    -49    -36       C  
ATOM   3375  CG1 ILE C  23      -5.492  -9.112  21.817  1.00 38.25           C  
ANISOU 3375  CG1 ILE C  23     5401   4133   4997   -840    141     -2       C  
ATOM   3376  CG2 ILE C  23      -3.539  -9.845  23.279  1.00 36.14           C  
ANISOU 3376  CG2 ILE C  23     5335   3709   4687   -715    -64     93       C  
ATOM   3377  CD1 ILE C  23      -5.146  -7.660  21.905  1.00 34.75           C  
ANISOU 3377  CD1 ILE C  23     4858   3889   4457   -785    284    -24       C  
ATOM   3378  N   PRO C  24      -0.998 -10.324  21.355  1.00 30.76           N  
ANISOU 3378  N   PRO C  24     4471   3118   4100   -193   -279   -305       N  
ATOM   3379  CA  PRO C  24       0.128 -11.247  21.569  1.00 34.06           C  
ANISOU 3379  CA  PRO C  24     4931   3416   4595     18   -478   -363       C  
ATOM   3380  C   PRO C  24      -0.153 -12.243  22.695  1.00 38.56           C  
ANISOU 3380  C   PRO C  24     5731   3671   5251    -61   -645   -170       C  
ATOM   3381  O   PRO C  24      -0.650 -11.847  23.755  1.00 37.85           O  
ANISOU 3381  O   PRO C  24     5722   3594   5063   -275   -575     44       O  
ATOM   3382  CB  PRO C  24       1.289 -10.308  21.919  1.00 30.51           C  
ANISOU 3382  CB  PRO C  24     4345   3239   4010     85   -425   -353       C  
ATOM   3383  CG  PRO C  24       0.654  -9.011  22.322  1.00 35.26           C  
ANISOU 3383  CG  PRO C  24     4932   3989   4475   -139   -227   -231       C  
ATOM   3384  CD  PRO C  24      -0.613  -8.916  21.544  1.00 27.04           C  
ANISOU 3384  CD  PRO C  24     3884   2911   3479   -240   -126   -270       C  
ATOM   3385  N   ASN C  25       0.143 -13.521  22.449  1.00 39.15           N  
ANISOU 3385  N   ASN C  25     5915   3464   5496    101   -874   -250       N  
ATOM   3386  CA  ASN C  25      -0.185 -14.602  23.380  1.00 45.97           C  
ANISOU 3386  CA  ASN C  25     7034   3966   6465      1  -1087    -43       C  
ATOM   3387  C   ASN C  25       0.399 -14.423  24.782  1.00 43.19           C  
ANISOU 3387  C   ASN C  25     6752   3641   6017    -60  -1154    208       C  
ATOM   3388  O   ASN C  25      -0.155 -14.944  25.757  1.00 44.17           O  
ANISOU 3388  O   ASN C  25     7076   3574   6131   -283  -1254    467       O  
ATOM   3389  CB  ASN C  25       0.243 -15.956  22.787  1.00 54.82           C  
ANISOU 3389  CB  ASN C  25     8269   4743   7818    252  -1363   -213       C  
ATOM   3390  CG  ASN C  25      -0.120 -17.138  23.677  1.00 68.27           C  
ANISOU 3390  CG  ASN C  25    10279   6003   9655    125  -1637     29       C  
ATOM   3391  OD1 ASN C  25      -1.298 -17.431  23.890  1.00 73.29           O  
ANISOU 3391  OD1 ASN C  25    11062   6498  10287   -190  -1625    189       O  
ATOM   3392  ND2 ASN C  25       0.894 -17.842  24.175  1.00 71.52           N  
ANISOU 3392  ND2 ASN C  25    10782   6204  10189    362  -1904     67       N  
ATOM   3393  N   HIS C  26       1.509 -13.692  24.891  1.00 40.98           N  
ANISOU 3393  N   HIS C  26     6304   3626   5643    101  -1107    145       N  
ATOM   3394  CA  HIS C  26       2.189 -13.570  26.184  1.00 43.87           C  
ANISOU 3394  CA  HIS C  26     6727   4034   5909     55  -1203    367       C  
ATOM   3395  C   HIS C  26       1.483 -12.620  27.148  1.00 43.78           C  
ANISOU 3395  C   HIS C  26     6754   4208   5674   -277  -1001    561       C  
ATOM   3396  O   HIS C  26       1.841 -12.553  28.321  1.00 45.44           O  
ANISOU 3396  O   HIS C  26     7045   4456   5762   -387  -1073    765       O  
ATOM   3397  CB  HIS C  26       3.692 -13.236  26.041  1.00 41.78           C  
ANISOU 3397  CB  HIS C  26     6260   3993   5620    333  -1265    242       C  
ATOM   3398  CG  HIS C  26       3.988 -11.967  25.299  1.00 42.12           C  
ANISOU 3398  CG  HIS C  26     6058   4423   5525    339  -1018     65       C  
ATOM   3399  ND1 HIS C  26       4.248 -11.933  23.942  1.00 44.99           N  
ANISOU 3399  ND1 HIS C  26     6238   4909   5947    531   -958   -210       N  
ATOM   3400  CD2 HIS C  26       4.119 -10.688  25.734  1.00 40.19           C  
ANISOU 3400  CD2 HIS C  26     5731   4464   5076    164   -840    130       C  
ATOM   3401  CE1 HIS C  26       4.502 -10.689  23.573  1.00 43.07           C  
ANISOU 3401  CE1 HIS C  26     5815   5013   5539    447   -761   -268       C  
ATOM   3402  NE2 HIS C  26       4.432  -9.915  24.641  1.00 40.10           N  
ANISOU 3402  NE2 HIS C  26     5506   4711   5018    233   -695    -70       N  
ATOM   3403  N   TYR C  27       0.477 -11.904  26.642  1.00 41.44           N  
ANISOU 3403  N   TYR C  27     6393   4032   5321   -425   -758    485       N  
ATOM   3404  CA  TYR C  27      -0.352 -11.015  27.456  1.00 41.42           C  
ANISOU 3404  CA  TYR C  27     6409   4199   5129   -701   -549    609       C  
ATOM   3405  C   TYR C  27      -1.805 -11.492  27.584  1.00 45.09           C  
ANISOU 3405  C   TYR C  27     6972   4547   5613   -939   -492    714       C  
ATOM   3406  O   TYR C  27      -2.657 -10.752  28.065  1.00 44.42           O  
ANISOU 3406  O   TYR C  27     6853   4640   5386  -1137   -286    760       O  
ATOM   3407  CB  TYR C  27      -0.341  -9.596  26.869  1.00 33.82           C  
ANISOU 3407  CB  TYR C  27     5265   3506   4078   -673   -312    442       C  
ATOM   3408  CG  TYR C  27       0.987  -8.879  26.974  1.00 33.05           C  
ANISOU 3408  CG  TYR C  27     5067   3598   3893   -551   -332    384       C  
ATOM   3409  CD1 TYR C  27       1.794  -9.022  28.100  1.00 32.12           C  
ANISOU 3409  CD1 TYR C  27     5021   3509   3674   -582   -459    527       C  
ATOM   3410  CD2 TYR C  27       1.429  -8.051  25.947  1.00 33.91           C  
ANISOU 3410  CD2 TYR C  27     5002   3883   4000   -442   -238    209       C  
ATOM   3411  CE1 TYR C  27       3.012  -8.358  28.200  1.00 34.82           C  
ANISOU 3411  CE1 TYR C  27     5249   4057   3925   -500   -487    480       C  
ATOM   3412  CE2 TYR C  27       2.634  -7.380  26.034  1.00 31.59           C  
ANISOU 3412  CE2 TYR C  27     4600   3795   3608   -383   -261    173       C  
ATOM   3413  CZ  TYR C  27       3.426  -7.537  27.151  1.00 34.80           C  
ANISOU 3413  CZ  TYR C  27     5064   4233   3925   -407   -383    299       C  
ATOM   3414  OH  TYR C  27       4.633  -6.864  27.216  1.00 33.16           O  
ANISOU 3414  OH  TYR C  27     4726   4261   3611   -373   -415    266       O  
ATOM   3415  N   ALA C  28      -2.088 -12.720  27.153  1.00 48.66           N  
ANISOU 3415  N   ALA C  28     7537   4712   6240   -920   -680    737       N  
ATOM   3416  CA  ALA C  28      -3.474 -13.196  27.062  1.00 51.79           C  
ANISOU 3416  CA  ALA C  28     7996   5016   6664  -1167   -637    821       C  
ATOM   3417  C   ALA C  28      -4.257 -13.162  28.385  1.00 52.23           C  
ANISOU 3417  C   ALA C  28     8139   5176   6531  -1511   -566   1084       C  
ATOM   3418  O   ALA C  28      -5.475 -12.976  28.380  1.00 57.23           O  
ANISOU 3418  O   ALA C  28     8710   5932   7104  -1730   -404   1115       O  
ATOM   3419  CB  ALA C  28      -3.526 -14.600  26.437  1.00 55.14           C  
ANISOU 3419  CB  ALA C  28     8573   5062   7314  -1109   -903    804       C  
ATOM   3420  N   GLU C  29      -3.552 -13.345  29.501  1.00 51.35           N  
ANISOU 3420  N   GLU C  29     8148   5054   6310  -1562   -689   1268       N  
ATOM   3421  CA  GLU C  29      -4.142 -13.345  30.841  1.00 52.51           C  
ANISOU 3421  CA  GLU C  29     8381   5346   6223  -1906   -636   1526       C  
ATOM   3422  C   GLU C  29      -4.091 -11.989  31.550  1.00 49.62           C  
ANISOU 3422  C   GLU C  29     7888   5360   5604  -1952   -369   1459       C  
ATOM   3423  O   GLU C  29      -4.767 -11.774  32.560  1.00 49.60           O  
ANISOU 3423  O   GLU C  29     7902   5576   5370  -2235   -242   1595       O  
ATOM   3424  CB  GLU C  29      -3.376 -14.330  31.715  1.00 60.47           C  
ANISOU 3424  CB  GLU C  29     9613   6132   7229  -1960   -956   1791       C  
ATOM   3425  CG  GLU C  29      -3.223 -15.699  31.114  1.00 67.46           C  
ANISOU 3425  CG  GLU C  29    10673   6566   8394  -1865  -1281   1845       C  
ATOM   3426  CD  GLU C  29      -3.950 -16.751  31.918  1.00 74.55           C  
ANISOU 3426  CD  GLU C  29    11716   7368   9243  -2169  -1432   2109       C  
ATOM   3427  OE1 GLU C  29      -3.782 -16.781  33.159  1.00 72.00           O  
ANISOU 3427  OE1 GLU C  29    11426   7216   8714  -2330  -1467   2305       O  
ATOM   3428  OE2 GLU C  29      -4.695 -17.543  31.303  1.00 80.46           O  
ANISOU 3428  OE2 GLU C  29    12500   7931  10142  -2226  -1502   2072       O  
ATOM   3429  N   ASP C  30      -3.269 -11.089  31.026  1.00 44.22           N  
ANISOU 3429  N   ASP C  30     7083   4763   4954  -1687   -295   1243       N  
ATOM   3430  CA  ASP C  30      -2.854  -9.886  31.750  1.00 41.20           C  
ANISOU 3430  CA  ASP C  30     6641   4657   4355  -1703   -131   1181       C  
ATOM   3431  C   ASP C  30      -3.671  -8.645  31.399  1.00 39.35           C  
ANISOU 3431  C   ASP C  30     6248   4636   4067  -1700    173    976       C  
ATOM   3432  O   ASP C  30      -3.461  -7.565  31.961  1.00 40.26           O  
ANISOU 3432  O   ASP C  30     6330   4951   4016  -1715    318    886       O  
ATOM   3433  CB  ASP C  30      -1.371  -9.625  31.458  1.00 40.99           C  
ANISOU 3433  CB  ASP C  30     6584   4603   4387  -1450   -266   1095       C  
ATOM   3434  CG  ASP C  30      -0.505 -10.843  31.737  1.00 46.49           C  
ANISOU 3434  CG  ASP C  30     7410   5075   5178  -1376   -594   1272       C  
ATOM   3435  OD1 ASP C  30      -0.758 -11.516  32.757  1.00 46.79           O  
ANISOU 3435  OD1 ASP C  30     7607   5063   5108  -1597   -713   1525       O  
ATOM   3436  OD2 ASP C  30       0.411 -11.131  30.937  1.00 50.58           O  
ANISOU 3436  OD2 ASP C  30     7864   5480   5875  -1096   -739   1159       O  
ATOM   3437  N   LEU C  31      -4.590  -8.788  30.454  1.00 34.91           N  
ANISOU 3437  N   LEU C  31     5593   4016   3654  -1673    248    896       N  
ATOM   3438  CA  LEU C  31      -5.370  -7.645  30.004  1.00 39.30           C  
ANISOU 3438  CA  LEU C  31     5986   4742   4202  -1626    496    710       C  
ATOM   3439  C   LEU C  31      -6.837  -7.927  30.252  1.00 41.74           C  
ANISOU 3439  C   LEU C  31     6229   5165   4465  -1833    628    772       C  
ATOM   3440  O   LEU C  31      -7.283  -9.062  30.107  1.00 42.89           O  
ANISOU 3440  O   LEU C  31     6430   5184   4681  -1969    504    917       O  
ATOM   3441  CB  LEU C  31      -5.130  -7.381  28.517  1.00 29.78           C  
ANISOU 3441  CB  LEU C  31     4675   3435   3204  -1394    469    548       C  
ATOM   3442  CG  LEU C  31      -3.694  -7.114  28.086  1.00 30.91           C  
ANISOU 3442  CG  LEU C  31     4828   3528   3388  -1198    350    473       C  
ATOM   3443  CD1 LEU C  31      -3.587  -6.927  26.578  1.00 29.88           C  
ANISOU 3443  CD1 LEU C  31     4576   3357   3419  -1020    338    324       C  
ATOM   3444  CD2 LEU C  31      -3.192  -5.872  28.807  1.00 34.22           C  
ANISOU 3444  CD2 LEU C  31     5248   4111   3642  -1210    459    417       C  
ATOM   3445  N   GLU C  32      -7.596  -6.908  30.635  1.00 39.78           N  
ANISOU 3445  N   GLU C  32     5857   5159   4098  -1860    869    655       N  
ATOM   3446  CA AGLU C  32      -9.012  -7.145  30.834  0.54 43.74           C  
ANISOU 3446  CA AGLU C  32     6233   5839   4548  -2044   1011    695       C  
ATOM   3447  CA BGLU C  32      -9.028  -7.051  30.860  0.46 43.91           C  
ANISOU 3447  CA BGLU C  32     6247   5876   4562  -2037   1027    682       C  
ATOM   3448  C   GLU C  32      -9.788  -6.892  29.545  1.00 43.29           C  
ANISOU 3448  C   GLU C  32     5997   5752   4698  -1905   1064    572       C  
ATOM   3449  O   GLU C  32     -10.637  -7.708  29.185  1.00 43.57           O  
ANISOU 3449  O   GLU C  32     5973   5784   4796  -2052   1028    667       O  
ATOM   3450  CB AGLU C  32      -9.575  -6.367  32.031  0.54 47.32           C  
ANISOU 3450  CB AGLU C  32     6615   6624   4741  -2160   1246    629       C  
ATOM   3451  CB BGLU C  32      -9.500  -5.992  31.860  0.46 46.35           C  
ANISOU 3451  CB BGLU C  32     6468   6495   4648  -2075   1276    556       C  
ATOM   3452  CG AGLU C  32     -10.680  -7.114  32.818  0.54 51.58           C  
ANISOU 3452  CG AGLU C  32     7069   7378   5153  -2401   1278    762       C  
ATOM   3453  CG BGLU C  32     -10.880  -6.248  32.447  0.46 51.70           C  
ANISOU 3453  CG BGLU C  32     6981   7458   5206  -2261   1421    590       C  
ATOM   3454  CD AGLU C  32     -10.187  -8.347  33.594  0.54 50.54           C  
ANISOU 3454  CD AGLU C  32     7129   7137   4937  -2605   1042   1025       C  
ATOM   3455  CD BGLU C  32     -11.876  -5.143  32.137  0.46 56.41           C  
ANISOU 3455  CD BGLU C  32     7331   8267   5836  -2105   1667    351       C  
ATOM   3456  OE1AGLU C  32      -9.649  -9.292  32.980  0.54 47.38           O  
ANISOU 3456  OE1AGLU C  32     6874   6430   4697  -2620    814   1173       O  
ATOM   3457  OE1BGLU C  32     -11.487  -3.957  32.157  0.46 58.29           O  
ANISOU 3457  OE1BGLU C  32     7574   8506   6067  -1906   1775    139       O  
ATOM   3458  OE2AGLU C  32     -10.357  -8.376  34.829  0.54 52.59           O  
ANISOU 3458  OE2AGLU C  32     7393   7615   4973  -2746   1075   1074       O  
ATOM   3459  OE2BGLU C  32     -13.053  -5.468  31.872  0.46 59.78           O  
ANISOU 3459  OE2BGLU C  32     7560   8840   6314  -2161   1721    372       O  
ATOM   3460  N   ARG C  33      -9.470  -5.808  28.832  1.00 38.05           N  
ANISOU 3460  N   ARG C  33     5263   5060   4135  -1652   1118    385       N  
ATOM   3461  CA  ARG C  33     -10.181  -5.431  27.617  1.00 37.00           C  
ANISOU 3461  CA  ARG C  33     4958   4920   4180  -1518   1154    284       C  
ATOM   3462  C   ARG C  33      -9.305  -4.586  26.716  1.00 34.39           C  
ANISOU 3462  C   ARG C  33     4644   4461   3961  -1280   1094    163       C  
ATOM   3463  O   ARG C  33      -8.367  -3.937  27.182  1.00 31.78           O  
ANISOU 3463  O   ARG C  33     4415   4107   3555  -1213   1092    115       O  
ATOM   3464  CB  ARG C  33     -11.407  -4.579  27.958  1.00 46.03           C  
ANISOU 3464  CB  ARG C  33     5897   6319   5273  -1503   1379    177       C  
ATOM   3465  CG  ARG C  33     -12.449  -5.243  28.834  1.00 60.35           C  
ANISOU 3465  CG  ARG C  33     7618   8375   6936  -1764   1487    279       C  
ATOM   3466  CD  ARG C  33     -13.235  -6.306  28.084  1.00 66.93           C  
ANISOU 3466  CD  ARG C  33     8366   9184   7879  -1920   1393    408       C  
ATOM   3467  NE  ARG C  33     -14.445  -5.747  27.492  1.00 73.47           N  
ANISOU 3467  NE  ARG C  33     8910  10211   8794  -1838   1520    307       N  
ATOM   3468  CZ  ARG C  33     -15.454  -6.474  27.028  1.00 77.63           C  
ANISOU 3468  CZ  ARG C  33     9284  10842   9370  -2012   1495    398       C  
ATOM   3469  NH1 ARG C  33     -15.396  -7.798  27.081  1.00 78.60           N  
ANISOU 3469  NH1 ARG C  33     9547  10845   9471  -2291   1340    590       N  
ATOM   3470  NH2 ARG C  33     -16.521  -5.877  26.512  1.00 79.10           N  
ANISOU 3470  NH2 ARG C  33     9182  11241   9634  -1910   1603    303       N  
ATOM   3471  N   VAL C  34      -9.632  -4.556  25.427  1.00 32.21           N  
ANISOU 3471  N   VAL C  34     4263   4130   3844  -1183   1043    123       N  
ATOM   3472  CA  VAL C  34      -9.056  -3.541  24.550  1.00 28.12           C  
ANISOU 3472  CA  VAL C  34     3722   3558   3405   -995   1014     24       C  
ATOM   3473  C   VAL C  34      -9.832  -2.250  24.830  1.00 29.40           C  
ANISOU 3473  C   VAL C  34     3778   3823   3571   -901   1168    -76       C  
ATOM   3474  O   VAL C  34     -11.060  -2.257  24.861  1.00 32.67           O  
ANISOU 3474  O   VAL C  34     4032   4364   4017   -917   1265    -88       O  
ATOM   3475  CB  VAL C  34      -9.143  -3.932  23.068  1.00 31.84           C  
ANISOU 3475  CB  VAL C  34     4117   3972   4009   -944    898     20       C  
ATOM   3476  CG1 VAL C  34      -8.674  -2.779  22.183  1.00 32.33           C  
ANISOU 3476  CG1 VAL C  34     4142   4026   4118   -798    873    -45       C  
ATOM   3477  CG2 VAL C  34      -8.311  -5.169  22.804  1.00 34.55           C  
ANISOU 3477  CG2 VAL C  34     4574   4192   4361   -984    741     59       C  
ATOM   3478  N   PHE C  35      -9.124  -1.152  25.069  1.00 30.75           N  
ANISOU 3478  N   PHE C  35     4033   3940   3711   -801   1180   -155       N  
ATOM   3479  CA  PHE C  35      -9.780   0.083  25.498  1.00 31.57           C  
ANISOU 3479  CA  PHE C  35     4082   4087   3827   -686   1307   -284       C  
ATOM   3480  C   PHE C  35      -9.838   1.065  24.323  1.00 33.36           C  
ANISOU 3480  C   PHE C  35     4258   4201   4216   -528   1225   -312       C  
ATOM   3481  O   PHE C  35     -10.870   1.684  24.053  1.00 34.59           O  
ANISOU 3481  O   PHE C  35     4273   4386   4482   -401   1276   -371       O  
ATOM   3482  CB  PHE C  35      -9.019   0.683  26.681  1.00 35.32           C  
ANISOU 3482  CB  PHE C  35     4722   4550   4149   -712   1359   -366       C  
ATOM   3483  CG  PHE C  35      -9.814   1.678  27.478  1.00 39.94           C  
ANISOU 3483  CG  PHE C  35     5262   5212   4703   -612   1522   -546       C  
ATOM   3484  CD1 PHE C  35     -10.977   1.296  28.124  1.00 43.76           C  
ANISOU 3484  CD1 PHE C  35     5586   5921   5120   -649   1688   -591       C  
ATOM   3485  CD2 PHE C  35      -9.383   2.992  27.594  1.00 42.45           C  
ANISOU 3485  CD2 PHE C  35     5695   5384   5050   -489   1504   -685       C  
ATOM   3486  CE1 PHE C  35     -11.711   2.212  28.862  1.00 48.32           C  
ANISOU 3486  CE1 PHE C  35     6090   6612   5659   -522   1855   -806       C  
ATOM   3487  CE2 PHE C  35     -10.105   3.914  28.330  1.00 46.12           C  
ANISOU 3487  CE2 PHE C  35     6131   5892   5501   -357   1644   -902       C  
ATOM   3488  CZ  PHE C  35     -11.274   3.524  28.965  1.00 47.20           C  
ANISOU 3488  CZ  PHE C  35     6078   6288   5569   -352   1831   -981       C  
ATOM   3489  N   ILE C  36      -8.721   1.197  23.619  1.00 28.56           N  
ANISOU 3489  N   ILE C  36     3752   3486   3615   -541   1085   -256       N  
ATOM   3490  CA  ILE C  36      -8.670   2.001  22.407  1.00 28.88           C  
ANISOU 3490  CA  ILE C  36     3757   3443   3772   -456    974   -226       C  
ATOM   3491  C   ILE C  36      -7.909   1.219  21.353  1.00 29.20           C  
ANISOU 3491  C   ILE C  36     3785   3515   3793   -534    848   -134       C  
ATOM   3492  O   ILE C  36      -6.686   1.107  21.426  1.00 25.96           O  
ANISOU 3492  O   ILE C  36     3475   3099   3291   -595    788   -119       O  
ATOM   3493  CB  ILE C  36      -7.966   3.362  22.640  1.00 26.04           C  
ANISOU 3493  CB  ILE C  36     3548   2938   3407   -414    928   -274       C  
ATOM   3494  CG1 ILE C  36      -8.412   3.999  23.951  1.00 29.29           C  
ANISOU 3494  CG1 ILE C  36     4022   3321   3786   -345   1062   -428       C  
ATOM   3495  CG2 ILE C  36      -8.202   4.315  21.463  1.00 32.18           C  
ANISOU 3495  CG2 ILE C  36     4294   3611   4323   -335    801   -213       C  
ATOM   3496  CD1 ILE C  36      -7.712   5.315  24.288  1.00 31.32           C  
ANISOU 3496  CD1 ILE C  36     4471   3393   4037   -323   1000   -505       C  
ATOM   3497  N   PRO C  37      -8.634   0.646  20.377  1.00 25.76           N  
ANISOU 3497  N   PRO C  37     3211   3144   3433   -531    809    -91       N  
ATOM   3498  CA  PRO C  37      -8.015  -0.087  19.267  1.00 25.19           C  
ANISOU 3498  CA  PRO C  37     3113   3126   3333   -588    696    -52       C  
ATOM   3499  C   PRO C  37      -6.953   0.747  18.557  1.00 27.29           C  
ANISOU 3499  C   PRO C  37     3427   3395   3545   -600    598    -17       C  
ATOM   3500  O   PRO C  37      -7.135   1.960  18.378  1.00 26.06           O  
ANISOU 3500  O   PRO C  37     3292   3172   3438   -566    567     22       O  
ATOM   3501  CB  PRO C  37      -9.204  -0.335  18.334  1.00 24.02           C  
ANISOU 3501  CB  PRO C  37     2804   3045   3278   -578    669    -21       C  
ATOM   3502  CG  PRO C  37     -10.366  -0.467  19.278  1.00 29.92           C  
ANISOU 3502  CG  PRO C  37     3483   3809   4078   -560    793    -45       C  
ATOM   3503  CD  PRO C  37     -10.109   0.600  20.313  1.00 26.67           C  
ANISOU 3503  CD  PRO C  37     3165   3320   3647   -481    874    -97       C  
ATOM   3504  N   HIS C  38      -5.859   0.102  18.160  1.00 24.69           N  
ANISOU 3504  N   HIS C  38     2727   3031   3624   -648   -266    159       N  
ATOM   3505  CA  HIS C  38      -4.760   0.770  17.454  1.00 23.67           C  
ANISOU 3505  CA  HIS C  38     2575   2761   3656   -496    -73     36       C  
ATOM   3506  C   HIS C  38      -5.257   1.623  16.298  1.00 24.12           C  
ANISOU 3506  C   HIS C  38     2770   2866   3528   -396    143   -110       C  
ATOM   3507  O   HIS C  38      -4.851   2.775  16.140  1.00 23.47           O  
ANISOU 3507  O   HIS C  38     2696   2811   3410   -341    286   -169       O  
ATOM   3508  CB  HIS C  38      -3.761  -0.269  16.926  1.00 25.85           C  
ANISOU 3508  CB  HIS C  38     2784   2737   4301   -416    -65      7       C  
ATOM   3509  CG  HIS C  38      -2.626   0.325  16.147  1.00 28.07           C  
ANISOU 3509  CG  HIS C  38     3014   2889   4763   -291    184   -150       C  
ATOM   3510  ND1 HIS C  38      -2.575   0.294  14.769  1.00 29.11           N  
ANISOU 3510  ND1 HIS C  38     3275   2917   4867   -223    444   -355       N  
ATOM   3511  CD2 HIS C  38      -1.512   0.978  16.552  1.00 27.48           C  
ANISOU 3511  CD2 HIS C  38     2778   2797   4868   -270    220   -135       C  
ATOM   3512  CE1 HIS C  38      -1.469   0.891  14.361  1.00 29.32           C  
ANISOU 3512  CE1 HIS C  38     3219   2867   5055   -163    657   -467       C  
ATOM   3513  NE2 HIS C  38      -0.806   1.316  15.420  1.00 30.21           N  
ANISOU 3513  NE2 HIS C  38     3138   3024   5317   -177    521   -334       N  
ATOM   3514  N   GLY C  39      -6.146   1.056  15.486  1.00 23.57           N  
ANISOU 3514  N   GLY C  39     2820   2800   3337   -405    137   -143       N  
ATOM   3515  CA  GLY C  39      -6.601   1.760  14.304  1.00 27.30           C  
ANISOU 3515  CA  GLY C  39     3438   3311   3622   -354    274   -225       C  
ATOM   3516  C   GLY C  39      -7.369   3.033  14.624  1.00 23.77           C  
ANISOU 3516  C   GLY C  39     2968   3045   3018   -317    270   -172       C  
ATOM   3517  O   GLY C  39      -7.311   4.014  13.873  1.00 25.10           O  
ANISOU 3517  O   GLY C  39     3225   3194   3116   -251    381   -195       O  
ATOM   3518  N   LEU C  40      -8.101   3.019  15.728  1.00 26.12           N  
ANISOU 3518  N   LEU C  40     3149   3500   3276   -375    157   -106       N  
ATOM   3519  CA  LEU C  40      -8.814   4.208  16.188  1.00 29.51           C  
ANISOU 3519  CA  LEU C  40     3509   4066   3635   -329    204   -112       C  
ATOM   3520  C   LEU C  40      -7.828   5.303  16.588  1.00 26.72           C  
ANISOU 3520  C   LEU C  40     3150   3639   3363   -283    342   -174       C  
ATOM   3521  O   LEU C  40      -8.055   6.493  16.325  1.00 24.16           O  
ANISOU 3521  O   LEU C  40     2849   3288   3042   -187    445   -208       O  
ATOM   3522  CB  LEU C  40      -9.729   3.861  17.367  1.00 30.41           C  
ANISOU 3522  CB  LEU C  40     3491   4381   3681   -456    119    -84       C  
ATOM   3523  CG  LEU C  40     -10.489   5.066  17.927  1.00 33.64           C  
ANISOU 3523  CG  LEU C  40     3791   4912   4078   -407    237   -161       C  
ATOM   3524  CD1 LEU C  40     -11.244   5.783  16.799  1.00 35.35           C  
ANISOU 3524  CD1 LEU C  40     4008   5080   4342   -226    249   -137       C  
ATOM   3525  CD2 LEU C  40     -11.429   4.660  19.044  1.00 38.62           C  
ANISOU 3525  CD2 LEU C  40     4285   5774   4616   -582    216   -178       C  
ATOM   3526  N   ILE C  41      -6.735   4.895  17.229  1.00 18.85           N  
ANISOU 3526  N   ILE C  41     2113   2589   2461   -364    320   -171       N  
ATOM   3527  CA  ILE C  41      -5.648   5.820  17.554  1.00 22.03           C  
ANISOU 3527  CA  ILE C  41     2501   2922   2948   -364    428   -224       C  
ATOM   3528  C   ILE C  41      -5.084   6.444  16.283  1.00 22.34           C  
ANISOU 3528  C   ILE C  41     2648   2806   3035   -249    586   -272       C  
ATOM   3529  O   ILE C  41      -4.794   7.644  16.239  1.00 23.14           O  
ANISOU 3529  O   ILE C  41     2791   2859   3142   -221    708   -317       O  
ATOM   3530  CB  ILE C  41      -4.517   5.103  18.323  1.00 21.02           C  
ANISOU 3530  CB  ILE C  41     2268   2758   2960   -480    311   -162       C  
ATOM   3531  CG1 ILE C  41      -5.023   4.623  19.677  1.00 23.31           C  
ANISOU 3531  CG1 ILE C  41     2497   3227   3133   -676    133    -75       C  
ATOM   3532  CG2 ILE C  41      -3.319   6.028  18.520  1.00 21.91           C  
ANISOU 3532  CG2 ILE C  41     2343   2806   3176   -502    410   -212       C  
ATOM   3533  CD1 ILE C  41      -3.967   3.912  20.529  1.00 27.23           C  
ANISOU 3533  CD1 ILE C  41     2888   3692   3768   -829    -76     69       C  
ATOM   3534  N   MET C  42      -4.900   5.619  15.252  1.00 20.54           N  
ANISOU 3534  N   MET C  42     2485   2489   2829   -220    601   -275       N  
ATOM   3535  CA  MET C  42      -4.381   6.103  13.990  1.00 24.52           C  
ANISOU 3535  CA  MET C  42     3127   2880   3311   -185    774   -329       C  
ATOM   3536  C   MET C  42      -5.311   7.138  13.374  1.00 23.77           C  
ANISOU 3536  C   MET C  42     3168   2817   3048   -138    778   -269       C  
ATOM   3537  O   MET C  42      -4.860   8.190  12.895  1.00 23.81           O  
ANISOU 3537  O   MET C  42     3268   2737   3041   -131    900   -266       O  
ATOM   3538  CB  MET C  42      -4.143   4.937  13.022  1.00 26.44           C  
ANISOU 3538  CB  MET C  42     3438   3038   3569   -213    823   -396       C  
ATOM   3539  CG  MET C  42      -3.082   3.957  13.479  1.00 28.26           C  
ANISOU 3539  CG  MET C  42     3499   3148   4089   -215    835   -453       C  
ATOM   3540  SD  MET C  42      -1.470   4.728  13.708  1.00 35.42           S  
ANISOU 3540  SD  MET C  42     4256   3967   5235   -211   1007   -513       S  
ATOM   3541  CE  MET C  42      -1.541   5.070  15.468  1.00 46.73           C  
ANISOU 3541  CE  MET C  42     5521   5523   6710   -258    759   -368       C  
ATOM   3542  N   ASP C  43      -6.604   6.844  13.386  1.00 22.90           N  
ANISOU 3542  N   ASP C  43     3047   2814   2839   -115    627   -198       N  
ATOM   3543  CA  ASP C  43      -7.576   7.743  12.779  1.00 24.57           C  
ANISOU 3543  CA  ASP C  43     3330   3038   2968    -49    570    -95       C  
ATOM   3544  C   ASP C  43      -7.596   9.085  13.499  1.00 23.14           C  
ANISOU 3544  C   ASP C  43     3079   2798   2916     40    640   -106       C  
ATOM   3545  O   ASP C  43      -7.666  10.138  12.860  1.00 24.25           O  
ANISOU 3545  O   ASP C  43     3323   2818   3074     96    665    -28       O  
ATOM   3546  CB  ASP C  43      -8.977   7.146  12.842  1.00 24.51           C  
ANISOU 3546  CB  ASP C  43     3236   3178   2900    -42    383    -20       C  
ATOM   3547  CG  ASP C  43      -9.168   5.972  11.881  1.00 31.81           C  
ANISOU 3547  CG  ASP C  43     4287   4136   3662   -160    298     -4       C  
ATOM   3548  OD1 ASP C  43      -8.472   5.895  10.837  1.00 29.41           O  
ANISOU 3548  OD1 ASP C  43     4181   3744   3249   -238    393    -36       O  
ATOM   3549  OD2 ASP C  43     -10.037   5.133  12.177  1.00 32.79           O  
ANISOU 3549  OD2 ASP C  43     4322   4380   3755   -207    159     19       O  
ATOM   3550  N   ARG C  44      -7.571   9.046  14.825  1.00 22.46           N  
ANISOU 3550  N   ARG C  44     2839   2785   2910     23    666   -201       N  
ATOM   3551  CA  ARG C  44      -7.611  10.272  15.618  1.00 22.99           C  
ANISOU 3551  CA  ARG C  44     2852   2791   3090     66    775   -281       C  
ATOM   3552  C   ARG C  44      -6.316  11.042  15.393  1.00 25.06           C  
ANISOU 3552  C   ARG C  44     3231   2893   3399     25    910   -317       C  
ATOM   3553  O   ARG C  44      -6.312  12.269  15.275  1.00 27.16           O  
ANISOU 3553  O   ARG C  44     3562   3002   3757     82    997   -325       O  
ATOM   3554  CB  ARG C  44      -7.798   9.936  17.107  1.00 23.44           C  
ANISOU 3554  CB  ARG C  44     2762   3010   3135    -41    789   -400       C  
ATOM   3555  CG  ARG C  44      -7.812  11.149  18.057  1.00 25.43           C  
ANISOU 3555  CG  ARG C  44     2980   3212   3470    -59    955   -562       C  
ATOM   3556  CD  ARG C  44      -8.782  12.244  17.595  1.00 26.00           C  
ANISOU 3556  CD  ARG C  44     3025   3133   3722    143   1022   -569       C  
ATOM   3557  NE  ARG C  44      -8.790  13.380  18.520  1.00 27.18           N  
ANISOU 3557  NE  ARG C  44     3148   3183   3998    126   1229   -783       N  
ATOM   3558  CZ  ARG C  44      -9.108  14.621  18.169  1.00 28.96           C  
ANISOU 3558  CZ  ARG C  44     3391   3146   4465    295   1327   -810       C  
ATOM   3559  NH1 ARG C  44      -9.463  14.877  16.915  1.00 27.78           N  
ANISOU 3559  NH1 ARG C  44     3287   2839   4430    478   1187   -581       N  
ATOM   3560  NH2 ARG C  44      -9.075  15.597  19.065  1.00 29.15           N  
ANISOU 3560  NH2 ARG C  44     3405   3053   4618    256   1551  -1059       N  
ATOM   3561  N   THR C  45      -5.210  10.309  15.322  1.00 22.89           N  
ANISOU 3561  N   THR C  45     2962   2634   3102    -77    928   -336       N  
ATOM   3562  CA  THR C  45      -3.895  10.932  15.144  1.00 25.73           C  
ANISOU 3562  CA  THR C  45     3376   2872   3527   -148   1066   -379       C  
ATOM   3563  C   THR C  45      -3.780  11.608  13.768  1.00 26.40           C  
ANISOU 3563  C   THR C  45     3655   2815   3561   -122   1151   -300       C  
ATOM   3564  O   THR C  45      -3.159  12.669  13.639  1.00 24.62           O  
ANISOU 3564  O   THR C  45     3514   2455   3387   -167   1269   -309       O  
ATOM   3565  CB  THR C  45      -2.754   9.908  15.363  1.00 23.48           C  
ANISOU 3565  CB  THR C  45     2976   2629   3316   -242   1059   -412       C  
ATOM   3566  OG1 THR C  45      -2.838   9.386  16.696  1.00 20.70           O  
ANISOU 3566  OG1 THR C  45     2475   2404   2987   -317    925   -421       O  
ATOM   3567  CG2 THR C  45      -1.380  10.551  15.160  1.00 26.41           C  
ANISOU 3567  CG2 THR C  45     3344   2898   3795   -328   1214   -462       C  
ATOM   3568  N   GLU C  46      -4.379  10.998  12.745  1.00 23.42           N  
ANISOU 3568  N   GLU C  46     3372   2472   3053    -98   1078   -211       N  
ATOM   3569  CA  GLU C  46      -4.436  11.617  11.428  1.00 24.52           C  
ANISOU 3569  CA  GLU C  46     3736   2513   3066   -138   1107    -90       C  
ATOM   3570  C   GLU C  46      -5.057  13.006  11.505  1.00 25.98           C  
ANISOU 3570  C   GLU C  46     3978   2551   3344    -45   1053     27       C  
ATOM   3571  O   GLU C  46      -4.552  13.959  10.912  1.00 25.66           O  
ANISOU 3571  O   GLU C  46     4104   2352   3295   -112   1131    105       O  
ATOM   3572  CB  GLU C  46      -5.238  10.749  10.441  1.00 22.65           C  
ANISOU 3572  CB  GLU C  46     3602   2375   2631   -169    977      0       C  
ATOM   3573  CG  GLU C  46      -5.344  11.384   9.059  1.00 29.61           C  
ANISOU 3573  CG  GLU C  46     4755   3189   3307   -284    959    169       C  
ATOM   3574  CD  GLU C  46      -6.163  10.540   8.086  1.00 34.78           C  
ANISOU 3574  CD  GLU C  46     5537   3969   3708   -383    800    258       C  
ATOM   3575  OE1 GLU C  46      -6.843   9.603   8.531  1.00 45.60           O  
ANISOU 3575  OE1 GLU C  46     6764   5455   5107   -320    683    208       O  
ATOM   3576  OE2 GLU C  46      -6.110  10.817   6.879  1.00 35.50           O  
ANISOU 3576  OE2 GLU C  46     5892   4053   3544   -570    790    381       O  
ATOM   3577  N   ARG C  47      -6.144  13.118  12.258  1.00 23.29           N  
ANISOU 3577  N   ARG C  47     3484   2240   3125    102    937     29       N  
ATOM   3578  CA  ARG C  47      -6.836  14.394  12.396  1.00 25.20           C  
ANISOU 3578  CA  ARG C  47     3721   2292   3561    237    903    106       C  
ATOM   3579  C   ARG C  47      -6.022  15.368  13.253  1.00 29.90           C  
ANISOU 3579  C   ARG C  47     4318   2731   4311    204   1096    -55       C  
ATOM   3580  O   ARG C  47      -5.988  16.563  12.965  1.00 30.32           O  
ANISOU 3580  O   ARG C  47     4486   2531   4505    241   1128     20       O  
ATOM   3581  CB  ARG C  47      -8.232  14.173  12.991  1.00 26.33           C  
ANISOU 3581  CB  ARG C  47     3642   2525   3838    399    783     96       C  
ATOM   3582  CG  ARG C  47      -8.956  15.467  13.360  1.00 27.98           C  
ANISOU 3582  CG  ARG C  47     3762   2500   4370    581    805    100       C  
ATOM   3583  CD  ARG C  47      -8.963  16.448  12.210  1.00 50.43           C  
ANISOU 3583  CD  ARG C  47     6793   5075   7291    624    688    369       C  
ATOM   3584  NE  ARG C  47     -10.313  16.691  11.731  1.00 57.42           N  
ANISOU 3584  NE  ARG C  47     7543   5893   8380    809    445    592       N  
ATOM   3585  CZ  ARG C  47     -11.032  17.767  12.012  1.00 50.59           C  
ANISOU 3585  CZ  ARG C  47     6533   4751   7937   1030    432    624       C  
ATOM   3586  NH1 ARG C  47     -10.532  18.741  12.756  1.00 57.85           N  
ANISOU 3586  NH1 ARG C  47     7477   5418   9085   1071    672    419       N  
ATOM   3587  NH2 ARG C  47     -12.255  17.868  11.527  1.00 52.69           N  
ANISOU 3587  NH2 ARG C  47     6616   4975   8429   1203    169    860       N  
ATOM   3588  N   LEU C  48      -5.341  14.869  14.284  1.00 26.83           N  
ANISOU 3588  N   LEU C  48     3819   2479   3896    104   1198   -254       N  
ATOM   3589  CA  LEU C  48      -4.501  15.762  15.104  1.00 30.48           C  
ANISOU 3589  CA  LEU C  48     4297   2824   4459      3   1360   -411       C  
ATOM   3590  C   LEU C  48      -3.348  16.358  14.298  1.00 28.59           C  
ANISOU 3590  C   LEU C  48     4233   2434   4195   -123   1455   -341       C  
ATOM   3591  O   LEU C  48      -2.953  17.503  14.513  1.00 30.72           O  
ANISOU 3591  O   LEU C  48     4593   2495   4583   -177   1562   -389       O  
ATOM   3592  CB  LEU C  48      -3.943  15.046  16.334  1.00 30.66           C  
ANISOU 3592  CB  LEU C  48     4172   3058   4418   -142   1382   -581       C  
ATOM   3593  CG  LEU C  48      -4.897  14.690  17.474  1.00 33.68           C  
ANISOU 3593  CG  LEU C  48     4408   3599   4790   -126   1353   -705       C  
ATOM   3594  CD1 LEU C  48      -4.134  14.020  18.609  1.00 29.70           C  
ANISOU 3594  CD1 LEU C  48     3814   3299   4170   -353   1325   -802       C  
ATOM   3595  CD2 LEU C  48      -5.660  15.909  17.991  1.00 33.44           C  
ANISOU 3595  CD2 LEU C  48     4381   3395   4928    -44   1492   -853       C  
ATOM   3596  N   ALA C  49      -2.787  15.576  13.391  1.00 27.05           N  
ANISOU 3596  N   ALA C  49     4086   2339   3852   -200   1448   -256       N  
ATOM   3597  CA  ALA C  49      -1.695  16.069  12.555  1.00 25.92           C  
ANISOU 3597  CA  ALA C  49     4097   2092   3660   -362   1586   -207       C  
ATOM   3598  C   ALA C  49      -2.177  17.263  11.744  1.00 29.35           C  
ANISOU 3598  C   ALA C  49     4764   2276   4110   -340   1553    -17       C  
ATOM   3599  O   ALA C  49      -1.449  18.243  11.557  1.00 30.16           O  
ANISOU 3599  O   ALA C  49     5001   2197   4260   -472   1670      4       O  
ATOM   3600  CB  ALA C  49      -1.193  14.979  11.643  1.00 25.49           C  
ANISOU 3600  CB  ALA C  49     4053   2185   3446   -449   1632   -193       C  
ATOM   3601  N   ARG C  50      -3.415  17.186  11.263  1.00 29.54           N  
ANISOU 3601  N   ARG C  50     4827   2281   4118   -186   1364    151       N  
ATOM   3602  CA  ARG C  50      -3.972  18.295  10.486  1.00 31.91           C  
ANISOU 3602  CA  ARG C  50     5322   2313   4488   -147   1251    405       C  
ATOM   3603  C   ARG C  50      -4.191  19.523  11.376  1.00 33.39           C  
ANISOU 3603  C   ARG C  50     5466   2210   5011    -25   1304    323       C  
ATOM   3604  O   ARG C  50      -3.896  20.657  10.978  1.00 36.03           O  
ANISOU 3604  O   ARG C  50     5991   2246   5454    -88   1327    451       O  
ATOM   3605  CB  ARG C  50      -5.280  17.869   9.805  1.00 34.31           C  
ANISOU 3605  CB  ARG C  50     5620   2681   4736    -15    981    630       C  
ATOM   3606  CG  ARG C  50      -5.647  18.740   8.594  1.00 45.23           C  
ANISOU 3606  CG  ARG C  50     7257   3845   6084    -72    788   1001       C  
ATOM   3607  CD  ARG C  50      -6.891  18.216   7.894  1.00 53.49           C  
ANISOU 3607  CD  ARG C  50     8275   5005   7045      7    469   1249       C  
ATOM   3608  NE  ARG C  50      -8.115  18.557   8.616  1.00 56.55           N  
ANISOU 3608  NE  ARG C  50     8383   5272   7830    325    315   1268       N  
ATOM   3609  CZ  ARG C  50      -9.304  17.999   8.397  1.00 58.28           C  
ANISOU 3609  CZ  ARG C  50     8437   5629   8078    445     57   1406       C  
ATOM   3610  NH1 ARG C  50      -9.441  17.051   7.482  1.00 55.03           N  
ANISOU 3610  NH1 ARG C  50     8151   5477   7281    254    -98   1538       N  
ATOM   3611  NH2 ARG C  50     -10.357  18.386   9.101  1.00 60.65           N  
ANISOU 3611  NH2 ARG C  50     8434   5809   8802    735    -24   1385       N  
ATOM   3612  N   ASP C  51      -4.699  19.293  12.586  1.00 35.03           N  
ANISOU 3612  N   ASP C  51     5442   2493   5375    115   1343     93       N  
ATOM   3613  CA  ASP C  51      -4.912  20.394  13.538  1.00 40.75           C  
ANISOU 3613  CA  ASP C  51     6123   2952   6409    200   1463    -82       C  
ATOM   3614  C   ASP C  51      -3.582  21.076  13.897  1.00 34.39           C  
ANISOU 3614  C   ASP C  51     5450   2031   5585    -38   1660   -224       C  
ATOM   3615  O   ASP C  51      -3.505  22.298  13.989  1.00 37.13           O  
ANISOU 3615  O   ASP C  51     5922   2027   6159    -41   1738   -239       O  
ATOM   3616  CB  ASP C  51      -5.575  19.888  14.825  1.00 40.02           C  
ANISOU 3616  CB  ASP C  51     5778   3042   6387    294   1528   -358       C  
ATOM   3617  CG  ASP C  51      -6.979  19.322  14.607  1.00 43.09           C  
ANISOU 3617  CG  ASP C  51     5986   3533   6852    521   1358   -248       C  
ATOM   3618  OD1 ASP C  51      -7.612  19.606  13.568  1.00 41.54           O  
ANISOU 3618  OD1 ASP C  51     5843   3188   6755    653   1164     44       O  
ATOM   3619  OD2 ASP C  51      -7.459  18.606  15.516  1.00 41.69           O  
ANISOU 3619  OD2 ASP C  51     5609   3598   6634    535   1403   -441       O  
ATOM   3620  N   VAL C  52      -2.542  20.273  14.112  1.00 34.16           N  
ANISOU 3620  N   VAL C  52     5371   2280   5329   -238   1730   -326       N  
ATOM   3621  CA  VAL C  52      -1.201  20.796  14.414  1.00 37.38           C  
ANISOU 3621  CA  VAL C  52     5848   2636   5718   -497   1890   -441       C  
ATOM   3622  C   VAL C  52      -0.681  21.666  13.284  1.00 37.61           C  
ANISOU 3622  C   VAL C  52     6128   2415   5748   -615   1926   -230       C  
ATOM   3623  O   VAL C  52      -0.171  22.766  13.510  1.00 41.85           O  
ANISOU 3623  O   VAL C  52     6766   2741   6393   -733   2009   -280       O  
ATOM   3624  CB  VAL C  52      -0.181  19.650  14.658  1.00 34.29           C  
ANISOU 3624  CB  VAL C  52     5292   2586   5149   -662   1913   -524       C  
ATOM   3625  CG1 VAL C  52       1.240  20.212  14.766  1.00 34.95           C  
ANISOU 3625  CG1 VAL C  52     5406   2623   5248   -941   2055   -595       C  
ATOM   3626  CG2 VAL C  52      -0.540  18.868  15.903  1.00 32.41           C  
ANISOU 3626  CG2 VAL C  52     4841   2582   4893   -626   1850   -699       C  
ATOM   3627  N   MET C  53      -0.811  21.175  12.058  1.00 37.03           N  
ANISOU 3627  N   MET C  53     6152   2422   5497   -615   1838      8       N  
ATOM   3628  CA  MET C  53      -0.335  21.934  10.905  1.00 41.41           C  
ANISOU 3628  CA  MET C  53     6983   2781   5971   -797   1865    243       C  
ATOM   3629  C   MET C  53      -1.132  23.208  10.675  1.00 40.99           C  
ANISOU 3629  C   MET C  53     7098   2328   6149   -672   1726    442       C  
ATOM   3630  O   MET C  53      -0.567  24.241  10.328  1.00 43.78           O  
ANISOU 3630  O   MET C  53     7592   2514   6527   -820   1728    528       O  
ATOM   3631  CB  MET C  53      -0.333  21.066   9.649  1.00 43.15           C  
ANISOU 3631  CB  MET C  53     7296   3219   5879   -887   1814    426       C  
ATOM   3632  CG  MET C  53       0.865  20.133   9.539  1.00 45.05           C  
ANISOU 3632  CG  MET C  53     7417   3755   5946  -1088   2027    242       C  
ATOM   3633  SD  MET C  53       2.389  20.964   9.019  1.00 77.05           S  
ANISOU 3633  SD  MET C  53    11547   7808   9921  -1400   2211    208       S  
ATOM   3634  CE  MET C  53       3.173  21.248  10.597  1.00 63.11           C  
ANISOU 3634  CE  MET C  53     9512   6052   8416  -1395   2293    -74       C  
ATOM   3635  N   LYS C  54      -2.444  23.138  10.865  1.00 43.84           N  
ANISOU 3635  N   LYS C  54     7369   2588   6700   -378   1559    509       N  
ATOM   3636  CA  LYS C  54      -3.293  24.324  10.755  1.00 49.07           C  
ANISOU 3636  CA  LYS C  54     8091   2851   7701   -192   1398    678       C  
ATOM   3637  C   LYS C  54      -2.844  25.412  11.733  1.00 49.03           C  
ANISOU 3637  C   LYS C  54     8038   2670   7923   -220   1532    407       C  
ATOM   3638  O   LYS C  54      -2.911  26.609  11.438  1.00 50.41           O  
ANISOU 3638  O   LYS C  54     8341   2513   8300   -216   1434    543       O  
ATOM   3639  CB  LYS C  54      -4.758  23.951  11.008  1.00 55.65           C  
ANISOU 3639  CB  LYS C  54     8720   3650   8775    154   1242    718       C  
ATOM   3640  CG  LYS C  54      -5.761  25.053  10.670  1.00 67.91           C  
ANISOU 3640  CG  LYS C  54    10262   4827  10712    379    991    952       C  
ATOM   3641  CD  LYS C  54      -7.201  24.542  10.723  1.00 77.52           C  
ANISOU 3641  CD  LYS C  54    11214   6089  12151    703    802   1037       C  
ATOM   3642  CE  LYS C  54      -7.763  24.533  12.144  1.00 82.35           C  
ANISOU 3642  CE  LYS C  54    11499   6770  13020    904   1002    590       C  
ATOM   3643  NZ  LYS C  54      -9.052  23.773  12.245  1.00 83.87           N  
ANISOU 3643  NZ  LYS C  54    11385   7125  13356   1158    869    625       N  
ATOM   3644  N   GLU C  55      -2.357  24.978  12.891  1.00 46.14           N  
ANISOU 3644  N   GLU C  55     7506   2532   7495   -284   1735     41       N  
ATOM   3645  CA  GLU C  55      -2.014  25.878  13.990  1.00 48.79           C  
ANISOU 3645  CA  GLU C  55     7791   2771   7976   -344   1872   -252       C  
ATOM   3646  C   GLU C  55      -0.530  26.291  14.009  1.00 47.69           C  
ANISOU 3646  C   GLU C  55     7764   2690   7665   -678   1993   -311       C  
ATOM   3647  O   GLU C  55      -0.200  27.426  14.349  1.00 49.04           O  
ANISOU 3647  O   GLU C  55     8020   2641   7973   -762   2042   -394       O  
ATOM   3648  CB  GLU C  55      -2.405  25.200  15.306  1.00 51.33           C  
ANISOU 3648  CB  GLU C  55     7873   3347   8282   -281   1983   -586       C  
ATOM   3649  CG  GLU C  55      -2.115  25.996  16.540  1.00 57.26           C  
ANISOU 3649  CG  GLU C  55     8586   4068   9103   -399   2140   -903       C  
ATOM   3650  CD  GLU C  55      -3.337  26.142  17.427  1.00 65.91           C  
ANISOU 3650  CD  GLU C  55     9508   5140  10397   -194   2191  -1115       C  
ATOM   3651  OE1 GLU C  55      -4.225  25.256  17.377  1.00 62.12           O  
ANISOU 3651  OE1 GLU C  55     8870   4817   9917    -11   2122  -1079       O  
ATOM   3652  OE2 GLU C  55      -3.400  27.151  18.162  1.00 72.07           O  
ANISOU 3652  OE2 GLU C  55    10306   5746  11330   -234   2318  -1327       O  
ATOM   3653  N   MET C  56       0.357  25.376  13.625  1.00 43.47           N  
ANISOU 3653  N   MET C  56     7210   2450   6857   -864   2044   -274       N  
ATOM   3654  CA  MET C  56       1.802  25.608  13.722  1.00 52.06           C  
ANISOU 3654  CA  MET C  56     8310   3667   7804  -1170   2162   -357       C  
ATOM   3655  C   MET C  56       2.532  25.624  12.367  1.00 53.14           C  
ANISOU 3655  C   MET C  56     8592   3833   7765  -1348   2160   -108       C  
ATOM   3656  O   MET C  56       3.748  25.833  12.311  1.00 55.58           O  
ANISOU 3656  O   MET C  56     8881   4259   7977  -1595   2263   -167       O  
ATOM   3657  CB  MET C  56       2.443  24.554  14.638  1.00 52.42           C  
ANISOU 3657  CB  MET C  56     8118   4078   7722  -1276   2236   -587       C  
ATOM   3658  CG  MET C  56       1.821  24.449  16.027  1.00 52.13           C  
ANISOU 3658  CG  MET C  56     7949   4095   7762  -1194   2244   -840       C  
ATOM   3659  SD  MET C  56       2.662  23.261  17.098  1.00 47.68           S  
ANISOU 3659  SD  MET C  56     7133   3950   7034  -1393   2241  -1030       S  
ATOM   3660  CE  MET C  56       4.179  24.168  17.420  1.00 48.71           C  
ANISOU 3660  CE  MET C  56     7281   4098   7127  -1716   2294  -1104       C  
ATOM   3661  N   GLY C  57       1.792  25.417  11.280  1.00 51.08           N  
ANISOU 3661  N   GLY C  57     8345   3436   7628   -842    184    349       N  
ATOM   3662  CA  GLY C  57       2.394  25.222   9.969  1.00 54.55           C  
ANISOU 3662  CA  GLY C  57     8746   4042   7940   -946    217    698       C  
ATOM   3663  C   GLY C  57       3.144  26.406   9.378  1.00 64.85           C  
ANISOU 3663  C   GLY C  57    10172   5088   9379  -1157    133   1003       C  
ATOM   3664  O   GLY C  57       3.819  26.273   8.357  1.00 67.97           O  
ANISOU 3664  O   GLY C  57    10515   5669   9640  -1293    171   1313       O  
ATOM   3665  N   GLY C  58       3.038  27.565  10.017  1.00 66.23           N  
ANISOU 3665  N   GLY C  58    10397   4949   9818  -1144     31    893       N  
ATOM   3666  CA  GLY C  58       3.625  28.773   9.471  1.00 72.11           C  
ANISOU 3666  CA  GLY C  58    11186   5491  10721  -1280    -14   1146       C  
ATOM   3667  C   GLY C  58       5.065  29.027   9.875  1.00 71.95           C  
ANISOU 3667  C   GLY C  58    11068   5536  10735  -1572     40   1171       C  
ATOM   3668  O   GLY C  58       5.615  30.092   9.576  1.00 74.30           O  
ANISOU 3668  O   GLY C  58    11418   5639  11172  -1709     18   1337       O  
ATOM   3669  N   HIS C  59       5.680  28.058  10.549  1.00 65.23           N  
ANISOU 3669  N   HIS C  59    10085   4959   9741  -1664    110   1004       N  
ATOM   3670  CA  HIS C  59       7.067  28.207  10.978  1.00 66.22           C  
ANISOU 3670  CA  HIS C  59    10095   5187   9878  -1917    151    999       C  
ATOM   3671  C   HIS C  59       7.756  26.859  11.199  1.00 58.45           C  
ANISOU 3671  C   HIS C  59     8962   4626   8620  -1993    248    929       C  
ATOM   3672  O   HIS C  59       7.107  25.815  11.242  1.00 57.78           O  
ANISOU 3672  O   HIS C  59     8876   4712   8367  -1852    297    826       O  
ATOM   3673  CB  HIS C  59       7.148  29.043  12.259  1.00 71.59           C  
ANISOU 3673  CB  HIS C  59    10796   5590  10814  -1932     77    704       C  
ATOM   3674  CG  HIS C  59       8.451  29.758  12.436  1.00 77.50           C  
ANISOU 3674  CG  HIS C  59    11483   6289  11674  -2191     90    761       C  
ATOM   3675  ND1 HIS C  59       8.705  30.993  11.872  1.00 84.49           N  
ANISOU 3675  ND1 HIS C  59    12472   6894  12737  -2303     70    955       N  
ATOM   3676  CD2 HIS C  59       9.574  29.421  13.115  1.00 77.65           C  
ANISOU 3676  CD2 HIS C  59    11361   6506  11638  -2361    115    648       C  
ATOM   3677  CE1 HIS C  59       9.925  31.379  12.193  1.00 85.28           C  
ANISOU 3677  CE1 HIS C  59    12485   7014  12904  -2544     92    951       C  
ATOM   3678  NE2 HIS C  59      10.475  30.443  12.947  1.00 81.02           N  
ANISOU 3678  NE2 HIS C  59    11785   6768  12232  -2574    115    762       N  
ATOM   3679  N   HIS C  60       9.081  26.904  11.319  1.00 55.74           N  
ANISOU 3679  N   HIS C  60     8498   4445   8236  -2211    288    975       N  
ATOM   3680  CA  HIS C  60       9.877  25.748  11.697  1.00 48.89           C  
ANISOU 3680  CA  HIS C  60     7485   3961   7130  -2278    371    865       C  
ATOM   3681  C   HIS C  60       9.348  25.213  13.021  1.00 44.82           C  
ANISOU 3681  C   HIS C  60     6991   3426   6613  -2152    363    517       C  
ATOM   3682  O   HIS C  60       9.030  25.984  13.924  1.00 47.94           O  
ANISOU 3682  O   HIS C  60     7449   3554   7210  -2115    278    328       O  
ATOM   3683  CB  HIS C  60      11.342  26.164  11.861  1.00 55.32           C  
ANISOU 3683  CB  HIS C  60     8183   4876   7959  -2514    383    909       C  
ATOM   3684  CG  HIS C  60      12.273  25.025  12.146  1.00 63.34           C  
ANISOU 3684  CG  HIS C  60     9043   6305   8719  -2574    460    810       C  
ATOM   3685  ND1 HIS C  60      13.287  24.658  11.281  1.00 70.54           N  
ANISOU 3685  ND1 HIS C  60     9814   7549   9439  -2694    520    990       N  
ATOM   3686  CD2 HIS C  60      12.357  24.176  13.198  1.00 61.10           C  
ANISOU 3686  CD2 HIS C  60     8716   6169   8330  -2515    485    542       C  
ATOM   3687  CE1 HIS C  60      13.942  23.628  11.786  1.00 66.28           C  
ANISOU 3687  CE1 HIS C  60     9154   7325   8703  -2695    566    824       C  
ATOM   3688  NE2 HIS C  60      13.396  23.312  12.947  1.00 59.40           N  
ANISOU 3688  NE2 HIS C  60     8346   6341   7882  -2593    552    565       N  
ATOM   3689  N   ILE C  61       9.271  23.893  13.132  1.00 39.19           N  
ANISOU 3689  N   ILE C  61     6209   3010   5672  -2081    455    428       N  
ATOM   3690  CA  ILE C  61       8.802  23.244  14.339  1.00 45.06           C  
ANISOU 3690  CA  ILE C  61     6950   3793   6376  -1963    483    130       C  
ATOM   3691  C   ILE C  61       9.907  22.344  14.870  1.00 44.74           C  
ANISOU 3691  C   ILE C  61     6767   4080   6153  -2063    552     44       C  
ATOM   3692  O   ILE C  61      10.531  21.611  14.103  1.00 40.99           O  
ANISOU 3692  O   ILE C  61     6192   3873   5510  -2118    606    182       O  
ATOM   3693  CB  ILE C  61       7.569  22.396  14.012  1.00 50.57           C  
ANISOU 3693  CB  ILE C  61     7694   4524   6997  -1764    541    101       C  
ATOM   3694  CG1 ILE C  61       6.379  23.307  13.713  1.00 57.19           C  
ANISOU 3694  CG1 ILE C  61     8682   5032   8015  -1621    461    121       C  
ATOM   3695  CG2 ILE C  61       7.244  21.416  15.132  1.00 45.54           C  
ANISOU 3695  CG2 ILE C  61     7001   4033   6269  -1668    606   -155       C  
ATOM   3696  CD1 ILE C  61       5.311  22.630  12.893  1.00 58.67           C  
ANISOU 3696  CD1 ILE C  61     8871   5301   8118  -1413    498    188       C  
ATOM   3697  N   VAL C  62      10.179  22.421  16.168  1.00 38.23           N  
ANISOU 3697  N   VAL C  62     5921   3254   5352  -2077    540   -192       N  
ATOM   3698  CA  VAL C  62      10.954  21.369  16.813  1.00 34.69           C  
ANISOU 3698  CA  VAL C  62     5352   3118   4711  -2113    609   -305       C  
ATOM   3699  C   VAL C  62       9.967  20.473  17.548  1.00 35.00           C  
ANISOU 3699  C   VAL C  62     5404   3208   4688  -1942    663   -475       C  
ATOM   3700  O   VAL C  62       9.323  20.911  18.497  1.00 32.80           O  
ANISOU 3700  O   VAL C  62     5174   2793   4494  -1862    637   -663       O  
ATOM   3701  CB  VAL C  62      11.992  21.913  17.803  1.00 39.37           C  
ANISOU 3701  CB  VAL C  62     5891   3738   5330  -2246    574   -452       C  
ATOM   3702  CG1 VAL C  62      12.792  20.757  18.416  1.00 38.28           C  
ANISOU 3702  CG1 VAL C  62     5628   3944   4973  -2268    642   -556       C  
ATOM   3703  CG2 VAL C  62      12.915  22.897  17.124  1.00 42.46           C  
ANISOU 3703  CG2 VAL C  62     6263   4046   5823  -2430    517   -284       C  
ATOM   3704  N   ALA C  63       9.827  19.230  17.094  1.00 32.84           N  
ANISOU 3704  N   ALA C  63     5069   3138   4272  -1880    729   -411       N  
ATOM   3705  CA  ALA C  63       8.973  18.256  17.772  1.00 32.03           C  
ANISOU 3705  CA  ALA C  63     4928   3136   4106  -1686    762   -526       C  
ATOM   3706  C   ALA C  63       9.764  17.538  18.868  1.00 34.89           C  
ANISOU 3706  C   ALA C  63     5192   3729   4336  -1721    785   -648       C  
ATOM   3707  O   ALA C  63      10.774  16.881  18.576  1.00 30.48           O  
ANISOU 3707  O   ALA C  63     4542   3380   3658  -1788    793   -587       O  
ATOM   3708  CB  ALA C  63       8.424  17.266  16.788  1.00 31.12           C  
ANISOU 3708  CB  ALA C  63     4765   3127   3931  -1550    781   -400       C  
ATOM   3709  N   LEU C  64       9.297  17.657  20.115  1.00 28.32           N  
ANISOU 3709  N   LEU C  64     4367   2887   3507  -1659    792   -826       N  
ATOM   3710  CA  LEU C  64      10.004  17.132  21.289  1.00 28.12           C  
ANISOU 3710  CA  LEU C  64     4252   3087   3346  -1683    807   -945       C  
ATOM   3711  C   LEU C  64       9.285  15.894  21.850  1.00 31.45           C  
ANISOU 3711  C   LEU C  64     4614   3671   3664  -1524    847   -936       C  
ATOM   3712  O   LEU C  64       8.190  16.000  22.403  1.00 32.73           O  
ANISOU 3712  O   LEU C  64     4794   3787   3854  -1418    865  -1010       O  
ATOM   3713  CB  LEU C  64      10.070  18.221  22.359  1.00 29.31           C  
ANISOU 3713  CB  LEU C  64     4427   3153   3557  -1734    778  -1163       C  
ATOM   3714  CG  LEU C  64      10.969  18.088  23.596  1.00 37.20           C  
ANISOU 3714  CG  LEU C  64     5330   4378   4424  -1787    778  -1326       C  
ATOM   3715  CD1 LEU C  64      12.399  17.755  23.219  1.00 38.26           C  
ANISOU 3715  CD1 LEU C  64     5396   4671   4471  -1933    774  -1251       C  
ATOM   3716  CD2 LEU C  64      10.953  19.374  24.402  1.00 34.01           C  
ANISOU 3716  CD2 LEU C  64     4953   3839   4129  -1836    726  -1569       C  
ATOM   3717  N   CYS C  65       9.904  14.726  21.707  1.00 26.63           N  
ANISOU 3717  N   CYS C  65     3926   3251   2939  -1510    851   -843       N  
ATOM   3718  CA  CYS C  65       9.305  13.472  22.163  1.00 23.83           C  
ANISOU 3718  CA  CYS C  65     3520   3017   2517  -1384    871   -790       C  
ATOM   3719  C   CYS C  65       9.625  13.226  23.633  1.00 29.51           C  
ANISOU 3719  C   CYS C  65     4180   3929   3102  -1380    885   -881       C  
ATOM   3720  O   CYS C  65      10.796  13.225  24.026  1.00 29.73           O  
ANISOU 3720  O   CYS C  65     4162   4101   3033  -1450    863   -929       O  
ATOM   3721  CB  CYS C  65       9.840  12.311  21.313  1.00 25.32           C  
ANISOU 3721  CB  CYS C  65     3654   3294   2672  -1353    838   -661       C  
ATOM   3722  SG  CYS C  65       9.247  10.693  21.840  1.00 30.66           S  
ANISOU 3722  SG  CYS C  65     4274   4064   3313  -1223    832   -571       S  
ATOM   3723  N   VAL C  66       8.594  13.044  24.457  1.00 29.07           N  
ANISOU 3723  N   VAL C  66     4111   3913   3022  -1295    923   -908       N  
ATOM   3724  CA  VAL C  66       8.817  12.695  25.855  1.00 28.96           C  
ANISOU 3724  CA  VAL C  66     4020   4139   2845  -1275    940   -960       C  
ATOM   3725  C   VAL C  66       8.903  11.172  26.004  1.00 31.51           C  
ANISOU 3725  C   VAL C  66     4291   4591   3089  -1221    933   -772       C  
ATOM   3726  O   VAL C  66       7.882  10.484  26.061  1.00 28.36           O  
ANISOU 3726  O   VAL C  66     3880   4177   2720  -1160    960   -661       O  
ATOM   3727  CB  VAL C  66       7.720  13.262  26.779  1.00 31.65           C  
ANISOU 3727  CB  VAL C  66     4338   4529   3158  -1213    984  -1085       C  
ATOM   3728  CG1 VAL C  66       8.087  13.025  28.250  1.00 34.48           C  
ANISOU 3728  CG1 VAL C  66     4594   5197   3308  -1195   1001  -1152       C  
ATOM   3729  CG2 VAL C  66       7.520  14.770  26.529  1.00 31.49           C  
ANISOU 3729  CG2 VAL C  66     4385   4312   3268  -1240    959  -1282       C  
ATOM   3730  N   LEU C  67      10.132  10.657  26.041  1.00 34.03           N  
ANISOU 3730  N   LEU C  67     4577   5027   3325  -1246    885   -741       N  
ATOM   3731  CA  LEU C  67      10.380   9.220  26.199  1.00 31.73           C  
ANISOU 3731  CA  LEU C  67     4246   4832   2979  -1181    844   -572       C  
ATOM   3732  C   LEU C  67       9.978   8.773  27.606  1.00 30.69           C  
ANISOU 3732  C   LEU C  67     4058   4900   2701  -1141    877   -513       C  
ATOM   3733  O   LEU C  67       9.949   9.602  28.526  1.00 29.58           O  
ANISOU 3733  O   LEU C  67     3884   4905   2450  -1158    920   -655       O  
ATOM   3734  CB  LEU C  67      11.869   8.940  25.973  1.00 36.27           C  
ANISOU 3734  CB  LEU C  67     4786   5515   3479  -1199    773   -598       C  
ATOM   3735  CG  LEU C  67      12.387   9.238  24.576  1.00 37.92           C  
ANISOU 3735  CG  LEU C  67     5015   5607   3788  -1243    739   -628       C  
ATOM   3736  CD1 LEU C  67      13.869   8.947  24.485  1.00 41.86           C  
ANISOU 3736  CD1 LEU C  67     5445   6283   4177  -1258    672   -675       C  
ATOM   3737  CD2 LEU C  67      11.616   8.412  23.578  1.00 31.74           C  
ANISOU 3737  CD2 LEU C  67     4252   4663   3143  -1166    712   -505       C  
ATOM   3738  N   LYS C  68       9.657   7.489  27.799  1.00 29.63           N  
ANISOU 3738  N   LYS C  68     3906   4785   2568  -1087    851   -306       N  
ATOM   3739  CA  LYS C  68       9.611   6.486  26.721  1.00 31.78           C  
ANISOU 3739  CA  LYS C  68     4207   4866   3001  -1050    779   -176       C  
ATOM   3740  C   LYS C  68       8.214   6.340  26.134  1.00 30.08           C  
ANISOU 3740  C   LYS C  68     4013   4467   2949  -1047    819   -112       C  
ATOM   3741  O   LYS C  68       8.055   6.084  24.928  1.00 31.10           O  
ANISOU 3741  O   LYS C  68     4167   4412   3235  -1024    776   -110       O  
ATOM   3742  CB  LYS C  68      10.055   5.120  27.258  1.00 34.31           C  
ANISOU 3742  CB  LYS C  68     4499   5264   3274   -991    697     10       C  
ATOM   3743  CG  LYS C  68      11.473   5.096  27.813  1.00 38.43           C  
ANISOU 3743  CG  LYS C  68     4988   5990   3625   -964    639    -49       C  
ATOM   3744  CD  LYS C  68      12.033   3.678  27.871  1.00 41.39           C  
ANISOU 3744  CD  LYS C  68     5356   6355   4018   -871    510    120       C  
ATOM   3745  CE  LYS C  68      12.141   3.178  29.291  1.00 47.87           C  
ANISOU 3745  CE  LYS C  68     6142   7389   4659   -842    508    276       C  
ATOM   3746  NZ  LYS C  68      12.695   1.790  29.338  1.00 48.92           N  
ANISOU 3746  NZ  LYS C  68     6283   7469   4834   -738    357    459       N  
ATOM   3747  N   GLY C  69       7.206   6.492  26.990  1.00 26.01           N  
ANISOU 3747  N   GLY C  69     3465   4039   2378  -1063    899    -72       N  
ATOM   3748  CA  GLY C  69       5.823   6.241  26.604  1.00 29.92           C  
ANISOU 3748  CA  GLY C  69     3952   4410   3006  -1063    940     -3       C  
ATOM   3749  C   GLY C  69       5.361   7.075  25.419  1.00 25.59           C  
ANISOU 3749  C   GLY C  69     3454   3672   2598  -1050    953   -147       C  
ATOM   3750  O   GLY C  69       4.441   6.695  24.688  1.00 29.62           O  
ANISOU 3750  O   GLY C  69     3960   4040   3254  -1029    952   -101       O  
ATOM   3751  N   GLY C  70       6.003   8.214  25.207  1.00 24.72           N  
ANISOU 3751  N   GLY C  70     3387   3555   2450  -1065    957   -314       N  
ATOM   3752  CA  GLY C  70       5.632   9.056  24.081  1.00 28.08           C  
ANISOU 3752  CA  GLY C  70     3870   3798   3002  -1055    960   -414       C  
ATOM   3753  C   GLY C  70       6.060   8.565  22.710  1.00 30.61           C  
ANISOU 3753  C   GLY C  70     4210   3984   3435  -1033    891   -364       C  
ATOM   3754  O   GLY C  70       5.596   9.097  21.701  1.00 23.99           O  
ANISOU 3754  O   GLY C  70     3406   3014   2696  -1010    892   -406       O  
ATOM   3755  N   TYR C  71       6.923   7.551  22.650  1.00 26.50           N  
ANISOU 3755  N   TYR C  71     3658   3517   2894  -1020    821   -284       N  
ATOM   3756  CA  TYR C  71       7.604   7.252  21.387  1.00 24.48           C  
ANISOU 3756  CA  TYR C  71     3395   3205   2701   -989    745   -294       C  
ATOM   3757  C   TYR C  71       6.694   6.820  20.235  1.00 22.85           C  
ANISOU 3757  C   TYR C  71     3176   2857   2651   -920    719   -272       C  
ATOM   3758  O   TYR C  71       6.931   7.209  19.087  1.00 24.33           O  
ANISOU 3758  O   TYR C  71     3363   3014   2868   -899    696   -320       O  
ATOM   3759  CB  TYR C  71       8.777   6.269  21.576  1.00 32.31           C  
ANISOU 3759  CB  TYR C  71     4342   4302   3632   -960    653   -254       C  
ATOM   3760  CG  TYR C  71       8.506   4.847  21.112  1.00 32.88           C  
ANISOU 3760  CG  TYR C  71     4375   4287   3833   -869    556   -169       C  
ATOM   3761  CD1 TYR C  71       8.693   4.472  19.782  1.00 33.45           C  
ANISOU 3761  CD1 TYR C  71     4407   4305   3997   -795    476   -225       C  
ATOM   3762  CD2 TYR C  71       8.094   3.875  22.019  1.00 29.80           C  
ANISOU 3762  CD2 TYR C  71     3975   3875   3473   -858    533    -35       C  
ATOM   3763  CE1 TYR C  71       8.437   3.166  19.364  1.00 34.98           C  
ANISOU 3763  CE1 TYR C  71     4554   4398   4338   -700    362   -189       C  
ATOM   3764  CE2 TYR C  71       7.843   2.574  21.619  1.00 29.36           C  
ANISOU 3764  CE2 TYR C  71     3889   3689   3578   -788    422     44       C  
ATOM   3765  CZ  TYR C  71       8.015   2.229  20.288  1.00 28.83           C  
ANISOU 3765  CZ  TYR C  71     3784   3543   3627   -703    330    -55       C  
ATOM   3766  OH  TYR C  71       7.762   0.932  19.887  1.00 27.58           O  
ANISOU 3766  OH  TYR C  71     3586   3236   3658   -621    198    -17       O  
ATOM   3767  N   LYS C  72       5.670   6.018  20.516  1.00 23.95           N  
ANISOU 3767  N   LYS C  72     3288   2930   2881   -890    722   -197       N  
ATOM   3768  CA  LYS C  72       4.790   5.553  19.428  1.00 26.98           C  
ANISOU 3768  CA  LYS C  72     3638   3189   3423   -821    688   -204       C  
ATOM   3769  C   LYS C  72       3.913   6.666  18.865  1.00 27.23           C  
ANISOU 3769  C   LYS C  72     3704   3166   3478   -808    758   -280       C  
ATOM   3770  O   LYS C  72       3.828   6.854  17.647  1.00 24.24           O  
ANISOU 3770  O   LYS C  72     3315   2743   3153   -748    725   -326       O  
ATOM   3771  CB  LYS C  72       3.912   4.384  19.885  1.00 25.93           C  
ANISOU 3771  CB  LYS C  72     3456   2989   3407   -820    667   -100       C  
ATOM   3772  CG  LYS C  72       4.571   3.029  19.760  1.00 39.63           C  
ANISOU 3772  CG  LYS C  72     5153   4677   5228   -778    535    -36       C  
ATOM   3773  CD  LYS C  72       5.033   2.780  18.344  1.00 43.15           C  
ANISOU 3773  CD  LYS C  72     5559   5085   5750   -676    433   -152       C  
ATOM   3774  CE  LYS C  72       3.864   2.513  17.429  1.00 50.35           C  
ANISOU 3774  CE  LYS C  72     6419   5883   6829   -624    419   -204       C  
ATOM   3775  NZ  LYS C  72       4.318   2.210  16.041  1.00 53.92           N  
ANISOU 3775  NZ  LYS C  72     6804   6348   7334   -503    310   -334       N  
ATOM   3776  N   PHE C  73       3.229   7.375  19.754  1.00 25.28           N  
ANISOU 3776  N   PHE C  73     3484   2940   3182   -848    845   -297       N  
ATOM   3777  CA  PHE C  73       2.447   8.547  19.366  1.00 26.72           C  
ANISOU 3777  CA  PHE C  73     3709   3061   3382   -818    895   -386       C  
ATOM   3778  C   PHE C  73       3.286   9.537  18.563  1.00 25.98           C  
ANISOU 3778  C   PHE C  73     3683   2928   3262   -828    872   -429       C  
ATOM   3779  O   PHE C  73       2.842  10.070  17.535  1.00 23.62           O  
ANISOU 3779  O   PHE C  73     3408   2547   3021   -771    862   -449       O  
ATOM   3780  CB  PHE C  73       1.871   9.216  20.613  1.00 25.54           C  
ANISOU 3780  CB  PHE C  73     3568   2981   3156   -847    972   -438       C  
ATOM   3781  CG  PHE C  73       0.906  10.330  20.321  1.00 25.85           C  
ANISOU 3781  CG  PHE C  73     3643   2947   3233   -786   1004   -551       C  
ATOM   3782  CD1 PHE C  73      -0.121  10.165  19.387  1.00 25.45           C  
ANISOU 3782  CD1 PHE C  73     3564   2817   3287   -701    995   -560       C  
ATOM   3783  CD2 PHE C  73       1.009  11.537  20.998  1.00 24.20           C  
ANISOU 3783  CD2 PHE C  73     3487   2746   2963   -796   1027   -668       C  
ATOM   3784  CE1 PHE C  73      -1.029  11.204  19.136  1.00 24.69           C  
ANISOU 3784  CE1 PHE C  73     3503   2658   3222   -618   1010   -669       C  
ATOM   3785  CE2 PHE C  73       0.111  12.583  20.753  1.00 26.70           C  
ANISOU 3785  CE2 PHE C  73     3843   2970   3334   -714   1030   -787       C  
ATOM   3786  CZ  PHE C  73      -0.910  12.411  19.821  1.00 24.75           C  
ANISOU 3786  CZ  PHE C  73     3575   2650   3178   -620   1023   -779       C  
ATOM   3787  N   PHE C  74       4.504   9.781  19.037  1.00 23.85           N  
ANISOU 3787  N   PHE C  74     3435   2730   2897   -906    863   -430       N  
ATOM   3788  CA  PHE C  74       5.400  10.725  18.394  1.00 20.84           C  
ANISOU 3788  CA  PHE C  74     3102   2329   2485   -960    845   -449       C  
ATOM   3789  C   PHE C  74       5.716  10.294  16.973  1.00 25.28           C  
ANISOU 3789  C   PHE C  74     3623   2909   3075   -912    791   -399       C  
ATOM   3790  O   PHE C  74       5.602  11.090  16.042  1.00 24.14           O  
ANISOU 3790  O   PHE C  74     3513   2708   2952   -907    789   -381       O  
ATOM   3791  CB  PHE C  74       6.663  10.859  19.241  1.00 23.47           C  
ANISOU 3791  CB  PHE C  74     3432   2777   2707  -1060    842   -472       C  
ATOM   3792  CG  PHE C  74       7.736  11.713  18.634  1.00 28.68           C  
ANISOU 3792  CG  PHE C  74     4117   3447   3334  -1154    823   -478       C  
ATOM   3793  CD1 PHE C  74       7.728  13.091  18.803  1.00 29.61           C  
ANISOU 3793  CD1 PHE C  74     4314   3451   3485  -1234    844   -532       C  
ATOM   3794  CD2 PHE C  74       8.781  11.131  17.943  1.00 24.96           C  
ANISOU 3794  CD2 PHE C  74     3577   3106   2802  -1170    776   -437       C  
ATOM   3795  CE1 PHE C  74       8.739  13.878  18.284  1.00 31.58           C  
ANISOU 3795  CE1 PHE C  74     4579   3699   3719  -1359    826   -510       C  
ATOM   3796  CE2 PHE C  74       9.793  11.911  17.403  1.00 28.31           C  
ANISOU 3796  CE2 PHE C  74     3998   3582   3176  -1284    768   -426       C  
ATOM   3797  CZ  PHE C  74       9.772  13.283  17.580  1.00 29.57           C  
ANISOU 3797  CZ  PHE C  74     4243   3612   3381  -1395    797   -445       C  
ATOM   3798  N   ALA C  75       6.115   9.033  16.805  1.00 21.87           N  
ANISOU 3798  N   ALA C  75     3108   2564   2639   -867    734   -377       N  
ATOM   3799  CA  ALA C  75       6.519   8.527  15.497  1.00 22.34           C  
ANISOU 3799  CA  ALA C  75     3093   2693   2703   -798    665   -373       C  
ATOM   3800  C   ALA C  75       5.352   8.604  14.524  1.00 24.69           C  
ANISOU 3800  C   ALA C  75     3378   2910   3092   -698    665   -379       C  
ATOM   3801  O   ALA C  75       5.506   9.059  13.379  1.00 22.67           O  
ANISOU 3801  O   ALA C  75     3101   2708   2804   -666    648   -364       O  
ATOM   3802  CB  ALA C  75       7.015   7.091  15.608  1.00 26.19           C  
ANISOU 3802  CB  ALA C  75     3492   3253   3205   -736    579   -386       C  
ATOM   3803  N   ASP C  76       4.192   8.151  14.979  1.00 20.82           N  
ANISOU 3803  N   ASP C  76     2885   2323   2701   -652    684   -394       N  
ATOM   3804  CA  ASP C  76       2.981   8.162  14.162  1.00 26.00           C  
ANISOU 3804  CA  ASP C  76     3514   2917   3448   -549    683   -424       C  
ATOM   3805  C   ASP C  76       2.473   9.559  13.844  1.00 22.75           C  
ANISOU 3805  C   ASP C  76     3189   2440   3016   -544    735   -418       C  
ATOM   3806  O   ASP C  76       2.131   9.833  12.697  1.00 24.47           O  
ANISOU 3806  O   ASP C  76     3385   2671   3241   -458    710   -415       O  
ATOM   3807  CB  ASP C  76       1.872   7.318  14.810  1.00 26.96           C  
ANISOU 3807  CB  ASP C  76     3593   2970   3682   -527    694   -440       C  
ATOM   3808  CG  ASP C  76       2.184   5.835  14.779  1.00 31.59           C  
ANISOU 3808  CG  ASP C  76     4089   3564   4349   -504    606   -436       C  
ATOM   3809  OD1 ASP C  76       2.978   5.442  13.905  1.00 31.97           O  
ANISOU 3809  OD1 ASP C  76     4082   3682   4382   -444    522   -473       O  
ATOM   3810  OD2 ASP C  76       1.642   5.063  15.609  1.00 26.68           O  
ANISOU 3810  OD2 ASP C  76     3443   2886   3809   -543    610   -394       O  
ATOM   3811  N   LEU C  77       2.400  10.432  14.848  1.00 21.00           N  
ANISOU 3811  N   LEU C  77     3059   2150   2772   -621    793   -425       N  
ATOM   3812  CA  LEU C  77       1.967  11.809  14.634  1.00 22.82           C  
ANISOU 3812  CA  LEU C  77     3386   2272   3013   -609    815   -433       C  
ATOM   3813  C   LEU C  77       2.869  12.471  13.607  1.00 25.20           C  
ANISOU 3813  C   LEU C  77     3719   2590   3265   -648    783   -346       C  
ATOM   3814  O   LEU C  77       2.393  13.125  12.679  1.00 25.93           O  
ANISOU 3814  O   LEU C  77     3844   2630   3379   -579    766   -301       O  
ATOM   3815  CB  LEU C  77       1.998  12.610  15.932  1.00 24.48           C  
ANISOU 3815  CB  LEU C  77     3673   2420   3208   -686    857   -492       C  
ATOM   3816  CG  LEU C  77       1.599  14.087  15.824  1.00 27.55           C  
ANISOU 3816  CG  LEU C  77     4174   2651   3645   -666    850   -527       C  
ATOM   3817  CD1 LEU C  77       0.135  14.232  15.420  1.00 24.64           C  
ANISOU 3817  CD1 LEU C  77     3797   2221   3344   -511    849   -581       C  
ATOM   3818  CD2 LEU C  77       1.855  14.818  17.150  1.00 29.47           C  
ANISOU 3818  CD2 LEU C  77     4469   2855   3872   -742    869   -630       C  
ATOM   3819  N   LEU C  78       4.179  12.300  13.769  1.00 23.75           N  
ANISOU 3819  N   LEU C  78     3515   2506   3002   -760    773   -310       N  
ATOM   3820  CA  LEU C  78       5.120  12.873  12.810  1.00 23.82           C  
ANISOU 3820  CA  LEU C  78     3524   2586   2942   -827    751   -210       C  
ATOM   3821  C   LEU C  78       4.957  12.280  11.406  1.00 24.22           C  
ANISOU 3821  C   LEU C  78     3469   2779   2956   -707    709   -171       C  
ATOM   3822  O   LEU C  78       5.104  12.985  10.418  1.00 23.98           O  
ANISOU 3822  O   LEU C  78     3447   2784   2879   -712    699    -64       O  
ATOM   3823  CB  LEU C  78       6.557  12.725  13.299  1.00 26.34           C  
ANISOU 3823  CB  LEU C  78     3810   3030   3169   -968    748   -206       C  
ATOM   3824  CG  LEU C  78       7.075  13.995  13.968  1.00 35.30           C  
ANISOU 3824  CG  LEU C  78     5049   4046   4317  -1127    774   -194       C  
ATOM   3825  CD1 LEU C  78       6.275  14.344  15.216  1.00 36.84           C  
ANISOU 3825  CD1 LEU C  78     5325   4081   4591  -1106    801   -305       C  
ATOM   3826  CD2 LEU C  78       8.541  13.860  14.294  1.00 40.91           C  
ANISOU 3826  CD2 LEU C  78     5700   4920   4922  -1269    769   -196       C  
ATOM   3827  N   ASP C  79       4.669  10.982  11.319  1.00 24.02           N  
ANISOU 3827  N   ASP C  79     3335   2840   2952   -601    675   -254       N  
ATOM   3828  CA  ASP C  79       4.434  10.378  10.016  1.00 22.78           C  
ANISOU 3828  CA  ASP C  79     3055   2828   2771   -462    620   -270       C  
ATOM   3829  C   ASP C  79       3.221  10.995   9.306  1.00 23.07           C  
ANISOU 3829  C   ASP C  79     3126   2785   2854   -351    629   -246       C  
ATOM   3830  O   ASP C  79       3.254  11.201   8.101  1.00 22.00           O  
ANISOU 3830  O   ASP C  79     2928   2787   2642   -276    601   -191       O  
ATOM   3831  CB  ASP C  79       4.304   8.846  10.118  1.00 28.50           C  
ANISOU 3831  CB  ASP C  79     3659   3609   3560   -368    556   -392       C  
ATOM   3832  CG  ASP C  79       5.655   8.149  10.145  1.00 32.90           C  
ANISOU 3832  CG  ASP C  79     4131   4336   4033   -402    500   -420       C  
ATOM   3833  OD1 ASP C  79       6.671   8.813   9.847  1.00 35.99           O  
ANISOU 3833  OD1 ASP C  79     4520   4864   4290   -492    517   -350       O  
ATOM   3834  OD2 ASP C  79       5.698   6.936  10.441  1.00 38.65           O  
ANISOU 3834  OD2 ASP C  79     4787   5061   4836   -339    431   -511       O  
ATOM   3835  N   TYR C  80       2.158  11.279  10.047  1.00 21.90           N  
ANISOU 3835  N   TYR C  80     3060   2451   2811   -329    666   -292       N  
ATOM   3836  CA  TYR C  80       0.994  11.943   9.463  1.00 22.07           C  
ANISOU 3836  CA  TYR C  80     3119   2394   2874   -209    667   -287       C  
ATOM   3837  C   TYR C  80       1.293  13.396   9.062  1.00 23.12           C  
ANISOU 3837  C   TYR C  80     3375   2445   2963   -260    673   -142       C  
ATOM   3838  O   TYR C  80       0.846  13.862   8.004  1.00 23.66           O  
ANISOU 3838  O   TYR C  80     3439   2549   3001   -154    645    -67       O  
ATOM   3839  CB  TYR C  80      -0.210  11.870  10.416  1.00 23.94           C  
ANISOU 3839  CB  TYR C  80     3388   2489   3220   -169    702   -395       C  
ATOM   3840  CG  TYR C  80      -0.931  10.533  10.386  1.00 26.29           C  
ANISOU 3840  CG  TYR C  80     3547   2851   3590    -88    683   -507       C  
ATOM   3841  CD1 TYR C  80      -1.609  10.118   9.246  1.00 27.01           C  
ANISOU 3841  CD1 TYR C  80     3530   3033   3700     65    636   -562       C  
ATOM   3842  CD2 TYR C  80      -0.938   9.690  11.496  1.00 24.30           C  
ANISOU 3842  CD2 TYR C  80     3267   2572   3395   -169    705   -550       C  
ATOM   3843  CE1 TYR C  80      -2.284   8.895   9.206  1.00 31.03           C  
ANISOU 3843  CE1 TYR C  80     3904   3575   4311    124    604   -681       C  
ATOM   3844  CE2 TYR C  80      -1.612   8.452  11.468  1.00 26.49           C  
ANISOU 3844  CE2 TYR C  80     3420   2871   3774   -122    675   -628       C  
ATOM   3845  CZ  TYR C  80      -2.276   8.069  10.316  1.00 28.49           C  
ANISOU 3845  CZ  TYR C  80     3566   3185   4072     19    622   -704       C  
ATOM   3846  OH  TYR C  80      -2.952   6.866  10.278  1.00 29.31           O  
ANISOU 3846  OH  TYR C  80     3540   3286   4309     51    580   -797       O  
ATOM   3847  N   ILE C  81       2.065  14.112   9.882  1.00 23.48           N  
ANISOU 3847  N   ILE C  81     3527   2383   3012   -424    698    -94       N  
ATOM   3848  CA  ILE C  81       2.515  15.469   9.490  1.00 24.67           C  
ANISOU 3848  CA  ILE C  81     3794   2426   3153   -513    687     65       C  
ATOM   3849  C   ILE C  81       3.356  15.441   8.212  1.00 26.24           C  
ANISOU 3849  C   ILE C  81     3909   2844   3217   -545    666    229       C  
ATOM   3850  O   ILE C  81       3.191  16.275   7.304  1.00 26.05           O  
ANISOU 3850  O   ILE C  81     3931   2800   3169   -520    642    394       O  
ATOM   3851  CB  ILE C  81       3.295  16.158  10.636  1.00 27.14           C  
ANISOU 3851  CB  ILE C  81     4209   2593   3508   -702    707     52       C  
ATOM   3852  CG1 ILE C  81       2.355  16.428  11.808  1.00 26.11           C  
ANISOU 3852  CG1 ILE C  81     4155   2277   3489   -645    720   -110       C  
ATOM   3853  CG2 ILE C  81       3.928  17.465  10.163  1.00 29.01           C  
ANISOU 3853  CG2 ILE C  81     4551   2710   3761   -835    681    233       C  
ATOM   3854  CD1 ILE C  81       3.074  16.912  13.108  1.00 26.40           C  
ANISOU 3854  CD1 ILE C  81     4256   2223   3554   -803    736   -187       C  
ATOM   3855  N   LYS C  82       4.263  14.476   8.135  1.00 25.36           N  
ANISOU 3855  N   LYS C  82     3664   2966   3008   -590    668    189       N  
ATOM   3856  CA  LYS C  82       5.100  14.328   6.954  1.00 27.26           C  
ANISOU 3856  CA  LYS C  82     3778   3494   3086   -606    648    308       C  
ATOM   3857  C   LYS C  82       4.261  14.044   5.712  1.00 27.84           C  
ANISOU 3857  C   LYS C  82     3757   3715   3105   -399    612    320       C  
ATOM   3858  O   LYS C  82       4.547  14.556   4.633  1.00 26.44           O  
ANISOU 3858  O   LYS C  82     3536   3707   2802   -398    600    494       O  
ATOM   3859  CB  LYS C  82       6.143  13.233   7.177  1.00 29.21           C  
ANISOU 3859  CB  LYS C  82     3882   3973   3245   -647    637    202       C  
ATOM   3860  CG  LYS C  82       7.304  13.686   8.051  1.00 33.92           C  
ANISOU 3860  CG  LYS C  82     4533   4533   3822   -870    668    238       C  
ATOM   3861  CD  LYS C  82       7.896  12.533   8.826  1.00 39.18           C  
ANISOU 3861  CD  LYS C  82     5115   5298   4474   -863    651     72       C  
ATOM   3862  CE  LYS C  82       8.384  11.443   7.894  1.00 43.63           C  
ANISOU 3862  CE  LYS C  82     5477   6188   4915   -743    591      4       C  
ATOM   3863  NZ  LYS C  82       8.748  10.225   8.670  1.00 48.59           N  
ANISOU 3863  NZ  LYS C  82     6041   6844   5576   -693    546   -165       N  
ATOM   3864  N   ALA C  83       3.200  13.255   5.880  1.00 23.76           N  
ANISOU 3864  N   ALA C  83     3200   3146   2681   -230    594    143       N  
ATOM   3865  CA  ALA C  83       2.314  12.929   4.750  1.00 27.27           C  
ANISOU 3865  CA  ALA C  83     3537   3737   3087    -17    553    108       C  
ATOM   3866  C   ALA C  83       1.637  14.202   4.254  1.00 28.17           C  
ANISOU 3866  C   ALA C  83     3776   3723   3203     28    555    278       C  
ATOM   3867  O   ALA C  83       1.514  14.427   3.056  1.00 29.15           O  
ANISOU 3867  O   ALA C  83     3826   4044   3204    133    525    389       O  
ATOM   3868  CB  ALA C  83       1.276  11.881   5.158  1.00 22.82           C  
ANISOU 3868  CB  ALA C  83     2910   3106   2656    121    533   -121       C  
ATOM   3869  N   LEU C  84       1.216  15.043   5.190  1.00 25.71           N  
ANISOU 3869  N   LEU C  84     3649   3091   3028    -41    578    295       N  
ATOM   3870  CA  LEU C  84       0.696  16.361   4.842  1.00 29.27           C  
ANISOU 3870  CA  LEU C  84     4248   3358   3514     -9    557    461       C  
ATOM   3871  C   LEU C  84       1.728  17.199   4.093  1.00 33.67           C  
ANISOU 3871  C   LEU C  84     4836   3998   3960   -154    549    747       C  
ATOM   3872  O   LEU C  84       1.431  17.815   3.058  1.00 31.93           O  
ANISOU 3872  O   LEU C  84     4627   3839   3667    -70    514    939       O  
ATOM   3873  CB  LEU C  84       0.260  17.093   6.101  1.00 29.23           C  
ANISOU 3873  CB  LEU C  84     4421   3001   3683    -68    566    385       C  
ATOM   3874  CG  LEU C  84      -0.958  16.474   6.784  1.00 32.66           C  
ANISOU 3874  CG  LEU C  84     4824   3373   4214     80    577    139       C  
ATOM   3875  CD1 LEU C  84      -1.297  17.262   8.043  1.00 33.48           C  
ANISOU 3875  CD1 LEU C  84     5078   3190   4454     26    584     52       C  
ATOM   3876  CD2 LEU C  84      -2.150  16.450   5.833  1.00 34.10           C  
ANISOU 3876  CD2 LEU C  84     4950   3628   4379    320    537    113       C  
ATOM   3877  N   ASN C  85       2.944  17.217   4.622  1.00 29.29           N  
ANISOU 3877  N   ASN C  85     4284   3462   3382   -379    582    789       N  
ATOM   3878  CA  ASN C  85       4.006  18.048   4.067  1.00 31.36           C  
ANISOU 3878  CA  ASN C  85     4568   3795   3552   -573    584   1067       C  
ATOM   3879  C   ASN C  85       4.399  17.694   2.642  1.00 32.42           C  
ANISOU 3879  C   ASN C  85     4516   4351   3451   -513    577   1217       C  
ATOM   3880  O   ASN C  85       4.883  18.550   1.897  1.00 40.08           O  
ANISOU 3880  O   ASN C  85     5507   5392   4331   -625    571   1513       O  
ATOM   3881  CB  ASN C  85       5.247  17.970   4.955  1.00 34.94           C  
ANISOU 3881  CB  ASN C  85     5019   4244   4013   -818    622   1029       C  
ATOM   3882  CG  ASN C  85       5.127  18.819   6.199  1.00 42.46           C  
ANISOU 3882  CG  ASN C  85     6169   4791   5173   -937    619    973       C  
ATOM   3883  OD1 ASN C  85       4.406  19.811   6.212  1.00 44.86           O  
ANISOU 3883  OD1 ASN C  85     6632   4803   5612   -896    577   1051       O  
ATOM   3884  ND2 ASN C  85       5.847  18.441   7.249  1.00 43.53           N  
ANISOU 3884  ND2 ASN C  85     6287   4922   5331  -1068    651    825       N  
ATOM   3885  N   ARG C  86       4.246  16.430   2.269  1.00 42.90           N  
ANISOU 3885  N   ARG C  86     6441   4762   5095   -504   -183    746       N  
ATOM   3886  CA  ARG C  86       4.704  16.006   0.945  1.00 43.25           C  
ANISOU 3886  CA  ARG C  86     6542   5003   4889   -956   -142    898       C  
ATOM   3887  C   ARG C  86       3.578  15.913  -0.064  1.00 45.49           C  
ANISOU 3887  C   ARG C  86     6809   5402   5072   -751   -403   1013       C  
ATOM   3888  O   ARG C  86       3.805  15.534  -1.213  1.00 46.14           O  
ANISOU 3888  O   ARG C  86     6925   5687   4919  -1118   -383   1131       O  
ATOM   3889  CB  ARG C  86       5.471  14.684   1.009  1.00 39.20           C  
ANISOU 3889  CB  ARG C  86     5563   4905   4428  -1292    262    733       C  
ATOM   3890  CG  ARG C  86       4.661  13.525   1.542  1.00 36.20           C  
ANISOU 3890  CG  ARG C  86     4613   4869   4271   -967    426    533       C  
ATOM   3891  CD  ARG C  86       5.404  12.217   1.389  1.00 32.98           C  
ANISOU 3891  CD  ARG C  86     3791   4822   3917  -1314    778    403       C  
ATOM   3892  NE  ARG C  86       4.562  11.131   1.853  1.00 30.60           N  
ANISOU 3892  NE  ARG C  86     3005   4812   3811  -1020    926    234       N  
ATOM   3893  CZ  ARG C  86       4.638  10.604   3.069  1.00 32.14           C  
ANISOU 3893  CZ  ARG C  86     2954   5047   4210   -858   1097     82       C  
ATOM   3894  NH1 ARG C  86       5.549  11.047   3.924  1.00 28.61           N  
ANISOU 3894  NH1 ARG C  86     2670   4394   3807   -951   1128     72       N  
ATOM   3895  NH2 ARG C  86       3.820   9.627   3.421  1.00 28.43           N  
ANISOU 3895  NH2 ARG C  86     2134   4784   3883   -609   1205    -45       N  
ATOM   3896  N   ASN C  87       2.371  16.273   0.356  1.00 47.02           N  
ANISOU 3896  N   ASN C  87     6937   5484   5443   -180   -650    950       N  
ATOM   3897  CA  ASN C  87       1.231  16.298  -0.553  1.00 49.84           C  
ANISOU 3897  CA  ASN C  87     7276   5929   5731     82   -969   1039       C  
ATOM   3898  C   ASN C  87       0.544  17.654  -0.609  1.00 56.34           C  
ANISOU 3898  C   ASN C  87     8552   6264   6590    482  -1466   1183       C  
ATOM   3899  O   ASN C  87      -0.543  17.789  -1.173  1.00 60.31           O  
ANISOU 3899  O   ASN C  87     9015   6792   7108    833  -1807   1219       O  
ATOM   3900  CB  ASN C  87       0.226  15.199  -0.196  1.00 51.08           C  
ANISOU 3900  CB  ASN C  87     6790   6518   6100    417   -807    760       C  
ATOM   3901  CG  ASN C  87       0.781  13.806  -0.438  1.00 45.84           C  
ANISOU 3901  CG  ASN C  87     5709   6320   5388     21   -381    659       C  
ATOM   3902  OD1 ASN C  87       0.983  13.405  -1.582  1.00 43.75           O  
ANISOU 3902  OD1 ASN C  87     5458   6267   4898   -321   -372    778       O  
ATOM   3903  ND2 ASN C  87       1.028  13.065   0.636  1.00 43.57           N  
ANISOU 3903  ND2 ASN C  87     5061   6182   5311     55    -36    433       N  
ATOM   3904  N   SER C  88       1.190  18.660  -0.034  1.00 56.27           N  
ANISOU 3904  N   SER C  88     8969   5801   6611    433  -1523   1252       N  
ATOM   3905  CA  SER C  88       0.640  20.010  -0.033  1.00 64.65           C  
ANISOU 3905  CA  SER C  88    10504   6317   7745    802  -1993   1382       C  
ATOM   3906  C   SER C  88       1.621  20.971  -0.689  1.00 68.25           C  
ANISOU 3906  C   SER C  88    11682   6350   7902    340  -2143   1722       C  
ATOM   3907  O   SER C  88       2.809  20.666  -0.794  1.00 65.25           O  
ANISOU 3907  O   SER C  88    11377   6090   7325   -235  -1811   1759       O  
ATOM   3908  CB  SER C  88       0.328  20.458   1.396  1.00 65.62           C  
ANISOU 3908  CB  SER C  88    10481   6223   8229   1233  -1935   1092       C  
ATOM   3909  OG  SER C  88      -0.502  19.513   2.055  1.00 62.70           O  
ANISOU 3909  OG  SER C  88     9455   6273   8095   1566  -1730    754       O  
ATOM   3910  N   ASP C  89       1.117  22.115  -1.141  1.00 76.90           N  
ANISOU 3910  N   ASP C  89    13305   6945   8968    584  -2648   1953       N  
ATOM   3911  CA  ASP C  89       1.961  23.149  -1.724  1.00 87.63           C  
ANISOU 3911  CA  ASP C  89    15438   7821  10037    156  -2823   2290       C  
ATOM   3912  C   ASP C  89       2.996  23.584  -0.702  1.00 91.38           C  
ANISOU 3912  C   ASP C  89    16043   8069  10609    -72  -2503   2148       C  
ATOM   3913  O   ASP C  89       4.196  23.422  -0.903  1.00 92.80           O  
ANISOU 3913  O   ASP C  89    16377   8342  10541   -700  -2192   2201       O  
ATOM   3914  CB  ASP C  89       1.122  24.357  -2.143  1.00 94.03           C  
ANISOU 3914  CB  ASP C  89    16784   8046  10897    584  -3464   2533       C  
ATOM   3915  CG  ASP C  89       0.047  23.999  -3.144  1.00 98.17           C  
ANISOU 3915  CG  ASP C  89    17184   8785  11331    854  -3855   2670       C  
ATOM   3916  OD1 ASP C  89       0.261  23.053  -3.930  1.00 95.98           O  
ANISOU 3916  OD1 ASP C  89    16692   9013  10763    457  -3660   2731       O  
ATOM   3917  OD2 ASP C  89      -1.014  24.662  -3.144  1.00103.30           O  
ANISOU 3917  OD2 ASP C  89    17868   9156  12226   1447  -4310   2650       O  
ATOM   3918  N   ARG C  90       2.516  24.123   0.410  1.00 92.34           N  
ANISOU 3918  N   ARG C  90    16069   7919  11099    435  -2571   1925       N  
ATOM   3919  CA  ARG C  90       3.401  24.597   1.458  1.00 92.41           C  
ANISOU 3919  CA  ARG C  90    16190   7708  11211    264  -2298   1764       C  
ATOM   3920  C   ARG C  90       3.740  23.503   2.457  1.00 85.49           C  
ANISOU 3920  C   ARG C  90    14650   7350  10481    218  -1805   1421       C  
ATOM   3921  O   ARG C  90       2.950  22.588   2.702  1.00 83.65           O  
ANISOU 3921  O   ARG C  90    13849   7525  10409    538  -1721   1230       O  
ATOM   3922  CB  ARG C  90       2.773  25.775   2.194  1.00 98.77           C  
ANISOU 3922  CB  ARG C  90    17248   7943  12336    790  -2601   1668       C  
ATOM   3923  CG  ARG C  90       3.151  27.137   1.660  1.00106.53           C  
ANISOU 3923  CG  ARG C  90    18969   8332  13174    603  -2891   1940       C  
ATOM   3924  CD  ARG C  90       2.237  28.183   2.264  1.00112.99           C  
ANISOU 3924  CD  ARG C  90    19785   8776  14370   1206  -3172   1761       C  
ATOM   3925  NE  ARG C  90       2.829  29.516   2.298  1.00120.27           N  
ANISOU 3925  NE  ARG C  90    21187   9270  15240    988  -3217   1838       N  
ATOM   3926  CZ  ARG C  90       2.885  30.342   1.258  1.00127.42           C  
ANISOU 3926  CZ  ARG C  90    22569   9923  15922    807  -3502   2134       C  
ATOM   3927  NH1 ARG C  90       2.399  29.974   0.078  1.00129.69           N  
ANISOU 3927  NH1 ARG C  90    22920  10358  15998    791  -3771   2385       N  
ATOM   3928  NH2 ARG C  90       3.432  31.540   1.403  1.00131.56           N  
ANISOU 3928  NH2 ARG C  90    23511  10051  16425    629  -3518   2170       N  
ATOM   3929  N   SER C  91       4.933  23.617   3.024  1.00 81.45           N  
ANISOU 3929  N   SER C  91    14237   6809   9903   -200  -1494   1346       N  
ATOM   3930  CA  SER C  91       5.378  22.766   4.114  1.00 71.84           C  
ANISOU 3930  CA  SER C  91    12489   5980   8826   -246  -1083   1043       C  
ATOM   3931  C   SER C  91       6.462  23.549   4.832  1.00 70.13           C  
ANISOU 3931  C   SER C  91    12588   5468   8589   -544   -938    975       C  
ATOM   3932  O   SER C  91       7.103  24.420   4.238  1.00 70.00           O  
ANISOU 3932  O   SER C  91    13138   5084   8374   -894  -1047   1177       O  
ATOM   3933  CB  SER C  91       5.939  21.448   3.585  1.00 65.92           C  
ANISOU 3933  CB  SER C  91    11351   5779   7916   -638   -785   1046       C  
ATOM   3934  OG  SER C  91       7.016  21.682   2.695  1.00 67.96           O  
ANISOU 3934  OG  SER C  91    11982   5968   7873  -1250   -725   1236       O  
ATOM   3935  N   ILE C  92       6.647  23.263   6.115  1.00 68.18           N  
ANISOU 3935  N   ILE C  92    11999   5378   8527   -426   -698    688       N  
ATOM   3936  CA  ILE C  92       7.720  23.874   6.886  1.00 67.67           C  
ANISOU 3936  CA  ILE C  92    12147   5123   8441   -726   -529    577       C  
ATOM   3937  C   ILE C  92       8.527  22.751   7.508  1.00 62.73           C  
ANISOU 3937  C   ILE C  92    11033   4997   7806   -981   -170    397       C  
ATOM   3938  O   ILE C  92       7.971  21.715   7.884  1.00 57.42           O  
ANISOU 3938  O   ILE C  92     9859   4709   7249   -739    -65    280       O  
ATOM   3939  CB  ILE C  92       7.158  24.790   7.957  1.00 71.47           C  
ANISOU 3939  CB  ILE C  92    12741   5252   9164   -316   -637    383       C  
ATOM   3940  N   PRO C  93       9.846  22.933   7.603  1.00 59.92           N  
ANISOU 3940  N   PRO C  93    10820   4630   7316  -1478      9    365       N  
ATOM   3941  CA  PRO C  93      10.629  21.813   8.129  1.00 57.23           C  
ANISOU 3941  CA  PRO C  93     9992   4757   6995  -1693    295    197       C  
ATOM   3942  C   PRO C  93      10.371  21.518   9.609  1.00 45.48           C  
ANISOU 3942  C   PRO C  93     8174   3414   5691  -1384    390    -42       C  
ATOM   3943  O   PRO C  93       9.844  22.337  10.360  1.00 47.41           O  
ANISOU 3943  O   PRO C  93     8590   3385   6038  -1101    295   -142       O  
ATOM   3944  CB  PRO C  93      12.079  22.267   7.919  1.00 59.01           C  
ANISOU 3944  CB  PRO C  93    10469   4895   7056  -2279    429    172       C  
ATOM   3945  CG  PRO C  93      12.009  23.761   7.816  1.00 64.84           C  
ANISOU 3945  CG  PRO C  93    11834   5075   7728  -2303    252    263       C  
ATOM   3946  CD  PRO C  93      10.691  24.052   7.157  1.00 64.66           C  
ANISOU 3946  CD  PRO C  93    12000   4826   7740  -1892    -38    472       C  
ATOM   3947  N   MET C  94      10.742  20.316  10.012  1.00 41.95           N  
ANISOU 3947  N   MET C  94     7258   3397   5285  -1456    575   -142       N  
ATOM   3948  CA  MET C  94      10.677  19.936  11.406  1.00 42.91           C  
ANISOU 3948  CA  MET C  94     7098   3690   5514  -1270    673   -342       C  
ATOM   3949  C   MET C  94      12.023  19.356  11.794  1.00 42.41           C  
ANISOU 3949  C   MET C  94     6831   3869   5413  -1645    831   -435       C  
ATOM   3950  O   MET C  94      12.627  18.617  11.018  1.00 39.64           O  
ANISOU 3950  O   MET C  94     6300   3726   5036  -1908    908   -380       O  
ATOM   3951  CB  MET C  94       9.603  18.875  11.614  1.00 39.65           C  
ANISOU 3951  CB  MET C  94     6284   3574   5207   -918    705   -366       C  
ATOM   3952  CG  MET C  94       8.164  19.345  11.431  1.00 43.82           C  
ANISOU 3952  CG  MET C  94     6899   3928   5822   -481    548   -361       C  
ATOM   3953  SD  MET C  94       7.047  18.004  11.914  1.00 60.74           S  
ANISOU 3953  SD  MET C  94     8515   6490   8074   -153    666   -477       S  
ATOM   3954  CE  MET C  94       8.092  17.244  13.130  1.00 34.66           C  
ANISOU 3954  CE  MET C  94     4989   3448   4733   -403    870   -587       C  
ATOM   3955  N   THR C  95      12.509  19.700  12.979  1.00 39.00           N  
ANISOU 3955  N   THR C  95     6412   3417   4989  -1675    869   -602       N  
ATOM   3956  CA  THR C  95      13.618  18.954  13.550  1.00 37.37           C  
ANISOU 3956  CA  THR C  95     5916   3498   4784  -1924    971   -711       C  
ATOM   3957  C   THR C  95      13.043  18.169  14.718  1.00 39.43           C  
ANISOU 3957  C   THR C  95     5881   3995   5106  -1636    991   -785       C  
ATOM   3958  O   THR C  95      11.956  18.494  15.196  1.00 36.30           O  
ANISOU 3958  O   THR C  95     5558   3504   4730  -1319    963   -819       O  
ATOM   3959  CB  THR C  95      14.774  19.857  13.978  1.00 39.44           C  
ANISOU 3959  CB  THR C  95     6403   3612   4969  -2255    990   -850       C  
ATOM   3960  OG1 THR C  95      14.262  20.971  14.708  1.00 41.68           O  
ANISOU 3960  OG1 THR C  95     6999   3602   5234  -2082    937   -928       O  
ATOM   3961  CG2 THR C  95      15.521  20.382  12.742  1.00 47.54           C  
ANISOU 3961  CG2 THR C  95     7660   4502   5901  -2621   1008   -779       C  
ATOM   3962  N   VAL C  96      13.741  17.129  15.157  1.00 33.90           N  
ANISOU 3962  N   VAL C  96     4851   3591   4438  -1751   1034   -822       N  
ATOM   3963  CA  VAL C  96      13.231  16.309  16.261  1.00 33.27           C  
ANISOU 3963  CA  VAL C  96     4540   3728   4373  -1530   1045   -857       C  
ATOM   3964  C   VAL C  96      14.218  16.274  17.417  1.00 34.82           C  
ANISOU 3964  C   VAL C  96     4684   4034   4511  -1696   1007   -977       C  
ATOM   3965  O   VAL C  96      15.418  16.498  17.235  1.00 36.90           O  
ANISOU 3965  O   VAL C  96     4946   4297   4778  -1983    983  -1042       O  
ATOM   3966  CB  VAL C  96      12.903  14.875  15.808  1.00 39.24           C  
ANISOU 3966  CB  VAL C  96     4946   4737   5227  -1442   1090   -749       C  
ATOM   3967  CG1 VAL C  96      11.908  14.891  14.653  1.00 38.85           C  
ANISOU 3967  CG1 VAL C  96     4927   4619   5216  -1288   1117   -645       C  
ATOM   3968  CG2 VAL C  96      14.171  14.137  15.404  1.00 37.52           C  
ANISOU 3968  CG2 VAL C  96     4490   4670   5096  -1718   1087   -752       C  
ATOM   3969  N   ASP C  97      13.709  16.034  18.621  1.00 35.60           N  
ANISOU 3969  N   ASP C  97     4748   4242   4538  -1539   1002  -1030       N  
ATOM   3970  CA  ASP C  97      14.581  15.803  19.768  1.00 37.77           C  
ANISOU 3970  CA  ASP C  97     4952   4673   4727  -1686    929  -1112       C  
ATOM   3971  C   ASP C  97      13.838  14.902  20.740  1.00 33.63           C  
ANISOU 3971  C   ASP C  97     4304   4348   4126  -1517    934  -1071       C  
ATOM   3972  O   ASP C  97      12.646  14.645  20.562  1.00 32.86           O  
ANISOU 3972  O   ASP C  97     4188   4253   4044  -1302   1028  -1035       O  
ATOM   3973  CB  ASP C  97      15.017  17.112  20.434  1.00 41.03           C  
ANISOU 3973  CB  ASP C  97     5639   4927   5023  -1824    916  -1290       C  
ATOM   3974  CG  ASP C  97      16.297  16.956  21.268  1.00 50.24           C  
ANISOU 3974  CG  ASP C  97     6711   6262   6117  -2063    807  -1384       C  
ATOM   3975  OD1 ASP C  97      16.950  15.888  21.202  1.00 48.99           O  
ANISOU 3975  OD1 ASP C  97     6274   6304   6036  -2117    713  -1309       O  
ATOM   3976  OD2 ASP C  97      16.660  17.915  21.982  1.00 57.52           O  
ANISOU 3976  OD2 ASP C  97     7825   7108   6921  -2192    802  -1553       O  
ATOM   3977  N   PHE C  98      14.552  14.409  21.742  1.00 34.33           N  
ANISOU 3977  N   PHE C  98     4314   4609   4122  -1633    825  -1081       N  
ATOM   3978  CA  PHE C  98      14.008  13.400  22.638  1.00 34.14           C  
ANISOU 3978  CA  PHE C  98     4203   4777   3992  -1543    808   -998       C  
ATOM   3979  C   PHE C  98      14.484  13.729  24.034  1.00 38.13           C  
ANISOU 3979  C   PHE C  98     4839   5380   4268  -1685    707  -1095       C  
ATOM   3980  O   PHE C  98      15.620  14.150  24.216  1.00 39.93           O  
ANISOU 3980  O   PHE C  98     5075   5607   4490  -1860    579  -1168       O  
ATOM   3981  CB  PHE C  98      14.522  12.020  22.250  1.00 32.72           C  
ANISOU 3981  CB  PHE C  98     3748   4722   3961  -1548    708   -827       C  
ATOM   3982  CG  PHE C  98      14.113  11.582  20.870  1.00 32.68           C  
ANISOU 3982  CG  PHE C  98     3584   4664   4170  -1448    818   -748       C  
ATOM   3983  CD1 PHE C  98      14.881  11.929  19.759  1.00 32.59           C  
ANISOU 3983  CD1 PHE C  98     3499   4564   4319  -1569    814   -784       C  
ATOM   3984  CD2 PHE C  98      12.969  10.826  20.682  1.00 34.79           C  
ANISOU 3984  CD2 PHE C  98     3775   4991   4454  -1275    938   -661       C  
ATOM   3985  CE1 PHE C  98      14.506  11.528  18.484  1.00 28.38           C  
ANISOU 3985  CE1 PHE C  98     2832   4010   3943  -1519    917   -717       C  
ATOM   3986  CE2 PHE C  98      12.583  10.424  19.402  1.00 27.45           C  
ANISOU 3986  CE2 PHE C  98     2687   4038   3703  -1200   1037   -602       C  
ATOM   3987  CZ  PHE C  98      13.356  10.781  18.312  1.00 27.03           C  
ANISOU 3987  CZ  PHE C  98     2576   3904   3791  -1323   1018   -623       C  
ATOM   3988  N   ILE C  99      13.620  13.550  25.018  1.00 37.42           N  
ANISOU 3988  N   ILE C  99     4849   5395   3975  -1639    774  -1122       N  
ATOM   3989  CA  ILE C  99      14.000  13.780  26.406  1.00 39.96           C  
ANISOU 3989  CA  ILE C  99     5311   5850   4023  -1811    681  -1208       C  
ATOM   3990  C   ILE C  99      13.291  12.783  27.305  1.00 40.59           C  
ANISOU 3990  C   ILE C  99     5413   6120   3889  -1814    696  -1103       C  
ATOM   3991  O   ILE C  99      12.254  12.245  26.926  1.00 39.28           O  
ANISOU 3991  O   ILE C  99     5188   5959   3778  -1672    855  -1054       O  
ATOM   3992  CB  ILE C  99      13.614  15.191  26.881  1.00 47.63           C  
ANISOU 3992  CB  ILE C  99     6502   6716   4878  -1853    819  -1483       C  
ATOM   3993  CG1 ILE C  99      12.131  15.460  26.617  1.00 43.37           C  
ANISOU 3993  CG1 ILE C  99     6002   6090   4387  -1647   1052  -1590       C  
ATOM   3994  CG2 ILE C  99      14.502  16.257  26.241  1.00 55.05           C  
ANISOU 3994  CG2 ILE C  99     7500   7457   5960  -1937    782  -1590       C  
ATOM   3995  CD1 ILE C  99      11.635  16.759  27.224  1.00 48.36           C  
ANISOU 3995  CD1 ILE C  99     6826   6614   4935  -1662   1186  -1903       C  
ATOM   3996  N   ARG C 100      13.874  12.533  28.478  1.00 42.88           N  
ANISOU 3996  N   ARG C 100     5801   6573   3920  -2001    521  -1070       N  
ATOM   3997  CA AARG C 100      13.229  11.750  29.522  0.51 45.58           C  
ANISOU 3997  CA AARG C 100     6263   7095   3962  -2092    536   -983       C  
ATOM   3998  CA BARG C 100      13.230  11.746  29.520  0.49 45.62           C  
ANISOU 3998  CA BARG C 100     6267   7099   3967  -2091    535   -983       C  
ATOM   3999  C   ARG C 100      13.113  12.646  30.738  1.00 48.30           C  
ANISOU 3999  C   ARG C 100     6833   7552   3967  -2298    593  -1216       C  
ATOM   4000  O   ARG C 100      13.956  13.521  30.943  1.00 49.65           O  
ANISOU 4000  O   ARG C 100     7045   7698   4122  -2399    493  -1353       O  
ATOM   4001  CB AARG C 100      14.086  10.554  29.930  0.51 49.09           C  
ANISOU 4001  CB AARG C 100     6667   7633   4351  -2166    215   -698       C  
ATOM   4002  CB BARG C 100      14.069  10.517  29.896  0.49 49.67           C  
ANISOU 4002  CB BARG C 100     6734   7703   4433  -2159    217   -691       C  
ATOM   4003  CG AARG C 100      14.278   9.450  28.914  0.51 49.90           C  
ANISOU 4003  CG AARG C 100     6535   7642   4782  -1994    132   -471       C  
ATOM   4004  CG BARG C 100      14.493   9.620  28.739  0.49 50.49           C  
ANISOU 4004  CG BARG C 100     6574   7693   4916  -1983    114   -497       C  
ATOM   4005  CD AARG C 100      15.452   8.601  29.389  0.51 53.46           C  
ANISOU 4005  CD AARG C 100     6937   8140   5235  -2057   -268   -262       C  
ATOM   4006  CD BARG C 100      15.085   8.299  29.241  0.49 52.74           C  
ANISOU 4006  CD BARG C 100     6839   8034   5166  -2018   -200   -215       C  
ATOM   4007  NE AARG C 100      15.387   7.208  28.968  0.51 52.65           N  
ANISOU 4007  NE AARG C 100     6705   7976   5324  -1940   -367     -7       N  
ATOM   4008  NE BARG C 100      14.053   7.381  29.716  0.49 53.81           N  
ANISOU 4008  NE BARG C 100     7123   8221   5100  -2047    -87    -57       N  
ATOM   4009  CZ AARG C 100      16.182   6.670  28.052  0.51 51.02           C  
ANISOU 4009  CZ AARG C 100     6209   7667   5508  -1811   -519     54       C  
ATOM   4010  CZ BARG C 100      13.830   7.085  30.993  0.49 56.17           C  
ANISOU 4010  CZ BARG C 100     7703   8653   4988  -2249   -172     32       C  
ATOM   4011  NH1AARG C 100      17.105   7.411  27.455  0.51 48.11           N  
ANISOU 4011  NH1AARG C 100     5657   7269   5353  -1810   -578   -124       N  
ATOM   4012  NH1BARG C 100      14.577   7.623  31.945  0.49 62.77           N  
ANISOU 4012  NH1BARG C 100     8686   9597   5567  -2422   -397    -13       N  
ATOM   4013  NH2AARG C 100      16.053   5.391  27.734  0.51 52.42           N  
ANISOU 4013  NH2AARG C 100     6280   7771   5866  -1709   -592    265       N  
ATOM   4014  NH2BARG C 100      12.862   6.242  31.316  0.49 54.39           N  
ANISOU 4014  NH2BARG C 100     7619   8463   4583  -2314    -25    159       N  
ATOM   4015  N   LEU C 101      12.086  12.430  31.551  1.00 48.17           N  
ANISOU 4015  N   LEU C 101     8370   6164   3767  -1427   -484    879       N  
ATOM   4016  CA  LEU C 101      11.965  13.175  32.804  1.00 53.23           C  
ANISOU 4016  CA  LEU C 101     8567   7346   4313  -1570   -519    782       C  
ATOM   4017  C   LEU C 101      12.251  12.298  34.024  1.00 58.59           C  
ANISOU 4017  C   LEU C 101     9225   8238   4799  -1637   -764   1026       C  
ATOM   4018  O   LEU C 101      11.904  11.120  34.039  1.00 62.71           O  
ANISOU 4018  O   LEU C 101    10086   8570   5172  -1767   -957   1337       O  
ATOM   4019  CB  LEU C 101      10.588  13.830  32.924  1.00 57.57           C  
ANISOU 4019  CB  LEU C 101     8990   8234   4650  -1827   -474    718       C  
ATOM   4020  CG  LEU C 101      10.371  15.139  32.164  1.00 58.84           C  
ANISOU 4020  CG  LEU C 101     9004   8371   4983  -1732   -227    398       C  
ATOM   4021  CD1 LEU C 101      11.698  15.750  31.751  1.00 58.31           C  
ANISOU 4021  CD1 LEU C 101     8803   8057   5294  -1466   -110    207       C  
ATOM   4022  CD2 LEU C 101       9.476  14.962  30.954  1.00 59.00           C  
ANISOU 4022  CD2 LEU C 101     9286   8146   4985  -1832   -124    467       C  
ATOM   4023  N   LYS C 102      12.897  12.880  35.034  1.00 62.56           N  
ANISOU 4023  N   LYS C 102     9357   9104   5307  -1557   -797    896       N  
ATOM   4024  CA  LYS C 102      13.150  12.190  36.303  1.00 73.03           C  
ANISOU 4024  CA  LYS C 102    10592  10738   6417  -1602  -1016   1113       C  
ATOM   4025  C   LYS C 102      12.713  13.037  37.497  1.00 77.21           C  
ANISOU 4025  C   LYS C 102    10754  11889   6692  -1677  -1076    952       C  
ATOM   4026  O   LYS C 102      12.690  14.268  37.427  1.00 78.63           O  
ANISOU 4026  O   LYS C 102    10748  12177   6949  -1607   -983    595       O  
ATOM   4027  CB  LYS C 102      14.620  11.817  36.429  1.00 74.38           C  
ANISOU 4027  CB  LYS C 102    10722  10752   6787  -1325  -1052   1163       C  
ATOM   4028  N   LYS C 114      14.093  16.116  36.809  1.00 65.63           N  
ANISOU 4028  N   LYS C 114     8845  10228   5866  -1407   -902     59       N  
ATOM   4029  CA  LYS C 114      15.060  16.789  35.940  1.00 67.09           C  
ANISOU 4029  CA  LYS C 114     8924  10068   6499  -1328   -816    -47       C  
ATOM   4030  C   LYS C 114      15.074  16.220  34.512  1.00 63.98           C  
ANISOU 4030  C   LYS C 114     8741   9265   6304  -1235   -565    142       C  
ATOM   4031  O   LYS C 114      14.900  15.017  34.316  1.00 64.68           O  
ANISOU 4031  O   LYS C 114     9088   9235   6254  -1191   -552    397       O  
ATOM   4032  CB  LYS C 114      16.451  16.715  36.550  1.00 69.81           C  
ANISOU 4032  CB  LYS C 114     9018  10495   7011  -1265  -1002     41       C  
ATOM   4033  N   VAL C 115      15.287  17.092  33.527  1.00 63.71           N  
ANISOU 4033  N   VAL C 115     8631   9000   6577  -1189   -403     20       N  
ATOM   4034  CA  VAL C 115      15.380  16.690  32.120  1.00 64.02           C  
ANISOU 4034  CA  VAL C 115     8848   8695   6780  -1020   -154    173       C  
ATOM   4035  C   VAL C 115      16.695  15.967  31.839  1.00 68.65           C  
ANISOU 4035  C   VAL C 115     9368   9197   7517   -738   -126    457       C  
ATOM   4036  O   VAL C 115      17.771  16.504  32.104  1.00 72.60           O  
ANISOU 4036  O   VAL C 115     9495   9837   8254   -702   -189    520       O  
ATOM   4037  CB  VAL C 115      15.270  17.905  31.164  1.00 75.15           C  
ANISOU 4037  CB  VAL C 115    10135   9949   8469  -1028     24      9       C  
ATOM   4038  CG1 VAL C 115      15.609  17.506  29.726  1.00 75.00           C  
ANISOU 4038  CG1 VAL C 115    10241   9650   8607   -763    286    202       C  
ATOM   4039  CG2 VAL C 115      13.883  18.523  31.229  1.00 72.59           C  
ANISOU 4039  CG2 VAL C 115     9938   9697   7946  -1198     52   -240       C  
ATOM   4040  N   ILE C 116      16.605  14.751  31.303  1.00 66.32           N  
ANISOU 4040  N   ILE C 116     9451   8681   7065   -522    -64    651       N  
ATOM   4041  CA  ILE C 116      17.797  13.975  30.964  1.00 65.70           C  
ANISOU 4041  CA  ILE C 116     9389   8533   7041   -108    -11    928       C  
ATOM   4042  C   ILE C 116      17.876  13.694  29.460  1.00 63.53           C  
ANISOU 4042  C   ILE C 116     9388   7951   6800    275    237   1009       C  
ATOM   4043  O   ILE C 116      16.851  13.542  28.781  1.00 55.49           O  
ANISOU 4043  O   ILE C 116     8751   6668   5664    195    283    884       O  
ATOM   4044  CB  ILE C 116      17.904  12.677  31.819  1.00 58.90           C  
ANISOU 4044  CB  ILE C 116     8795   7674   5909    -43   -226   1106       C  
ATOM   4045  CG1 ILE C 116      18.488  11.511  31.021  1.00 57.94           C  
ANISOU 4045  CG1 ILE C 116     9087   7245   5683    480   -157   1339       C  
ATOM   4046  CG2 ILE C 116      16.552  12.304  32.408  1.00 62.61           C  
ANISOU 4046  CG2 ILE C 116     9552   8121   6115   -431   -404   1024       C  
ATOM   4047  CD1 ILE C 116      18.576  10.211  31.802  1.00 63.07           C  
ANISOU 4047  CD1 ILE C 116    10083   7803   6077    558   -403   1532       C  
ATOM   4048  N   GLY C 117      19.100  13.662  28.941  1.00 68.38           N  
ANISOU 4048  N   GLY C 117     9771   8662   7547    714    392   1247       N  
ATOM   4049  CA  GLY C 117      19.320  13.481  27.521  1.00 69.63           C  
ANISOU 4049  CA  GLY C 117    10124   8639   7694   1198    656   1352       C  
ATOM   4050  C   GLY C 117      18.858  14.711  26.773  1.00 70.55           C  
ANISOU 4050  C   GLY C 117     9995   8762   8049    985    840   1210       C  
ATOM   4051  O   GLY C 117      18.625  15.763  27.373  1.00 72.71           O  
ANISOU 4051  O   GLY C 117     9904   9188   8536    524    755   1064       O  
ATOM   4052  N   GLY C 118      18.719  14.583  25.460  1.00 69.82           N  
ANISOU 4052  N   GLY C 118    10146   8489   7892   1360   1072   1243       N  
ATOM   4053  CA  GLY C 118      18.256  15.694  24.651  1.00 66.94           C  
ANISOU 4053  CA  GLY C 118     9577   8121   7738   1201   1267   1142       C  
ATOM   4054  C   GLY C 118      19.356  16.682  24.325  1.00 65.88           C  
ANISOU 4054  C   GLY C 118     8760   8320   7951   1307   1440   1434       C  
ATOM   4055  O   GLY C 118      20.401  16.716  24.980  1.00 63.54           O  
ANISOU 4055  O   GLY C 118     8046   8314   7781   1331   1351   1686       O  
ATOM   4056  N   ASP C 119      19.123  17.481  23.292  1.00 66.22           N  
ANISOU 4056  N   ASP C 119     8666   8343   8150   1346   1668   1456       N  
ATOM   4057  CA  ASP C 119      20.073  18.510  22.913  1.00 69.85           C  
ANISOU 4057  CA  ASP C 119     8448   9112   8980   1355   1801   1810       C  
ATOM   4058  C   ASP C 119      20.078  19.600  23.967  1.00 70.76           C  
ANISOU 4058  C   ASP C 119     8184   9265   9436    690   1513   1693       C  
ATOM   4059  O   ASP C 119      19.159  19.682  24.785  1.00 67.92           O  
ANISOU 4059  O   ASP C 119     8112   8713   8983    306   1300   1288       O  
ATOM   4060  CB  ASP C 119      19.706  19.106  21.551  1.00 67.06           C  
ANISOU 4060  CB  ASP C 119     8076   8707   8698   1538   2102   1867       C  
ATOM   4061  CG  ASP C 119      19.891  18.122  20.416  1.00 70.40           C  
ANISOU 4061  CG  ASP C 119     8848   9144   8759   2308   2374   2016       C  
ATOM   4062  OD1 ASP C 119      20.610  17.123  20.612  1.00 72.15           O  
ANISOU 4062  OD1 ASP C 119     9194   9483   8736   2772   2358   2188       O  
ATOM   4063  OD2 ASP C 119      19.326  18.359  19.327  1.00 72.25           O  
ANISOU 4063  OD2 ASP C 119     9260   9271   8922   2495   2590   1953       O  
ATOM   4064  N   ASP C 120      21.130  20.412  23.958  1.00 76.77           N  
ANISOU 4064  N   ASP C 120     8309  10299  10562    577   1474   2082       N  
ATOM   4065  CA  ASP C 120      21.148  21.636  24.735  1.00 80.64           C  
ANISOU 4065  CA  ASP C 120     8499  10728  11414    -52   1143   1972       C  
ATOM   4066  C   ASP C 120      19.836  22.335  24.411  1.00 78.10           C  
ANISOU 4066  C   ASP C 120     8528  10052  11093   -283   1184   1541       C  
ATOM   4067  O   ASP C 120      19.549  22.605  23.246  1.00 78.51           O  
ANISOU 4067  O   ASP C 120     8593  10046  11192    -85   1476   1643       O  
ATOM   4068  CB  ASP C 120      22.327  22.508  24.302  1.00 86.95           C  
ANISOU 4068  CB  ASP C 120     8588  11803  12647   -154   1122   2551       C  
ATOM   4069  CG  ASP C 120      22.727  23.525  25.354  1.00 90.53           C  
ANISOU 4069  CG  ASP C 120     8737  12201  13458   -802    620   2525       C  
ATOM   4070  OD1 ASP C 120      21.908  24.416  25.671  1.00 88.38           O  
ANISOU 4070  OD1 ASP C 120     8719  11560  13300  -1199    401   2099       O  
ATOM   4071  OD2 ASP C 120      23.872  23.440  25.848  1.00 95.52           O  
ANISOU 4071  OD2 ASP C 120     8893  13167  14233   -883    420   2940       O  
ATOM   4072  N   LEU C 121      19.022  22.600  25.428  1.00 74.55           N  
ANISOU 4072  N   LEU C 121     8360   9424  10542   -638    911   1079       N  
ATOM   4073  CA  LEU C 121      17.693  23.161  25.193  1.00 67.56           C  
ANISOU 4073  CA  LEU C 121     7821   8285   9563   -774    969    680       C  
ATOM   4074  C   LEU C 121      17.728  24.572  24.595  1.00 63.61           C  
ANISOU 4074  C   LEU C 121     7086   7625   9457   -980    957    748       C  
ATOM   4075  O   LEU C 121      16.685  25.171  24.336  1.00 60.05           O  
ANISOU 4075  O   LEU C 121     6889   6975   8951  -1054   1016    451       O  
ATOM   4076  CB  LEU C 121      16.843  23.113  26.465  1.00 65.03           C  
ANISOU 4076  CB  LEU C 121     7808   7931   8970  -1009    696    233       C  
ATOM   4077  CG  LEU C 121      16.421  21.718  26.926  1.00 65.00           C  
ANISOU 4077  CG  LEU C 121     8121   8036   8539   -850    727    167       C  
ATOM   4078  CD1 LEU C 121      15.325  21.803  27.974  1.00 65.10           C  
ANISOU 4078  CD1 LEU C 121     8393   8099   8243  -1055    534   -210       C  
ATOM   4079  CD2 LEU C 121      15.970  20.869  25.747  1.00 62.24           C  
ANISOU 4079  CD2 LEU C 121     8050   7591   8005   -533   1052    278       C  
ATOM   4080  N   SER C 122      18.934  25.089  24.371  1.00 63.20           N  
ANISOU 4080  N   SER C 122     6530   7684   9799  -1077    868   1196       N  
ATOM   4081  CA  SER C 122      19.116  26.335  23.640  1.00 64.75           C  
ANISOU 4081  CA  SER C 122     6454   7733  10415  -1275    856   1417       C  
ATOM   4082  C   SER C 122      18.753  26.126  22.167  1.00 60.78           C  
ANISOU 4082  C   SER C 122     5971   7284   9838   -881   1354   1610       C  
ATOM   4083  O   SER C 122      18.569  27.084  21.420  1.00 58.62           O  
ANISOU 4083  O   SER C 122     5575   6869   9829   -982   1429   1733       O  
ATOM   4084  CB  SER C 122      20.556  26.837  23.779  1.00 69.08           C  
ANISOU 4084  CB  SER C 122     6382   8462  11401  -1529    596   1982       C  
ATOM   4085  OG  SER C 122      21.475  25.767  23.697  1.00 69.35           O  
ANISOU 4085  OG  SER C 122     6125   8932  11294  -1186    775   2390       O  
ATOM   4086  N   THR C 123      18.651  24.861  21.761  1.00 56.35           N  
ANISOU 4086  N   THR C 123     5611   6904   8897   -416   1655   1631       N  
ATOM   4087  CA  THR C 123      18.187  24.514  20.423  1.00 55.69           C  
ANISOU 4087  CA  THR C 123     5686   6844   8628     18   2080   1713       C  
ATOM   4088  C   THR C 123      16.715  24.873  20.268  1.00 50.29           C  
ANISOU 4088  C   THR C 123     5454   5868   7787   -119   2124   1232       C  
ATOM   4089  O   THR C 123      16.216  25.015  19.154  1.00 48.00           O  
ANISOU 4089  O   THR C 123     5249   5549   7438    105   2415   1277       O  
ATOM   4090  CB  THR C 123      18.380  23.021  20.121  1.00 57.50           C  
ANISOU 4090  CB  THR C 123     6178   7237   8434    564   2282   1775       C  
ATOM   4091  OG1 THR C 123      17.695  22.238  21.104  1.00 57.15           O  
ANISOU 4091  OG1 THR C 123     6601   7032   8083    427   2072   1350       O  
ATOM   4092  CG2 THR C 123      19.851  22.663  20.137  1.00 64.31           C  
ANISOU 4092  CG2 THR C 123     6557   8485   9393    838   2310   2317       C  
ATOM   4093  N   LEU C 124      16.023  25.013  21.396  1.00 44.32           N  
ANISOU 4093  N   LEU C 124     4958   4958   6922   -445   1839    803       N  
ATOM   4094  CA  LEU C 124      14.625  25.429  21.392  1.00 38.84           C  
ANISOU 4094  CA  LEU C 124     4622   4090   6045   -560   1863    395       C  
ATOM   4095  C   LEU C 124      14.495  26.947  21.329  1.00 39.94           C  
ANISOU 4095  C   LEU C 124     4613   4028   6535   -814   1745    346       C  
ATOM   4096  O   LEU C 124      13.406  27.472  21.095  1.00 42.07           O  
ANISOU 4096  O   LEU C 124     5122   4178   6685   -823   1824     83       O  
ATOM   4097  CB  LEU C 124      13.899  24.916  22.641  1.00 36.35           C  
ANISOU 4097  CB  LEU C 124     4623   3802   5387   -716   1629     14       C  
ATOM   4098  CG  LEU C 124      14.076  23.441  23.001  1.00 36.63           C  
ANISOU 4098  CG  LEU C 124     4838   3971   5109   -563   1617     66       C  
ATOM   4099  CD1 LEU C 124      13.227  23.076  24.210  1.00 34.10           C  
ANISOU 4099  CD1 LEU C 124     4773   3728   4456   -760   1391   -243       C  
ATOM   4100  CD2 LEU C 124      13.719  22.574  21.818  1.00 37.06           C  
ANISOU 4100  CD2 LEU C 124     5143   3995   4943   -236   1903    180       C  
ATOM   4101  N   THR C 125      15.599  27.657  21.551  1.00 41.98           N  
ANISOU 4101  N   THR C 125     4489   4240   7220  -1030   1517    628       N  
ATOM   4102  CA  THR C 125      15.511  29.107  21.690  1.00 45.44           C  
ANISOU 4102  CA  THR C 125     4887   4371   8005  -1340   1255    554       C  
ATOM   4103  C   THR C 125      14.990  29.743  20.410  1.00 48.26           C  
ANISOU 4103  C   THR C 125     5228   4626   8485  -1205   1569    690       C  
ATOM   4104  O   THR C 125      15.552  29.536  19.333  1.00 50.86           O  
ANISOU 4104  O   THR C 125     5237   5137   8950  -1009   1869   1153       O  
ATOM   4105  CB  THR C 125      16.849  29.738  22.099  1.00 52.47           C  
ANISOU 4105  CB  THR C 125     5356   5204   9376  -1687    869    925       C  
ATOM   4106  OG1 THR C 125      17.273  29.183  23.352  1.00 54.74           O  
ANISOU 4106  OG1 THR C 125     5681   5598   9519  -1809    553    760       O  
ATOM   4107  CG2 THR C 125      16.701  31.237  22.247  1.00 56.61           C  
ANISOU 4107  CG2 THR C 125     5967   5285  10257  -2035    498    822       C  
ATOM   4108  N   GLY C 126      13.897  30.493  20.530  1.00 47.69           N  
ANISOU 4108  N   GLY C 126     5498   4314   8308  -1244   1518    299       N  
ATOM   4109  CA  GLY C 126      13.314  31.185  19.395  1.00 48.72           C  
ANISOU 4109  CA  GLY C 126     5639   4333   8540  -1120   1791    398       C  
ATOM   4110  C   GLY C 126      12.634  30.262  18.399  1.00 50.41           C  
ANISOU 4110  C   GLY C 126     5945   4818   8391   -750   2276    428       C  
ATOM   4111  O   GLY C 126      12.357  30.661  17.271  1.00 54.02           O  
ANISOU 4111  O   GLY C 126     6335   5295   8894   -569   2511    599       O  
ATOM   4112  N   LYS C 127      12.356  29.028  18.810  1.00 48.38           N  
ANISOU 4112  N   LYS C 127     5884   4771   7728   -620   2331    252       N  
ATOM   4113  CA ALYS C 127      11.727  28.066  17.913  0.73 45.38           C  
ANISOU 4113  CA ALYS C 127     5691   4579   6971   -298   2631    256       C  
ATOM   4114  CA BLYS C 127      11.737  28.042  17.931  0.27 46.01           C  
ANISOU 4114  CA BLYS C 127     5772   4661   7049   -300   2630    256       C  
ATOM   4115  C   LYS C 127      10.284  27.769  18.312  1.00 42.07           C  
ANISOU 4115  C   LYS C 127     5663   4206   6114   -318   2560   -138       C  
ATOM   4116  O   LYS C 127       9.857  28.072  19.429  1.00 42.69           O  
ANISOU 4116  O   LYS C 127     5855   4266   6097   -515   2421   -418       O  
ATOM   4117  CB ALYS C 127      12.536  26.763  17.868  0.73 47.94           C  
ANISOU 4117  CB ALYS C 127     5984   5079   7150    -97   2656    450       C  
ATOM   4118  CB BLYS C 127      12.529  26.732  17.980  0.27 47.86           C  
ANISOU 4118  CB BLYS C 127     5983   5067   7135   -119   2653    433       C  
ATOM   4119  CG ALYS C 127      13.956  26.919  17.339  0.73 53.12           C  
ANISOU 4119  CG ALYS C 127     6199   5854   8128     44   2697    931       C  
ATOM   4120  CG BLYS C 127      14.022  26.887  17.723  0.27 52.31           C  
ANISOU 4120  CG BLYS C 127     6083   5731   8062    -50   2678    904       C  
ATOM   4121  CD ALYS C 127      13.967  27.268  15.854  0.73 55.06           C  
ANISOU 4121  CD ALYS C 127     6389   6179   8352    349   2741   1127       C  
ATOM   4122  CD BLYS C 127      14.317  27.500  16.355  0.27 55.35           C  
ANISOU 4122  CD BLYS C 127     6275   6197   8559    194   2714   1188       C  
ATOM   4123  CE ALYS C 127      15.381  27.488  15.348  0.73 58.93           C  
ANISOU 4123  CE ALYS C 127     6408   6878   9104    495   2766   1653       C  
ATOM   4124  CE BLYS C 127      13.812  26.625  15.212  0.27 54.54           C  
ANISOU 4124  CE BLYS C 127     6497   6182   8043    602   2765   1123       C  
ATOM   4125  NZ ALYS C 127      15.526  28.812  14.672  0.73 60.95           N  
ANISOU 4125  NZ ALYS C 127     6399   7087   9674    383   2716   1878       N  
ATOM   4126  NZ BLYS C 127      12.397  26.933  14.843  0.27 51.11           N  
ANISOU 4126  NZ BLYS C 127     6387   5614   7417    522   2674    799       N  
ATOM   4127  N   ASN C 128       9.529  27.187  17.386  1.00 39.58           N  
ANISOU 4127  N   ASN C 128     5747   4127   5165   -599    830    949       N  
ATOM   4128  CA  ASN C 128       8.181  26.708  17.687  1.00 41.56           C  
ANISOU 4128  CA  ASN C 128     6015   4432   5342   -472    655    773       C  
ATOM   4129  C   ASN C 128       8.278  25.266  18.163  1.00 38.41           C  
ANISOU 4129  C   ASN C 128     5557   4167   4872   -440    812    549       C  
ATOM   4130  O   ASN C 128       8.647  24.382  17.394  1.00 43.02           O  
ANISOU 4130  O   ASN C 128     6261   4849   5238   -487   1036    536       O  
ATOM   4131  CB  ASN C 128       7.289  26.756  16.447  1.00 48.67           C  
ANISOU 4131  CB  ASN C 128     7092   5448   5953   -498    536    908       C  
ATOM   4132  CG  ASN C 128       6.635  28.106  16.236  1.00 53.55           C  
ANISOU 4132  CG  ASN C 128     7732   5915   6700   -418    291   1143       C  
ATOM   4133  OD1 ASN C 128       7.146  29.141  16.669  1.00 53.52           O  
ANISOU 4133  OD1 ASN C 128     7724   5654   6957   -404    295   1233       O  
ATOM   4134  ND2 ASN C 128       5.486  28.100  15.560  1.00 56.50           N  
ANISOU 4134  ND2 ASN C 128     8132   6440   6894   -378     71   1267       N  
ATOM   4135  N   VAL C 129       7.946  25.025  19.424  1.00 32.32           N  
ANISOU 4135  N   VAL C 129     4645   3368   4268   -361    730    376       N  
ATOM   4136  CA  VAL C 129       8.171  23.714  20.023  1.00 29.69           C  
ANISOU 4136  CA  VAL C 129     4257   3113   3913   -324    882    222       C  
ATOM   4137  C   VAL C 129       6.854  22.965  20.165  1.00 32.56           C  
ANISOU 4137  C   VAL C 129     4677   3552   4142   -307    791     45       C  
ATOM   4138  O   VAL C 129       5.871  23.513  20.679  1.00 26.87           O  
ANISOU 4138  O   VAL C 129     3876   2830   3501   -259    591     -5       O  
ATOM   4139  CB  VAL C 129       8.886  23.822  21.390  1.00 31.63           C  
ANISOU 4139  CB  VAL C 129     4303   3326   4388   -309    859    199       C  
ATOM   4140  CG1 VAL C 129       9.146  22.443  21.983  1.00 30.53           C  
ANISOU 4140  CG1 VAL C 129     4105   3258   4237   -237   1011    124       C  
ATOM   4141  CG2 VAL C 129      10.201  24.554  21.231  1.00 35.89           C  
ANISOU 4141  CG2 VAL C 129     4732   3843   5061   -407    916    403       C  
ATOM   4142  N   LEU C 130       6.838  21.726  19.679  1.00 29.33           N  
ANISOU 4142  N   LEU C 130     4416   3191   3537   -356    971    -45       N  
ATOM   4143  CA  LEU C 130       5.701  20.830  19.878  1.00 29.48           C  
ANISOU 4143  CA  LEU C 130     4496   3280   3425   -424    907   -218       C  
ATOM   4144  C   LEU C 130       6.146  19.722  20.826  1.00 25.00           C  
ANISOU 4144  C   LEU C 130     3915   2633   2951   -361   1101   -321       C  
ATOM   4145  O   LEU C 130       6.998  18.903  20.479  1.00 28.47           O  
ANISOU 4145  O   LEU C 130     4489   2977   3353   -324   1387   -311       O  
ATOM   4146  CB  LEU C 130       5.265  20.226  18.535  1.00 32.74           C  
ANISOU 4146  CB  LEU C 130     5191   3768   3482   -617    955   -257       C  
ATOM   4147  CG  LEU C 130       3.835  19.701  18.272  1.00 36.91           C  
ANISOU 4147  CG  LEU C 130     5775   4458   3791   -826    751   -363       C  
ATOM   4148  CD1 LEU C 130       3.838  18.313  17.586  1.00 36.37           C  
ANISOU 4148  CD1 LEU C 130     6089   4335   3395  -1065    975   -552       C  
ATOM   4149  CD2 LEU C 130       2.942  19.725  19.493  1.00 34.77           C  
ANISOU 4149  CD2 LEU C 130     5224   4249   3738   -757    589   -424       C  
ATOM   4150  N   ILE C 131       5.599  19.706  22.035  1.00 26.01           N  
ANISOU 4150  N   ILE C 131     3888   2789   3208   -325    977   -392       N  
ATOM   4151  CA  ILE C 131       5.938  18.662  22.991  1.00 28.11           C  
ANISOU 4151  CA  ILE C 131     4150   2991   3538   -277   1123   -435       C  
ATOM   4152  C   ILE C 131       4.948  17.530  22.815  1.00 27.12           C  
ANISOU 4152  C   ILE C 131     4206   2859   3240   -424   1179   -586       C  
ATOM   4153  O   ILE C 131       3.736  17.761  22.803  1.00 29.25           O  
ANISOU 4153  O   ILE C 131     4412   3265   3436   -548    993   -663       O  
ATOM   4154  CB  ILE C 131       5.851  19.173  24.433  1.00 27.45           C  
ANISOU 4154  CB  ILE C 131     3867   2959   3604   -226    975   -437       C  
ATOM   4155  CG1 ILE C 131       6.913  20.242  24.672  1.00 29.15           C  
ANISOU 4155  CG1 ILE C 131     3946   3164   3966   -176    905   -304       C  
ATOM   4156  CG2 ILE C 131       6.053  18.028  25.415  1.00 30.11           C  
ANISOU 4156  CG2 ILE C 131     4221   3265   3956   -203   1089   -433       C  
ATOM   4157  CD1 ILE C 131       6.763  20.959  25.997  1.00 27.69           C  
ANISOU 4157  CD1 ILE C 131     3660   3012   3850   -203    744   -362       C  
ATOM   4158  N   VAL C 132       5.453  16.308  22.674  1.00 24.92           N  
ANISOU 4158  N   VAL C 132     4142   2410   2916   -416   1451   -610       N  
ATOM   4159  CA  VAL C 132       4.568  15.174  22.428  1.00 30.54           C  
ANISOU 4159  CA  VAL C 132     5115   3049   3441   -632   1532   -774       C  
ATOM   4160  C   VAL C 132       4.640  14.173  23.579  1.00 31.91           C  
ANISOU 4160  C   VAL C 132     5315   3082   3728   -577   1665   -759       C  
ATOM   4161  O   VAL C 132       5.694  13.595  23.845  1.00 30.74           O  
ANISOU 4161  O   VAL C 132     5216   2746   3719   -368   1892   -626       O  
ATOM   4162  CB  VAL C 132       4.907  14.462  21.113  1.00 28.43           C  
ANISOU 4162  CB  VAL C 132     5203   2620   2978   -733   1755   -831       C  
ATOM   4163  CG1 VAL C 132       3.929  13.330  20.850  1.00 28.94           C  
ANISOU 4163  CG1 VAL C 132     5508   2625   2864  -1040   1745   -955       C  
ATOM   4164  CG2 VAL C 132       4.895  15.435  19.932  1.00 29.18           C  
ANISOU 4164  CG2 VAL C 132     5350   2864   2874   -817   1668   -838       C  
ATOM   4165  N   GLU C 133       3.496  13.944  24.217  1.00 29.15           N  
ANISOU 4165  N   GLU C 133     4906   2842   3327   -764   1523   -844       N  
ATOM   4166  CA  GLU C 133       3.407  13.148  25.434  1.00 30.66           C  
ANISOU 4166  CA  GLU C 133     5102   2949   3597   -751   1605   -796       C  
ATOM   4167  C   GLU C 133       2.420  11.994  25.243  1.00 30.46           C  
ANISOU 4167  C   GLU C 133     5347   2814   3411  -1076   1698   -940       C  
ATOM   4168  O   GLU C 133       1.545  12.064  24.372  1.00 30.17           O  
ANISOU 4168  O   GLU C 133     5349   2911   3203  -1350   1571  -1059       O  
ATOM   4169  CB  GLU C 133       2.958  14.079  26.573  1.00 30.91           C  
ANISOU 4169  CB  GLU C 133     4796   3241   3707   -704   1380   -759       C  
ATOM   4170  CG  GLU C 133       2.854  13.472  27.951  1.00 41.25           C  
ANISOU 4170  CG  GLU C 133     6091   4542   5039   -711   1431   -685       C  
ATOM   4171  CD  GLU C 133       4.185  13.001  28.499  1.00 43.93           C  
ANISOU 4171  CD  GLU C 133     6480   4720   5490   -486   1546   -461       C  
ATOM   4172  OE1 GLU C 133       4.697  11.987  27.987  1.00 39.33           O  
ANISOU 4172  OE1 GLU C 133     6136   3862   4947   -421   1778   -396       O  
ATOM   4173  OE2 GLU C 133       4.705  13.630  29.453  1.00 43.28           O  
ANISOU 4173  OE2 GLU C 133     6206   4788   5452   -384   1410   -338       O  
ATOM   4174  N   ASP C 134       2.566  10.913  26.012  1.00 29.14           N  
ANISOU 4174  N   ASP C 134     5358   2419   3294  -1076   1890   -876       N  
ATOM   4175  CA  ASP C 134       1.582   9.831  25.954  1.00 30.17           C  
ANISOU 4175  CA  ASP C 134     5697   2487   3280  -1419   1944   -952       C  
ATOM   4176  C   ASP C 134       0.320  10.124  26.786  1.00 32.56           C  
ANISOU 4176  C   ASP C 134     5759   3063   3550  -1687   1767  -1020       C  
ATOM   4177  O   ASP C 134      -0.808   9.867  26.338  1.00 34.82           O  
ANISOU 4177  O   ASP C 134     6023   3519   3686  -2040   1661  -1122       O  
ATOM   4178  CB  ASP C 134       2.195   8.470  26.341  1.00 32.74           C  
ANISOU 4178  CB  ASP C 134     6335   2450   3654  -1304   2245   -828       C  
ATOM   4179  CG  ASP C 134       2.875   8.485  27.711  1.00 34.93           C  
ANISOU 4179  CG  ASP C 134     6519   2609   4142  -1042   2306   -613       C  
ATOM   4180  OD1 ASP C 134       3.125   9.571  28.272  1.00 33.66           O  
ANISOU 4180  OD1 ASP C 134     5996   2745   4050   -884   2092   -527       O  
ATOM   4181  OD2 ASP C 134       3.181   7.387  28.219  1.00 39.77           O  
ANISOU 4181  OD2 ASP C 134     7329   2978   4803   -944   2489   -466       O  
ATOM   4182  N   ILE C 135       0.505  10.654  27.986  1.00 33.26           N  
ANISOU 4182  N   ILE C 135     5575   3311   3753  -1473   1703   -883       N  
ATOM   4183  CA  ILE C 135      -0.631  10.813  28.895  1.00 30.70           C  
ANISOU 4183  CA  ILE C 135     5003   3269   3392  -1661   1621   -897       C  
ATOM   4184  C   ILE C 135      -0.450  11.948  29.890  1.00 31.34           C  
ANISOU 4184  C   ILE C 135     4770   3595   3543  -1406   1515   -836       C  
ATOM   4185  O   ILE C 135       0.643  12.167  30.426  1.00 32.13           O  
ANISOU 4185  O   ILE C 135     4905   3606   3697  -1156   1522   -712       O  
ATOM   4186  CB  ILE C 135      -0.954   9.467  29.602  1.00 38.94           C  
ANISOU 4186  CB  ILE C 135     6305   4111   4381  -1899   1816   -829       C  
ATOM   4187  CG1 ILE C 135      -2.203   9.584  30.481  1.00 36.70           C  
ANISOU 4187  CG1 ILE C 135     5748   4157   4041  -2142   1783   -839       C  
ATOM   4188  CG2 ILE C 135       0.247   8.969  30.405  1.00 40.31           C  
ANISOU 4188  CG2 ILE C 135     6666   4016   4636  -1607   1959   -604       C  
ATOM   4189  CD1 ILE C 135      -2.730   8.232  30.918  1.00 39.27           C  
ANISOU 4189  CD1 ILE C 135     6313   4325   4284  -2388   1889   -791       C  
ATOM   4190  N   ILE C 136      -1.523  12.701  30.112  1.00 30.01           N  
ANISOU 4190  N   ILE C 136     4288   3740   3373  -1480   1424   -920       N  
ATOM   4191  CA  ILE C 136      -1.529  13.685  31.180  1.00 30.34           C  
ANISOU 4191  CA  ILE C 136     4124   3963   3442  -1289   1410   -922       C  
ATOM   4192  C   ILE C 136      -2.469  13.141  32.239  1.00 31.08           C  
ANISOU 4192  C   ILE C 136     4154   4213   3442  -1493   1561   -914       C  
ATOM   4193  O   ILE C 136      -3.587  12.709  31.917  1.00 34.74           O  
ANISOU 4193  O   ILE C 136     4478   4819   3902  -1752   1593   -947       O  
ATOM   4194  CB  ILE C 136      -2.035  15.068  30.713  1.00 29.53           C  
ANISOU 4194  CB  ILE C 136     3722   4050   3449  -1131   1286  -1011       C  
ATOM   4195  CG1 ILE C 136      -1.199  15.614  29.543  1.00 31.29           C  
ANISOU 4195  CG1 ILE C 136     4015   4134   3741   -982   1140   -992       C  
ATOM   4196  CG2 ILE C 136      -2.079  16.056  31.915  1.00 31.56           C  
ANISOU 4196  CG2 ILE C 136     3868   4413   3710   -952   1356  -1072       C  
ATOM   4197  CD1 ILE C 136       0.246  15.901  29.877  1.00 32.78           C  
ANISOU 4197  CD1 ILE C 136     4360   4145   3952   -791   1133   -925       C  
ATOM   4198  N   ASP C 137      -2.023  13.129  33.495  1.00 33.92           N  
ANISOU 4198  N   ASP C 137     4612   4578   3697  -1428   1644   -847       N  
ATOM   4199  CA  ASP C 137      -2.853  12.641  34.587  1.00 38.66           C  
ANISOU 4199  CA  ASP C 137     5189   5340   4160  -1630   1827   -821       C  
ATOM   4200  C   ASP C 137      -3.081  13.769  35.590  1.00 36.66           C  
ANISOU 4200  C   ASP C 137     4797   5287   3845  -1461   1856   -920       C  
ATOM   4201  O   ASP C 137      -4.112  14.431  35.564  1.00 38.69           O  
ANISOU 4201  O   ASP C 137     4777   5730   4194  -1409   1917  -1031       O  
ATOM   4202  CB  ASP C 137      -2.202  11.418  35.249  1.00 37.74           C  
ANISOU 4202  CB  ASP C 137     5403   5012   3923  -1729   1883   -606       C  
ATOM   4203  CG  ASP C 137      -3.045  10.825  36.363  1.00 43.20           C  
ANISOU 4203  CG  ASP C 137     6100   5828   4484  -1906   1985   -536       C  
ATOM   4204  OD1 ASP C 137      -4.262  11.118  36.441  1.00 43.26           O  
ANISOU 4204  OD1 ASP C 137     5847   6067   4524  -2000   2043   -650       O  
ATOM   4205  OD2 ASP C 137      -2.480  10.046  37.165  1.00 46.82           O  
ANISOU 4205  OD2 ASP C 137     6810   6165   4815  -1940   2019   -323       O  
ATOM   4206  N   THR C 138      -2.117  13.999  36.468  1.00 34.15           N  
ANISOU 4206  N   THR C 138     4684   4928   3364  -1384   1825   -867       N  
ATOM   4207  CA  THR C 138      -2.249  15.078  37.441  1.00 39.15           C  
ANISOU 4207  CA  THR C 138     5299   5692   3886  -1280   1858  -1001       C  
ATOM   4208  C   THR C 138      -1.912  16.381  36.736  1.00 38.70           C  
ANISOU 4208  C   THR C 138     5145   5570   3989  -1059   1763  -1163       C  
ATOM   4209  O   THR C 138      -2.377  17.447  37.124  1.00 40.41           O  
ANISOU 4209  O   THR C 138     5298   5822   4235   -926   1832  -1317       O  
ATOM   4210  CB  THR C 138      -1.280  14.905  38.613  1.00 40.09           C  
ANISOU 4210  CB  THR C 138     5702   5833   3698  -1367   1810   -886       C  
ATOM   4211  OG1 THR C 138       0.068  14.914  38.113  1.00 35.67           O  
ANISOU 4211  OG1 THR C 138     5238   5143   3172  -1295   1602   -757       O  
ATOM   4212  CG2 THR C 138      -1.552  13.599  39.337  1.00 43.94           C  
ANISOU 4212  CG2 THR C 138     6317   6349   4028  -1564   1894   -664       C  
ATOM   4213  N   GLY C 139      -1.100  16.279  35.689  1.00 32.93           N  
ANISOU 4213  N   GLY C 139     4430   4693   3390   -997   1603  -1096       N  
ATOM   4214  CA  GLY C 139      -0.625  17.450  34.972  1.00 34.91           C  
ANISOU 4214  CA  GLY C 139     4621   4839   3803   -803   1464  -1187       C  
ATOM   4215  C   GLY C 139       0.680  18.010  35.514  1.00 38.21           C  
ANISOU 4215  C   GLY C 139     5225   5184   4109   -793   1309  -1157       C  
ATOM   4216  O   GLY C 139       1.244  18.955  34.961  1.00 31.79           O  
ANISOU 4216  O   GLY C 139     4399   4258   3421   -686   1185  -1205       O  
ATOM   4217  N   LYS C 140       1.182  17.429  36.597  1.00 38.36           N  
ANISOU 4217  N   LYS C 140     5409   5287   3877   -943   1291  -1041       N  
ATOM   4218  CA ALYS C 140       2.415  17.915  37.210  0.72 41.25           C  
ANISOU 4218  CA ALYS C 140     5912   5670   4091  -1014   1084   -966       C  
ATOM   4219  CA BLYS C 140       2.409  17.935  37.201  0.28 41.37           C  
ANISOU 4219  CA BLYS C 140     5926   5684   4109  -1012   1084   -970       C  
ATOM   4220  C   LYS C 140       3.628  17.776  36.295  1.00 39.16           C  
ANISOU 4220  C   LYS C 140     5548   5293   4037   -916    869   -743       C  
ATOM   4221  O   LYS C 140       4.463  18.677  36.219  1.00 45.54           O  
ANISOU 4221  O   LYS C 140     6352   6082   4869   -937    700   -757       O  
ATOM   4222  CB ALYS C 140       2.668  17.202  38.534  0.72 45.38           C  
ANISOU 4222  CB ALYS C 140     6606   6366   4270  -1215   1064   -804       C  
ATOM   4223  CB BLYS C 140       2.656  17.306  38.574  0.28 45.93           C  
ANISOU 4223  CB BLYS C 140     6684   6440   4329  -1220   1065   -827       C  
ATOM   4224  CG ALYS C 140       1.564  17.407  39.549  0.72 50.78           C  
ANISOU 4224  CG ALYS C 140     7424   7189   4682  -1342   1326  -1032       C  
ATOM   4225  CG BLYS C 140       1.927  18.013  39.708  0.28 51.33           C  
ANISOU 4225  CG BLYS C 140     7558   7252   4693  -1367   1249  -1109       C  
ATOM   4226  CD ALYS C 140       1.687  16.407  40.691  0.72 55.77           C  
ANISOU 4226  CD ALYS C 140     8229   7996   4966  -1553   1329   -795       C  
ATOM   4227  CD BLYS C 140       0.963  17.078  40.424  0.28 55.25           C  
ANISOU 4227  CD BLYS C 140     8087   7876   5027  -1459   1482  -1050       C  
ATOM   4228  CE ALYS C 140       0.542  16.539  41.679  0.72 59.79           C  
ANISOU 4228  CE ALYS C 140     8803   8597   5318  -1621   1570   -964       C  
ATOM   4229  CE BLYS C 140       1.696  15.947  41.130  0.28 57.04           C  
ANISOU 4229  CE BLYS C 140     8457   8223   4992  -1636   1337   -681       C  
ATOM   4230  NZ ALYS C 140       0.679  17.750  42.532  0.72 65.41           N  
ANISOU 4230  NZ ALYS C 140     9693   9330   5831  -1683   1548  -1199       N  
ATOM   4231  NZ BLYS C 140       0.778  14.873  41.603  0.28 59.25           N  
ANISOU 4231  NZ BLYS C 140     8754   8548   5211  -1713   1549   -560       N  
ATOM   4232  N   THR C 141       3.730  16.648  35.596  1.00 34.12           N  
ANISOU 4232  N   THR C 141     4851   4565   3550   -828    914   -545       N  
ATOM   4233  CA  THR C 141       4.870  16.447  34.699  1.00 33.60           C  
ANISOU 4233  CA  THR C 141     4693   4383   3692   -692    808   -334       C  
ATOM   4234  C   THR C 141       4.892  17.541  33.634  1.00 35.31           C  
ANISOU 4234  C   THR C 141     4819   4513   4084   -607    770   -503       C  
ATOM   4235  O   THR C 141       5.933  18.168  33.394  1.00 33.95           O  
ANISOU 4235  O   THR C 141     4573   4336   3991   -590    627   -406       O  
ATOM   4236  CB  THR C 141       4.865  15.047  34.054  1.00 39.30           C  
ANISOU 4236  CB  THR C 141     5457   4935   4539   -597    961   -159       C  
ATOM   4237  OG1 THR C 141       4.972  14.060  35.086  1.00 44.03           O  
ANISOU 4237  OG1 THR C 141     6160   5572   4997   -658    986     69       O  
ATOM   4238  CG2 THR C 141       6.033  14.888  33.083  1.00 40.49           C  
ANISOU 4238  CG2 THR C 141     5523   4950   4913   -408    949     31       C  
ATOM   4239  N   MET C 142       3.738  17.813  33.026  1.00 30.64           N  
ANISOU 4239  N   MET C 142     4210   3880   3551   -575    883   -714       N  
ATOM   4240  CA  MET C 142       3.703  18.810  31.952  1.00 29.22           C  
ANISOU 4240  CA  MET C 142     3956   3613   3534   -478    834   -807       C  
ATOM   4241  C   MET C 142       3.924  20.223  32.487  1.00 31.59           C  
ANISOU 4241  C   MET C 142     4291   3897   3815   -501    750   -939       C  
ATOM   4242  O   MET C 142       4.611  21.022  31.855  1.00 30.53           O  
ANISOU 4242  O   MET C 142     4138   3664   3798   -472    651   -902       O  
ATOM   4243  CB  MET C 142       2.412  18.719  31.137  1.00 30.65           C  
ANISOU 4243  CB  MET C 142     4062   3802   3781   -444    922   -921       C  
ATOM   4244  CG  MET C 142       2.483  19.440  29.783  1.00 38.20           C  
ANISOU 4244  CG  MET C 142     4959   4676   4878   -347    844   -908       C  
ATOM   4245  SD  MET C 142       3.987  19.141  28.821  1.00 45.35           S  
ANISOU 4245  SD  MET C 142     5931   5459   5840   -314    810   -719       S  
ATOM   4246  CE  MET C 142       3.882  17.379  28.529  1.00 30.69           C  
ANISOU 4246  CE  MET C 142     4199   3555   3908   -376    971   -659       C  
ATOM   4247  N   GLN C 143       3.351  20.522  33.653  1.00 29.69           N  
ANISOU 4247  N   GLN C 143     4145   3728   3407   -581    823  -1102       N  
ATOM   4248  CA  GLN C 143       3.639  21.771  34.348  1.00 33.99           C  
ANISOU 4248  CA  GLN C 143     4843   4207   3865   -664    783  -1273       C  
ATOM   4249  C   GLN C 143       5.148  21.981  34.453  1.00 39.60           C  
ANISOU 4249  C   GLN C 143     5579   4932   4536   -827    540  -1103       C  
ATOM   4250  O   GLN C 143       5.670  23.057  34.137  1.00 44.45           O  
ANISOU 4250  O   GLN C 143     6246   5407   5236   -880    449  -1157       O  
ATOM   4251  CB  GLN C 143       3.079  21.705  35.770  1.00 44.66           C  
ANISOU 4251  CB  GLN C 143     6365   5676   4927   -796    919  -1441       C  
ATOM   4252  CG  GLN C 143       1.953  22.662  36.085  1.00 51.56           C  
ANISOU 4252  CG  GLN C 143     7322   6444   5825   -677   1175  -1738       C  
ATOM   4253  CD  GLN C 143       1.562  22.604  37.564  1.00 58.57           C  
ANISOU 4253  CD  GLN C 143     8388   7454   6412   -809   1293  -1823       C  
ATOM   4254  OE1 GLN C 143       2.212  21.922  38.366  1.00 59.42           O  
ANISOU 4254  OE1 GLN C 143     8630   7736   6211  -1063   1189  -1743       O  
ATOM   4255  NE2 GLN C 143       0.499  23.313  37.925  1.00 57.89           N  
ANISOU 4255  NE2 GLN C 143     8308   7288   6398   -635   1520  -1965       N  
ATOM   4256  N   THR C 144       5.840  20.939  34.902  1.00 40.20           N  
ANISOU 4256  N   THR C 144     5592   5180   4502   -910    437   -857       N  
ATOM   4257  CA  THR C 144       7.278  21.008  35.152  1.00 49.90           C  
ANISOU 4257  CA  THR C 144     6741   6520   5698  -1069    184   -610       C  
ATOM   4258  C   THR C 144       8.064  21.174  33.853  1.00 48.03           C  
ANISOU 4258  C   THR C 144     6303   6186   5760   -942    145   -437       C  
ATOM   4259  O   THR C 144       8.954  22.015  33.766  1.00 52.03           O  
ANISOU 4259  O   THR C 144     6761   6699   6309  -1098    -20   -380       O  
ATOM   4260  CB  THR C 144       7.776  19.768  35.933  1.00 58.17           C  
ANISOU 4260  CB  THR C 144     7720   7783   6600  -1113     95   -298       C  
ATOM   4261  OG1 THR C 144       6.956  19.571  37.094  1.00 59.87           O  
ANISOU 4261  OG1 THR C 144     8153   8097   6497  -1249    171   -452       O  
ATOM   4262  CG2 THR C 144       9.225  19.948  36.372  1.00 63.77           C  
ANISOU 4262  CG2 THR C 144     8275   8697   7258  -1305   -219      6       C  
ATOM   4263  N   LEU C 145       7.721  20.382  32.841  1.00 44.08           N  
ANISOU 4263  N   LEU C 145     5716   5598   5435   -705    313   -364       N  
ATOM   4264  CA  LEU C 145       8.413  20.449  31.554  1.00 42.53           C  
ANISOU 4264  CA  LEU C 145     5378   5315   5467   -582    347   -215       C  
ATOM   4265  C   LEU C 145       8.227  21.813  30.888  1.00 40.79           C  
ANISOU 4265  C   LEU C 145     5217   4952   5331   -622    318   -381       C  
ATOM   4266  O   LEU C 145       9.192  22.419  30.408  1.00 42.39           O  
ANISOU 4266  O   LEU C 145     5322   5140   5645   -693    237   -245       O  
ATOM   4267  CB  LEU C 145       7.932  19.337  30.629  1.00 40.31           C  
ANISOU 4267  CB  LEU C 145     5110   4938   5267   -381    563   -180       C  
ATOM   4268  CG  LEU C 145       8.605  19.248  29.264  1.00 44.83           C  
ANISOU 4268  CG  LEU C 145     5607   5420   6008   -255    676    -50       C  
ATOM   4269  CD1 LEU C 145      10.121  19.352  29.396  1.00 47.76           C  
ANISOU 4269  CD1 LEU C 145     5745   5898   6503   -257    604    252       C  
ATOM   4270  CD2 LEU C 145       8.218  17.953  28.556  1.00 43.99           C  
ANISOU 4270  CD2 LEU C 145     5614   5195   5905   -120    915    -42       C  
ATOM   4271  N   LEU C 146       6.987  22.297  30.870  1.00 33.99           N  
ANISOU 4271  N   LEU C 146     4494   3982   4438   -567    398   -635       N  
ATOM   4272  CA  LEU C 146       6.701  23.615  30.310  1.00 32.66           C  
ANISOU 4272  CA  LEU C 146     4407   3625   4377   -549    388   -756       C  
ATOM   4273  C   LEU C 146       7.536  24.706  30.959  1.00 38.61           C  
ANISOU 4273  C   LEU C 146     5267   4305   5096   -787    249   -796       C  
ATOM   4274  O   LEU C 146       8.067  25.587  30.274  1.00 38.00           O  
ANISOU 4274  O   LEU C 146     5206   4082   5151   -845    199   -731       O  
ATOM   4275  CB  LEU C 146       5.221  23.946  30.432  1.00 33.90           C  
ANISOU 4275  CB  LEU C 146     4640   3704   4537   -407    513   -976       C  
ATOM   4276  CG  LEU C 146       4.319  23.283  29.407  1.00 34.96           C  
ANISOU 4276  CG  LEU C 146     4652   3892   4738   -240    587   -921       C  
ATOM   4277  CD1 LEU C 146       2.884  23.586  29.713  1.00 39.38           C  
ANISOU 4277  CD1 LEU C 146     5177   4459   5327   -112    694  -1080       C  
ATOM   4278  CD2 LEU C 146       4.683  23.805  28.028  1.00 32.23           C  
ANISOU 4278  CD2 LEU C 146     4285   3445   4517   -182    530   -776       C  
ATOM   4279  N   SER C 147       7.660  24.650  32.283  1.00 44.68           N  
ANISOU 4279  N   SER C 147     6142   5180   5653   -981    180   -897       N  
ATOM   4280  CA  SER C 147       8.482  25.620  32.998  1.00 46.62           C  
ANISOU 4280  CA  SER C 147     6539   5386   5787  -1320      9   -958       C  
ATOM   4281  C   SER C 147       9.953  25.514  32.588  1.00 49.95           C  
ANISOU 4281  C   SER C 147     6705   5968   6305  -1496   -195   -625       C  
ATOM   4282  O   SER C 147      10.628  26.522  32.415  1.00 52.67           O  
ANISOU 4282  O   SER C 147     7106   6200   6705  -1740   -307   -617       O  
ATOM   4283  CB  SER C 147       8.339  25.446  34.512  1.00 52.34           C  
ANISOU 4283  CB  SER C 147     7455   6260   6173  -1547    -44  -1115       C  
ATOM   4284  OG  SER C 147       9.175  26.358  35.196  1.00 56.18           O  
ANISOU 4284  OG  SER C 147     8129   6730   6486  -1970   -248  -1188       O  
ATOM   4285  N   LEU C 148      10.440  24.288  32.429  1.00 50.72           N  
ANISOU 4285  N   LEU C 148     6516   6308   6446  -1364   -209   -335       N  
ATOM   4286  CA  LEU C 148      11.821  24.054  32.016  1.00 56.12           C  
ANISOU 4286  CA  LEU C 148     6866   7180   7278  -1441   -332     37       C  
ATOM   4287  C   LEU C 148      12.097  24.617  30.620  1.00 56.49           C  
ANISOU 4287  C   LEU C 148     6839   7056   7567  -1347   -209    105       C  
ATOM   4288  O   LEU C 148      13.033  25.398  30.421  1.00 55.74           O  
ANISOU 4288  O   LEU C 148     6635   6987   7556  -1600   -332    240       O  
ATOM   4289  CB  LEU C 148      12.121  22.558  32.030  1.00 60.69           C  
ANISOU 4289  CB  LEU C 148     7193   7958   7909  -1195   -261    330       C  
ATOM   4290  CG  LEU C 148      13.263  22.123  32.934  1.00 67.50           C  
ANISOU 4290  CG  LEU C 148     7771   9160   8715  -1371   -516    690       C  
ATOM   4291  CD1 LEU C 148      12.881  20.856  33.689  1.00 70.95           C  
ANISOU 4291  CD1 LEU C 148     8226   9705   9028  -1199   -482    804       C  
ATOM   4292  CD2 LEU C 148      14.542  21.928  32.128  1.00 66.67           C  
ANISOU 4292  CD2 LEU C 148     7229   9196   8906  -1279   -493   1097       C  
ATOM   4293  N   VAL C 149      11.271  24.204  29.663  1.00 51.81           N  
ANISOU 4293  N   VAL C 149     6315   6314   7055  -1033     22     28       N  
ATOM   4294  CA  VAL C 149      11.408  24.616  28.273  1.00 45.32           C  
ANISOU 4294  CA  VAL C 149     5473   5357   6390   -935    154    106       C  
ATOM   4295  C   VAL C 149      11.394  26.134  28.138  1.00 46.47           C  
ANISOU 4295  C   VAL C 149     5803   5279   6574  -1146     62     -2       C  
ATOM   4296  O   VAL C 149      12.195  26.716  27.401  1.00 47.50           O  
ANISOU 4296  O   VAL C 149     5846   5378   6825  -1269     65    179       O  
ATOM   4297  CB  VAL C 149      10.290  23.998  27.415  1.00 40.25           C  
ANISOU 4297  CB  VAL C 149     4952   4613   5728   -649    349     -7       C  
ATOM   4298  CG1 VAL C 149      10.234  24.653  26.045  1.00 42.08           C  
ANISOU 4298  CG1 VAL C 149     5249   4706   6034   -603    433     50       C  
ATOM   4299  CG2 VAL C 149      10.499  22.501  27.287  1.00 38.30           C  
ANISOU 4299  CG2 VAL C 149     4584   4495   5472   -472    501    121       C  
ATOM   4300  N   ARG C 150      10.500  26.775  28.877  1.00 46.36           N  
ANISOU 4300  N   ARG C 150     6062   5086   6467  -1189     22   -290       N  
ATOM   4301  CA  ARG C 150      10.354  28.221  28.791  1.00 50.75           C  
ANISOU 4301  CA  ARG C 150     6882   5318   7084  -1337     -4   -422       C  
ATOM   4302  C   ARG C 150      11.587  28.987  29.270  1.00 56.67           C  
ANISOU 4302  C   ARG C 150     7636   6077   7820  -1792   -191   -344       C  
ATOM   4303  O   ARG C 150      11.768  30.153  28.912  1.00 56.97           O  
ANISOU 4303  O   ARG C 150     7875   5819   7953  -1969   -197   -367       O  
ATOM   4304  CB  ARG C 150       9.092  28.682  29.518  1.00 49.48           C  
ANISOU 4304  CB  ARG C 150     7018   4931   6850  -1218     82   -758       C  
ATOM   4305  CG  ARG C 150       7.830  28.377  28.733  1.00 48.29           C  
ANISOU 4305  CG  ARG C 150     6833   4722   6793   -815    241   -776       C  
ATOM   4306  CD  ARG C 150       6.565  28.850  29.435  1.00 56.12           C  
ANISOU 4306  CD  ARG C 150     8025   5523   7776   -642    379  -1058       C  
ATOM   4307  NE  ARG C 150       5.395  28.602  28.595  1.00 59.49           N  
ANISOU 4307  NE  ARG C 150     8317   5963   8323   -286    478   -991       N  
ATOM   4308  CZ  ARG C 150       4.234  28.122  29.031  1.00 58.35           C  
ANISOU 4308  CZ  ARG C 150     8093   5926   8152    -85    598  -1120       C  
ATOM   4309  NH1 ARG C 150       4.067  27.838  30.314  1.00 59.24           N  
ANISOU 4309  NH1 ARG C 150     8296   6113   8100   -180    681  -1343       N  
ATOM   4310  NH2 ARG C 150       3.238  27.932  28.176  1.00 58.46           N  
ANISOU 4310  NH2 ARG C 150     7924   6009   8278    174    625  -1000       N  
ATOM   4311  N   GLN C 151      12.439  28.327  30.056  1.00 58.84           N  
ANISOU 4311  N   GLN C 151     7678   6697   7982  -2004   -359   -211       N  
ATOM   4312  CA  GLN C 151      13.691  28.938  30.518  1.00 63.51           C  
ANISOU 4312  CA  GLN C 151     8172   7415   8544  -2508   -604    -68       C  
ATOM   4313  C   GLN C 151      14.666  29.117  29.357  1.00 62.14           C  
ANISOU 4313  C   GLN C 151     7689   7310   8612  -2555   -561    278       C  
ATOM   4314  O   GLN C 151      15.688  29.781  29.493  1.00 64.02           O  
ANISOU 4314  O   GLN C 151     7814   7631   8879  -2975   -730    427       O  
ATOM   4315  CB  GLN C 151      14.361  28.080  31.596  1.00 66.19           C  
ANISOU 4315  CB  GLN C 151     8243   8195   8709  -2688   -836     94       C  
ATOM   4316  CG  GLN C 151      13.471  27.701  32.768  1.00 68.25           C  
ANISOU 4316  CG  GLN C 151     8782   8470   8680  -2651   -855   -192       C  
ATOM   4317  CD  GLN C 151      13.442  28.750  33.862  1.00 77.54           C  
ANISOU 4317  CD  GLN C 151    10375   9513   9576  -3075   -997   -499       C  
ATOM   4318  OE1 GLN C 151      14.385  29.527  34.026  1.00 81.26           O  
ANISOU 4318  OE1 GLN C 151    10820  10032  10025  -3381  -1159   -404       O  
ATOM   4319  NE2 GLN C 151      12.353  28.773  34.625  1.00 80.32           N  
ANISOU 4319  NE2 GLN C 151    11096   9711   9710  -2951   -850   -851       N  
ATOM   4320  N   TYR C 152      14.351  28.505  28.221  1.00 59.99           N  
ANISOU 4320  N   TYR C 152     7290   7027   8476  -2137   -316    401       N  
ATOM   4321  CA  TYR C 152      15.217  28.572  27.053  1.00 57.20           C  
ANISOU 4321  CA  TYR C 152     6671   6754   8308  -2140   -190    722       C  
ATOM   4322  C   TYR C 152      14.618  29.437  25.950  1.00 52.34           C  
ANISOU 4322  C   TYR C 152     6358   5774   7756  -2049    -36    657       C  
ATOM   4323  O   TYR C 152      15.099  29.443  24.814  1.00 47.97           O  
ANISOU 4323  O   TYR C 152     5668   5261   7298  -1996    131    898       O  
ATOM   4324  CB  TYR C 152      15.550  27.164  26.564  1.00 55.53           C  
ANISOU 4324  CB  TYR C 152     6101   6833   8163  -1784      5    955       C  
ATOM   4325  CG  TYR C 152      16.530  26.475  27.484  1.00 62.92           C  
ANISOU 4325  CG  TYR C 152     6624   8156   9127  -1900   -159   1204       C  
ATOM   4326  CD1 TYR C 152      17.898  26.679  27.345  1.00 65.83           C  
ANISOU 4326  CD1 TYR C 152     6545   8805   9663  -2148   -221   1580       C  
ATOM   4327  CD2 TYR C 152      16.088  25.652  28.519  1.00 65.30           C  
ANISOU 4327  CD2 TYR C 152     6951   8572   9289  -1783   -269   1111       C  
ATOM   4328  CE1 TYR C 152      18.805  26.065  28.195  1.00 71.69           C  
ANISOU 4328  CE1 TYR C 152     6895   9931  10412  -2176   -409   1839       C  
ATOM   4329  CE2 TYR C 152      16.991  25.028  29.373  1.00 69.57           C  
ANISOU 4329  CE2 TYR C 152     7100   9488   9845  -1881   -462   1416       C  
ATOM   4330  CZ  TYR C 152      18.349  25.242  29.206  1.00 73.00           C  
ANISOU 4330  CZ  TYR C 152     7050  10220  10466  -2097   -554   1819       C  
ATOM   4331  OH  TYR C 152      19.250  24.630  30.050  1.00 77.01           O  
ANISOU 4331  OH  TYR C 152     7198  11105  10958  -2094   -765   2135       O  
ATOM   4332  N   ASN C 153      13.566  30.168  26.309  1.00 47.90           N  
ANISOU 4332  N   ASN C 153     7026   4058   7115  -1805    733   -179       N  
ATOM   4333  CA  ASN C 153      12.991  31.199  25.452  1.00 45.58           C  
ANISOU 4333  CA  ASN C 153     6855   3667   6797  -1755    876   -108       C  
ATOM   4334  C   ASN C 153      12.521  30.731  24.075  1.00 42.07           C  
ANISOU 4334  C   ASN C 153     6359   3339   6287  -1697   1064    -20       C  
ATOM   4335  O   ASN C 153      12.899  31.312  23.055  1.00 41.40           O  
ANISOU 4335  O   ASN C 153     6258   3253   6219  -1800   1149    126       O  
ATOM   4336  CB  ASN C 153      13.976  32.364  25.319  1.00 53.70           C  
ANISOU 4336  CB  ASN C 153     7878   4564   7961  -1920    820    -13       C  
ATOM   4337  CG  ASN C 153      14.472  32.856  26.667  1.00 62.74           C  
ANISOU 4337  CG  ASN C 153     9086   5597   9157  -2030    634   -113       C  
ATOM   4338  OD1 ASN C 153      15.646  32.693  27.008  1.00 70.49           O  
ANISOU 4338  OD1 ASN C 153     9917   6602  10264  -2192    495    -78       O  
ATOM   4339  ND2 ASN C 153      13.575  33.453  27.447  1.00 57.44           N  
ANISOU 4339  ND2 ASN C 153     8620   4797   8406  -1964    647   -250       N  
ATOM   4340  N   PRO C 154      11.664  29.699  24.040  1.00 43.13           N  
ANISOU 4340  N   PRO C 154     6484   3584   6320  -1570   1126    -97       N  
ATOM   4341  CA  PRO C 154      11.132  29.297  22.738  1.00 42.28           C  
ANISOU 4341  CA  PRO C 154     6361   3594   6109  -1565   1297    -18       C  
ATOM   4342  C   PRO C 154      10.181  30.378  22.254  1.00 43.34           C  
ANISOU 4342  C   PRO C 154     6672   3573   6222  -1524   1291    157       C  
ATOM   4343  O   PRO C 154       9.732  31.203  23.051  1.00 48.09           O  
ANISOU 4343  O   PRO C 154     7376   3962   6934  -1429   1203    130       O  
ATOM   4344  CB  PRO C 154      10.355  28.021  23.059  1.00 35.47           C  
ANISOU 4344  CB  PRO C 154     5463   2837   5178  -1441   1322   -154       C  
ATOM   4345  CG  PRO C 154       9.911  28.215  24.484  1.00 36.41           C  
ANISOU 4345  CG  PRO C 154     5679   2847   5309  -1343   1176   -251       C  
ATOM   4346  CD  PRO C 154      10.980  29.022  25.159  1.00 41.10           C  
ANISOU 4346  CD  PRO C 154     6274   3343   5999  -1462   1044   -238       C  
ATOM   4347  N   LYS C 155       9.888  30.389  20.964  1.00 44.50           N  
ANISOU 4347  N   LYS C 155     6843   3825   6239  -1616   1375    344       N  
ATOM   4348  CA  LYS C 155       8.987  31.388  20.424  1.00 50.45           C  
ANISOU 4348  CA  LYS C 155     7736   4404   7027  -1593   1296    614       C  
ATOM   4349  C   LYS C 155       7.567  31.023  20.819  1.00 48.05           C  
ANISOU 4349  C   LYS C 155     7451   4037   6768  -1358   1254    569       C  
ATOM   4350  O   LYS C 155       6.764  31.877  21.201  1.00 50.60           O  
ANISOU 4350  O   LYS C 155     7827   4070   7329  -1208   1180    642       O  
ATOM   4351  CB  LYS C 155       9.108  31.421  18.905  1.00 55.86           C  
ANISOU 4351  CB  LYS C 155     8448   5311   7468  -1822   1330    880       C  
ATOM   4352  CG  LYS C 155       8.299  32.512  18.233  1.00 66.16           C  
ANISOU 4352  CG  LYS C 155     9882   6430   8826  -1848   1152   1283       C  
ATOM   4353  CD  LYS C 155       8.199  32.249  16.741  1.00 70.60           C  
ANISOU 4353  CD  LYS C 155    10480   7341   9002  -2108   1125   1543       C  
ATOM   4354  CE  LYS C 155       7.305  33.261  16.054  1.00 76.58           C  
ANISOU 4354  CE  LYS C 155    11329   7935   9832  -2132    837   2030       C  
ATOM   4355  NZ  LYS C 155       6.994  32.845  14.659  1.00 80.55           N  
ANISOU 4355  NZ  LYS C 155    11868   8858   9881  -2379    747   2253       N  
ATOM   4356  N   MET C 156       7.278  29.731  20.732  1.00 44.37           N  
ANISOU 4356  N   MET C 156     6887   3854   6119  -1307   1301    418       N  
ATOM   4357  CA  MET C 156       5.944  29.187  20.978  1.00 42.98           C  
ANISOU 4357  CA  MET C 156     6664   3726   5942  -1095   1247    367       C  
ATOM   4358  C   MET C 156       6.091  27.759  21.504  1.00 41.32           C  
ANISOU 4358  C   MET C 156     6364   3718   5619  -1066   1326     94       C  
ATOM   4359  O   MET C 156       7.004  27.043  21.088  1.00 39.65           O  
ANISOU 4359  O   MET C 156     6082   3680   5302  -1206   1411     15       O  
ATOM   4360  CB  MET C 156       5.132  29.203  19.672  1.00 44.48           C  
ANISOU 4360  CB  MET C 156     6834   4087   5981  -1136   1133    652       C  
ATOM   4361  CG  MET C 156       3.937  28.253  19.632  1.00 48.68           C  
ANISOU 4361  CG  MET C 156     7264   4797   6436   -997   1082    588       C  
ATOM   4362  SD  MET C 156       3.233  28.071  17.976  1.00 65.42           S  
ANISOU 4362  SD  MET C 156     9382   7219   8257  -1182    900    922       S  
ATOM   4363  CE  MET C 156       2.588  29.719  17.693  1.00 69.12           C  
ANISOU 4363  CE  MET C 156     9863   7344   9056  -1110    636   1383       C  
ATOM   4364  N   VAL C 157       5.225  27.357  22.437  1.00 36.17           N  
ANISOU 4364  N   VAL C 157     5698   3015   5032   -899   1317    -54       N  
ATOM   4365  CA  VAL C 157       5.174  25.963  22.886  1.00 35.17           C  
ANISOU 4365  CA  VAL C 157     5492   3062   4809   -881   1350   -246       C  
ATOM   4366  C   VAL C 157       3.747  25.454  22.896  1.00 38.13           C  
ANISOU 4366  C   VAL C 157     5811   3523   5153   -735   1331   -262       C  
ATOM   4367  O   VAL C 157       2.872  26.039  23.543  1.00 37.28           O  
ANISOU 4367  O   VAL C 157     5723   3254   5187   -608   1341   -283       O  
ATOM   4368  CB  VAL C 157       5.719  25.751  24.316  1.00 41.75           C  
ANISOU 4368  CB  VAL C 157     6377   3775   5710   -915   1342   -422       C  
ATOM   4369  CG1 VAL C 157       5.910  24.257  24.584  1.00 37.35           C  
ANISOU 4369  CG1 VAL C 157     5714   3375   5104   -937   1322   -531       C  
ATOM   4370  CG2 VAL C 157       7.020  26.471  24.521  1.00 45.40           C  
ANISOU 4370  CG2 VAL C 157     6883   4108   6258  -1062   1315   -395       C  
ATOM   4371  N   LYS C 158       3.516  24.341  22.212  1.00 32.49           N  
ANISOU 4371  N   LYS C 158     5008   3048   4290   -768   1333   -289       N  
ATOM   4372  CA  LYS C 158       2.233  23.662  22.296  1.00 30.91           C  
ANISOU 4372  CA  LYS C 158     4731   2949   4064   -665   1306   -324       C  
ATOM   4373  C   LYS C 158       2.482  22.219  22.737  1.00 29.14           C  
ANISOU 4373  C   LYS C 158     4456   2832   3784   -706   1352   -517       C  
ATOM   4374  O   LYS C 158       3.567  21.672  22.497  1.00 27.90           O  
ANISOU 4374  O   LYS C 158     4272   2707   3623   -811   1396   -590       O  
ATOM   4375  CB  LYS C 158       1.531  23.676  20.935  1.00 33.44           C  
ANISOU 4375  CB  LYS C 158     4998   3453   4255   -711   1212   -137       C  
ATOM   4376  CG  LYS C 158       1.390  25.045  20.298  1.00 39.64           C  
ANISOU 4376  CG  LYS C 158     5823   4123   5116   -716   1096    152       C  
ATOM   4377  CD  LYS C 158       0.132  25.745  20.731  1.00 49.31           C  
ANISOU 4377  CD  LYS C 158     6946   5156   6635   -507   1008    262       C  
ATOM   4378  CE  LYS C 158      -0.342  26.670  19.620  1.00 55.13           C  
ANISOU 4378  CE  LYS C 158     7646   5861   7439   -546    779    656       C  
ATOM   4379  NZ  LYS C 158      -0.946  27.917  20.140  1.00 61.73           N  
ANISOU 4379  NZ  LYS C 158     8395   6312   8747   -334    735    781       N  
ATOM   4380  N   VAL C 159       1.483  21.611  23.368  1.00 27.65           N  
ANISOU 4380  N   VAL C 159     4226   2671   3608   -631   1349   -591       N  
ATOM   4381  CA  VAL C 159       1.578  20.226  23.817  1.00 30.72           C  
ANISOU 4381  CA  VAL C 159     4571   3124   3979   -681   1358   -725       C  
ATOM   4382  C   VAL C 159       0.526  19.359  23.132  1.00 28.36           C  
ANISOU 4382  C   VAL C 159     4172   3003   3602   -677   1347   -745       C  
ATOM   4383  O   VAL C 159      -0.644  19.737  23.079  1.00 30.32           O  
ANISOU 4383  O   VAL C 159     4370   3291   3860   -599   1320   -676       O  
ATOM   4384  CB  VAL C 159       1.379  20.149  25.341  1.00 26.24           C  
ANISOU 4384  CB  VAL C 159     4082   2443   3444   -685   1362   -792       C  
ATOM   4385  CG1 VAL C 159       1.463  18.721  25.840  1.00 28.68           C  
ANISOU 4385  CG1 VAL C 159     4352   2788   3756   -765   1315   -851       C  
ATOM   4386  CG2 VAL C 159       2.407  21.030  26.054  1.00 30.10           C  
ANISOU 4386  CG2 VAL C 159     4696   2770   3971   -749   1342   -782       C  
ATOM   4387  N   ALA C 160       0.950  18.210  22.597  1.00 27.62           N  
ANISOU 4387  N   ALA C 160     4022   2991   3481   -771   1374   -853       N  
ATOM   4388  CA  ALA C 160       0.026  17.191  22.120  1.00 27.17           C  
ANISOU 4388  CA  ALA C 160     3889   3079   3355   -815   1364   -923       C  
ATOM   4389  C   ALA C 160       0.143  15.999  23.069  1.00 30.85           C  
ANISOU 4389  C   ALA C 160     4324   3440   3959   -830   1367  -1029       C  
ATOM   4390  O   ALA C 160       1.246  15.511  23.325  1.00 30.37           O  
ANISOU 4390  O   ALA C 160     4243   3243   4053   -864   1381  -1088       O  
ATOM   4391  CB  ALA C 160       0.366  16.772  20.677  1.00 26.78           C  
ANISOU 4391  CB  ALA C 160     3828   3190   3159   -971   1423  -1008       C  
ATOM   4392  N   SER C 161      -0.979  15.523  23.592  1.00 27.11           N  
ANISOU 4392  N   SER C 161     3820   3010   3471   -820   1339  -1025       N  
ATOM   4393  CA  SER C 161      -0.955  14.310  24.418  1.00 23.96           C  
ANISOU 4393  CA  SER C 161     3406   2514   3184   -885   1314  -1076       C  
ATOM   4394  C   SER C 161      -1.960  13.331  23.867  1.00 24.14           C  
ANISOU 4394  C   SER C 161     3340   2653   3178   -949   1318  -1153       C  
ATOM   4395  O   SER C 161      -3.112  13.706  23.618  1.00 28.51           O  
ANISOU 4395  O   SER C 161     3842   3359   3632   -927   1310  -1109       O  
ATOM   4396  CB  SER C 161      -1.285  14.649  25.881  1.00 27.29           C  
ANISOU 4396  CB  SER C 161     3922   2871   3577   -896   1296   -995       C  
ATOM   4397  OG  SER C 161      -1.221  13.501  26.705  1.00 28.64           O  
ANISOU 4397  OG  SER C 161     4109   2953   3820  -1016   1223   -971       O  
ATOM   4398  N   LEU C 162      -1.533  12.088  23.649  1.00 23.62           N  
ANISOU 4398  N   LEU C 162     3227   2491   3258  -1033   1325  -1270       N  
ATOM   4399  CA  LEU C 162      -2.438  11.077  23.147  1.00 25.44           C  
ANISOU 4399  CA  LEU C 162     3389   2804   3475  -1134   1331  -1374       C  
ATOM   4400  C   LEU C 162      -3.647  10.982  24.066  1.00 27.15           C  
ANISOU 4400  C   LEU C 162     3591   3079   3646  -1148   1285  -1264       C  
ATOM   4401  O   LEU C 162      -4.789  10.945  23.595  1.00 25.29           O  
ANISOU 4401  O   LEU C 162     3273   3021   3315  -1186   1275  -1273       O  
ATOM   4402  CB  LEU C 162      -1.763   9.708  23.054  1.00 27.17           C  
ANISOU 4402  CB  LEU C 162     3542   2825   3956  -1194   1350  -1498       C  
ATOM   4403  CG  LEU C 162      -2.711   8.577  22.644  1.00 30.78           C  
ANISOU 4403  CG  LEU C 162     3940   3337   4417  -1310   1351  -1604       C  
ATOM   4404  CD1 LEU C 162      -3.308   8.815  21.243  1.00 30.85           C  
ANISOU 4404  CD1 LEU C 162     3956   3603   4162  -1439   1412  -1766       C  
ATOM   4405  CD2 LEU C 162      -2.017   7.216  22.678  1.00 33.70           C  
ANISOU 4405  CD2 LEU C 162     4215   3488   5100  -1275   1346  -1647       C  
ATOM   4406  N   LEU C 163      -3.390  10.941  25.374  1.00 25.88           N  
ANISOU 4406  N   LEU C 163     3504   2785   3546  -1158   1256  -1155       N  
ATOM   4407  CA  LEU C 163      -4.451  10.723  26.359  1.00 26.53           C  
ANISOU 4407  CA  LEU C 163     3594   2923   3563  -1243   1275  -1084       C  
ATOM   4408  C   LEU C 163      -4.476  11.799  27.424  1.00 26.05           C  
ANISOU 4408  C   LEU C 163     3644   2876   3378  -1223   1342  -1009       C  
ATOM   4409  O   LEU C 163      -3.436  12.314  27.836  1.00 31.26           O  
ANISOU 4409  O   LEU C 163     4422   3428   4028  -1206   1295   -960       O  
ATOM   4410  CB  LEU C 163      -4.287   9.365  27.053  1.00 26.90           C  
ANISOU 4410  CB  LEU C 163     3672   2803   3746  -1408   1187  -1026       C  
ATOM   4411  CG  LEU C 163      -4.179   8.112  26.198  1.00 28.25           C  
ANISOU 4411  CG  LEU C 163     3744   2862   4130  -1460   1150  -1143       C  
ATOM   4412  CD1 LEU C 163      -3.952   6.881  27.083  1.00 28.19           C  
ANISOU 4412  CD1 LEU C 163     3757   2654   4300  -1543    992   -976       C  
ATOM   4413  CD2 LEU C 163      -5.415   7.919  25.302  1.00 28.07           C  
ANISOU 4413  CD2 LEU C 163     3609   3052   4003  -1502   1213  -1270       C  
ATOM   4414  N   VAL C 164      -5.679  12.140  27.873  1.00 28.18           N  
ANISOU 4414  N   VAL C 164     3860   3272   3577  -1246   1475  -1031       N  
ATOM   4415  CA  VAL C 164      -5.844  13.008  29.034  1.00 25.95           C  
ANISOU 4415  CA  VAL C 164     3694   2989   3176  -1294   1625  -1043       C  
ATOM   4416  C   VAL C 164      -6.832  12.327  29.958  1.00 27.79           C  
ANISOU 4416  C   VAL C 164     3928   3302   3328  -1509   1750  -1054       C  
ATOM   4417  O   VAL C 164      -7.904  11.918  29.531  1.00 30.92           O  
ANISOU 4417  O   VAL C 164     4124   3804   3820  -1499   1811  -1093       O  
ATOM   4418  CB  VAL C 164      -6.335  14.422  28.654  1.00 32.31           C  
ANISOU 4418  CB  VAL C 164     4392   3829   4055  -1092   1766  -1117       C  
ATOM   4419  CG1 VAL C 164      -6.675  15.234  29.913  1.00 32.09           C  
ANISOU 4419  CG1 VAL C 164     4470   3774   3948  -1175   2009  -1224       C  
ATOM   4420  CG2 VAL C 164      -5.283  15.145  27.833  1.00 35.33           C  
ANISOU 4420  CG2 VAL C 164     4819   4133   4474   -941   1643  -1070       C  
ATOM   4421  N   LYS C 165      -6.467  12.176  31.226  1.00 29.34           N  
ANISOU 4421  N   LYS C 165     4356   3466   3326  -1753   1771  -1001       N  
ATOM   4422  CA  LYS C 165      -7.347  11.510  32.174  1.00 34.33           C  
ANISOU 4422  CA  LYS C 165     5034   4194   3815  -2026   1895   -993       C  
ATOM   4423  C   LYS C 165      -8.278  12.495  32.865  1.00 33.48           C  
ANISOU 4423  C   LYS C 165     4902   4165   3653  -1994   2145  -1185       C  
ATOM   4424  O   LYS C 165      -7.866  13.608  33.195  1.00 36.79           O  
ANISOU 4424  O   LYS C 165     5419   4520   4039  -1933   2213  -1275       O  
ATOM   4425  CB  LYS C 165      -6.538  10.774  33.239  1.00 37.83           C  
ANISOU 4425  CB  LYS C 165     5756   4569   4049  -2310   1668   -789       C  
ATOM   4426  CG  LYS C 165      -6.031   9.418  32.805  1.00 39.29           C  
ANISOU 4426  CG  LYS C 165     5885   4609   4434  -2319   1356   -580       C  
ATOM   4427  CD  LYS C 165      -5.468   8.651  33.987  1.00 43.95           C  
ANISOU 4427  CD  LYS C 165     6684   5144   4869  -2571   1084   -306       C  
ATOM   4428  CE  LYS C 165      -5.237   7.204  33.630  1.00 42.67           C  
ANISOU 4428  CE  LYS C 165     6399   4794   5020  -2552    815   -106       C  
ATOM   4429  NZ  LYS C 165      -4.615   6.460  34.753  1.00 37.94           N  
ANISOU 4429  NZ  LYS C 165     5955   4101   4360  -2777    498    225       N  
ATOM   4430  N   ARG C 166      -9.532  12.099  33.064  1.00 36.47           N  
ANISOU 4430  N   ARG C 166     3841   5674   4343   -440   2120   -755       N  
ATOM   4431  CA  ARG C 166     -10.418  12.861  33.934  1.00 38.94           C  
ANISOU 4431  CA  ARG C 166     4232   5998   4566   -264   2327   -835       C  
ATOM   4432  C   ARG C 166     -10.100  12.426  35.357  1.00 47.64           C  
ANISOU 4432  C   ARG C 166     5369   7227   5505   -430   2349   -915       C  
ATOM   4433  O   ARG C 166     -10.265  11.257  35.697  1.00 48.59           O  
ANISOU 4433  O   ARG C 166     5293   7561   5608   -529   2270   -827       O  
ATOM   4434  CB  ARG C 166     -11.892  12.587  33.610  1.00 40.20           C  
ANISOU 4434  CB  ARG C 166     4142   6348   4783    -35   2400   -693       C  
ATOM   4435  CG  ARG C 166     -12.339  13.126  32.247  1.00 40.65           C  
ANISOU 4435  CG  ARG C 166     4150   6314   4981    164   2404   -603       C  
ATOM   4436  CD  ARG C 166     -13.835  12.959  32.051  1.00 43.68           C  
ANISOU 4436  CD  ARG C 166     4263   6962   5370    391   2495   -445       C  
ATOM   4437  NE  ARG C 166     -14.226  11.551  32.096  1.00 43.33           N  
ANISOU 4437  NE  ARG C 166     3944   7205   5316    200   2364   -312       N  
ATOM   4438  CZ  ARG C 166     -14.128  10.717  31.065  1.00 40.72           C  
ANISOU 4438  CZ  ARG C 166     3494   6893   5084     58   2178   -178       C  
ATOM   4439  NH1 ARG C 166     -13.652  11.144  29.905  1.00 39.93           N  
ANISOU 4439  NH1 ARG C 166     3446   6620   5106     93   2124   -175       N  
ATOM   4440  NH2 ARG C 166     -14.503   9.452  31.192  1.00 46.63           N  
ANISOU 4440  NH2 ARG C 166     4152   7750   5814   -122   2025    -54       N  
ATOM   4441  N   THR C 167      -9.620  13.356  36.176  1.00 43.99           N  
ANISOU 4441  N   THR C 167     5183   6625   4906   -480   2458  -1080       N  
ATOM   4442  CA  THR C 167      -9.247  13.036  37.557  1.00 43.45           C  
ANISOU 4442  CA  THR C 167     5167   6677   4666   -657   2481  -1165       C  
ATOM   4443  C   THR C 167      -9.338  14.253  38.471  1.00 46.42           C  
ANISOU 4443  C   THR C 167     5870   6889   4877   -614   2683  -1339       C  
ATOM   4444  O   THR C 167      -9.063  15.376  38.041  1.00 47.07           O  
ANISOU 4444  O   THR C 167     6235   6711   4938   -574   2760  -1428       O  
ATOM   4445  CB  THR C 167      -7.813  12.451  37.625  1.00 46.02           C  
ANISOU 4445  CB  THR C 167     5490   7062   4933   -962   2298  -1164       C  
ATOM   4446  OG1 THR C 167      -7.354  12.446  38.983  1.00 49.26           O  
ANISOU 4446  OG1 THR C 167     6001   7571   5144  -1141   2341  -1266       O  
ATOM   4447  CG2 THR C 167      -6.861  13.279  36.786  1.00 44.86           C  
ANISOU 4447  CG2 THR C 167     5530   6707   4807  -1054   2237  -1214       C  
ATOM   4448  N   PRO C 168      -9.725  14.034  39.739  1.00 48.46           N  
ANISOU 4448  N   PRO C 168     6128   7283   5000   -629   2781  -1389       N  
ATOM   4449  CA  PRO C 168      -9.773  15.139  40.707  1.00 50.75           C  
ANISOU 4449  CA  PRO C 168     6776   7399   5106   -604   2965  -1548       C  
ATOM   4450  C   PRO C 168      -8.379  15.643  41.073  1.00 52.00           C  
ANISOU 4450  C   PRO C 168     7222   7436   5101   -958   2909  -1693       C  
ATOM   4451  O   PRO C 168      -8.254  16.702  41.688  1.00 54.26           O  
ANISOU 4451  O   PRO C 168     7882   7509   5226   -994   3031  -1825       O  
ATOM   4452  CB  PRO C 168     -10.452  14.511  41.936  1.00 50.38           C  
ANISOU 4452  CB  PRO C 168     6586   7562   4995   -551   2977  -1504       C  
ATOM   4453  CG  PRO C 168     -10.297  13.040  41.764  1.00 48.90           C  
ANISOU 4453  CG  PRO C 168     6036   7631   4912   -673   2762  -1357       C  
ATOM   4454  CD  PRO C 168     -10.304  12.794  40.287  1.00 48.67           C  
ANISOU 4454  CD  PRO C 168     5853   7583   5058   -615   2684  -1256       C  
ATOM   4455  N   ARG C 169      -7.347  14.896  40.697  1.00 48.76           N  
ANISOU 4455  N   ARG C 169     6637   7167   4721  -1212   2699  -1635       N  
ATOM   4456  CA  ARG C 169      -5.974  15.282  41.007  1.00 53.54           C  
ANISOU 4456  CA  ARG C 169     7441   7755   5148  -1574   2614  -1727       C  
ATOM   4457  C   ARG C 169      -5.381  16.278  40.017  1.00 52.67           C  
ANISOU 4457  C   ARG C 169     7576   7387   5049  -1641   2597  -1778       C  
ATOM   4458  O   ARG C 169      -4.312  16.831  40.267  1.00 56.51           O  
ANISOU 4458  O   ARG C 169     8284   7842   5344  -1966   2554  -1868       O  
ATOM   4459  CB  ARG C 169      -5.072  14.053  41.071  1.00 51.67           C  
ANISOU 4459  CB  ARG C 169     6899   7822   4912  -1778   2392  -1600       C  
ATOM   4460  CG  ARG C 169      -5.418  13.084  42.180  1.00 54.71           C  
ANISOU 4460  CG  ARG C 169     7090   8415   5281  -1747   2334  -1529       C  
ATOM   4461  CD  ARG C 169      -4.264  12.134  42.410  1.00 56.59           C  
ANISOU 4461  CD  ARG C 169     7144   8892   5465  -1948   2110  -1413       C  
ATOM   4462  NE  ARG C 169      -3.904  11.410  41.193  1.00 54.94           N  
ANISOU 4462  NE  ARG C 169     6742   8730   5402  -1881   1969  -1257       N  
ATOM   4463  CZ  ARG C 169      -2.831  10.634  41.073  1.00 53.67           C  
ANISOU 4463  CZ  ARG C 169     6445   8740   5206  -1977   1774  -1123       C  
ATOM   4464  NH1 ARG C 169      -2.007  10.473  42.099  1.00 52.47           N  
ANISOU 4464  NH1 ARG C 169     6291   8762   4882  -2152   1691  -1122       N  
ATOM   4465  NH2 ARG C 169      -2.580  10.019  39.926  1.00 49.21           N  
ANISOU 4465  NH2 ARG C 169     5753   8172   4772  -1875   1664   -978       N  
ATOM   4466  N   SER C 170      -6.071  16.486  38.896  1.00 52.59           N  
ANISOU 4466  N   SER C 170     7517   7221   5245  -1353   2626  -1710       N  
ATOM   4467  CA  SER C 170      -5.633  17.422  37.856  1.00 56.05           C  
ANISOU 4467  CA  SER C 170     8184   7394   5718  -1370   2621  -1748       C  
ATOM   4468  C   SER C 170      -5.359  18.813  38.419  1.00 61.75           C  
ANISOU 4468  C   SER C 170     9435   7834   6195  -1507   2798  -1945       C  
ATOM   4469  O   SER C 170      -6.178  19.361  39.161  1.00 63.06           O  
ANISOU 4469  O   SER C 170     9832   7870   6259  -1330   3019  -2030       O  
ATOM   4470  CB  SER C 170      -6.679  17.501  36.738  1.00 58.09           C  
ANISOU 4470  CB  SER C 170     8322   7536   6214   -981   2676  -1647       C  
ATOM   4471  OG  SER C 170      -6.557  18.698  35.997  1.00 63.60           O  
ANISOU 4471  OG  SER C 170     9352   7910   6901   -918   2766  -1721       O  
ATOM   4472  N   VAL C 171      -4.198  19.375  38.088  1.00 64.91           N  
ANISOU 4472  N   VAL C 171    10047   8145   6472  -1837   2706  -2008       N  
ATOM   4473  CA  VAL C 171      -3.859  20.714  38.571  1.00 71.45           C  
ANISOU 4473  CA  VAL C 171    11411   8677   7059  -2026   2833  -2165       C  
ATOM   4474  C   VAL C 171      -4.536  21.782  37.716  1.00 72.52           C  
ANISOU 4474  C   VAL C 171    11846   8418   7290  -1711   2982  -2176       C  
ATOM   4475  O   VAL C 171      -4.488  22.972  38.031  1.00 75.58           O  
ANISOU 4475  O   VAL C 171    12679   8502   7536  -1758   3081  -2235       O  
ATOM   4476  CB  VAL C 171      -2.326  20.962  38.654  1.00 70.51           C  
ANISOU 4476  CB  VAL C 171    11391   8653   6745  -2553   2651  -2190       C  
ATOM   4477  CG1 VAL C 171      -1.738  20.304  39.900  1.00 70.95           C  
ANISOU 4477  CG1 VAL C 171    11275   9045   6639  -2850   2548  -2174       C  
ATOM   4478  CG2 VAL C 171      -1.621  20.489  37.397  1.00 67.66           C  
ANISOU 4478  CG2 VAL C 171    10782   8427   6499  -2631   2476  -2107       C  
ATOM   4479  N   GLY C 172      -5.181  21.344  36.640  1.00 69.40           N  
ANISOU 4479  N   GLY C 172    11197   8043   7130  -1383   2999  -2092       N  
ATOM   4480  CA  GLY C 172      -5.924  22.249  35.787  1.00 69.22           C  
ANISOU 4480  CA  GLY C 172    11379   7704   7219  -1020   3128  -2057       C  
ATOM   4481  C   GLY C 172      -5.192  22.546  34.499  1.00 67.22           C  
ANISOU 4481  C   GLY C 172    11174   7320   7048  -1138   3018  -2050       C  
ATOM   4482  O   GLY C 172      -5.573  23.447  33.752  1.00 67.34           O  
ANISOU 4482  O   GLY C 172    11409   7051   7126   -905   3097  -2018       O  
ATOM   4483  N   TYR C 173      -4.130  21.794  34.235  1.00 64.61           N  
ANISOU 4483  N   TYR C 173    10572   7231   6747  -1475   2770  -2006       N  
ATOM   4484  CA  TYR C 173      -3.418  21.953  32.977  1.00 63.34           C  
ANISOU 4484  CA  TYR C 173    10373   6997   6697  -1573   2616  -1952       C  
ATOM   4485  C   TYR C 173      -4.135  21.217  31.837  1.00 57.67           C  
ANISOU 4485  C   TYR C 173     9238   6359   6315  -1208   2532  -1771       C  
ATOM   4486  O   TYR C 173      -4.533  20.068  32.007  1.00 60.37           O  
ANISOU 4486  O   TYR C 173     9167   6980   6789  -1104   2441  -1649       O  
ATOM   4487  CB  TYR C 173      -1.973  21.453  33.073  1.00 61.09           C  
ANISOU 4487  CB  TYR C 173     9931   6979   6301  -2042   2372  -1924       C  
ATOM   4488  CG  TYR C 173      -1.356  21.477  31.710  1.00 58.32           C  
ANISOU 4488  CG  TYR C 173     9472   6591   6097  -2077   2211  -1836       C  
ATOM   4489  CD1 TYR C 173      -0.939  22.677  31.152  1.00 59.00           C  
ANISOU 4489  CD1 TYR C 173     9977   6368   6073  -2213   2274  -1941       C  
ATOM   4490  CD2 TYR C 173      -1.262  20.317  30.944  1.00 56.27           C  
ANISOU 4490  CD2 TYR C 173     8729   6571   6078  -1954   2016  -1647       C  
ATOM   4491  CE1 TYR C 173      -0.418  22.723  29.889  1.00 56.50           C  
ANISOU 4491  CE1 TYR C 173     9562   6011   5895  -2231   2133  -1860       C  
ATOM   4492  CE2 TYR C 173      -0.739  20.352  29.667  1.00 53.81           C  
ANISOU 4492  CE2 TYR C 173     8333   6209   5902  -1961   1882  -1563       C  
ATOM   4493  CZ  TYR C 173      -0.318  21.562  29.153  1.00 54.21           C  
ANISOU 4493  CZ  TYR C 173     8766   5977   5853  -2099   1936  -1670       C  
ATOM   4494  OH  TYR C 173       0.201  21.625  27.893  1.00 49.23           O  
ANISOU 4494  OH  TYR C 173     8055   5296   5354  -2109   1804  -1589       O  
ATOM   4495  N   LYS C 174      -4.275  21.864  30.677  1.00 52.27           N  
ANISOU 4495  N   LYS C 174     8680   5432   5748  -1041   2561  -1753       N  
ATOM   4496  CA  LYS C 174      -4.873  21.213  29.505  1.00 49.39           C  
ANISOU 4496  CA  LYS C 174     7935   5148   5682   -744   2467  -1579       C  
ATOM   4497  C   LYS C 174      -4.037  21.382  28.236  1.00 44.55           C  
ANISOU 4497  C   LYS C 174     7311   4440   5174   -869   2304  -1535       C  
ATOM   4498  O   LYS C 174      -3.676  22.499  27.875  1.00 45.63           O  
ANISOU 4498  O   LYS C 174     7838   4287   5214   -937   2387  -1639       O  
ATOM   4499  CB  LYS C 174      -6.304  21.703  29.263  1.00 56.81           C  
ANISOU 4499  CB  LYS C 174     8931   5948   6705   -269   2693  -1543       C  
ATOM   4500  CG  LYS C 174      -7.334  21.048  30.175  1.00 64.48           C  
ANISOU 4500  CG  LYS C 174     9673   7154   7673    -69   2786  -1487       C  
ATOM   4501  CD  LYS C 174      -8.670  20.831  29.466  1.00 67.89           C  
ANISOU 4501  CD  LYS C 174     9829   7679   8286    370   2863  -1323       C  
ATOM   4502  CE  LYS C 174      -9.668  20.089  30.360  1.00 71.71           C  
ANISOU 4502  CE  LYS C 174    10040   8457   8750    523   2932  -1247       C  
ATOM   4503  NZ  LYS C 174     -10.975  19.832  29.683  1.00 72.78           N  
ANISOU 4503  NZ  LYS C 174     9860   8770   9024    905   2993  -1059       N  
ATOM   4504  N   PRO C 175      -3.738  20.264  27.549  1.00 40.72           N  
ANISOU 4504  N   PRO C 175     6408   4189   4874   -895   2084  -1377       N  
ATOM   4505  CA  PRO C 175      -2.897  20.310  26.345  1.00 40.61           C  
ANISOU 4505  CA  PRO C 175     6350   4120   4961  -1008   1918  -1317       C  
ATOM   4506  C   PRO C 175      -3.601  21.000  25.175  1.00 40.08           C  
ANISOU 4506  C   PRO C 175     6378   3790   5061   -703   2004  -1291       C  
ATOM   4507  O   PRO C 175      -4.827  21.107  25.172  1.00 38.92           O  
ANISOU 4507  O   PRO C 175     6192   3602   4994   -360   2157  -1257       O  
ATOM   4508  CB  PRO C 175      -2.670  18.827  26.003  1.00 37.75           C  
ANISOU 4508  CB  PRO C 175     5535   4064   4744  -1023   1709  -1137       C  
ATOM   4509  CG  PRO C 175      -3.172  18.036  27.168  1.00 39.34           C  
ANISOU 4509  CG  PRO C 175     5580   4489   4878  -1005   1751  -1124       C  
ATOM   4510  CD  PRO C 175      -4.189  18.898  27.864  1.00 40.07           C  
ANISOU 4510  CD  PRO C 175     5913   4417   4896   -818   1993  -1244       C  
ATOM   4511  N   ASP C 176      -2.830  21.456  24.193  1.00 37.57           N  
ANISOU 4511  N   ASP C 176     6164   3330   4782   -820   1909  -1291       N  
ATOM   4512  CA  ASP C 176      -3.404  22.088  23.016  1.00 40.41           C  
ANISOU 4512  CA  ASP C 176     6605   3448   5300   -539   1978  -1256       C  
ATOM   4513  C   ASP C 176      -4.056  21.062  22.098  1.00 37.82           C  
ANISOU 4513  C   ASP C 176     5838   3293   5240   -303   1861  -1064       C  
ATOM   4514  O   ASP C 176      -5.110  21.317  21.522  1.00 40.31           O  
ANISOU 4514  O   ASP C 176     6108   3531   5678     33   1970  -1001       O  
ATOM   4515  CB  ASP C 176      -2.325  22.871  22.270  1.00 38.73           C  
ANISOU 4515  CB  ASP C 176     6647   3036   5031   -774   1903  -1318       C  
ATOM   4516  CG  ASP C 176      -1.604  23.837  23.175  1.00 44.83           C  
ANISOU 4516  CG  ASP C 176     7878   3662   5493  -1100   2001  -1505       C  
ATOM   4517  OD1 ASP C 176      -2.113  24.956  23.368  1.00 45.71           O  
ANISOU 4517  OD1 ASP C 176     8320   3560   5488   -944   2165  -1540       O  
ATOM   4518  OD2 ASP C 176      -0.553  23.461  23.727  1.00 40.34           O  
ANISOU 4518  OD2 ASP C 176     7244   3312   4772  -1484   1857  -1518       O  
ATOM   4519  N   PHE C 177      -3.426  19.898  21.975  1.00 32.62           N  
ANISOU 4519  N   PHE C 177     4873   2881   4640   -481   1650   -958       N  
ATOM   4520  CA  PHE C 177      -3.945  18.834  21.134  1.00 30.31           C  
ANISOU 4520  CA  PHE C 177     4220   2739   4558   -324   1534   -778       C  
ATOM   4521  C   PHE C 177      -4.107  17.577  21.977  1.00 35.65           C  
ANISOU 4521  C   PHE C 177     4646   3706   5194   -394   1475   -706       C  
ATOM   4522  O   PHE C 177      -3.170  17.150  22.660  1.00 33.65           O  
ANISOU 4522  O   PHE C 177     4389   3588   4808   -637   1392   -727       O  
ATOM   4523  CB  PHE C 177      -3.001  18.572  19.959  1.00 28.27           C  
ANISOU 4523  CB  PHE C 177     3886   2452   4405   -440   1344   -694       C  
ATOM   4524  CG  PHE C 177      -2.572  19.832  19.245  1.00 34.80           C  
ANISOU 4524  CG  PHE C 177     4997   2996   5228   -453   1385   -783       C  
ATOM   4525  CD1 PHE C 177      -3.430  20.469  18.357  1.00 37.28           C  
ANISOU 4525  CD1 PHE C 177     5368   3115   5681   -170   1483   -763       C  
ATOM   4526  CD2 PHE C 177      -1.325  20.398  19.491  1.00 35.05           C  
ANISOU 4526  CD2 PHE C 177     5247   2979   5090   -761   1334   -879       C  
ATOM   4527  CE1 PHE C 177      -3.042  21.646  17.708  1.00 38.55           C  
ANISOU 4527  CE1 PHE C 177     5831   2989   5825   -173   1536   -847       C  
ATOM   4528  CE2 PHE C 177      -0.928  21.564  18.845  1.00 33.23           C  
ANISOU 4528  CE2 PHE C 177     5316   2478   4831   -811   1375   -966       C  
ATOM   4529  CZ  PHE C 177      -1.790  22.188  17.955  1.00 35.92           C  
ANISOU 4529  CZ  PHE C 177     5745   2579   5323   -506   1482   -956       C  
ATOM   4530  N   VAL C 178      -5.301  16.996  21.937  1.00 29.26           N  
ANISOU 4530  N   VAL C 178     3627   3015   4477   -187   1523   -611       N  
ATOM   4531  CA  VAL C 178      -5.602  15.828  22.755  1.00 28.71           C  
ANISOU 4531  CA  VAL C 178     3351   3203   4354   -249   1489   -547       C  
ATOM   4532  C   VAL C 178      -6.220  14.731  21.905  1.00 29.72           C  
ANISOU 4532  C   VAL C 178     3208   3464   4621   -176   1387   -366       C  
ATOM   4533  O   VAL C 178      -7.215  14.970  21.220  1.00 28.21           O  
ANISOU 4533  O   VAL C 178     2926   3259   4534     22   1442   -299       O  
ATOM   4534  CB  VAL C 178      -6.606  16.169  23.862  1.00 33.24           C  
ANISOU 4534  CB  VAL C 178     3960   3839   4829   -116   1678   -617       C  
ATOM   4535  CG1 VAL C 178      -6.981  14.916  24.645  1.00 32.35           C  
ANISOU 4535  CG1 VAL C 178     3625   4000   4667   -187   1638   -541       C  
ATOM   4536  CG2 VAL C 178      -6.045  17.228  24.802  1.00 38.92           C  
ANISOU 4536  CG2 VAL C 178     5007   4409   5372   -215   1798   -804       C  
ATOM   4537  N   GLY C 179      -5.656  13.531  21.965  1.00 27.62           N  
ANISOU 4537  N   GLY C 179     2830   3336   4327   -335   1252   -276       N  
ATOM   4538  CA  GLY C 179      -6.250  12.408  21.261  1.00 27.27           C  
ANISOU 4538  CA  GLY C 179     2598   3401   4364   -313   1170   -110       C  
ATOM   4539  C   GLY C 179      -7.556  11.957  21.879  1.00 25.84           C  
ANISOU 4539  C   GLY C 179     2266   3411   4140   -248   1259    -67       C  
ATOM   4540  O   GLY C 179      -8.618  12.064  21.266  1.00 28.11           O  
ANISOU 4540  O   GLY C 179     2425   3751   4503   -118   1296     13       O  
ATOM   4541  N   PHE C 180      -7.481  11.459  23.115  1.00 25.11           N  
ANISOU 4541  N   PHE C 180     3554   2353   3634   -937   1144   -443       N  
ATOM   4542  CA  PHE C 180      -8.625  10.872  23.790  1.00 26.83           C  
ANISOU 4542  CA  PHE C 180     3789   2547   3857   -881   1246   -555       C  
ATOM   4543  C   PHE C 180      -8.694  11.340  25.235  1.00 30.27           C  
ANISOU 4543  C   PHE C 180     4375   2893   4234   -923   1341   -707       C  
ATOM   4544  O   PHE C 180      -7.668  11.479  25.896  1.00 28.88           O  
ANISOU 4544  O   PHE C 180     4304   2734   3935  -1021   1271   -760       O  
ATOM   4545  CB  PHE C 180      -8.525   9.343  23.763  1.00 28.62           C  
ANISOU 4545  CB  PHE C 180     3969   2925   3981   -871   1204   -536       C  
ATOM   4546  CG  PHE C 180      -8.454   8.768  22.374  1.00 27.04           C  
ANISOU 4546  CG  PHE C 180     3663   2823   3787   -779   1079   -454       C  
ATOM   4547  CD1 PHE C 180      -7.262   8.762  21.662  1.00 22.86           C  
ANISOU 4547  CD1 PHE C 180     3126   2424   3137   -769    998   -364       C  
ATOM   4548  CD2 PHE C 180      -9.582   8.229  21.782  1.00 27.42           C  
ANISOU 4548  CD2 PHE C 180     3613   2844   3960   -681   1034   -469       C  
ATOM   4549  CE1 PHE C 180      -7.214   8.234  20.371  1.00 21.54           C  
ANISOU 4549  CE1 PHE C 180     2893   2387   2905   -619    897   -313       C  
ATOM   4550  CE2 PHE C 180      -9.543   7.704  20.503  1.00 24.87           C  
ANISOU 4550  CE2 PHE C 180     3232   2616   3600   -559    874   -448       C  
ATOM   4551  CZ  PHE C 180      -8.361   7.704  19.797  1.00 24.48           C  
ANISOU 4551  CZ  PHE C 180     3215   2725   3361   -506    816   -382       C  
ATOM   4552  N   GLU C 181      -9.907  11.596  25.721  1.00 29.88           N  
ANISOU 4552  N   GLU C 181     4329   2762   4262   -825   1494   -779       N  
ATOM   4553  CA  GLU C 181     -10.099  11.947  27.122  1.00 30.56           C  
ANISOU 4553  CA  GLU C 181     4578   2812   4221   -791   1621   -939       C  
ATOM   4554  C   GLU C 181     -10.714  10.717  27.769  1.00 33.95           C  
ANISOU 4554  C   GLU C 181     4955   3392   4551   -745   1765   -878       C  
ATOM   4555  O   GLU C 181     -11.769  10.234  27.331  1.00 36.30           O  
ANISOU 4555  O   GLU C 181     5076   3690   5027   -680   1851   -773       O  
ATOM   4556  CB  GLU C 181     -11.032  13.152  27.284  1.00 30.58           C  
ANISOU 4556  CB  GLU C 181     4615   2627   4376   -663   1739  -1046       C  
ATOM   4557  CG  GLU C 181     -11.150  13.625  28.732  1.00 32.77           C  
ANISOU 4557  CG  GLU C 181     5110   2878   4462   -568   1861  -1266       C  
ATOM   4558  CD  GLU C 181     -12.367  14.489  28.971  1.00 39.19           C  
ANISOU 4558  CD  GLU C 181     5925   3553   5413   -365   2054  -1363       C  
ATOM   4559  OE1 GLU C 181     -13.472  13.927  29.092  1.00 40.24           O  
ANISOU 4559  OE1 GLU C 181     5910   3786   5592   -244   2272  -1257       O  
ATOM   4560  OE2 GLU C 181     -12.218  15.722  29.032  1.00 46.77           O  
ANISOU 4560  OE2 GLU C 181     7011   4286   6473   -324   1981  -1530       O  
ATOM   4561  N   ILE C 182     -10.042  10.189  28.788  1.00 31.50           N  
ANISOU 4561  N   ILE C 182     4777   3201   3989   -785   1770   -914       N  
ATOM   4562  CA  ILE C 182     -10.369   8.870  29.319  1.00 31.73           C  
ANISOU 4562  CA  ILE C 182     4738   3377   3942   -773   1875   -779       C  
ATOM   4563  C   ILE C 182     -10.666   8.948  30.810  1.00 32.28           C  
ANISOU 4563  C   ILE C 182     4964   3548   3753   -663   2079   -835       C  
ATOM   4564  O   ILE C 182     -10.301   9.929  31.467  1.00 36.02           O  
ANISOU 4564  O   ILE C 182     5653   3990   4044   -612   2063  -1042       O  
ATOM   4565  CB  ILE C 182      -9.216   7.851  29.067  1.00 32.59           C  
ANISOU 4565  CB  ILE C 182     4833   3585   3964   -895   1685   -693       C  
ATOM   4566  CG1 ILE C 182      -7.940   8.279  29.806  1.00 34.42           C  
ANISOU 4566  CG1 ILE C 182     5264   3872   3944   -963   1561   -806       C  
ATOM   4567  CG2 ILE C 182      -8.951   7.678  27.563  1.00 33.28           C  
ANISOU 4567  CG2 ILE C 182     4777   3624   4245   -938   1512   -638       C  
ATOM   4568  CD1 ILE C 182      -6.845   7.196  29.838  1.00 32.03           C  
ANISOU 4568  CD1 ILE C 182     4940   3693   3536  -1051   1412   -700       C  
ATOM   4569  N   PRO C 183     -11.357   7.927  31.349  1.00 36.46           N  
ANISOU 4569  N   PRO C 183     5385   4195   4274   -609   2268   -645       N  
ATOM   4570  CA  PRO C 183     -11.547   7.849  32.805  1.00 37.91           C  
ANISOU 4570  CA  PRO C 183     5721   4548   4133   -472   2490   -636       C  
ATOM   4571  C   PRO C 183     -10.226   7.529  33.513  1.00 38.81           C  
ANISOU 4571  C   PRO C 183     6048   4791   3905   -541   2317   -692       C  
ATOM   4572  O   PRO C 183      -9.231   7.198  32.859  1.00 37.66           O  
ANISOU 4572  O   PRO C 183     5874   4603   3830   -703   2056   -688       O  
ATOM   4573  CB  PRO C 183     -12.562   6.703  32.980  1.00 42.86           C  
ANISOU 4573  CB  PRO C 183     6085   5248   4952   -427   2652   -308       C  
ATOM   4574  CG  PRO C 183     -12.483   5.907  31.730  1.00 39.04           C  
ANISOU 4574  CG  PRO C 183     5390   4631   4813   -603   2497   -202       C  
ATOM   4575  CD  PRO C 183     -12.106   6.879  30.630  1.00 33.80           C  
ANISOU 4575  CD  PRO C 183     4767   3821   4254   -652   2285   -418       C  
ATOM   4576  N   ASP C 184     -10.199   7.636  34.834  1.00 42.64           N  
ANISOU 4576  N   ASP C 184     6708   5451   4041   -384   2394   -722       N  
ATOM   4577  CA  ASP C 184      -8.976   7.300  35.550  1.00 49.44           C  
ANISOU 4577  CA  ASP C 184     7762   6450   4572   -436   2207   -764       C  
ATOM   4578  C   ASP C 184      -8.887   5.799  35.782  1.00 47.65           C  
ANISOU 4578  C   ASP C 184     7394   6364   4347   -482   2256   -426       C  
ATOM   4579  O   ASP C 184      -9.055   5.332  36.908  1.00 45.24           O  
ANISOU 4579  O   ASP C 184     7132   6275   3784   -334   2359   -276       O  
ATOM   4580  CB  ASP C 184      -8.855   8.054  36.880  1.00 54.93           C  
ANISOU 4580  CB  ASP C 184     8714   7292   4864   -223   2184   -965       C  
ATOM   4581  CG  ASP C 184      -7.443   7.982  37.460  1.00 53.54           C  
ANISOU 4581  CG  ASP C 184     8749   7206   4387   -302   1887  -1087       C  
ATOM   4582  OD1 ASP C 184      -6.545   7.443  36.776  1.00 56.41           O  
ANISOU 4582  OD1 ASP C 184     9054   7509   4871   -533   1715  -1017       O  
ATOM   4583  OD2 ASP C 184      -7.223   8.471  38.583  1.00 51.79           O  
ANISOU 4583  OD2 ASP C 184     8735   7130   3814   -124   1805  -1262       O  
ATOM   4584  N   LYS C 185      -8.646   5.062  34.698  1.00 46.14           N  
ANISOU 4584  N   LYS C 185     7020   6048   4464   -665   2165   -304       N  
ATOM   4585  CA  LYS C 185      -8.315   3.638  34.748  1.00 45.99           C  
ANISOU 4585  CA  LYS C 185     6875   6082   4515   -738   2118    -23       C  
ATOM   4586  C   LYS C 185      -6.865   3.499  34.320  1.00 38.61           C  
ANISOU 4586  C   LYS C 185     5996   5130   3544   -870   1787   -119       C  
ATOM   4587  O   LYS C 185      -6.362   4.329  33.556  1.00 35.87           O  
ANISOU 4587  O   LYS C 185     5669   4679   3283   -941   1617   -326       O  
ATOM   4588  CB  LYS C 185      -9.164   2.852  33.759  1.00 46.76           C  
ANISOU 4588  CB  LYS C 185     6675   6012   5080   -800   2161    162       C  
ATOM   4589  CG  LYS C 185     -10.630   2.704  34.129  1.00 54.25           C  
ANISOU 4589  CG  LYS C 185     7439   6970   6204   -676   2404    355       C  
ATOM   4590  CD  LYS C 185     -11.357   2.027  32.973  1.00 55.62           C  
ANISOU 4590  CD  LYS C 185     7320   6926   6888   -772   2332    470       C  
ATOM   4591  CE  LYS C 185     -12.861   2.059  33.146  1.00 59.97           C  
ANISOU 4591  CE  LYS C 185     7645   7458   7682   -672   2511    633       C  
ATOM   4592  NZ  LYS C 185     -13.352   0.820  33.799  1.00 63.54           N  
ANISOU 4592  NZ  LYS C 185     7911   7953   8277   -674   2565    984       N  
ATOM   4593  N   PHE C 186      -6.191   2.452  34.790  1.00 39.62           N  
ANISOU 4593  N   PHE C 186     6122   5358   3574   -894   1705     69       N  
ATOM   4594  CA  PHE C 186      -4.801   2.243  34.401  1.00 38.84           C  
ANISOU 4594  CA  PHE C 186     6034   5258   3465   -997   1407     12       C  
ATOM   4595  C   PHE C 186      -4.725   1.560  33.047  1.00 35.58           C  
ANISOU 4595  C   PHE C 186     5404   4682   3432  -1066   1303     68       C  
ATOM   4596  O   PHE C 186      -5.126   0.406  32.901  1.00 39.09           O  
ANISOU 4596  O   PHE C 186     5713   5062   4078  -1056   1342    269       O  
ATOM   4597  CB  PHE C 186      -4.025   1.442  35.453  1.00 42.71           C  
ANISOU 4597  CB  PHE C 186     6615   5925   3688   -970   1332    183       C  
ATOM   4598  CG  PHE C 186      -2.542   1.585  35.309  1.00 42.63           C  
ANISOU 4598  CG  PHE C 186     6642   5952   3604  -1054   1022     82       C  
ATOM   4599  CD1 PHE C 186      -1.856   0.868  34.338  1.00 43.15           C  
ANISOU 4599  CD1 PHE C 186     6528   5929   3939  -1119    872    158       C  
ATOM   4600  CD2 PHE C 186      -1.841   2.479  36.101  1.00 45.98           C  
ANISOU 4600  CD2 PHE C 186     7268   6491   3713  -1054    866   -105       C  
ATOM   4601  CE1 PHE C 186      -0.490   1.022  34.172  1.00 44.47           C  
ANISOU 4601  CE1 PHE C 186     6677   6147   4073  -1183    619    104       C  
ATOM   4602  CE2 PHE C 186      -0.474   2.639  35.945  1.00 49.50           C  
ANISOU 4602  CE2 PHE C 186     7690   6953   4164  -1154    560   -169       C  
ATOM   4603  CZ  PHE C 186       0.205   1.906  34.980  1.00 43.62           C  
ANISOU 4603  CZ  PHE C 186     6726   6145   3702  -1218    459    -38       C  
ATOM   4604  N   VAL C 187      -4.209   2.274  32.054  1.00 29.79           N  
ANISOU 4604  N   VAL C 187     4641   3876   2801  -1120   1160   -106       N  
ATOM   4605  CA  VAL C 187      -4.173   1.755  30.694  1.00 25.65           C  
ANISOU 4605  CA  VAL C 187     3945   3238   2562  -1126   1070    -94       C  
ATOM   4606  C   VAL C 187      -2.727   1.531  30.249  1.00 29.34           C  
ANISOU 4606  C   VAL C 187     4382   3769   2996  -1152    863    -98       C  
ATOM   4607  O   VAL C 187      -1.801   2.191  30.731  1.00 32.22           O  
ANISOU 4607  O   VAL C 187     4826   4226   3190  -1207    766   -150       O  
ATOM   4608  CB  VAL C 187      -4.908   2.695  29.727  1.00 29.56           C  
ANISOU 4608  CB  VAL C 187     4392   3627   3212  -1116   1119   -228       C  
ATOM   4609  CG1 VAL C 187      -6.381   2.818  30.147  1.00 30.59           C  
ANISOU 4609  CG1 VAL C 187     4502   3696   3425  -1071   1335   -192       C  
ATOM   4610  CG2 VAL C 187      -4.245   4.065  29.733  1.00 32.83           C  
ANISOU 4610  CG2 VAL C 187     4905   4066   3504  -1166   1057   -374       C  
ATOM   4611  N   VAL C 188      -2.538   0.574  29.347  1.00 25.02           N  
ANISOU 4611  N   VAL C 188     3710   3167   2631  -1096    783    -48       N  
ATOM   4612  CA  VAL C 188      -1.205   0.206  28.873  1.00 25.14           C  
ANISOU 4612  CA  VAL C 188     3664   3261   2629  -1067    626    -24       C  
ATOM   4613  C   VAL C 188      -1.295  -0.037  27.390  1.00 26.30           C  
ANISOU 4613  C   VAL C 188     3705   3351   2936   -958    585    -94       C  
ATOM   4614  O   VAL C 188      -2.399  -0.143  26.841  1.00 24.84           O  
ANISOU 4614  O   VAL C 188     3499   3045   2894   -920    628   -155       O  
ATOM   4615  CB  VAL C 188      -0.695  -1.093  29.560  1.00 24.23           C  
ANISOU 4615  CB  VAL C 188     3535   3164   2506  -1033    555    131       C  
ATOM   4616  CG1 VAL C 188      -0.502  -0.870  31.042  1.00 25.77           C  
ANISOU 4616  CG1 VAL C 188     3856   3472   2465  -1103    576    215       C  
ATOM   4617  CG2 VAL C 188      -1.669  -2.252  29.321  1.00 24.55           C  
ANISOU 4617  CG2 VAL C 188     3516   3026   2785   -973    585    197       C  
ATOM   4618  N   GLY C 189      -0.144  -0.151  26.734  1.00 24.31           N  
ANISOU 4618  N   GLY C 189     3378   3203   2655   -885    496    -79       N  
ATOM   4619  CA  GLY C 189      -0.150  -0.436  25.316  1.00 24.27           C  
ANISOU 4619  CA  GLY C 189     3300   3198   2723   -716    465   -151       C  
ATOM   4620  C   GLY C 189       0.136   0.822  24.519  1.00 23.50           C  
ANISOU 4620  C   GLY C 189     3159   3207   2562   -716    519   -159       C  
ATOM   4621  O   GLY C 189       0.107   1.925  25.073  1.00 26.96           O  
ANISOU 4621  O   GLY C 189     3630   3644   2970   -872    566   -139       O  
ATOM   4622  N   TYR C 190       0.385   0.656  23.224  1.00 24.76           N  
ANISOU 4622  N   TYR C 190     3254   3451   2702   -522    509   -184       N  
ATOM   4623  CA  TYR C 190       0.814   1.755  22.345  1.00 24.63           C  
ANISOU 4623  CA  TYR C 190     3161   3575   2624   -485    582   -106       C  
ATOM   4624  C   TYR C 190       1.939   2.572  23.009  1.00 26.89           C  
ANISOU 4624  C   TYR C 190     3359   3945   2913   -655    595     56       C  
ATOM   4625  O   TYR C 190       1.906   3.805  23.037  1.00 28.29           O  
ANISOU 4625  O   TYR C 190     3515   4096   3140   -790    633    114       O  
ATOM   4626  CB  TYR C 190      -0.382   2.632  21.961  1.00 21.91           C  
ANISOU 4626  CB  TYR C 190     2873   3131   2322   -527    632   -173       C  
ATOM   4627  CG  TYR C 190      -0.130   3.548  20.773  1.00 24.45           C  
ANISOU 4627  CG  TYR C 190     3116   3589   2584   -420    702    -69       C  
ATOM   4628  CD1 TYR C 190      -0.014   3.045  19.487  1.00 24.06           C  
ANISOU 4628  CD1 TYR C 190     3043   3695   2406   -137    694    -86       C  
ATOM   4629  CD2 TYR C 190      -0.042   4.932  20.950  1.00 21.98           C  
ANISOU 4629  CD2 TYR C 190     2765   3243   2343   -584    767     50       C  
ATOM   4630  CE1 TYR C 190       0.213   3.906  18.384  1.00 27.25           C  
ANISOU 4630  CE1 TYR C 190     3373   4270   2710     -7    788     68       C  
ATOM   4631  CE2 TYR C 190       0.166   5.783  19.890  1.00 22.98           C  
ANISOU 4631  CE2 TYR C 190     2800   3480   2451   -494    843    212       C  
ATOM   4632  CZ  TYR C 190       0.298   5.280  18.608  1.00 23.92           C  
ANISOU 4632  CZ  TYR C 190     2883   3803   2401   -203    872    248       C  
ATOM   4633  OH  TYR C 190       0.510   6.156  17.563  1.00 25.38           O  
ANISOU 4633  OH  TYR C 190     2974   4139   2531    -90    975    466       O  
ATOM   4634  N   ALA C 191       2.931   1.843  23.522  1.00 27.52           N  
ANISOU 4634  N   ALA C 191     3377   4101   2979   -643    531    126       N  
ATOM   4635  CA  ALA C 191       4.111   2.373  24.216  1.00 28.10           C  
ANISOU 4635  CA  ALA C 191     3336   4252   3087   -798    473    277       C  
ATOM   4636  C   ALA C 191       3.890   2.765  25.682  1.00 26.96           C  
ANISOU 4636  C   ALA C 191     3320   3987   2935  -1034    376    213       C  
ATOM   4637  O   ALA C 191       4.849   3.065  26.387  1.00 30.00           O  
ANISOU 4637  O   ALA C 191     3635   4419   3342  -1160    257    297       O  
ATOM   4638  CB  ALA C 191       4.793   3.512  23.430  1.00 25.76           C  
ANISOU 4638  CB  ALA C 191     2860   4062   2867   -823    538    456       C  
ATOM   4639  N   LEU C 192       2.641   2.762  26.143  1.00 25.23           N  
ANISOU 4639  N   LEU C 192     3280   3629   2678  -1072    419     68       N  
ATOM   4640  CA  LEU C 192       2.381   2.998  27.562  1.00 25.67           C  
ANISOU 4640  CA  LEU C 192     3485   3620   2649  -1221    362      3       C  
ATOM   4641  C   LEU C 192       2.672   1.731  28.339  1.00 30.22           C  
ANISOU 4641  C   LEU C 192     4091   4244   3147  -1173    299     62       C  
ATOM   4642  O   LEU C 192       2.307   0.642  27.908  1.00 29.88           O  
ANISOU 4642  O   LEU C 192     4028   4170   3157  -1040    340     80       O  
ATOM   4643  CB  LEU C 192       0.936   3.435  27.809  1.00 27.92           C  
ANISOU 4643  CB  LEU C 192     3921   3770   2917  -1241    479   -130       C  
ATOM   4644  CG  LEU C 192       0.691   4.917  27.514  1.00 36.16           C  
ANISOU 4644  CG  LEU C 192     4978   4728   4031  -1326    503   -198       C  
ATOM   4645  CD1 LEU C 192       0.419   5.152  26.036  1.00 32.10           C  
ANISOU 4645  CD1 LEU C 192     4346   4213   3637  -1227    584   -148       C  
ATOM   4646  CD2 LEU C 192      -0.443   5.476  28.385  1.00 38.77           C  
ANISOU 4646  CD2 LEU C 192     5491   4944   4296  -1362    584   -346       C  
ATOM   4647  N   ASP C 193       3.314   1.868  29.492  1.00 29.54           N  
ANISOU 4647  N   ASP C 193     4060   4216   2948  -1275    171     91       N  
ATOM   4648  CA  ASP C 193       3.775   0.693  30.207  1.00 30.24           C  
ANISOU 4648  CA  ASP C 193     4152   4372   2965  -1219     92    204       C  
ATOM   4649  C   ASP C 193       3.148   0.496  31.575  1.00 32.55           C  
ANISOU 4649  C   ASP C 193     4644   4668   3058  -1254    103    197       C  
ATOM   4650  O   ASP C 193       2.585   1.420  32.169  1.00 32.80           O  
ANISOU 4650  O   ASP C 193     4826   4679   2957  -1323    137     72       O  
ATOM   4651  CB  ASP C 193       5.282   0.765  30.405  1.00 30.57           C  
ANISOU 4651  CB  ASP C 193     4049   4541   3024  -1262   -100    313       C  
ATOM   4652  CG  ASP C 193       5.666   1.768  31.453  1.00 33.38           C  
ANISOU 4652  CG  ASP C 193     4500   4923   3261  -1428   -274    243       C  
ATOM   4653  OD1 ASP C 193       5.237   2.933  31.334  1.00 33.11           O  
ANISOU 4653  OD1 ASP C 193     4532   4797   3250  -1524   -253    105       O  
ATOM   4654  OD2 ASP C 193       6.385   1.384  32.395  1.00 32.03           O  
ANISOU 4654  OD2 ASP C 193     4346   4848   2974  -1449   -458    314       O  
ATOM   4655  N   TYR C 194       3.276  -0.730  32.068  1.00 30.98           N  
ANISOU 4655  N   TYR C 194     4441   4498   2831  -1176     81    349       N  
ATOM   4656  CA  TYR C 194       3.173  -1.002  33.491  1.00 35.11           C  
ANISOU 4656  CA  TYR C 194     5120   5110   3110  -1185     47    435       C  
ATOM   4657  C   TYR C 194       4.468  -1.709  33.877  1.00 38.49           C  
ANISOU 4657  C   TYR C 194     5456   5650   3518  -1157   -162    595       C  
ATOM   4658  O   TYR C 194       4.715  -2.844  33.450  1.00 34.28           O  
ANISOU 4658  O   TYR C 194     4800   5066   3158  -1057   -161    738       O  
ATOM   4659  CB  TYR C 194       1.965  -1.873  33.789  1.00 30.61           C  
ANISOU 4659  CB  TYR C 194     4605   4459   2568  -1114    243    555       C  
ATOM   4660  CG  TYR C 194       1.904  -2.321  35.216  1.00 34.15           C  
ANISOU 4660  CG  TYR C 194     5190   5039   2747  -1079    248    732       C  
ATOM   4661  CD1 TYR C 194       1.352  -1.504  36.191  1.00 38.14           C  
ANISOU 4661  CD1 TYR C 194     5897   5661   2932  -1080    333    650       C  
ATOM   4662  CD2 TYR C 194       2.398  -3.560  35.597  1.00 38.11           C  
ANISOU 4662  CD2 TYR C 194     5627   5559   3293  -1013    171    987       C  
ATOM   4663  CE1 TYR C 194       1.288  -1.908  37.499  1.00 40.56           C  
ANISOU 4663  CE1 TYR C 194     6349   6143   2919  -1000    357    828       C  
ATOM   4664  CE2 TYR C 194       2.337  -3.974  36.910  1.00 44.61           C  
ANISOU 4664  CE2 TYR C 194     6577   6533   3840   -961    185   1200       C  
ATOM   4665  CZ  TYR C 194       1.789  -3.142  37.855  1.00 45.64           C  
ANISOU 4665  CZ  TYR C 194     6916   6822   3601   -948    284   1124       C  
ATOM   4666  OH  TYR C 194       1.724  -3.557  39.164  1.00 52.86           O  
ANISOU 4666  OH  TYR C 194     7975   7939   4171   -849    317   1353       O  
ATOM   4667  N   ASN C 195       5.294  -1.023  34.668  1.00 34.92           N  
ANISOU 4667  N   ASN C 195     5060   5331   2878  -1237   -369    555       N  
ATOM   4668  CA AASN C 195       6.618  -1.523  35.023  0.45 38.04           C  
ANISOU 4668  CA AASN C 195     5333   5844   3276  -1225   -612    705       C  
ATOM   4669  CA BASN C 195       6.636  -1.493  35.009  0.55 35.68           C  
ANISOU 4669  CA BASN C 195     5031   5546   2980  -1228   -615    700       C  
ATOM   4670  C   ASN C 195       7.442  -2.010  33.821  1.00 39.18           C  
ANISOU 4670  C   ASN C 195     5196   5955   3737  -1164   -624    791       C  
ATOM   4671  O   ASN C 195       8.015  -3.103  33.864  1.00 39.04           O  
ANISOU 4671  O   ASN C 195     5070   5965   3798  -1049   -682    972       O  
ATOM   4672  CB AASN C 195       6.493  -2.635  36.060  0.45 41.70           C  
ANISOU 4672  CB AASN C 195     5898   6387   3560  -1124   -625    919       C  
ATOM   4673  CB BASN C 195       6.594  -2.514  36.142  0.55 42.81           C  
ANISOU 4673  CB BASN C 195     6045   6545   3676  -1136   -656    906       C  
ATOM   4674  CG AASN C 195       7.784  -2.888  36.797  0.45 42.21           C  
ANISOU 4674  CG AASN C 195     5900   6612   3524  -1120   -928   1051       C  
ATOM   4675  CG BASN C 195       6.628  -1.856  37.499  0.55 46.48           C  
ANISOU 4675  CG BASN C 195     6745   7172   3742  -1172   -806    834       C  
ATOM   4676  OD1AASN C 195       8.708  -2.071  36.760  0.45 41.54           O  
ANISOU 4676  OD1AASN C 195     5726   6589   3470  -1223  -1158    951       O  
ATOM   4677  OD1BASN C 195       7.212  -0.783  37.658  0.55 49.08           O  
ANISOU 4677  OD1BASN C 195     7097   7539   4011  -1280  -1022    643       O  
ATOM   4678  ND2AASN C 195       7.858  -4.024  37.474  0.45 42.73           N  
ANISOU 4678  ND2AASN C 195     5992   6735   3509  -1007   -947   1305       N  
ATOM   4679  ND2BASN C 195       6.010  -2.490  38.488  0.55 52.88           N  
ANISOU 4679  ND2BASN C 195     7731   8079   4282  -1067   -705    993       N  
ATOM   4680  N   GLU C 196       7.479  -1.193  32.764  1.00 36.95           N  
ANISOU 4680  N   GLU C 196     4801   5621   3619  -1211   -554    676       N  
ATOM   4681  CA  GLU C 196       8.223  -1.454  31.519  1.00 38.68           C  
ANISOU 4681  CA  GLU C 196     4758   5858   4082  -1113   -513    752       C  
ATOM   4682  C   GLU C 196       7.581  -2.481  30.583  1.00 37.40           C  
ANISOU 4682  C   GLU C 196     4584   5595   4031   -916   -327    745       C  
ATOM   4683  O   GLU C 196       7.959  -2.578  29.415  1.00 37.13           O  
ANISOU 4683  O   GLU C 196     4388   5586   4134   -786   -250    747       O  
ATOM   4684  CB  GLU C 196       9.699  -1.784  31.787  1.00 42.66           C  
ANISOU 4684  CB  GLU C 196     5041   6501   4665  -1093   -722    934       C  
ATOM   4685  CG  GLU C 196      10.442  -0.675  32.523  1.00 46.46           C  
ANISOU 4685  CG  GLU C 196     5484   7054   5116  -1303   -977    918       C  
ATOM   4686  CD  GLU C 196      10.317   0.687  31.834  1.00 51.83           C  
ANISOU 4686  CD  GLU C 196     6100   7664   5927  -1445   -927    811       C  
ATOM   4687  OE1 GLU C 196      10.362   0.744  30.584  1.00 44.44           O  
ANISOU 4687  OE1 GLU C 196     4991   6729   5164  -1358   -734    870       O  
ATOM   4688  OE2 GLU C 196      10.174   1.703  32.552  1.00 55.55           O  
ANISOU 4688  OE2 GLU C 196     6708   8079   6321  -1625  -1090    668       O  
ATOM   4689  N   TYR C 197       6.592  -3.220  31.074  1.00 33.74           N  
ANISOU 4689  N   TYR C 197     4287   5015   3515   -883   -260    739       N  
ATOM   4690  CA  TYR C 197       5.874  -4.166  30.219  1.00 34.04           C  
ANISOU 4690  CA  TYR C 197     4321   4894   3718   -723   -145    698       C  
ATOM   4691  C   TYR C 197       4.722  -3.514  29.465  1.00 29.76           C  
ANISOU 4691  C   TYR C 197     3853   4253   3202   -754      4    520       C  
ATOM   4692  O   TYR C 197       4.299  -2.406  29.811  1.00 29.24           O  
ANISOU 4692  O   TYR C 197     3873   4217   3021   -903     50    447       O  
ATOM   4693  CB  TYR C 197       5.360  -5.357  31.032  1.00 38.51           C  
ANISOU 4693  CB  TYR C 197     4973   5338   4323   -683   -163    833       C  
ATOM   4694  CG  TYR C 197       6.475  -6.277  31.459  1.00 47.07           C  
ANISOU 4694  CG  TYR C 197     5956   6476   5452   -581   -313   1022       C  
ATOM   4695  CD1 TYR C 197       6.884  -7.324  30.644  1.00 49.14           C  
ANISOU 4695  CD1 TYR C 197     6101   6630   5942   -368   -346   1028       C  
ATOM   4696  CD2 TYR C 197       7.143  -6.079  32.664  1.00 48.01           C  
ANISOU 4696  CD2 TYR C 197     6103   6758   5381   -669   -445   1175       C  
ATOM   4697  CE1 TYR C 197       7.914  -8.158  31.019  1.00 52.02           C  
ANISOU 4697  CE1 TYR C 197     6357   7033   6376   -250   -479   1207       C  
ATOM   4698  CE2 TYR C 197       8.172  -6.908  33.050  1.00 50.75           C  
ANISOU 4698  CE2 TYR C 197     6338   7161   5783   -568   -601   1368       C  
ATOM   4699  CZ  TYR C 197       8.555  -7.944  32.222  1.00 54.24           C  
ANISOU 4699  CZ  TYR C 197     6641   7480   6486   -360   -605   1396       C  
ATOM   4700  OH  TYR C 197       9.583  -8.772  32.601  1.00 61.07           O  
ANISOU 4700  OH  TYR C 197     7381   8388   7434   -235   -756   1596       O  
ATOM   4701  N   PHE C 198       4.238  -4.219  28.439  1.00 26.82           N  
ANISOU 4701  N   PHE C 198     3229   3465   3496  -1125     71    -96       N  
ATOM   4702  CA  PHE C 198       3.059  -3.848  27.648  1.00 25.69           C  
ANISOU 4702  CA  PHE C 198     3235   3204   3322  -1049    275   -174       C  
ATOM   4703  C   PHE C 198       3.331  -2.741  26.620  1.00 26.27           C  
ANISOU 4703  C   PHE C 198     3336   3146   3499  -1023    464   -322       C  
ATOM   4704  O   PHE C 198       2.430  -2.332  25.899  1.00 27.98           O  
ANISOU 4704  O   PHE C 198     3669   3270   3691   -946    611   -366       O  
ATOM   4705  CB  PHE C 198       1.869  -3.446  28.537  1.00 27.05           C  
ANISOU 4705  CB  PHE C 198     3542   3487   3251  -1109    327   -198       C  
ATOM   4706  CG  PHE C 198       1.413  -4.524  29.502  1.00 28.17           C  
ANISOU 4706  CG  PHE C 198     3668   3764   3272  -1126    205     13       C  
ATOM   4707  CD1 PHE C 198       0.658  -5.598  29.058  1.00 29.30           C  
ANISOU 4707  CD1 PHE C 198     3778   3803   3551  -1048    195    182       C  
ATOM   4708  CD2 PHE C 198       1.717  -4.435  30.857  1.00 32.51           C  
ANISOU 4708  CD2 PHE C 198     4249   4538   3564  -1229     93     49       C  
ATOM   4709  CE1 PHE C 198       0.219  -6.589  29.948  1.00 28.54           C  
ANISOU 4709  CE1 PHE C 198     3648   3797   3398  -1079    109    433       C  
ATOM   4710  CE2 PHE C 198       1.290  -5.415  31.761  1.00 32.08           C  
ANISOU 4710  CE2 PHE C 198     4193   4626   3369  -1234     12    309       C  
ATOM   4711  CZ  PHE C 198       0.545  -6.497  31.307  1.00 34.03           C  
ANISOU 4711  CZ  PHE C 198     4375   4741   3814  -1162     38    525       C  
ATOM   4712  N   ARG C 199       4.563  -2.249  26.562  1.00 24.00           N  
ANISOU 4712  N   ARG C 199     2919   2849   3352  -1092    455   -362       N  
ATOM   4713  CA  ARG C 199       4.903  -1.240  25.561  1.00 26.48           C  
ANISOU 4713  CA  ARG C 199     3236   3022   3805  -1074    667   -434       C  
ATOM   4714  C   ARG C 199       4.783  -1.840  24.157  1.00 31.40           C  
ANISOU 4714  C   ARG C 199     3894   3545   4491   -862    814   -358       C  
ATOM   4715  O   ARG C 199       4.461  -1.137  23.199  1.00 36.07           O  
ANISOU 4715  O   ARG C 199     4591   4039   5076   -787   1009   -378       O  
ATOM   4716  CB  ARG C 199       6.314  -0.685  25.777  1.00 28.32           C  
ANISOU 4716  CB  ARG C 199     3258   3252   4251  -1213    626   -450       C  
ATOM   4717  CG  ARG C 199       6.552   0.040  27.114  1.00 27.25           C  
ANISOU 4717  CG  ARG C 199     3117   3202   4035  -1447    429   -590       C  
ATOM   4718  CD  ARG C 199       7.631   1.083  26.967  1.00 29.58           C  
ANISOU 4718  CD  ARG C 199     3245   3386   4610  -1615    454   -658       C  
ATOM   4719  NE  ARG C 199       8.198   1.574  28.233  1.00 32.71           N  
ANISOU 4719  NE  ARG C 199     3585   3869   4974  -1863    162   -810       N  
ATOM   4720  CZ  ARG C 199       7.736   2.623  28.907  1.00 33.33           C  
ANISOU 4720  CZ  ARG C 199     3864   3884   4914  -2009    134  -1059       C  
ATOM   4721  NH1 ARG C 199       6.671   3.279  28.462  1.00 36.20           N  
ANISOU 4721  NH1 ARG C 199     4463   4097   5194  -1898    395  -1133       N  
ATOM   4722  NH2 ARG C 199       8.313   2.996  30.042  1.00 35.48           N  
ANISOU 4722  NH2 ARG C 199     4119   4249   5112  -2203   -178  -1215       N  
ATOM   4723  N   ASP C 200       5.026  -3.146  24.065  1.00 30.00           N  
ANISOU 4723  N   ASP C 200     3652   3387   4359   -756    707   -273       N  
ATOM   4724  CA  ASP C 200       5.054  -3.900  22.813  1.00 32.92           C  
ANISOU 4724  CA  ASP C 200     4081   3657   4769   -542    813   -256       C  
ATOM   4725  C   ASP C 200       3.671  -4.438  22.447  1.00 34.97           C  
ANISOU 4725  C   ASP C 200     4541   3864   4882   -465    744   -288       C  
ATOM   4726  O   ASP C 200       3.517  -5.590  22.031  1.00 42.89           O  
ANISOU 4726  O   ASP C 200     5587   4787   5922   -345    659   -287       O  
ATOM   4727  CB  ASP C 200       6.013  -5.079  22.950  1.00 34.94           C  
ANISOU 4727  CB  ASP C 200     4166   3905   5207   -454    722   -174       C  
ATOM   4728  CG  ASP C 200       5.598  -6.033  24.050  1.00 38.18           C  
ANISOU 4728  CG  ASP C 200     4547   4356   5603   -518    459    -88       C  
ATOM   4729  OD1 ASP C 200       5.100  -5.551  25.090  1.00 33.29           O  
ANISOU 4729  OD1 ASP C 200     3949   3855   4845   -689    351    -75       O  
ATOM   4730  OD2 ASP C 200       5.744  -7.261  23.859  1.00 40.02           O  
ANISOU 4730  OD2 ASP C 200     4756   4490   5961   -386    382    -28       O  
ATOM   4731  N   LEU C 201       2.668  -3.597  22.627  1.00 37.07           N  
ANISOU 4731  N   LEU C 201     4908   4151   5024   -538    770   -321       N  
ATOM   4732  CA  LEU C 201       1.279  -3.947  22.380  1.00 33.86           C  
ANISOU 4732  CA  LEU C 201     4622   3712   4531   -496    687   -324       C  
ATOM   4733  C   LEU C 201       0.756  -2.789  21.537  1.00 31.25           C  
ANISOU 4733  C   LEU C 201     4410   3348   4115   -436    841   -359       C  
ATOM   4734  O   LEU C 201       1.020  -1.640  21.863  1.00 27.01           O  
ANISOU 4734  O   LEU C 201     3853   2818   3590   -510    974   -373       O  
ATOM   4735  CB  LEU C 201       0.546  -4.066  23.718  1.00 33.63           C  
ANISOU 4735  CB  LEU C 201     4534   3773   4469   -635    581   -264       C  
ATOM   4736  CG  LEU C 201      -0.967  -4.226  23.820  1.00 35.13           C  
ANISOU 4736  CG  LEU C 201     4757   3960   4632   -641    530   -218       C  
ATOM   4737  CD1 LEU C 201      -1.420  -5.521  23.153  1.00 40.10           C  
ANISOU 4737  CD1 LEU C 201     5398   4473   5365   -577    358   -184       C  
ATOM   4738  CD2 LEU C 201      -1.410  -4.183  25.307  1.00 27.37           C  
ANISOU 4738  CD2 LEU C 201     3705   3114   3580   -768    527   -136       C  
ATOM   4739  N   ASN C 202       0.057  -3.073  20.438  1.00 30.30           N  
ANISOU 4739  N   ASN C 202     4421   3175   3917   -301    801   -373       N  
ATOM   4740  CA AASN C 202      -0.351  -1.987  19.546  0.47 28.64           C  
ANISOU 4740  CA AASN C 202     4328   2944   3609   -213    933   -352       C  
ATOM   4741  CA BASN C 202      -0.393  -2.036  19.500  0.53 28.83           C  
ANISOU 4741  CA BASN C 202     4359   2968   3629   -206    924   -353       C  
ATOM   4742  C   ASN C 202      -1.611  -1.254  20.005  1.00 28.14           C  
ANISOU 4742  C   ASN C 202     4245   2886   3562   -258    908   -311       C  
ATOM   4743  O   ASN C 202      -1.756  -0.061  19.752  1.00 31.82           O  
ANISOU 4743  O   ASN C 202     4753   3311   4027   -226   1061   -271       O  
ATOM   4744  CB AASN C 202      -0.441  -2.435  18.073  0.47 30.27           C  
ANISOU 4744  CB AASN C 202     4718   3129   3656    -23    903   -379       C  
ATOM   4745  CB BASN C 202      -0.716  -2.677  18.142  0.53 30.22           C  
ANISOU 4745  CB BASN C 202     4709   3118   3654    -31    832   -390       C  
ATOM   4746  CG AASN C 202      -1.472  -3.527  17.845  0.47 29.89           C  
ANISOU 4746  CG AASN C 202     4722   3052   3585      0    611   -441       C  
ATOM   4747  CG BASN C 202      -0.046  -1.970  16.977  0.53 37.42           C  
ANISOU 4747  CG BASN C 202     5763   4040   4415    119   1057   -351       C  
ATOM   4748  OD1AASN C 202      -1.819  -4.267  18.762  0.47 26.79           O  
ANISOU 4748  OD1AASN C 202     4200   2637   3341   -120    463   -438       O  
ATOM   4749  OD1BASN C 202       0.882  -1.176  17.159  0.53 45.70           O  
ANISOU 4749  OD1BASN C 202     6734   5083   5548     77   1295   -284       O  
ATOM   4750  ND2AASN C 202      -1.963  -3.635  16.609  0.47 28.92           N  
ANISOU 4750  ND2AASN C 202     4791   2925   3274    145    513   -485       N  
ATOM   4751  ND2BASN C 202      -0.512  -2.263  15.766  0.53 43.97           N  
ANISOU 4751  ND2BASN C 202     6804   4886   5016    288    974   -381       N  
ATOM   4752  N   HIS C 203      -2.502  -1.944  20.712  1.00 28.46           N  
ANISOU 4752  N   HIS C 203     4200   2958   3655   -326    746   -297       N  
ATOM   4753  CA  HIS C 203      -3.714  -1.298  21.210  1.00 24.60           C  
ANISOU 4753  CA  HIS C 203     3646   2487   3215   -344    771   -242       C  
ATOM   4754  C   HIS C 203      -3.491  -0.729  22.611  1.00 28.07           C  
ANISOU 4754  C   HIS C 203     4017   2978   3670   -463    913   -276       C  
ATOM   4755  O   HIS C 203      -2.619  -1.206  23.343  1.00 28.75           O  
ANISOU 4755  O   HIS C 203     4072   3120   3731   -565    885   -310       O  
ATOM   4756  CB  HIS C 203      -4.855  -2.306  21.319  1.00 23.83           C  
ANISOU 4756  CB  HIS C 203     3447   2405   3201   -367    559   -176       C  
ATOM   4757  CG  HIS C 203      -5.041  -3.162  20.112  1.00 24.07           C  
ANISOU 4757  CG  HIS C 203     3563   2375   3209   -291    329   -207       C  
ATOM   4758  ND1 HIS C 203      -5.518  -2.670  18.918  1.00 27.24           N  
ANISOU 4758  ND1 HIS C 203     4071   2761   3517   -157    262   -201       N  
ATOM   4759  CD2 HIS C 203      -4.827  -4.486  19.921  1.00 25.93           C  
ANISOU 4759  CD2 HIS C 203     3817   2546   3489   -321    132   -260       C  
ATOM   4760  CE1 HIS C 203      -5.593  -3.656  18.040  1.00 28.38           C  
ANISOU 4760  CE1 HIS C 203     4320   2860   3603   -115     18   -284       C  
ATOM   4761  NE2 HIS C 203      -5.180  -4.764  18.623  1.00 26.26           N  
ANISOU 4761  NE2 HIS C 203     4000   2535   3443   -213    -54   -337       N  
ATOM   4762  N   VAL C 204      -4.308   0.252  23.005  1.00 22.87           N  
ANISOU 4762  N   VAL C 204     3340   2305   3044   -436   1051   -271       N  
ATOM   4763  CA  VAL C 204      -4.388   0.637  24.414  1.00 22.09           C  
ANISOU 4763  CA  VAL C 204     3213   2277   2904   -526   1174   -338       C  
ATOM   4764  C   VAL C 204      -5.388  -0.282  25.096  1.00 28.53           C  
ANISOU 4764  C   VAL C 204     3899   3209   3730   -550   1111   -220       C  
ATOM   4765  O   VAL C 204      -6.476  -0.521  24.572  1.00 31.15           O  
ANISOU 4765  O   VAL C 204     4129   3520   4186   -476   1056   -104       O  
ATOM   4766  CB  VAL C 204      -4.780   2.105  24.591  1.00 21.26           C  
ANISOU 4766  CB  VAL C 204     3165   2068   2846   -460   1396   -419       C  
ATOM   4767  CG1 VAL C 204      -5.140   2.400  26.048  1.00 25.93           C  
ANISOU 4767  CG1 VAL C 204     3761   2750   3342   -511   1536   -520       C  
ATOM   4768  CG2 VAL C 204      -3.641   3.017  24.131  1.00 25.47           C  
ANISOU 4768  CG2 VAL C 204     3806   2455   3416   -493   1472   -513       C  
ATOM   4769  N   CYS C 205      -5.010  -0.819  26.252  1.00 28.39           N  
ANISOU 4769  N   CYS C 205     3870   3322   3597   -662   1103   -218       N  
ATOM   4770  CA  CYS C 205      -5.813  -1.824  26.941  1.00 30.76           C  
ANISOU 4770  CA  CYS C 205     4040   3734   3915   -704   1064    -41       C  
ATOM   4771  C   CYS C 205      -5.815  -1.546  28.419  1.00 31.14           C  
ANISOU 4771  C   CYS C 205     4130   3955   3746   -757   1230    -63       C  
ATOM   4772  O   CYS C 205      -4.888  -0.932  28.941  1.00 30.75           O  
ANISOU 4772  O   CYS C 205     4221   3944   3519   -807   1256   -237       O  
ATOM   4773  CB  CYS C 205      -5.252  -3.230  26.682  1.00 31.35           C  
ANISOU 4773  CB  CYS C 205     4074   3785   4055   -775    821     63       C  
ATOM   4774  N   VAL C 206      -6.859  -2.002  29.098  1.00 29.70           N  
ANISOU 4774  N   VAL C 206     3825   3886   3573   -750   1339    119       N  
ATOM   4775  CA  VAL C 206      -6.888  -1.940  30.545  1.00 38.94           C  
ANISOU 4775  CA  VAL C 206     5064   5272   4458   -784   1510    138       C  
ATOM   4776  C   VAL C 206      -6.224  -3.211  31.055  1.00 38.56           C  
ANISOU 4776  C   VAL C 206     4999   5326   4328   -904   1307    328       C  
ATOM   4777  O   VAL C 206      -6.557  -4.316  30.627  1.00 36.73           O  
ANISOU 4777  O   VAL C 206     4611   5013   4332   -942   1165    554       O  
ATOM   4778  CB  VAL C 206      -8.325  -1.833  31.084  1.00 40.21           C  
ANISOU 4778  CB  VAL C 206     5081   5531   4665   -695   1798    297       C  
ATOM   4779  CG1 VAL C 206      -8.322  -1.665  32.598  1.00 38.97           C  
ANISOU 4779  CG1 VAL C 206     5048   5629   4129   -672   1982    291       C  
ATOM   4780  CG2 VAL C 206      -9.040  -0.658  30.436  1.00 43.77           C  
ANISOU 4780  CG2 VAL C 206     5498   5840   5293   -539   1968    157       C  
ATOM   4781  N   ILE C 207      -5.259  -3.042  31.950  1.00 38.91           N  
ANISOU 4781  N   ILE C 207     5204   5520   4059   -966   1263    230       N  
ATOM   4782  CA  ILE C 207      -4.552  -4.162  32.560  1.00 38.52           C  
ANISOU 4782  CA  ILE C 207     5143   5587   3907  -1058   1060    440       C  
ATOM   4783  C   ILE C 207      -5.453  -4.810  33.612  1.00 44.14           C  
ANISOU 4783  C   ILE C 207     5801   6499   4469  -1061   1228    750       C  
ATOM   4784  O   ILE C 207      -6.204  -4.112  34.294  1.00 47.76           O  
ANISOU 4784  O   ILE C 207     6325   7111   4709   -996   1522    698       O  
ATOM   4785  CB  ILE C 207      -3.222  -3.663  33.194  1.00 49.00           C  
ANISOU 4785  CB  ILE C 207     6639   7037   4942  -1125    913    239       C  
ATOM   4786  CG1 ILE C 207      -2.355  -4.826  33.688  1.00 47.24           C  
ANISOU 4786  CG1 ILE C 207     6368   6914   4669  -1195    646    484       C  
ATOM   4787  CG2 ILE C 207      -3.497  -2.645  34.317  1.00 52.18           C  
ANISOU 4787  CG2 ILE C 207     7247   7648   4931  -1111   1117     41       C  
ATOM   4788  CD1 ILE C 207      -0.964  -4.389  34.167  1.00 48.76           C  
ANISOU 4788  CD1 ILE C 207     6653   7216   4658  -1273    419    306       C  
ATOM   4789  N   SER C 208      -5.399  -6.139  33.726  1.00 37.79           N  
ANISOU 4789  N   SER C 208     4874   5676   3809  -1123   1075   1087       N  
ATOM   4790  CA  SER C 208      -6.170  -6.859  34.731  1.00 48.00           C  
ANISOU 4790  CA  SER C 208     6098   7146   4994  -1141   1240   1463       C  
ATOM   4791  C   SER C 208      -5.460  -6.864  36.092  1.00 53.33           C  
ANISOU 4791  C   SER C 208     6979   8120   5165  -1139   1215   1519       C  
ATOM   4792  O   SER C 208      -4.319  -6.420  36.208  1.00 52.00           O  
ANISOU 4792  O   SER C 208     6964   8035   4760  -1183   1017   1301       O  
ATOM   4793  CB  SER C 208      -6.420  -8.302  34.289  1.00 49.86           C  
ANISOU 4793  CB  SER C 208     6132   7139   5674  -1184   1053   1769       C  
ATOM   4794  OG  SER C 208      -5.219  -9.044  34.222  1.00 47.37           O  
ANISOU 4794  OG  SER C 208     5849   6775   5376  -1252    759   1873       O  
ATOM   4795  N   GLU C 209      -6.138  -7.366  37.122  1.00 54.80           N  
ANISOU 4795  N   GLU C 209     7177   8419   5225  -1071   1385   1773       N  
ATOM   4796  CA  GLU C 209      -5.503  -7.511  38.433  1.00 58.95           C  
ANISOU 4796  CA  GLU C 209     7913   9230   5257  -1052   1326   1871       C  
ATOM   4797  C   GLU C 209      -4.422  -8.595  38.372  1.00 58.01           C  
ANISOU 4797  C   GLU C 209     7724   9081   5237  -1146    945   2129       C  
ATOM   4798  O   GLU C 209      -3.357  -8.448  38.964  1.00 60.47           O  
ANISOU 4798  O   GLU C 209     8186   9601   5187  -1175    718   2084       O  
ATOM   4799  CB  GLU C 209      -6.534  -7.817  39.528  1.00 68.09           C  
ANISOU 4799  CB  GLU C 209     9123  10497   6249   -967   1639   2099       C  
ATOM   4800  CG  GLU C 209      -7.792  -6.941  39.486  1.00 75.23           C  
ANISOU 4800  CG  GLU C 209    10024  11360   7198   -886   2046   1913       C  
ATOM   4801  CD  GLU C 209      -7.516  -5.453  39.696  1.00 82.16           C  
ANISOU 4801  CD  GLU C 209    11162  12346   7708   -762   2177   1474       C  
ATOM   4802  OE1 GLU C 209      -8.334  -4.628  39.230  1.00 83.44           O  
ANISOU 4802  OE1 GLU C 209    11273  12380   8050   -688   2440   1272       O  
ATOM   4803  OE2 GLU C 209      -6.496  -5.106  40.333  1.00 86.20           O  
ANISOU 4803  OE2 GLU C 209    11909  13063   7780   -742   1982   1318       O  
ATOM   4804  N   THR C 210      -4.695  -9.670  37.635  1.00 58.90           N  
ANISOU 4804  N   THR C 210     7604   8901   5874  -1183    848   2373       N  
ATOM   4805  CA  THR C 210      -3.711 -10.734  37.427  1.00 62.15           C  
ANISOU 4805  CA  THR C 210     7930   9185   6499  -1232    508   2604       C  
ATOM   4806  C   THR C 210      -2.430 -10.195  36.782  1.00 59.69           C  
ANISOU 4806  C   THR C 210     7669   8872   6138  -1292    248   2365       C  
ATOM   4807  O   THR C 210      -1.320 -10.555  37.184  1.00 60.41           O  
ANISOU 4807  O   THR C 210     7784   9046   6124  -1290    -30   2461       O  
ATOM   4808  CB  THR C 210      -4.293 -11.879  36.571  1.00 68.99           C  
ANISOU 4808  CB  THR C 210     8566   9652   7995  -1244    452   2776       C  
ATOM   4809  OG1 THR C 210      -5.381 -12.492  37.275  1.00 74.86           O  
ANISOU 4809  OG1 THR C 210     9238  10406   8798  -1222    651   3032       O  
ATOM   4810  CG2 THR C 210      -3.230 -12.935  36.278  1.00 72.27           C  
ANISOU 4810  CG2 THR C 210     8909   9868   8683  -1251    123   2957       C  
ATOM   4811  N   GLY C 211      -2.591  -9.319  35.791  1.00 51.45           N  
ANISOU 4811  N   GLY C 211     6621   7667   5259  -1274    324   1952       N  
ATOM   4812  CA  GLY C 211      -1.458  -8.690  35.141  1.00 45.15           C  
ANISOU 4812  CA  GLY C 211     5856   6784   4514  -1263    130   1592       C  
ATOM   4813  C   GLY C 211      -0.698  -7.764  36.076  1.00 47.57           C  
ANISOU 4813  C   GLY C 211     6341   7399   4333  -1299     54   1392       C  
ATOM   4814  O   GLY C 211       0.531  -7.707  36.038  1.00 49.82           O  
ANISOU 4814  O   GLY C 211     6600   7695   4637  -1324   -218   1300       O  
ATOM   4815  N   LYS C 212      -1.429  -7.037  36.916  1.00 50.21           N  
ANISOU 4815  N   LYS C 212     6851   7979   4249  -1297    290   1312       N  
ATOM   4816  CA  LYS C 212      -0.818  -6.110  37.861  1.00 56.39           C  
ANISOU 4816  CA  LYS C 212     7862   9046   4519  -1338    209   1055       C  
ATOM   4817  C   LYS C 212       0.085  -6.839  38.851  1.00 58.69           C  
ANISOU 4817  C   LYS C 212     8189   9595   4516  -1378   -115   1335       C  
ATOM   4818  O   LYS C 212       1.110  -6.308  39.279  1.00 57.80           O  
ANISOU 4818  O   LYS C 212     8166   9628   4166  -1446   -397   1121       O  
ATOM   4819  CB  LYS C 212      -1.896  -5.329  38.615  1.00 64.20           C  
ANISOU 4819  CB  LYS C 212     9060  10241   5091  -1285    579    930       C  
ATOM   4820  CG  LYS C 212      -2.388  -4.089  37.887  1.00 67.49           C  
ANISOU 4820  CG  LYS C 212     9517  10457   5670  -1245    813    503       C  
ATOM   4821  CD  LYS C 212      -3.611  -3.483  38.573  1.00 74.20           C  
ANISOU 4821  CD  LYS C 212    10484  11383   6326  -1069   1206    430       C  
ATOM   4822  CE  LYS C 212      -4.026  -2.180  37.893  1.00 72.16           C  
ANISOU 4822  CE  LYS C 212    10258  10905   6256  -1001   1402     26       C  
ATOM   4823  NZ  LYS C 212      -5.204  -1.549  38.552  1.00 75.14           N  
ANISOU 4823  NZ  LYS C 212    10702  11338   6511   -767   1765    -26       N  
ATOM   4824  N   ALA C 213      -0.305  -8.061  39.201  1.00 58.49           N  
ANISOU 4824  N   ALA C 213     8073   9607   4543  -1342    -97   1836       N  
ATOM   4825  CA  ALA C 213       0.416  -8.853  40.191  1.00 62.18           C  
ANISOU 4825  CA  ALA C 213     8559  10274   4794  -1321   -377   2162       C  
ATOM   4826  C   ALA C 213       1.624  -9.589  39.609  1.00 61.14           C  
ANISOU 4826  C   ALA C 213     8207   9981   5041  -1351   -774   2334       C  
ATOM   4827  O   ALA C 213       2.639  -9.748  40.288  1.00 65.31           O  
ANISOU 4827  O   ALA C 213     8742  10705   5369  -1360  -1119   2428       O  
ATOM   4828  CB  ALA C 213      -0.528  -9.832  40.874  1.00 63.51           C  
ANISOU 4828  CB  ALA C 213     8709  10430   4992  -1211   -150   2571       C  
ATOM   4829  N   LYS C 214       1.508 -10.053  38.367  1.00 53.91           N  
ANISOU 4829  N   LYS C 214     7081   8659   4743  -1314   -713   2318       N  
ATOM   4830  CA  LYS C 214       2.610 -10.753  37.707  1.00 58.28           C  
ANISOU 4830  CA  LYS C 214     7412   8974   5758  -1268  -1002   2402       C  
ATOM   4831  C   LYS C 214       3.780  -9.807  37.436  1.00 55.12           C  
ANISOU 4831  C   LYS C 214     6972   8625   5347  -1312  -1211   2015       C  
ATOM   4832  O   LYS C 214       4.948 -10.195  37.542  1.00 56.91           O  
ANISOU 4832  O   LYS C 214     7034   8870   5720  -1290  -1529   2138       O  
ATOM   4833  CB  LYS C 214       2.146 -11.384  36.384  1.00 58.17           C  
ANISOU 4833  CB  LYS C 214     7245   8511   6345  -1205   -857   2390       C  
ATOM   4834  CG  LYS C 214       3.220 -12.220  35.674  1.00 61.80           C  
ANISOU 4834  CG  LYS C 214     7495   8693   7293  -1107  -1086   2474       C  
ATOM   4835  CD  LYS C 214       2.839 -12.551  34.231  1.00 60.35           C  
ANISOU 4835  CD  LYS C 214     7240   8086   7604  -1038   -939   2288       C  
ATOM   4836  CE  LYS C 214       1.510 -13.289  34.153  1.00 64.29           C  
ANISOU 4836  CE  LYS C 214     7765   8403   8259  -1067   -778   2503       C  
ATOM   4837  NZ  LYS C 214       1.096 -13.526  32.741  1.00 63.01           N  
ANISOU 4837  NZ  LYS C 214     7571   7855   8516  -1019   -696   2260       N  
ATOM   4838  N   TYR C 215       3.456  -8.562  37.097  1.00 49.39           N  
ANISOU 4838  N   TYR C 215     6368   7903   4495  -1374  -1027   1576       N  
ATOM   4839  CA  TYR C 215       4.456  -7.606  36.624  1.00 47.86           C  
ANISOU 4839  CA  TYR C 215     6105   7663   4418  -1439  -1163   1204       C  
ATOM   4840  C   TYR C 215       4.845  -6.530  37.631  1.00 54.62           C  
ANISOU 4840  C   TYR C 215     7144   8825   4785  -1573  -1325    941       C  
ATOM   4841  O   TYR C 215       5.664  -5.665  37.326  1.00 60.09           O  
ANISOU 4841  O   TYR C 215     7768   9462   5600  -1669  -1456    632       O  
ATOM   4842  CB  TYR C 215       3.986  -6.953  35.324  1.00 45.94           C  
ANISOU 4842  CB  TYR C 215     5846   7121   4489  -1413   -874    896       C  
ATOM   4843  CG  TYR C 215       3.847  -7.936  34.195  1.00 49.03           C  
ANISOU 4843  CG  TYR C 215     6072   7197   5359  -1288   -792   1057       C  
ATOM   4844  CD1 TYR C 215       4.962  -8.583  33.674  1.00 48.16           C  
ANISOU 4844  CD1 TYR C 215     5740   6947   5612  -1216   -974   1158       C  
ATOM   4845  CD2 TYR C 215       2.601  -8.221  33.647  1.00 50.73           C  
ANISOU 4845  CD2 TYR C 215     6347   7248   5679  -1236   -543   1092       C  
ATOM   4846  CE1 TYR C 215       4.836  -9.492  32.638  1.00 49.29           C  
ANISOU 4846  CE1 TYR C 215     5784   6781   6161  -1079   -888   1247       C  
ATOM   4847  CE2 TYR C 215       2.468  -9.123  32.609  1.00 50.82           C  
ANISOU 4847  CE2 TYR C 215     6248   6957   6105  -1136   -517   1181       C  
ATOM   4848  CZ  TYR C 215       3.587  -9.755  32.110  1.00 51.73           C  
ANISOU 4848  CZ  TYR C 215     6203   6925   6529  -1051   -680   1236       C  
ATOM   4849  OH  TYR C 215       3.447 -10.654  31.076  1.00 54.61           O  
ANISOU 4849  OH  TYR C 215     6508   6968   7271   -931   -641   1267       O  
ATOM   4850  N   LYS C 216       4.272  -6.577  38.828  1.00 52.59           N  
ANISOU 4850  N   LYS C 216     7125   8881   3975  -1584  -1312   1059       N  
ATOM   4851  CA  LYS C 216       4.647  -5.611  39.856  1.00 64.12           C  
ANISOU 4851  CA  LYS C 216     8821  10647   4896  -1702  -1503    768       C  
ATOM   4852  C   LYS C 216       6.092  -5.833  40.295  1.00 71.37           C  
ANISOU 4852  C   LYS C 216     9574  11718   5826  -1788  -2038    856       C  
ATOM   4853  O   LYS C 216       6.592  -6.959  40.281  1.00 71.90           O  
ANISOU 4853  O   LYS C 216     9416  11782   6120  -1711  -2238   1285       O  
ATOM   4854  CB  LYS C 216       3.707  -5.685  41.060  1.00 67.35           C  
ANISOU 4854  CB  LYS C 216     9535  11340   4714  -1620  -1308    877       C  
ATOM   4855  CG  LYS C 216       4.229  -6.504  42.226  1.00 75.36           C  
ANISOU 4855  CG  LYS C 216    10572  12591   5470  -1539  -1586   1216       C  
ATOM   4856  CD  LYS C 216       3.229  -6.480  43.361  1.00 82.63           C  
ANISOU 4856  CD  LYS C 216    11802  13712   5881  -1394  -1294   1274       C  
ATOM   4857  CE  LYS C 216       2.787  -5.052  43.649  1.00 85.85           C  
ANISOU 4857  CE  LYS C 216    12500  14141   5980  -1387  -1093    718       C  
ATOM   4858  NZ  LYS C 216       1.475  -5.002  44.353  1.00 90.15           N  
ANISOU 4858  NZ  LYS C 216    13292  14781   6179  -1200   -635    784       N  
ATOM   4859  N   ALA C 217       6.764  -4.750  40.669  1.00 78.12           N  
ANISOU 4859  N   ALA C 217    10503  12605   6573  -1897  -2229    437       N  
ATOM   4860  CA  ALA C 217       8.163  -4.827  41.064  1.00 87.35           C  
ANISOU 4860  CA  ALA C 217    11459  13836   7892  -1946  -2699    466       C  
ATOM   4861  C   ALA C 217       8.296  -4.931  42.577  1.00 98.36           C  
ANISOU 4861  C   ALA C 217    13093  15541   8738  -1873  -2922    514       C  
ATOM   4862  O   ALA C 217       7.671  -4.174  43.320  1.00102.33           O  
ANISOU 4862  O   ALA C 217    13956  16158   8767  -1851  -2781    215       O  
ATOM   4863  CB  ALA C 217       8.928  -3.622  40.540  1.00 86.57           C  
ANISOU 4863  CB  ALA C 217    11244  13540   8109  -2110  -2807     12       C  
ATOM   4864  OXT ALA C 217       9.038  -5.771  43.090  1.00104.60           O  
ANISOU 4864  OXT ALA C 217    13727  16465   9551  -1809  -3241    850       O  
TER    4865      ALA C 217                                                      
ATOM   4866  N   SER D   4     -19.172 -16.669  17.512  1.00 59.28           N  
ANISOU 4866  N   SER D   4     9750   5310   7462  -1899  -1688    880       N  
ATOM   4867  CA  SER D   4     -18.826 -15.245  17.570  1.00 59.00           C  
ANISOU 4867  CA  SER D   4     9325   5571   7522  -1711  -1497    792       C  
ATOM   4868  C   SER D   4     -19.710 -14.397  16.655  1.00 58.71           C  
ANISOU 4868  C   SER D   4     8828   5837   7641  -1705  -1201    668       C  
ATOM   4869  O   SER D   4     -19.670 -14.540  15.428  1.00 58.39           O  
ANISOU 4869  O   SER D   4     8596   5810   7780  -1509  -1242    585       O  
ATOM   4870  CB  SER D   4     -17.351 -15.031  17.218  1.00 56.05           C  
ANISOU 4870  CB  SER D   4     8882   5137   7279  -1269  -1723    730       C  
ATOM   4871  OG  SER D   4     -17.012 -13.654  17.222  1.00 56.21           O  
ANISOU 4871  OG  SER D   4     8555   5432   7372  -1123  -1534    642       O  
ATOM   4872  N   PRO D   5     -20.515 -13.504  17.252  1.00 54.28           N  
ANISOU 4872  N   PRO D   5     8089   5527   7009  -1912   -909    646       N  
ATOM   4873  CA  PRO D   5     -21.354 -12.624  16.435  1.00 50.89           C  
ANISOU 4873  CA  PRO D   5     7224   5384   6730  -1862   -651    526       C  
ATOM   4874  C   PRO D   5     -20.563 -11.418  15.944  1.00 46.84           C  
ANISOU 4874  C   PRO D   5     6419   4991   6388  -1501   -611    441       C  
ATOM   4875  O   PRO D   5     -21.144 -10.538  15.297  1.00 43.86           O  
ANISOU 4875  O   PRO D   5     5702   4827   6136  -1416   -420    352       O  
ATOM   4876  CB  PRO D   5     -22.430 -12.172  17.420  1.00 52.28           C  
ANISOU 4876  CB  PRO D   5     7356   5765   6743  -2206   -379    514       C  
ATOM   4877  CG  PRO D   5     -21.717 -12.158  18.740  1.00 49.94           C  
ANISOU 4877  CG  PRO D   5     7359   5353   6265  -2303   -456    603       C  
ATOM   4878  CD  PRO D   5     -20.754 -13.318  18.696  1.00 50.10           C  
ANISOU 4878  CD  PRO D   5     7758   5032   6247  -2211   -810    719       C  
ATOM   4879  N   GLY D   6     -19.266 -11.376  16.258  1.00 39.33           N  
ANISOU 4879  N   GLY D   6     5608   3911   5426  -1303   -798    465       N  
ATOM   4880  CA  GLY D   6     -18.413 -10.258  15.891  1.00 32.34           C  
ANISOU 4880  CA  GLY D   6     4488   3143   4655  -1016   -765    381       C  
ATOM   4881  C   GLY D   6     -18.439  -9.127  16.905  1.00 32.16           C  
ANISOU 4881  C   GLY D   6     4417   3261   4542  -1099   -563    368       C  
ATOM   4882  O   GLY D   6     -18.930  -9.294  18.020  1.00 33.86           O  
ANISOU 4882  O   GLY D   6     4805   3472   4587  -1368   -481    428       O  
ATOM   4883  N   VAL D   7     -17.890  -7.980  16.530  1.00 30.33           N  
ANISOU 4883  N   VAL D   7     3969   3151   4405   -891   -481    284       N  
ATOM   4884  CA  VAL D   7     -17.969  -6.794  17.377  1.00 30.82           C  
ANISOU 4884  CA  VAL D   7     3970   3340   4399   -957   -264    247       C  
ATOM   4885  C   VAL D   7     -19.417  -6.300  17.367  1.00 35.29           C  
ANISOU 4885  C   VAL D   7     4356   4052   5002  -1097      3    200       C  
ATOM   4886  O   VAL D   7     -19.941  -5.905  16.324  1.00 29.67           O  
ANISOU 4886  O   VAL D   7     3404   3422   4447   -964     73    142       O  
ATOM   4887  CB  VAL D   7     -17.056  -5.678  16.891  1.00 30.17           C  
ANISOU 4887  CB  VAL D   7     3729   3334   4399   -723   -241    163       C  
ATOM   4888  CG1 VAL D   7     -17.229  -4.442  17.771  1.00 31.66           C  
ANISOU 4888  CG1 VAL D   7     3883   3629   4518   -807     -3    114       C  
ATOM   4889  CG2 VAL D   7     -15.607  -6.128  16.909  1.00 28.64           C  
ANISOU 4889  CG2 VAL D   7     3660   3065   4157   -582   -497    168       C  
ATOM   4890  N   VAL D   8     -20.066  -6.344  18.525  1.00 36.39           N  
ANISOU 4890  N   VAL D   8     4601   4240   4984  -1370    142    214       N  
ATOM   4891  CA  VAL D   8     -21.473  -5.961  18.616  1.00 34.80           C  
ANISOU 4891  CA  VAL D   8     4207   4220   4796  -1517    395    134       C  
ATOM   4892  C   VAL D   8     -21.599  -4.457  18.844  1.00 36.70           C  
ANISOU 4892  C   VAL D   8     4253   4595   5098  -1397    622     14       C  
ATOM   4893  O   VAL D   8     -21.069  -3.919  19.815  1.00 36.95           O  
ANISOU 4893  O   VAL D   8     4399   4622   5017  -1461    685      1       O  
ATOM   4894  CB  VAL D   8     -22.186  -6.729  19.735  1.00 37.79           C  
ANISOU 4894  CB  VAL D   8     4777   4626   4954  -1910    459    174       C  
ATOM   4895  CG1 VAL D   8     -23.615  -6.232  19.897  1.00 42.17           C  
ANISOU 4895  CG1 VAL D   8     5079   5437   5508  -2063    744     39       C  
ATOM   4896  CG2 VAL D   8     -22.186  -8.220  19.434  1.00 38.62           C  
ANISOU 4896  CG2 VAL D   8     5112   4564   4998  -2041    235    293       C  
ATOM   4897  N   ILE D   9     -22.277  -3.777  17.926  1.00 34.72           N  
ANISOU 4897  N   ILE D   9     3723   4449   5020  -1215    728    -74       N  
ATOM   4898  CA  ILE D   9     -22.562  -2.355  18.078  1.00 34.94           C  
ANISOU 4898  CA  ILE D   9     3583   4574   5119  -1080    935   -197       C  
ATOM   4899  C   ILE D   9     -24.022  -2.217  18.516  1.00 36.33           C  
ANISOU 4899  C   ILE D   9     3572   4958   5273  -1230   1159   -318       C  
ATOM   4900  O   ILE D   9     -24.935  -2.717  17.851  1.00 36.60           O  
ANISOU 4900  O   ILE D   9     3437   5101   5370  -1246   1158   -338       O  
ATOM   4901  CB  ILE D   9     -22.261  -1.606  16.782  1.00 34.54           C  
ANISOU 4901  CB  ILE D   9     3379   4483   5263   -757    875   -212       C  
ATOM   4902  CG1 ILE D   9     -20.769  -1.717  16.486  1.00 38.06           C  
ANISOU 4902  CG1 ILE D   9     3991   4779   5690   -658    678   -133       C  
ATOM   4903  CG2 ILE D   9     -22.684  -0.137  16.871  1.00 35.11           C  
ANISOU 4903  CG2 ILE D   9     3311   4614   5416   -600   1071   -337       C  
ATOM   4904  CD1 ILE D   9     -20.341  -1.040  15.228  1.00 41.61           C  
ANISOU 4904  CD1 ILE D   9     4328   5197   6284   -404    610   -145       C  
ATOM   4905  N   SER D  10     -24.243  -1.589  19.666  1.00 35.75           N  
ANISOU 4905  N   SER D  10     3522   4970   5093  -1362   1354   -418       N  
ATOM   4906  CA  SER D  10     -25.569  -1.577  20.271  1.00 40.25           C  
ANISOU 4906  CA  SER D  10     3919   5779   5595  -1561   1575   -565       C  
ATOM   4907  C   SER D  10     -26.498  -0.624  19.533  1.00 38.78           C  
ANISOU 4907  C   SER D  10     3392   5736   5607  -1282   1703   -726       C  
ATOM   4908  O   SER D  10     -26.042   0.233  18.772  1.00 37.48           O  
ANISOU 4908  O   SER D  10     3182   5450   5608   -955   1645   -718       O  
ATOM   4909  CB  SER D  10     -25.492  -1.184  21.744  1.00 45.76           C  
ANISOU 4909  CB  SER D  10     4739   6541   6105  -1799   1752   -646       C  
ATOM   4910  OG  SER D  10     -24.960   0.116  21.866  1.00 50.33           O  
ANISOU 4910  OG  SER D  10     5303   7050   6770  -1566   1837   -726       O  
ATOM   4911  N   ASP D  11     -27.795  -0.787  19.770  1.00 42.46           N  
ANISOU 4911  N   ASP D  11     3625   6468   6038  -1423   1865   -876       N  
ATOM   4912  CA  ASP D  11     -28.821   0.059  19.174  1.00 49.43           C  
ANISOU 4912  CA  ASP D  11     4151   7533   7095  -1153   1980  -1058       C  
ATOM   4913  C   ASP D  11     -28.616   1.539  19.500  1.00 54.89           C  
ANISOU 4913  C   ASP D  11     4813   8157   7886   -883   2105  -1191       C  
ATOM   4914  O   ASP D  11     -28.920   2.414  18.689  1.00 58.40           O  
ANISOU 4914  O   ASP D  11     5091   8577   8523   -519   2083  -1253       O  
ATOM   4915  CB  ASP D  11     -30.200  -0.385  19.660  1.00 51.42           C  
ANISOU 4915  CB  ASP D  11     4226   8094   7217  -1369   2097  -1203       C  
ATOM   4916  CG  ASP D  11     -30.644  -1.687  19.035  1.00 54.82           C  
ANISOU 4916  CG  ASP D  11     4636   8604   7589  -1566   1977  -1102       C  
ATOM   4917  OD1 ASP D  11     -29.994  -2.135  18.069  1.00 55.27           O  
ANISOU 4917  OD1 ASP D  11     4733   8510   7759  -1486   1823   -954       O  
ATOM   4918  OD2 ASP D  11     -31.645  -2.253  19.501  1.00 55.10           O  
ANISOU 4918  OD2 ASP D  11     4622   8852   7461  -1807   2036  -1186       O  
ATOM   4919  N   ASP D  12     -28.078   1.809  20.683  1.00 52.39           N  
ANISOU 4919  N   ASP D  12     4694   7790   7424  -1069   2217  -1222       N  
ATOM   4920  CA  ASP D  12     -27.983   3.172  21.173  1.00 54.22           C  
ANISOU 4920  CA  ASP D  12     4912   7974   7715   -878   2374  -1384       C  
ATOM   4921  C   ASP D  12     -26.589   3.796  21.020  1.00 52.18           C  
ANISOU 4921  C   ASP D  12     4934   7407   7486   -730   2261  -1248       C  
ATOM   4922  O   ASP D  12     -26.328   4.874  21.552  1.00 53.40           O  
ANISOU 4922  O   ASP D  12     5156   7484   7648   -637   2390  -1364       O  
ATOM   4923  CB  ASP D  12     -28.487   3.246  22.620  1.00 59.22           C  
ANISOU 4923  CB  ASP D  12     5586   8775   8142  -1153   2543  -1533       C  
ATOM   4924  CG  ASP D  12     -29.956   2.825  22.752  1.00 68.69           C  
ANISOU 4924  CG  ASP D  12     6553  10262   9284  -1241   2579  -1665       C  
ATOM   4925  OD1 ASP D  12     -30.822   3.517  22.180  1.00 72.87           O  
ANISOU 4925  OD1 ASP D  12     6844  10877   9968   -926   2581  -1791       O  
ATOM   4926  OD2 ASP D  12     -30.250   1.810  23.429  1.00 70.92           O  
ANISOU 4926  OD2 ASP D  12     6913  10681   9352  -1627   2591  -1638       O  
ATOM   4927  N   GLU D  13     -25.702   3.129  20.284  1.00 47.37           N  
ANISOU 4927  N   GLU D  13     4480   6636   6884   -717   2027  -1025       N  
ATOM   4928  CA  GLU D  13     -24.374   3.683  20.008  1.00 46.17           C  
ANISOU 4928  CA  GLU D  13     4553   6241   6748   -588   1911   -916       C  
ATOM   4929  C   GLU D  13     -24.493   4.995  19.234  1.00 50.20           C  
ANISOU 4929  C   GLU D  13     4990   6641   7442   -231   1935   -994       C  
ATOM   4930  O   GLU D  13     -25.084   5.034  18.154  1.00 53.60           O  
ANISOU 4930  O   GLU D  13     5247   7089   8030    -10   1851   -981       O  
ATOM   4931  CB  GLU D  13     -23.510   2.691  19.223  1.00 46.82           C  
ANISOU 4931  CB  GLU D  13     4752   6216   6820   -608   1651   -705       C  
ATOM   4932  CG  GLU D  13     -22.308   3.319  18.496  1.00 52.17           C  
ANISOU 4932  CG  GLU D  13     5566   6703   7555   -416   1517   -624       C  
ATOM   4933  CD  GLU D  13     -21.184   3.752  19.431  1.00 58.03           C  
ANISOU 4933  CD  GLU D  13     6541   7366   8144   -542   1553   -624       C  
ATOM   4934  OE1 GLU D  13     -20.842   2.984  20.357  1.00 65.03           O  
ANISOU 4934  OE1 GLU D  13     7550   8296   8863   -789   1534   -577       O  
ATOM   4935  OE2 GLU D  13     -20.638   4.860  19.235  1.00 58.35           O  
ANISOU 4935  OE2 GLU D  13     6657   7299   8216   -408   1592   -668       O  
ATOM   4936  N   PRO D  14     -23.935   6.079  19.797  1.00 52.49           N  
ANISOU 4936  N   PRO D  14     5435   6807   7700   -188   2043  -1071       N  
ATOM   4937  CA  PRO D  14     -23.954   7.432  19.222  1.00 53.65           C  
ANISOU 4937  CA  PRO D  14     5604   6790   7989    121   2069  -1146       C  
ATOM   4938  C   PRO D  14     -22.959   7.649  18.072  1.00 48.11           C  
ANISOU 4938  C   PRO D  14     5053   5891   7334    256   1863   -980       C  
ATOM   4939  O   PRO D  14     -23.084   8.648  17.357  1.00 51.35           O  
ANISOU 4939  O   PRO D  14     5492   6154   7864    511   1840  -1006       O  
ATOM   4940  CB  PRO D  14     -23.572   8.318  20.417  1.00 51.33           C  
ANISOU 4940  CB  PRO D  14     5480   6438   7586     16   2266  -1284       C  
ATOM   4941  CG  PRO D  14     -22.689   7.441  21.247  1.00 51.69           C  
ANISOU 4941  CG  PRO D  14     5679   6543   7418   -329   2237  -1180       C  
ATOM   4942  CD  PRO D  14     -23.274   6.049  21.116  1.00 52.76           C  
ANISOU 4942  CD  PRO D  14     5661   6853   7533   -468   2149  -1096       C  
ATOM   4943  N   GLY D  15     -22.001   6.742  17.886  1.00 42.41           N  
ANISOU 4943  N   GLY D  15     4431   5169   6514     89   1708   -823       N  
ATOM   4944  CA  GLY D  15     -20.959   6.954  16.898  1.00 38.66           C  
ANISOU 4944  CA  GLY D  15     4087   4555   6049    170   1535   -705       C  
ATOM   4945  C   GLY D  15     -20.038   8.080  17.340  1.00 42.57           C  
ANISOU 4945  C   GLY D  15     4820   4906   6449    137   1616   -755       C  
ATOM   4946  O   GLY D  15     -20.003   8.425  18.525  1.00 44.58           O  
ANISOU 4946  O   GLY D  15     5154   5181   6604      4   1783   -857       O  
ATOM   4947  N   TYR D  16     -19.303   8.670  16.399  1.00 41.01           N  
ANISOU 4947  N   TYR D  16     4744   4575   6261    226   1507   -694       N  
ATOM   4948  CA  TYR D  16     -18.401   9.773  16.733  1.00 39.17           C  
ANISOU 4948  CA  TYR D  16     4762   4205   5915    159   1583   -746       C  
ATOM   4949  C   TYR D  16     -18.696  11.043  15.944  1.00 40.46           C  
ANISOU 4949  C   TYR D  16     5042   4155   6174    370   1590   -771       C  
ATOM   4950  O   TYR D  16     -19.025  10.982  14.752  1.00 35.14           O  
ANISOU 4950  O   TYR D  16     4298   3443   5612    535   1446   -686       O  
ATOM   4951  CB  TYR D  16     -16.951   9.374  16.475  1.00 38.94           C  
ANISOU 4951  CB  TYR D  16     4840   4224   5732    -15   1448   -665       C  
ATOM   4952  CG  TYR D  16     -16.475   8.165  17.239  1.00 36.98           C  
ANISOU 4952  CG  TYR D  16     4532   4147   5373   -199   1395   -631       C  
ATOM   4953  CD1 TYR D  16     -16.701   6.886  16.758  1.00 34.75           C  
ANISOU 4953  CD1 TYR D  16     4089   3961   5152   -173   1237   -540       C  
ATOM   4954  CD2 TYR D  16     -15.779   8.306  18.432  1.00 44.52           C  
ANISOU 4954  CD2 TYR D  16     5615   5152   6149   -400   1487   -686       C  
ATOM   4955  CE1 TYR D  16     -16.255   5.779  17.448  1.00 37.89           C  
ANISOU 4955  CE1 TYR D  16     4484   4469   5444   -325   1159   -498       C  
ATOM   4956  CE2 TYR D  16     -15.330   7.204  19.131  1.00 42.03           C  
ANISOU 4956  CE2 TYR D  16     5276   4974   5721   -554   1404   -637       C  
ATOM   4957  CZ  TYR D  16     -15.569   5.946  18.630  1.00 38.21           C  
ANISOU 4957  CZ  TYR D  16     4660   4550   5308   -506   1232   -540       C  
ATOM   4958  OH  TYR D  16     -15.134   4.840  19.316  1.00 39.68           O  
ANISOU 4958  OH  TYR D  16     4869   4827   5379   -641   1121   -482       O  
ATOM   4959  N   ASP D  17     -18.561  12.182  16.627  1.00 39.37           N  
ANISOU 4959  N   ASP D  17     5108   3870   5980    352   1749   -885       N  
ATOM   4960  CA  ASP D  17     -18.590  13.513  16.019  1.00 42.56           C  
ANISOU 4960  CA  ASP D  17     5737   4008   6426    510   1749   -907       C  
ATOM   4961  C   ASP D  17     -17.614  13.550  14.845  1.00 40.17           C  
ANISOU 4961  C   ASP D  17     5568   3654   6042    435   1567   -769       C  
ATOM   4962  O   ASP D  17     -16.450  13.187  14.998  1.00 33.77           O  
ANISOU 4962  O   ASP D  17     4819   2955   5057    186   1537   -740       O  
ATOM   4963  CB  ASP D  17     -18.169  14.548  17.071  1.00 47.71           C  
ANISOU 4963  CB  ASP D  17     6644   4526   6956    387   1947  -1047       C  
ATOM   4964  CG  ASP D  17     -18.356  15.986  16.616  1.00 54.33           C  
ANISOU 4964  CG  ASP D  17     7764   5036   7843    563   1966  -1095       C  
ATOM   4965  OD1 ASP D  17     -18.270  16.276  15.405  1.00 55.62           O  
ANISOU 4965  OD1 ASP D  17     8026   5062   8046    675   1797   -976       O  
ATOM   4966  OD2 ASP D  17     -18.570  16.851  17.492  1.00 60.89           O  
ANISOU 4966  OD2 ASP D  17     8745   5731   8659    578   2147  -1254       O  
ATOM   4967  N   LEU D  18     -18.083  14.015  13.688  1.00 41.80           N  
ANISOU 4967  N   LEU D  18     5815   3709   6359    644   1441   -696       N  
ATOM   4968  CA  LEU D  18     -17.263  14.082  12.473  1.00 39.97           C  
ANISOU 4968  CA  LEU D  18     5707   3441   6039    556   1268   -570       C  
ATOM   4969  C   LEU D  18     -16.022  14.962  12.669  1.00 35.94           C  
ANISOU 4969  C   LEU D  18     5536   2819   5302    300   1326   -603       C  
ATOM   4970  O   LEU D  18     -14.983  14.735  12.049  1.00 35.39           O  
ANISOU 4970  O   LEU D  18     5517   2849   5079     92   1229   -548       O  
ATOM   4971  CB  LEU D  18     -18.097  14.626  11.303  1.00 42.98           C  
ANISOU 4971  CB  LEU D  18     6125   3642   6563    827   1131   -489       C  
ATOM   4972  CG  LEU D  18     -19.328  13.827  10.855  1.00 46.00           C  
ANISOU 4972  CG  LEU D  18     6164   4160   7154   1078   1045   -452       C  
ATOM   4973  CD1 LEU D  18     -20.208  14.652   9.911  1.00 46.14           C  
ANISOU 4973  CD1 LEU D  18     6260   3967   7304   1385    923   -399       C  
ATOM   4974  CD2 LEU D  18     -18.923  12.520  10.197  1.00 40.94           C  
ANISOU 4974  CD2 LEU D  18     5299   3769   6487    944    913   -354       C  
ATOM   4975  N   ASP D  19     -16.131  15.956  13.545  1.00 36.78           N  
ANISOU 4975  N   ASP D  19     5862   2737   5374    298   1495   -717       N  
ATOM   4976  CA  ASP D  19     -15.041  16.906  13.752  1.00 42.66           C  
ANISOU 4976  CA  ASP D  19     6963   3354   5892     38   1569   -762       C  
ATOM   4977  C   ASP D  19     -13.793  16.302  14.401  1.00 39.82           C  
ANISOU 4977  C   ASP D  19     6544   3270   5315   -300   1618   -804       C  
ATOM   4978  O   ASP D  19     -12.732  16.926  14.422  1.00 43.18           O  
ANISOU 4978  O   ASP D  19     7214   3676   5516   -568   1655   -841       O  
ATOM   4979  CB  ASP D  19     -15.539  18.097  14.574  1.00 46.88           C  
ANISOU 4979  CB  ASP D  19     7751   3607   6456    133   1745   -893       C  
ATOM   4980  CG  ASP D  19     -16.561  18.914  13.830  1.00 57.46           C  
ANISOU 4980  CG  ASP D  19     9230   4628   7974    475   1662   -860       C  
ATOM   4981  OD1 ASP D  19     -16.350  19.149  12.622  1.00 58.12           O  
ANISOU 4981  OD1 ASP D  19     9457   4599   8026    484   1484   -723       O  
ATOM   4982  OD2 ASP D  19     -17.577  19.307  14.445  1.00 63.88           O  
ANISOU 4982  OD2 ASP D  19    10000   5319   8952    736   1764   -979       O  
ATOM   4983  N   LEU D  20     -13.938  15.090  14.920  1.00 36.89           N  
ANISOU 4983  N   LEU D  20     5858   3157   5002   -289   1605   -802       N  
ATOM   4984  CA  LEU D  20     -12.872  14.396  15.623  1.00 39.18           C  
ANISOU 4984  CA  LEU D  20     6065   3712   5110   -548   1618   -839       C  
ATOM   4985  C   LEU D  20     -12.010  13.633  14.632  1.00 43.28           C  
ANISOU 4985  C   LEU D  20     6461   4429   5555   -639   1424   -765       C  
ATOM   4986  O   LEU D  20     -10.939  13.144  14.978  1.00 29.96           O  
ANISOU 4986  O   LEU D  20     4717   2971   3697   -841   1393   -807       O  
ATOM   4987  CB  LEU D  20     -13.464  13.416  16.637  1.00 40.11           C  
ANISOU 4987  CB  LEU D  20     5943   3986   5313   -494   1670   -859       C  
ATOM   4988  CG  LEU D  20     -14.263  14.080  17.756  1.00 45.50           C  
ANISOU 4988  CG  LEU D  20     6703   4543   6042   -446   1885   -974       C  
ATOM   4989  CD1 LEU D  20     -15.074  13.056  18.541  1.00 44.96           C  
ANISOU 4989  CD1 LEU D  20     6380   4636   6067   -394   1921   -982       C  
ATOM   4990  CD2 LEU D  20     -13.323  14.835  18.676  1.00 47.89           C  
ANISOU 4990  CD2 LEU D  20     7238   4842   6114   -713   2033  -1082       C  
ATOM   4991  N   PHE D  21     -12.484  13.547  13.395  1.00 30.62           N  
ANISOU 4991  N   PHE D  21     4807   2751   4075   -482   1289   -670       N  
ATOM   4992  CA  PHE D  21     -11.816  12.757  12.379  1.00 29.09           C  
ANISOU 4992  CA  PHE D  21     4464   2754   3837   -546   1108   -618       C  
ATOM   4993  C   PHE D  21     -11.553  13.544  11.099  1.00 33.35           C  
ANISOU 4993  C   PHE D  21     5191   3175   4305   -604   1028   -569       C  
ATOM   4994  O   PHE D  21     -12.049  14.656  10.923  1.00 32.29           O  
ANISOU 4994  O   PHE D  21     5316   2761   4192   -542   1083   -545       O  
ATOM   4995  CB  PHE D  21     -12.649  11.515  12.072  1.00 27.99           C  
ANISOU 4995  CB  PHE D  21     4021   2710   3905   -335    996   -542       C  
ATOM   4996  CG  PHE D  21     -12.752  10.570  13.221  1.00 33.74           C  
ANISOU 4996  CG  PHE D  21     4587   3578   4655   -340   1037   -574       C  
ATOM   4997  CD1 PHE D  21     -11.816   9.564  13.384  1.00 37.64           C  
ANISOU 4997  CD1 PHE D  21     4951   4301   5048   -453    930   -594       C  
ATOM   4998  CD2 PHE D  21     -13.772  10.692  14.152  1.00 39.89           C  
ANISOU 4998  CD2 PHE D  21     5353   4263   5541   -237   1174   -595       C  
ATOM   4999  CE1 PHE D  21     -11.894   8.686  14.463  1.00 40.29           C  
ANISOU 4999  CE1 PHE D  21     5188   4736   5383   -468    941   -601       C  
ATOM   5000  CE2 PHE D  21     -13.859   9.823  15.229  1.00 46.07           C  
ANISOU 5000  CE2 PHE D  21     6020   5176   6308   -292   1210   -615       C  
ATOM   5001  CZ  PHE D  21     -12.920   8.814  15.382  1.00 45.58           C  
ANISOU 5001  CZ  PHE D  21     5872   5308   6138   -410   1084   -601       C  
ATOM   5002  N   CYS D  22     -10.740  12.965  10.218  1.00 34.50           N  
ANISOU 5002  N   CYS D  22     5219   3535   4353   -732    891   -564       N  
ATOM   5003  CA  CYS D  22     -10.502  13.549   8.907  1.00 34.41           C  
ANISOU 5003  CA  CYS D  22     5360   3459   4256   -824    797   -511       C  
ATOM   5004  C   CYS D  22     -11.587  13.011   7.987  1.00 33.11           C  
ANISOU 5004  C   CYS D  22     5027   3233   4318   -559    664   -387       C  
ATOM   5005  O   CYS D  22     -11.686  11.804   7.788  1.00 32.40           O  
ANISOU 5005  O   CYS D  22     4636   3345   4331   -475    573   -381       O  
ATOM   5006  CB  CYS D  22      -9.124  13.165   8.387  1.00 36.87           C  
ANISOU 5006  CB  CYS D  22     5588   4082   4339  -1106    726   -601       C  
ATOM   5007  N   ILE D  23     -12.397  13.911   7.432  1.00 30.82           N  
ANISOU 5007  N   ILE D  23     4946   2663   4102   -426    642   -293       N  
ATOM   5008  CA  ILE D  23     -13.550  13.538   6.603  1.00 31.65           C  
ANISOU 5008  CA  ILE D  23     4899   2706   4423   -153    516   -176       C  
ATOM   5009  C   ILE D  23     -13.434  14.237   5.249  1.00 32.18           C  
ANISOU 5009  C   ILE D  23     5185   2654   4388   -234    382    -75       C  
ATOM   5010  O   ILE D  23     -13.027  15.391   5.196  1.00 38.42           O  
ANISOU 5010  O   ILE D  23     6344   3239   5016   -383    419    -70       O  
ATOM   5011  CB  ILE D  23     -14.874  13.992   7.288  1.00 40.78           C  
ANISOU 5011  CB  ILE D  23     6077   3628   5790    158    596   -162       C  
ATOM   5012  CG1 ILE D  23     -15.028  13.336   8.668  1.00 35.64           C  
ANISOU 5012  CG1 ILE D  23     5232   3102   5209    190    740   -264       C  
ATOM   5013  CG2 ILE D  23     -16.093  13.707   6.410  1.00 38.33           C  
ANISOU 5013  CG2 ILE D  23     5600   3279   5686    445    459    -55       C  
ATOM   5014  CD1 ILE D  23     -15.066  11.813   8.637  1.00 32.06           C  
ANISOU 5014  CD1 ILE D  23     4420   2930   4833    201    670   -257       C  
ATOM   5015  N   PRO D  24     -13.788  13.544   4.151  1.00 32.74           N  
ANISOU 5015  N   PRO D  24     5055   2848   4535   -162    225      8       N  
ATOM   5016  CA  PRO D  24     -13.736  14.238   2.855  1.00 35.47           C  
ANISOU 5016  CA  PRO D  24     5632   3078   4766   -255     87    119       C  
ATOM   5017  C   PRO D  24     -14.676  15.435   2.831  1.00 37.25           C  
ANISOU 5017  C   PRO D  24     6169   2912   5073    -30     62    222       C  
ATOM   5018  O   PRO D  24     -15.842  15.305   3.208  1.00 37.80           O  
ANISOU 5018  O   PRO D  24     6089   2889   5383    315     65    243       O  
ATOM   5019  CB  PRO D  24     -14.190  13.167   1.848  1.00 33.29           C  
ANISOU 5019  CB  PRO D  24     5031   3013   4605   -161    -64    182       C  
ATOM   5020  CG  PRO D  24     -14.783  12.054   2.655  1.00 32.79           C  
ANISOU 5020  CG  PRO D  24     4610   3091   4759     50     -6    125       C  
ATOM   5021  CD  PRO D  24     -14.133  12.119   4.014  1.00 33.68           C  
ANISOU 5021  CD  PRO D  24     4768   3221   4808    -47    164     -1       C  
ATOM   5022  N   ASN D  25     -14.160  16.590   2.411  1.00 45.17           N  
ANISOU 5022  N   ASN D  25     7607   3692   5866   -230     35    270       N  
ATOM   5023  CA  ASN D  25     -14.918  17.833   2.414  1.00 54.25           C  
ANISOU 5023  CA  ASN D  25     9134   4411   7066    -21     -6    359       C  
ATOM   5024  C   ASN D  25     -16.246  17.751   1.680  1.00 51.87           C  
ANISOU 5024  C   ASN D  25     8717   4001   6989    365   -187    494       C  
ATOM   5025  O   ASN D  25     -17.219  18.407   2.059  1.00 55.38           O  
ANISOU 5025  O   ASN D  25     9272   4165   7603    711   -199    509       O  
ATOM   5026  CB  ASN D  25     -14.092  18.962   1.787  1.00 68.58           C  
ANISOU 5026  CB  ASN D  25    11470   6012   8576   -360    -56    421       C  
ATOM   5027  CG  ASN D  25     -12.768  19.185   2.495  1.00 78.77           C  
ANISOU 5027  CG  ASN D  25    12898   7422   9610   -770    126    271       C  
ATOM   5028  OD1 ASN D  25     -11.802  18.451   2.272  1.00 82.24           O  
ANISOU 5028  OD1 ASN D  25    13118   8234   9894  -1069    152    188       O  
ATOM   5029  ND2 ASN D  25     -12.713  20.208   3.343  1.00 80.85           N  
ANISOU 5029  ND2 ASN D  25    13519   7381   9821   -780    250    219       N  
ATOM   5030  N   HIS D  26     -16.283  16.967   0.611  1.00 43.39           N  
ANISOU 5030  N   HIS D  26     7414   3164   5909    309   -333    575       N  
ATOM   5031  CA  HIS D  26     -17.470  16.936  -0.231  1.00 45.02           C  
ANISOU 5031  CA  HIS D  26     7526   3294   6283    631   -528    715       C  
ATOM   5032  C   HIS D  26     -18.631  16.160   0.402  1.00 43.49           C  
ANISOU 5032  C   HIS D  26     6897   3231   6397   1013   -479    650       C  
ATOM   5033  O   HIS D  26     -19.769  16.257  -0.058  1.00 49.25           O  
ANISOU 5033  O   HIS D  26     7529   3891   7291   1342   -618    731       O  
ATOM   5034  CB  HIS D  26     -17.131  16.406  -1.631  1.00 42.57           C  
ANISOU 5034  CB  HIS D  26     7135   3200   5840    410   -698    820       C  
ATOM   5035  CG  HIS D  26     -16.587  15.010  -1.641  1.00 38.45           C  
ANISOU 5035  CG  HIS D  26     6182   3105   5322    233   -628    711       C  
ATOM   5036  ND1 HIS D  26     -15.244  14.729  -1.505  1.00 36.92           N  
ANISOU 5036  ND1 HIS D  26     6000   3112   4915   -151   -527    593       N  
ATOM   5037  CD2 HIS D  26     -17.208  13.815  -1.793  1.00 36.61           C  
ANISOU 5037  CD2 HIS D  26     5505   3130   5276    394   -657    691       C  
ATOM   5038  CE1 HIS D  26     -15.062  13.421  -1.564  1.00 34.35           C  
ANISOU 5038  CE1 HIS D  26     5263   3126   4661   -182   -510    506       C  
ATOM   5039  NE2 HIS D  26     -16.236  12.844  -1.741  1.00 37.94           N  
ANISOU 5039  NE2 HIS D  26     5456   3606   5352    129   -583    570       N  
ATOM   5040  N   TYR D  27     -18.337  15.399   1.456  1.00 40.66           N  
ANISOU 5040  N   TYR D  27     6282   3075   6093    951   -289    502       N  
ATOM   5041  CA  TYR D  27     -19.370  14.684   2.201  1.00 38.38           C  
ANISOU 5041  CA  TYR D  27     5616   2916   6051   1240   -212    422       C  
ATOM   5042  C   TYR D  27     -19.661  15.336   3.558  1.00 48.71           C  
ANISOU 5042  C   TYR D  27     7030   4041   7436   1388    -30    296       C  
ATOM   5043  O   TYR D  27     -20.472  14.825   4.326  1.00 46.29           O  
ANISOU 5043  O   TYR D  27     6432   3852   7305   1584     67    201       O  
ATOM   5044  CB  TYR D  27     -18.982  13.211   2.406  1.00 35.12           C  
ANISOU 5044  CB  TYR D  27     4826   2867   5651   1073   -149    353       C  
ATOM   5045  CG  TYR D  27     -19.008  12.381   1.143  1.00 38.60           C  
ANISOU 5045  CG  TYR D  27     5066   3522   6079   1001   -315    441       C  
ATOM   5046  CD1 TYR D  27     -19.959  12.609   0.153  1.00 38.28           C  
ANISOU 5046  CD1 TYR D  27     4991   3431   6122   1209   -489    562       C  
ATOM   5047  CD2 TYR D  27     -18.082  11.372   0.943  1.00 34.33           C  
ANISOU 5047  CD2 TYR D  27     4367   3238   5439    736   -305    389       C  
ATOM   5048  CE1 TYR D  27     -19.982  11.842  -0.996  1.00 35.65           C  
ANISOU 5048  CE1 TYR D  27     4472   3309   5764   1118   -632    635       C  
ATOM   5049  CE2 TYR D  27     -18.092  10.613  -0.196  1.00 30.88           C  
ANISOU 5049  CE2 TYR D  27     3748   2997   4989    663   -443    443       C  
ATOM   5050  CZ  TYR D  27     -19.039  10.854  -1.161  1.00 32.89           C  
ANISOU 5050  CZ  TYR D  27     3975   3205   5316    836   -598    568       C  
ATOM   5051  OH  TYR D  27     -19.034  10.086  -2.293  1.00 31.76           O  
ANISOU 5051  OH  TYR D  27     3649   3273   5145    736   -727    613       O  
ATOM   5052  N   ALA D  28     -19.013  16.468   3.831  1.00 52.51           N  
ANISOU 5052  N   ALA D  28     7936   4243   7770   1268     21    285       N  
ATOM   5053  CA  ALA D  28     -19.091  17.140   5.140  1.00 56.66           C  
ANISOU 5053  CA  ALA D  28     8606   4591   8329   1344    214    145       C  
ATOM   5054  C   ALA D  28     -20.483  17.233   5.783  1.00 53.97           C  
ANISOU 5054  C   ALA D  28     8058   4203   8248   1763    264     52       C  
ATOM   5055  O   ALA D  28     -20.673  16.790   6.912  1.00 54.51           O  
ANISOU 5055  O   ALA D  28     7912   4415   8386   1772    449    -92       O  
ATOM   5056  CB  ALA D  28     -18.451  18.522   5.071  1.00 59.61           C  
ANISOU 5056  CB  ALA D  28     9528   4599   8523   1213    213    171       C  
ATOM   5057  N   GLU D  29     -21.451  17.816   5.083  1.00 55.87           N  
ANISOU 5057  N   GLU D  29     8355   4259   8615   2103     95    122       N  
ATOM   5058  CA  GLU D  29     -22.792  17.943   5.654  1.00 58.92           C  
ANISOU 5058  CA  GLU D  29     8501   4643   9241   2516    134     -4       C  
ATOM   5059  C   GLU D  29     -23.755  16.849   5.194  1.00 52.03           C  
ANISOU 5059  C   GLU D  29     7121   4125   8525   2664     44     10       C  
ATOM   5060  O   GLU D  29     -24.963  16.941   5.407  1.00 56.14           O  
ANISOU 5060  O   GLU D  29     7348   4753   9231   2883     50    -75       O  
ATOM   5061  CB  GLU D  29     -23.383  19.338   5.409  1.00 71.11           C  
ANISOU 5061  CB  GLU D  29    10275   5890  10854   2713     11      4       C  
ATOM   5062  CG  GLU D  29     -22.797  20.413   6.327  1.00 81.64           C  
ANISOU 5062  CG  GLU D  29    11991   6936  12093   2609    151   -109       C  
ATOM   5063  CD  GLU D  29     -23.793  21.506   6.691  1.00 92.90           C  
ANISOU 5063  CD  GLU D  29    13427   8176  13695   2907    129   -219       C  
ATOM   5064  OE1 GLU D  29     -24.612  21.893   5.829  1.00 98.37           O  
ANISOU 5064  OE1 GLU D  29    14069   8808  14498   3143    -48   -113       O  
ATOM   5065  OE2 GLU D  29     -23.758  21.980   7.847  1.00 95.97           O  
ANISOU 5065  OE2 GLU D  29    13877   8487  14102   2906    299   -415       O  
ATOM   5066  N   ASP D  30     -23.210  15.805   4.579  1.00 49.20           N  
ANISOU 5066  N   ASP D  30     6605   4008   8081   2420     -4    116       N  
ATOM   5067  CA  ASP D  30     -24.021  14.704   4.072  1.00 47.34           C  
ANISOU 5067  CA  ASP D  30     5928   4096   7963   2515    -82    139       C  
ATOM   5068  C   ASP D  30     -24.015  13.539   5.056  1.00 50.49           C  
ANISOU 5068  C   ASP D  30     5997   4798   8389   2351    113     13       C  
ATOM   5069  O   ASP D  30     -24.771  12.577   4.906  1.00 50.45           O  
ANISOU 5069  O   ASP D  30     5660   5120   8389   2360     88    -12       O  
ATOM   5070  CB  ASP D  30     -23.490  14.231   2.710  1.00 45.91           C  
ANISOU 5070  CB  ASP D  30     5768   4005   7670   2323   -276    320       C  
ATOM   5071  CG  ASP D  30     -23.606  15.300   1.628  1.00 51.09           C  
ANISOU 5071  CG  ASP D  30     6751   4382   8280   2465   -503    473       C  
ATOM   5072  OD1 ASP D  30     -24.606  16.055   1.630  1.00 52.25           O  
ANISOU 5072  OD1 ASP D  30     6904   4429   8518   2758   -524    473       O  
ATOM   5073  OD2 ASP D  30     -22.692  15.382   0.776  1.00 50.94           O  
ANISOU 5073  OD2 ASP D  30     6962   4318   8075   2190   -606    602       O  
ATOM   5074  N   LEU D  31     -23.146  13.623   6.057  1.00 48.21           N  
ANISOU 5074  N   LEU D  31     5865   4455   7995   2127    290    -67       N  
ATOM   5075  CA  LEU D  31     -23.019  12.555   7.041  1.00 38.51           C  
ANISOU 5075  CA  LEU D  31     4394   3478   6759   1942    455   -166       C  
ATOM   5076  C   LEU D  31     -23.452  13.094   8.395  1.00 43.32           C  
ANISOU 5076  C   LEU D  31     5020   4021   7419   2040    663   -344       C  
ATOM   5077  O   LEU D  31     -23.461  14.305   8.609  1.00 51.47           O  
ANISOU 5077  O   LEU D  31     6320   4782   8456   2181    692   -391       O  
ATOM   5078  CB  LEU D  31     -21.582  12.054   7.101  1.00 38.64           C  
ANISOU 5078  CB  LEU D  31     4545   3544   6591   1580    473   -118       C  
ATOM   5079  CG  LEU D  31     -21.022  11.468   5.801  1.00 37.60           C  
ANISOU 5079  CG  LEU D  31     4385   3512   6390   1445    288     18       C  
ATOM   5080  CD1 LEU D  31     -19.519  11.262   5.910  1.00 33.20           C  
ANISOU 5080  CD1 LEU D  31     3991   2988   5637   1119    311     17       C  
ATOM   5081  CD2 LEU D  31     -21.714  10.157   5.476  1.00 39.39           C  
ANISOU 5081  CD2 LEU D  31     4240   4008   6719   1475    234     31       C  
ATOM   5082  N   GLU D  32     -23.828  12.199   9.301  1.00 42.49           N  
ANISOU 5082  N   GLU D  32     4647   4157   7340   1951    804   -448       N  
ATOM   5083  CA AGLU D  32     -24.267  12.622  10.627  0.58 47.68           C  
ANISOU 5083  CA AGLU D  32     5287   4805   8023   2000   1017   -638       C  
ATOM   5084  CA BGLU D  32     -24.288  12.584  10.631  0.42 47.97           C  
ANISOU 5084  CA BGLU D  32     5313   4853   8061   1997   1017   -638       C  
ATOM   5085  C   GLU D  32     -23.208  12.292  11.676  1.00 45.10           C  
ANISOU 5085  C   GLU D  32     5094   4506   7534   1664   1167   -669       C  
ATOM   5086  O   GLU D  32     -22.857  13.146  12.491  1.00 44.52           O  
ANISOU 5086  O   GLU D  32     5240   4272   7402   1632   1304   -768       O  
ATOM   5087  CB AGLU D  32     -25.603  11.973  11.004  0.58 51.08           C  
ANISOU 5087  CB AGLU D  32     5370   5564   8474   2075   1040   -740       C  
ATOM   5088  CB BGLU D  32     -25.556  11.798  10.970  0.42 50.63           C  
ANISOU 5088  CB BGLU D  32     5291   5532   8415   2044   1036   -727       C  
ATOM   5089  CG AGLU D  32     -26.369  12.707  12.103  0.58 57.10           C  
ANISOU 5089  CG AGLU D  32     6113   6343   9239   2206   1198   -947       C  
ATOM   5090  CG BGLU D  32     -26.595  12.558  11.767  0.42 57.32           C  
ANISOU 5090  CG BGLU D  32     6081   6422   9275   2246   1139   -915       C  
ATOM   5091  CD AGLU D  32     -27.214  13.855  11.571  0.58 62.65           C  
ANISOU 5091  CD AGLU D  32     6893   6931   9981   2582   1076   -982       C  
ATOM   5092  CD BGLU D  32     -27.986  11.970  11.594  0.42 62.19           C  
ANISOU 5092  CD BGLU D  32     6361   7372   9896   2363   1103   -956       C  
ATOM   5093  OE1AGLU D  32     -26.669  14.962  11.387  0.58 63.21           O  
ANISOU 5093  OE1AGLU D  32     7293   6668  10057   2689   1028   -970       O  
ATOM   5094  OE1BGLU D  32     -28.945  12.754  11.429  0.42 68.16           O  
ANISOU 5094  OE1BGLU D  32     7082   8135  10679   2664   1071  -1014       O  
ATOM   5095  OE2AGLU D  32     -28.425  13.650  11.335  0.58 69.27           O  
ANISOU 5095  OE2AGLU D  32     7482   8005  10833   2766   1037  -1009       O  
ATOM   5096  OE2BGLU D  32     -28.117  10.726  11.614  0.42 60.57           O  
ANISOU 5096  OE2BGLU D  32     5942   7411   9660   2148   1117   -917       O  
ATOM   5097  N   ARG D  33     -22.697  11.062  11.646  1.00 41.49           N  
ANISOU 5097  N   ARG D  33     4517   4248   6999   1422   1126   -589       N  
ATOM   5098  CA  ARG D  33     -21.700  10.596  12.612  1.00 41.35           C  
ANISOU 5098  CA  ARG D  33     4601   4288   6821   1120   1225   -607       C  
ATOM   5099  C   ARG D  33     -20.781   9.585  11.950  1.00 37.23           C  
ANISOU 5099  C   ARG D  33     4062   3868   6215    935   1070   -472       C  
ATOM   5100  O   ARG D  33     -21.172   8.936  10.981  1.00 40.49           O  
ANISOU 5100  O   ARG D  33     4307   4371   6705   1006    930   -391       O  
ATOM   5101  CB  ARG D  33     -22.378   9.885  13.794  1.00 44.47           C  
ANISOU 5101  CB  ARG D  33     4798   4881   7219   1028   1382   -720       C  
ATOM   5102  CG  ARG D  33     -23.529  10.624  14.461  1.00 51.56           C  
ANISOU 5102  CG  ARG D  33     5595   5777   8218   1218   1548   -903       C  
ATOM   5103  CD  ARG D  33     -23.027  11.753  15.339  1.00 55.25           C  
ANISOU 5103  CD  ARG D  33     6326   6056   8611   1188   1703  -1015       C  
ATOM   5104  NE  ARG D  33     -22.411  11.245  16.561  1.00 57.19           N  
ANISOU 5104  NE  ARG D  33     6624   6415   8692    874   1838  -1056       N  
ATOM   5105  CZ  ARG D  33     -21.957  12.012  17.547  1.00 56.97           C  
ANISOU 5105  CZ  ARG D  33     6794   6290   8562    768   2002  -1169       C  
ATOM   5106  NH1 ARG D  33     -22.038  13.331  17.454  1.00 55.82           N  
ANISOU 5106  NH1 ARG D  33     6835   5905   8469    952   2058  -1259       N  
ATOM   5107  NH2 ARG D  33     -21.415  11.454  18.622  1.00 55.27           N  
ANISOU 5107  NH2 ARG D  33     6611   6205   8183    472   2099  -1188       N  
ATOM   5108  N   VAL D  34     -19.567   9.433  12.477  1.00 30.92           N  
ANISOU 5108  N   VAL D  34     3421   3074   5254    703   1091   -467       N  
ATOM   5109  CA  VAL D  34     -18.752   8.282  12.125  1.00 31.63           C  
ANISOU 5109  CA  VAL D  34     3446   3303   5269    542    958   -389       C  
ATOM   5110  C   VAL D  34     -19.268   7.135  12.992  1.00 35.34           C  
ANISOU 5110  C   VAL D  34     3750   3929   5749    457   1006   -410       C  
ATOM   5111  O   VAL D  34     -19.467   7.303  14.194  1.00 33.23           O  
ANISOU 5111  O   VAL D  34     3520   3675   5431    378   1162   -492       O  
ATOM   5112  CB  VAL D  34     -17.252   8.519  12.390  1.00 33.59           C  
ANISOU 5112  CB  VAL D  34     3895   3538   5330    342    946   -398       C  
ATOM   5113  CG1 VAL D  34     -16.480   7.223  12.241  1.00 30.32           C  
ANISOU 5113  CG1 VAL D  34     3381   3289   4851    216    808   -357       C  
ATOM   5114  CG2 VAL D  34     -16.699   9.539  11.423  1.00 33.67           C  
ANISOU 5114  CG2 VAL D  34     4085   3416   5292    358    887   -371       C  
ATOM   5115  N   PHE D  35     -19.503   5.976  12.386  1.00 35.37           N  
ANISOU 5115  N   PHE D  35     3589   4047   5803    450    876   -342       N  
ATOM   5116  CA  PHE D  35     -20.148   4.873  13.090  1.00 33.52           C  
ANISOU 5116  CA  PHE D  35     3225   3940   5571    352    911   -351       C  
ATOM   5117  C   PHE D  35     -19.123   3.801  13.431  1.00 33.09           C  
ANISOU 5117  C   PHE D  35     3249   3927   5395    172    800   -300       C  
ATOM   5118  O   PHE D  35     -19.085   3.277  14.543  1.00 32.74           O  
ANISOU 5118  O   PHE D  35     3260   3923   5258     19    857   -314       O  
ATOM   5119  CB  PHE D  35     -21.251   4.303  12.202  1.00 34.43           C  
ANISOU 5119  CB  PHE D  35     3115   4146   5821    462    844   -320       C  
ATOM   5120  CG  PHE D  35     -22.293   3.533  12.942  1.00 37.71           C  
ANISOU 5120  CG  PHE D  35     3386   4701   6241    366    938   -367       C  
ATOM   5121  CD1 PHE D  35     -23.046   4.137  13.938  1.00 38.52           C  
ANISOU 5121  CD1 PHE D  35     3449   4846   6339    366   1136   -487       C  
ATOM   5122  CD2 PHE D  35     -22.549   2.210  12.611  1.00 41.28           C  
ANISOU 5122  CD2 PHE D  35     3744   5251   6691    258    836   -308       C  
ATOM   5123  CE1 PHE D  35     -24.025   3.429  14.609  1.00 43.93           C  
ANISOU 5123  CE1 PHE D  35     3989   5703   6999    231   1236   -552       C  
ATOM   5124  CE2 PHE D  35     -23.525   1.493  13.277  1.00 40.41           C  
ANISOU 5124  CE2 PHE D  35     3524   5279   6552    116    928   -353       C  
ATOM   5125  CZ  PHE D  35     -24.264   2.102  14.278  1.00 43.21           C  
ANISOU 5125  CZ  PHE D  35     3824   5709   6884     89   1132   -477       C  
ATOM   5126  N   ILE D  36     -18.287   3.469  12.460  1.00 27.44           N  
ANISOU 5126  N   ILE D  36     2543   3208   4675    195    630   -248       N  
ATOM   5127  CA  ILE D  36     -17.184   2.552  12.689  1.00 23.52           C  
ANISOU 5127  CA  ILE D  36     2116   2747   4072     82    497   -228       C  
ATOM   5128  C   ILE D  36     -15.955   3.149  12.032  1.00 31.13           C  
ANISOU 5128  C   ILE D  36     3152   3708   4968     94    420   -254       C  
ATOM   5129  O   ILE D  36     -15.864   3.192  10.805  1.00 33.06           O  
ANISOU 5129  O   ILE D  36     3324   3968   5270    167    324   -237       O  
ATOM   5130  CB  ILE D  36     -17.463   1.157  12.092  1.00 25.84           C  
ANISOU 5130  CB  ILE D  36     2302   3088   4427     83    342   -175       C  
ATOM   5131  CG1 ILE D  36     -18.843   0.648  12.493  1.00 27.32           C  
ANISOU 5131  CG1 ILE D  36     2397   3308   4675     44    430   -158       C  
ATOM   5132  CG2 ILE D  36     -16.389   0.154  12.494  1.00 24.30           C  
ANISOU 5132  CG2 ILE D  36     2201   2901   4129      3    188   -167       C  
ATOM   5133  CD1 ILE D  36     -19.226  -0.678  11.824  1.00 32.22           C  
ANISOU 5133  CD1 ILE D  36     2930   3964   5350     20    290   -109       C  
ATOM   5134  N   PRO D  37     -15.011   3.642  12.848  1.00 30.69           N  
ANISOU 5134  N   PRO D  37     3236   3657   4769     -7    470   -304       N  
ATOM   5135  CA  PRO D  37     -13.806   4.250  12.282  1.00 29.09           C  
ANISOU 5135  CA  PRO D  37     3096   3493   4463    -46    415   -354       C  
ATOM   5136  C   PRO D  37     -13.033   3.248  11.426  1.00 28.00           C  
ANISOU 5136  C   PRO D  37     2851   3469   4319    -27    208   -366       C  
ATOM   5137  O   PRO D  37     -13.012   2.055  11.732  1.00 27.43           O  
ANISOU 5137  O   PRO D  37     2728   3428   4266    -13     98   -348       O  
ATOM   5138  CB  PRO D  37     -13.000   4.644  13.526  1.00 30.47           C  
ANISOU 5138  CB  PRO D  37     3411   3697   4469   -183    498   -413       C  
ATOM   5139  CG  PRO D  37     -14.044   4.871  14.588  1.00 31.38           C  
ANISOU 5139  CG  PRO D  37     3569   3730   4623   -196    668   -399       C  
ATOM   5140  CD  PRO D  37     -15.088   3.814  14.311  1.00 30.80           C  
ANISOU 5140  CD  PRO D  37     3354   3658   4691   -116    604   -330       C  
ATOM   5141  N   HIS D  38     -12.422   3.737  10.355  1.00 28.06           N  
ANISOU 5141  N   HIS D  38     3701   2642   4319   -361    344   -438       N  
ATOM   5142  CA  HIS D  38     -11.639   2.903   9.454  1.00 25.26           C  
ANISOU 5142  CA  HIS D  38     3340   2329   3930   -421    329   -340       C  
ATOM   5143  C   HIS D  38     -10.650   2.008  10.197  1.00 23.49           C  
ANISOU 5143  C   HIS D  38     3028   2269   3628   -492    336   -366       C  
ATOM   5144  O   HIS D  38     -10.544   0.815   9.922  1.00 23.85           O  
ANISOU 5144  O   HIS D  38     3022   2404   3635   -478    310   -297       O  
ATOM   5145  CB  HIS D  38     -10.859   3.788   8.477  1.00 28.04           C  
ANISOU 5145  CB  HIS D  38     3800   2542   4311   -497    345   -308       C  
ATOM   5146  CG  HIS D  38     -10.025   3.009   7.509  1.00 27.59           C  
ANISOU 5146  CG  HIS D  38     3724   2553   4206   -555    333   -223       C  
ATOM   5147  ND1 HIS D  38      -8.652   2.936   7.597  1.00 31.10           N  
ANISOU 5147  ND1 HIS D  38     4142   3073   4602   -679    357   -257       N  
ATOM   5148  CD2 HIS D  38     -10.374   2.250   6.441  1.00 26.07           C  
ANISOU 5148  CD2 HIS D  38     3521   2386   3998   -498    296   -125       C  
ATOM   5149  CE1 HIS D  38      -8.188   2.178   6.619  1.00 29.32           C  
ANISOU 5149  CE1 HIS D  38     3892   2915   4333   -688    337   -181       C  
ATOM   5150  NE2 HIS D  38      -9.212   1.746   5.907  1.00 31.38           N  
ANISOU 5150  NE2 HIS D  38     4166   3143   4614   -581    298   -102       N  
ATOM   5151  N   GLY D  39      -9.922   2.604  11.133  1.00 29.37           N  
ANISOU 5151  N   GLY D  39     3759   3051   4349   -559    366   -475       N  
ATOM   5152  CA  GLY D  39      -8.885   1.893  11.863  1.00 29.14           C  
ANISOU 5152  CA  GLY D  39     3645   3196   4231   -612    367   -512       C  
ATOM   5153  C   GLY D  39      -9.431   0.719  12.657  1.00 29.59           C  
ANISOU 5153  C   GLY D  39     3622   3393   4227   -535    350   -472       C  
ATOM   5154  O   GLY D  39      -8.783  -0.327  12.781  1.00 28.07           O  
ANISOU 5154  O   GLY D  39     3382   3318   3967   -535    330   -428       O  
ATOM   5155  N   LEU D  40     -10.637   0.882  13.191  1.00 25.89           N  
ANISOU 5155  N   LEU D  40     3142   2915   3781   -467    360   -485       N  
ATOM   5156  CA ALEU D  40     -11.304  -0.192  13.925  0.07 27.03           C  
ANISOU 5156  CA ALEU D  40     3216   3184   3870   -414    358   -431       C  
ATOM   5157  CA BLEU D  40     -11.282  -0.202  13.927  0.93 26.29           C  
ANISOU 5157  CA BLEU D  40     3122   3092   3775   -415    358   -431       C  
ATOM   5158  C   LEU D  40     -11.639  -1.332  12.965  1.00 27.36           C  
ANISOU 5158  C   LEU D  40     3267   3192   3939   -394    327   -301       C  
ATOM   5159  O   LEU D  40     -11.520  -2.512  13.305  1.00 24.40           O  
ANISOU 5159  O   LEU D  40     2857   2900   3514   -387    317   -231       O  
ATOM   5160  CB ALEU D  40     -12.582   0.326  14.588  0.07 28.70           C  
ANISOU 5160  CB ALEU D  40     3399   3407   4098   -354    382   -485       C  
ATOM   5161  CB BLEU D  40     -12.527   0.309  14.664  0.93 27.68           C  
ANISOU 5161  CB BLEU D  40     3266   3288   3963   -356    383   -488       C  
ATOM   5162  CG ALEU D  40     -13.017  -0.213  15.952  0.07 30.59           C  
ANISOU 5162  CG ALEU D  40     3549   3828   4244   -330    410   -498       C  
ATOM   5163  CG BLEU D  40     -13.331  -0.711  15.461  0.93 29.62           C  
ANISOU 5163  CG BLEU D  40     3434   3674   4146   -324    399   -428       C  
ATOM   5164  CD1ALEU D  40     -14.529  -0.102  16.100  0.07 31.65           C  
ANISOU 5164  CD1ALEU D  40     3643   3976   4407   -269    428   -503       C  
ATOM   5165  CD1BLEU D  40     -12.404  -1.484  16.373  0.93 31.66           C  
ANISOU 5165  CD1BLEU D  40     3655   4084   4292   -350    404   -402       C  
ATOM   5166  CD2ALEU D  40     -12.554  -1.642  16.193  0.07 30.49           C  
ANISOU 5166  CD2ALEU D  40     3510   3918   4157   -348    401   -379       C  
ATOM   5167  CD2BLEU D  40     -14.427  -0.016  16.272  0.93 32.96           C  
ANISOU 5167  CD2BLEU D  40     3805   4156   4561   -271    431   -520       C  
ATOM   5168  N   ILE D  41     -12.071  -0.970  11.761  1.00 23.49           N  
ANISOU 5168  N   ILE D  41     2828   2573   3526   -378    309   -271       N  
ATOM   5169  CA  ILE D  41     -12.355  -1.960  10.738  1.00 24.02           C  
ANISOU 5169  CA  ILE D  41     2897   2611   3619   -361    274   -176       C  
ATOM   5170  C   ILE D  41     -11.074  -2.735  10.443  1.00 24.87           C  
ANISOU 5170  C   ILE D  41     3005   2764   3682   -398    251   -144       C  
ATOM   5171  O   ILE D  41     -11.092  -3.958  10.354  1.00 22.49           O  
ANISOU 5171  O   ILE D  41     2682   2496   3368   -381    226    -82       O  
ATOM   5172  CB  ILE D  41     -12.886  -1.304   9.453  1.00 23.94           C  
ANISOU 5172  CB  ILE D  41     2940   2480   3676   -328    254   -158       C  
ATOM   5173  CG1 ILE D  41     -14.249  -0.664   9.712  1.00 22.02           C  
ANISOU 5173  CG1 ILE D  41     2684   2210   3472   -257    264   -194       C  
ATOM   5174  CG2 ILE D  41     -13.008  -2.324   8.344  1.00 21.50           C  
ANISOU 5174  CG2 ILE D  41     2621   2166   3381   -313    213    -84       C  
ATOM   5175  CD1 ILE D  41     -14.704   0.255   8.572  1.00 26.57           C  
ANISOU 5175  CD1 ILE D  41     3331   2664   4102   -198    242   -182       C  
ATOM   5176  N   MET D  42      -9.958  -2.021  10.315  1.00 23.97           N  
ANISOU 5176  N   MET D  42     2913   2652   3544   -449    260   -195       N  
ATOM   5177  CA  MET D  42      -8.662  -2.669  10.068  1.00 27.55           C  
ANISOU 5177  CA  MET D  42     3346   3185   3939   -477    238   -190       C  
ATOM   5178  C   MET D  42      -8.279  -3.656  11.177  1.00 23.79           C  
ANISOU 5178  C   MET D  42     2817   2836   3386   -445    227   -183       C  
ATOM   5179  O   MET D  42      -7.913  -4.798  10.899  1.00 22.25           O  
ANISOU 5179  O   MET D  42     2613   2674   3167   -406    189   -129       O  
ATOM   5180  CB  MET D  42      -7.553  -1.621   9.869  1.00 25.89           C  
ANISOU 5180  CB  MET D  42     3148   2980   3709   -562    263   -265       C  
ATOM   5181  CG  MET D  42      -7.726  -0.707   8.661  1.00 29.40           C  
ANISOU 5181  CG  MET D  42     3666   3291   4214   -600    276   -241       C  
ATOM   5182  SD  MET D  42      -7.778  -1.611   7.095  1.00 33.38           S  
ANISOU 5182  SD  MET D  42     4177   3787   4721   -558    230   -145       S  
ATOM   5183  CE  MET D  42      -9.560  -1.776   6.933  1.00 41.72           C  
ANISOU 5183  CE  MET D  42     5255   4745   5850   -462    211    -91       C  
ATOM   5184  N   ASP D  43      -8.367  -3.224  12.429  1.00 21.27           N  
ANISOU 5184  N   ASP D  43     2469   2590   3022   -449    258   -237       N  
ATOM   5185  CA  ASP D  43      -8.002  -4.095  13.544  1.00 24.73           C  
ANISOU 5185  CA  ASP D  43     2864   3168   3365   -408    250   -217       C  
ATOM   5186  C   ASP D  43      -8.858  -5.356  13.588  1.00 24.51           C  
ANISOU 5186  C   ASP D  43     2851   3107   3353   -357    236    -95       C  
ATOM   5187  O   ASP D  43      -8.343  -6.450  13.829  1.00 25.47           O  
ANISOU 5187  O   ASP D  43     2975   3280   3423   -312    206    -32       O  
ATOM   5188  CB  ASP D  43      -8.114  -3.363  14.896  1.00 21.91           C  
ANISOU 5188  CB  ASP D  43     2465   2915   2946   -416    288   -302       C  
ATOM   5189  CG  ASP D  43      -7.102  -2.233  15.043  1.00 28.74           C  
ANISOU 5189  CG  ASP D  43     3306   3826   3787   -481    301   -443       C  
ATOM   5190  OD1 ASP D  43      -5.995  -2.341  14.485  1.00 28.77           O  
ANISOU 5190  OD1 ASP D  43     3298   3864   3769   -513    279   -465       O  
ATOM   5191  OD2 ASP D  43      -7.416  -1.251  15.741  1.00 32.41           O  
ANISOU 5191  OD2 ASP D  43     3757   4301   4255   -505    335   -544       O  
ATOM   5192  N   ARG D  44     -10.165  -5.199  13.386  1.00 21.75           N  
ANISOU 5192  N   ARG D  44     2511   2675   3076   -363    258    -67       N  
ATOM   5193  CA  ARG D  44     -11.063  -6.357  13.360  1.00 20.73           C  
ANISOU 5193  CA  ARG D  44     2390   2509   2978   -348    254     37       C  
ATOM   5194  C   ARG D  44     -10.759  -7.267  12.171  1.00 23.26           C  
ANISOU 5194  C   ARG D  44     2746   2739   3353   -335    203     86       C  
ATOM   5195  O   ARG D  44     -10.782  -8.492  12.291  1.00 23.37           O  
ANISOU 5195  O   ARG D  44     2781   2732   3366   -316    183    166       O  
ATOM   5196  CB  ARG D  44     -12.530  -5.913  13.320  1.00 22.67           C  
ANISOU 5196  CB  ARG D  44     2612   2716   3286   -363    288     29       C  
ATOM   5197  CG  ARG D  44     -13.517  -7.063  13.271  1.00 23.11           C  
ANISOU 5197  CG  ARG D  44     2659   2742   3379   -379    295    120       C  
ATOM   5198  CD  ARG D  44     -13.469  -7.924  14.523  1.00 21.39           C  
ANISOU 5198  CD  ARG D  44     2437   2613   3078   -388    326    203       C  
ATOM   5199  NE  ARG D  44     -14.478  -8.986  14.437  1.00 24.89           N  
ANISOU 5199  NE  ARG D  44     2880   3006   3572   -435    344    294       N  
ATOM   5200  CZ  ARG D  44     -14.300 -10.223  14.871  1.00 28.81           C  
ANISOU 5200  CZ  ARG D  44     3422   3478   4045   -450    346    410       C  
ATOM   5201  NH1 ARG D  44     -13.146 -10.576  15.426  1.00 28.54           N  
ANISOU 5201  NH1 ARG D  44     3435   3484   3925   -394    323    452       N  
ATOM   5202  NH2 ARG D  44     -15.277 -11.109  14.741  1.00 26.23           N  
ANISOU 5202  NH2 ARG D  44     3098   3088   3782   -521    371    481       N  
ATOM   5203  N   THR D  45     -10.465  -6.660  11.025  1.00 21.74           N  
ANISOU 5203  N   THR D  45     2566   2490   3206   -343    181     38       N  
ATOM   5204  CA  THR D  45     -10.148  -7.413   9.810  1.00 22.29           C  
ANISOU 5204  CA  THR D  45     2655   2500   3315   -324    130     61       C  
ATOM   5205  C   THR D  45      -8.858  -8.218   9.985  1.00 24.87           C  
ANISOU 5205  C   THR D  45     2985   2889   3575   -284     93     67       C  
ATOM   5206  O   THR D  45      -8.748  -9.357   9.498  1.00 25.43           O  
ANISOU 5206  O   THR D  45     3077   2915   3672   -243     48    103       O  
ATOM   5207  CB  THR D  45     -10.068  -6.458   8.599  1.00 24.56           C  
ANISOU 5207  CB  THR D  45     2951   2744   3636   -340    124     16       C  
ATOM   5208  OG1 THR D  45     -11.362  -5.870   8.383  1.00 23.58           O  
ANISOU 5208  OG1 THR D  45     2828   2561   3572   -342    144     18       O  
ATOM   5209  CG2 THR D  45      -9.640  -7.195   7.338  1.00 23.54           C  
ANISOU 5209  CG2 THR D  45     2828   2594   3523   -315     72     24       C  
ATOM   5210  N   GLU D  46      -7.892  -7.655  10.712  1.00 22.30           N  
ANISOU 5210  N   GLU D  46     2635   2674   3165   -287    106     17       N  
ATOM   5211  CA  GLU D  46      -6.657  -8.386  10.998  1.00 22.17           C  
ANISOU 5211  CA  GLU D  46     2605   2754   3066   -227     65     11       C  
ATOM   5212  C   GLU D  46      -6.970  -9.678  11.756  1.00 23.09           C  
ANISOU 5212  C   GLU D  46     2758   2849   3167   -161     47    109       C  
ATOM   5213  O   GLU D  46      -6.418 -10.739  11.460  1.00 22.67           O  
ANISOU 5213  O   GLU D  46     2731   2777   3106    -85     -8    138       O  
ATOM   5214  CB  GLU D  46      -5.667  -7.528  11.811  1.00 24.23           C  
ANISOU 5214  CB  GLU D  46     2812   3166   3227   -247     86    -75       C  
ATOM   5215  CG  GLU D  46      -4.377  -8.281  12.100  1.00 22.79           C  
ANISOU 5215  CG  GLU D  46     2596   3119   2944   -165     36    -95       C  
ATOM   5216  CD  GLU D  46      -3.409  -7.498  12.968  1.00 34.51           C  
ANISOU 5216  CD  GLU D  46     4005   4787   4319   -187     52   -199       C  
ATOM   5217  OE1 GLU D  46      -2.352  -8.059  13.314  1.00 34.51           O  
ANISOU 5217  OE1 GLU D  46     3960   4934   4218   -105      8   -228       O  
ATOM   5218  OE2 GLU D  46      -3.700  -6.329  13.295  1.00 44.03           O  
ANISOU 5218  OE2 GLU D  46     5194   5994   5541   -278    105   -263       O  
ATOM   5219  N   ARG D  47      -7.857  -9.603  12.742  1.00 21.69           N  
ANISOU 5219  N   ARG D  47     2588   2672   2982   -186     93    162       N  
ATOM   5220  CA  ARG D  47      -8.220 -10.807  13.480  1.00 24.38           C  
ANISOU 5220  CA  ARG D  47     2977   2982   3305   -145     90    281       C  
ATOM   5221  C   ARG D  47      -8.985 -11.776  12.576  1.00 26.55           C  
ANISOU 5221  C   ARG D  47     3304   3085   3700   -160     68    340       C  
ATOM   5222  O   ARG D  47      -8.760 -12.999  12.621  1.00 24.74           O  
ANISOU 5222  O   ARG D  47     3138   2782   3480   -105     31    415       O  
ATOM   5223  CB  ARG D  47      -9.027 -10.452  14.734  1.00 23.87           C  
ANISOU 5223  CB  ARG D  47     2893   2989   3189   -184    157    323       C  
ATOM   5224  CG  ARG D  47      -9.806 -11.615  15.350  1.00 30.56           C  
ANISOU 5224  CG  ARG D  47     3796   3775   4041   -189    179    470       C  
ATOM   5225  CD  ARG D  47      -8.942 -12.857  15.601  1.00 43.95           C  
ANISOU 5225  CD  ARG D  47     5567   5445   5685    -90    125    564       C  
ATOM   5226  NE  ARG D  47      -8.394 -12.896  16.938  1.00 52.35           N  
ANISOU 5226  NE  ARG D  47     6626   6670   6592    -24    137    615       N  
ATOM   5227  CZ  ARG D  47      -8.790 -13.730  17.891  1.00 49.02           C  
ANISOU 5227  CZ  ARG D  47     6266   6247   6110     -9    166    770       C  
ATOM   5228  NH1 ARG D  47      -9.733 -14.633  17.658  1.00 56.72           N  
ANISOU 5228  NH1 ARG D  47     7317   7048   7185    -76    192    887       N  
ATOM   5229  NH2 ARG D  47      -8.222 -13.664  19.079  1.00 39.98           N  
ANISOU 5229  NH2 ARG D  47     5107   5286   4800     67    171    807       N  
ATOM   5230  N   LEU D  48      -9.893 -11.248  11.763  1.00 25.42           N  
ANISOU 5230  N   LEU D  48     3137   2874   3648   -228     87    299       N  
ATOM   5231  CA  LEU D  48     -10.660 -12.127  10.872  1.00 27.59           C  
ANISOU 5231  CA  LEU D  48     3440   3008   4035   -251     65    327       C  
ATOM   5232  C   LEU D  48      -9.732 -12.899   9.934  1.00 25.49           C  
ANISOU 5232  C   LEU D  48     3205   2691   3789   -179    -11    297       C  
ATOM   5233  O   LEU D  48      -9.955 -14.074   9.676  1.00 22.44           O  
ANISOU 5233  O   LEU D  48     2872   2187   3467   -164    -42    339       O  
ATOM   5234  CB  LEU D  48     -11.719 -11.363  10.069  1.00 27.76           C  
ANISOU 5234  CB  LEU D  48     3413   3001   4131   -312     86    271       C  
ATOM   5235  CG  LEU D  48     -12.908 -10.804  10.850  1.00 27.04           C  
ANISOU 5235  CG  LEU D  48     3282   2950   4042   -372    154    288       C  
ATOM   5236  CD1 LEU D  48     -13.870 -10.039   9.943  1.00 27.31           C  
ANISOU 5236  CD1 LEU D  48     3267   2967   4143   -394    157    221       C  
ATOM   5237  CD2 LEU D  48     -13.632 -11.914  11.594  1.00 25.43           C  
ANISOU 5237  CD2 LEU D  48     3099   2706   3856   -422    186    387       C  
ATOM   5238  N   ALA D  49      -8.693 -12.249   9.423  1.00 20.67           N  
ANISOU 5238  N   ALA D  49     2560   2168   3124   -140    -38    217       N  
ATOM   5239  CA  ALA D  49      -7.754 -12.943   8.519  1.00 21.56           C  
ANISOU 5239  CA  ALA D  49     2681   2272   3237    -61   -110    169       C  
ATOM   5240  C   ALA D  49      -7.150 -14.156   9.216  1.00 22.78           C  
ANISOU 5240  C   ALA D  49     2898   2399   3360     35   -151    229       C  
ATOM   5241  O   ALA D  49      -6.967 -15.223   8.621  1.00 24.37           O  
ANISOU 5241  O   ALA D  49     3144   2503   3614    101   -210    222       O  
ATOM   5242  CB  ALA D  49      -6.653 -11.992   8.054  1.00 23.03           C  
ANISOU 5242  CB  ALA D  49     2807   2600   3345    -51   -116     78       C  
ATOM   5243  N   ARG D  50      -6.835 -13.989  10.494  1.00 24.10           N  
ANISOU 5243  N   ARG D  50     3071   2652   3434     56   -124    284       N  
ATOM   5244  CA  ARG D  50      -6.255 -15.087  11.257  1.00 26.52           C  
ANISOU 5244  CA  ARG D  50     3446   2941   3688    169   -164    362       C  
ATOM   5245  C   ARG D  50      -7.278 -16.198  11.482  1.00 27.99           C  
ANISOU 5245  C   ARG D  50     3735   2930   3971    138   -152    484       C  
ATOM   5246  O   ARG D  50      -6.952 -17.385  11.367  1.00 24.85           O  
ANISOU 5246  O   ARG D  50     3425   2412   3606    228   -209    528       O  
ATOM   5247  CB  ARG D  50      -5.685 -14.576  12.585  1.00 31.62           C  
ANISOU 5247  CB  ARG D  50     4062   3762   4189    203   -137    388       C  
ATOM   5248  CG  ARG D  50      -4.519 -15.409  13.108  1.00 38.31           C  
ANISOU 5248  CG  ARG D  50     4943   4680   4934    371   -206    415       C  
ATOM   5249  CD  ARG D  50      -3.965 -14.842  14.407  1.00 43.24           C  
ANISOU 5249  CD  ARG D  50     5517   5516   5397    409   -184    422       C  
ATOM   5250  NE  ARG D  50      -4.921 -14.969  15.504  1.00 49.52           N  
ANISOU 5250  NE  ARG D  50     6364   6279   6172    357   -120    558       N  
ATOM   5251  CZ  ARG D  50      -4.795 -14.374  16.689  1.00 56.43           C  
ANISOU 5251  CZ  ARG D  50     7190   7338   6914    359    -82    567       C  
ATOM   5252  NH1 ARG D  50      -3.753 -13.590  16.941  1.00 57.19           N  
ANISOU 5252  NH1 ARG D  50     7182   7650   6896    402   -102    438       N  
ATOM   5253  NH2 ARG D  50      -5.717 -14.557  17.626  1.00 55.59           N  
ANISOU 5253  NH2 ARG D  50     7126   7213   6782    310    -19    696       N  
ATOM   5254  N   ASP D  51      -8.519 -15.822  11.778  1.00 29.59           N  
ANISOU 5254  N   ASP D  51     3925   3095   4223      8    -78    530       N  
ATOM   5255  CA  ASP D  51      -9.585 -16.808  11.932  1.00 28.40           C  
ANISOU 5255  CA  ASP D  51     3852   2768   4171    -64    -52    635       C  
ATOM   5256  C   ASP D  51      -9.802 -17.564  10.611  1.00 26.42           C  
ANISOU 5256  C   ASP D  51     3629   2351   4058    -68   -108    567       C  
ATOM   5257  O   ASP D  51     -10.018 -18.774  10.596  1.00 28.88           O  
ANISOU 5257  O   ASP D  51     4039   2485   4449    -63   -130    632       O  
ATOM   5258  CB  ASP D  51     -10.893 -16.107  12.335  1.00 31.07           C  
ANISOU 5258  CB  ASP D  51     4131   3145   4530   -207     38    656       C  
ATOM   5259  CG  ASP D  51     -10.815 -15.435  13.700  1.00 34.24           C  
ANISOU 5259  CG  ASP D  51     4502   3711   4795   -206     97    713       C  
ATOM   5260  OD1 ASP D  51      -9.885 -15.742  14.469  1.00 32.45           O  
ANISOU 5260  OD1 ASP D  51     4319   3551   4461   -106     73    770       O  
ATOM   5261  OD2 ASP D  51     -11.705 -14.612  14.012  1.00 38.03           O  
ANISOU 5261  OD2 ASP D  51     4911   4268   5272   -295    163    691       O  
ATOM   5262  N   VAL D  52      -9.776 -16.828   9.504  1.00 24.84           N  
ANISOU 5262  N   VAL D  52     3344   2210   3886    -81   -128    437       N  
ATOM   5263  CA  VAL D  52      -9.983 -17.435   8.191  1.00 28.36           C  
ANISOU 5263  CA  VAL D  52     3791   2541   4442    -79   -184    350       C  
ATOM   5264  C   VAL D  52      -8.910 -18.469   7.895  1.00 30.36           C  
ANISOU 5264  C   VAL D  52     4116   2725   4697     61   -270    326       C  
ATOM   5265  O   VAL D  52      -9.213 -19.609   7.514  1.00 29.68           O  
ANISOU 5265  O   VAL D  52     4105   2455   4719     66   -307    326       O  
ATOM   5266  CB  VAL D  52     -10.024 -16.383   7.083  1.00 26.53           C  
ANISOU 5266  CB  VAL D  52     3456   2419   4203    -98   -191    229       C  
ATOM   5267  CG1 VAL D  52      -9.842 -17.030   5.723  1.00 29.86           C  
ANISOU 5267  CG1 VAL D  52     3871   2779   4694    -51   -265    122       C  
ATOM   5268  CG2 VAL D  52     -11.343 -15.614   7.140  1.00 27.37           C  
ANISOU 5268  CG2 VAL D  52     3505   2545   4347   -219   -124    237       C  
ATOM   5269  N   MET D  53      -7.652 -18.093   8.099  1.00 25.98           N  
ANISOU 5269  N   MET D  53     3535   2315   4022    177   -302    296       N  
ATOM   5270  CA AMET D  53      -6.564 -19.034   7.833  0.63 27.95           C  
ANISOU 5270  CA AMET D  53     3835   2531   4255    340   -391    257       C  
ATOM   5271  CA BMET D  53      -6.531 -19.012   7.869  0.37 29.00           C  
ANISOU 5271  CA BMET D  53     3967   2670   4382    342   -391    258       C  
ATOM   5272  C   MET D  53      -6.616 -20.265   8.731  1.00 32.28           C  
ANISOU 5272  C   MET D  53     4529   2902   4833    403   -409    389       C  
ATOM   5273  O   MET D  53      -6.250 -21.368   8.300  1.00 32.57           O  
ANISOU 5273  O   MET D  53     4648   2793   4935    510   -484    361       O  
ATOM   5274  CB AMET D  53      -5.203 -18.335   7.897  0.63 30.86           C  
ANISOU 5274  CB AMET D  53     4119   3130   4475    444   -418    184       C  
ATOM   5275  CB BMET D  53      -5.190 -18.311   8.121  0.37 31.42           C  
ANISOU 5275  CB BMET D  53     4197   3209   4534    444   -412    203       C  
ATOM   5276  CG AMET D  53      -4.957 -17.420   6.707  0.63 30.55           C  
ANISOU 5276  CG AMET D  53     3963   3226   4419    400   -419     48       C  
ATOM   5277  CG BMET D  53      -4.617 -17.532   6.941  0.37 30.84           C  
ANISOU 5277  CG BMET D  53     4005   3287   4425    441   -430     53       C  
ATOM   5278  SD AMET D  53      -4.967 -18.347   5.154  0.63 37.40           S  
ANISOU 5278  SD AMET D  53     4833   3993   5385    463   -500    -75       S  
ATOM   5279  SD BMET D  53      -4.052 -18.558   5.562  0.37 37.70           S  
ANISOU 5279  SD BMET D  53     4873   4104   5347    569   -533    -81       S  
ATOM   5280  CE AMET D  53      -3.524 -19.380   5.395  0.63 41.22           C  
ANISOU 5280  CE AMET D  53     5353   4509   5798    689   -598   -118       C  
ATOM   5281  CE BMET D  53      -5.520 -18.510   4.541  0.37 39.37           C  
ANISOU 5281  CE BMET D  53     5081   4174   5704    422   -505   -106       C  
ATOM   5282  N   LYS D  54      -7.088 -20.098   9.964  1.00 32.14           N  
ANISOU 5282  N   LYS D  54     4551   2891   4769    339   -339    534       N  
ATOM   5283  CA  LYS D  54      -7.193 -21.240  10.876  1.00 34.51           C  
ANISOU 5283  CA  LYS D  54     5006   3023   5086    387   -342    695       C  
ATOM   5284  C   LYS D  54      -8.193 -22.261  10.347  1.00 33.68           C  
ANISOU 5284  C   LYS D  54     4995   2639   5163    286   -339    720       C  
ATOM   5285  O   LYS D  54      -7.981 -23.466  10.461  1.00 31.34           O  
ANISOU 5285  O   LYS D  54     4845   2135   4929    368   -387    785       O  
ATOM   5286  CB  LYS D  54      -7.581 -20.790  12.295  1.00 40.69           C  
ANISOU 5286  CB  LYS D  54     5796   3903   5763    322   -256    848       C  
ATOM   5287  CG  LYS D  54      -7.232 -21.791  13.392  1.00 49.40           C  
ANISOU 5287  CG  LYS D  54     7051   4915   6804    431   -270   1029       C  
ATOM   5288  CD  LYS D  54      -7.736 -21.353  14.767  1.00 56.04           C  
ANISOU 5288  CD  LYS D  54     7888   5876   7529    354   -176   1181       C  
ATOM   5289  CE  LYS D  54      -9.261 -21.264  14.816  1.00 58.83           C  
ANISOU 5289  CE  LYS D  54     8231   6137   7986    121    -72   1238       C  
ATOM   5290  NZ  LYS D  54      -9.729 -19.869  15.095  1.00 58.23           N  
ANISOU 5290  NZ  LYS D  54     7996   6292   7838     19      0   1167       N  
ATOM   5291  N   GLU D  55      -9.280 -21.789   9.754  1.00 31.68           N  
ANISOU 5291  N   GLU D  55     4661   2378   4998    113   -286    658       N  
ATOM   5292  CA  GLU D  55     -10.307 -22.717   9.284  1.00 36.31           C  
ANISOU 5292  CA  GLU D  55     5314   2725   5758    -10   -275    662       C  
ATOM   5293  C   GLU D  55     -10.084 -23.205   7.849  1.00 34.65           C  
ANISOU 5293  C   GLU D  55     5085   2424   5655     45   -364    482       C  
ATOM   5294  O   GLU D  55     -10.440 -24.335   7.512  1.00 36.71           O  
ANISOU 5294  O   GLU D  55     5448   2444   6058     17   -394    471       O  
ATOM   5295  CB  GLU D  55     -11.697 -22.091   9.406  1.00 39.04           C  
ANISOU 5295  CB  GLU D  55     5570   3120   6143   -223   -176    678       C  
ATOM   5296  CG  GLU D  55     -12.167 -21.892  10.831  1.00 54.47           C  
ANISOU 5296  CG  GLU D  55     7553   5127   8015   -304    -79    858       C  
ATOM   5297  CD  GLU D  55     -13.639 -21.516  10.909  1.00 65.29           C  
ANISOU 5297  CD  GLU D  55     8836   6528   9443   -514     16    862       C  
ATOM   5298  OE1 GLU D  55     -13.959 -20.524  11.606  1.00 67.90           O  
ANISOU 5298  OE1 GLU D  55     9079   7052   9670   -555     84    893       O  
ATOM   5299  OE2 GLU D  55     -14.467 -22.216  10.279  1.00 68.82           O  
ANISOU 5299  OE2 GLU D  55     9295   6817  10038   -635     20    817       O  
ATOM   5300  N   MET D  56      -9.491 -22.348   7.021  1.00 30.48           N  
ANISOU 5300  N   MET D  56     4430   2093   5058    116   -403    338       N  
ATOM   5301  CA  MET D  56      -9.456 -22.550   5.573  1.00 30.18           C  
ANISOU 5301  CA  MET D  56     4332   2039   5095    143   -472    154       C  
ATOM   5302  C   MET D  56      -8.056 -22.697   4.993  1.00 33.88           C  
ANISOU 5302  C   MET D  56     4786   2598   5490    346   -566     44       C  
ATOM   5303  O   MET D  56      -7.907 -23.017   3.814  1.00 32.12           O  
ANISOU 5303  O   MET D  56     4520   2366   5317    394   -631   -114       O  
ATOM   5304  CB  MET D  56     -10.149 -21.371   4.883  1.00 32.79           C  
ANISOU 5304  CB  MET D  56     4511   2542   5405     33   -428     73       C  
ATOM   5305  CG  MET D  56     -11.580 -21.160   5.340  1.00 33.96           C  
ANISOU 5305  CG  MET D  56     4640   2644   5619   -156   -340    146       C  
ATOM   5306  SD  MET D  56     -12.372 -19.892   4.356  1.00 31.20           S  
ANISOU 5306  SD  MET D  56     4122   2483   5250   -234   -316     32       S  
ATOM   5307  CE  MET D  56     -12.676 -20.783   2.823  1.00 27.12           C  
ANISOU 5307  CE  MET D  56     3577   1872   4855   -226   -399   -151       C  
ATOM   5308  N   GLY D  57      -7.032 -22.477   5.814  1.00 36.44           N  
ANISOU 5308  N   GLY D  57     5129   3031   5684    469   -576    114       N  
ATOM   5309  CA  GLY D  57      -5.663 -22.480   5.321  1.00 35.01           C  
ANISOU 5309  CA  GLY D  57     4899   2995   5407    657   -658     -1       C  
ATOM   5310  C   GLY D  57      -5.064 -23.818   4.934  1.00 37.18           C  
ANISOU 5310  C   GLY D  57     5273   3105   5748    832   -763    -71       C  
ATOM   5311  O   GLY D  57      -3.881 -23.893   4.589  1.00 38.27           O  
ANISOU 5311  O   GLY D  57     5363   3382   5795   1011   -836   -174       O  
ATOM   5312  N   GLY D  58      -5.858 -24.885   4.980  1.00 34.71           N  
ANISOU 5312  N   GLY D  58     5095   2496   5595    781   -771    -25       N  
ATOM   5313  CA  GLY D  58      -5.330 -26.213   4.744  1.00 40.19           C  
ANISOU 5313  CA  GLY D  58     5918   2981   6371    953   -871    -79       C  
ATOM   5314  C   GLY D  58      -5.332 -26.627   3.284  1.00 36.82           C  
ANISOU 5314  C   GLY D  58     5430   2525   6033    990   -945   -308       C  
ATOM   5315  O   GLY D  58      -4.761 -27.647   2.922  1.00 40.66           O  
ANISOU 5315  O   GLY D  58     5999   2871   6578   1161  -1043   -403       O  
ATOM   5316  N   HIS D  59      -5.974 -25.833   2.440  1.00 34.02           N  
ANISOU 5316  N   HIS D  59     4931   2311   5683    842   -904   -402       N  
ATOM   5317  CA  HIS D  59      -6.086 -26.193   1.035  1.00 34.21           C  
ANISOU 5317  CA  HIS D  59     4884   2337   5779    866   -970   -621       C  
ATOM   5318  C   HIS D  59      -6.247 -24.920   0.223  1.00 29.99           C  
ANISOU 5318  C   HIS D  59     4158   2097   5139    779   -928   -698       C  
ATOM   5319  O   HIS D  59      -6.643 -23.905   0.757  1.00 32.09           O  
ANISOU 5319  O   HIS D  59     4378   2476   5340    657   -841   -578       O  
ATOM   5320  CB  HIS D  59      -7.294 -27.104   0.826  1.00 37.22           C  
ANISOU 5320  CB  HIS D  59     5359   2417   6367    725   -964   -642       C  
ATOM   5321  CG  HIS D  59      -7.410 -27.655  -0.562  1.00 46.19           C  
ANISOU 5321  CG  HIS D  59     6434   3530   7587    762  -1045   -888       C  
ATOM   5322  ND1 HIS D  59      -6.567 -28.633  -1.048  1.00 56.01           N  
ANISOU 5322  ND1 HIS D  59     7719   4741   8822    942  -1128  -1010       N  
ATOM   5323  CD2 HIS D  59      -8.287 -27.386  -1.561  1.00 48.00           C  
ANISOU 5323  CD2 HIS D  59     6543   3831   7865    633  -1034  -1023       C  
ATOM   5324  CE1 HIS D  59      -6.913 -28.935  -2.288  1.00 57.18           C  
ANISOU 5324  CE1 HIS D  59     7775   4934   9015    918  -1168  -1213       C  
ATOM   5325  NE2 HIS D  59      -7.953 -28.193  -2.624  1.00 51.82           N  
ANISOU 5325  NE2 HIS D  59     6999   4321   8371    736  -1116  -1227       N  
ATOM   5326  N   HIS D  60      -5.930 -24.986  -1.066  1.00 35.75           N  
ANISOU 5326  N   HIS D  60     4785   2950   5848    853   -992   -898       N  
ATOM   5327  CA  HIS D  60      -6.096 -23.849  -1.978  1.00 30.02           C  
ANISOU 5327  CA  HIS D  60     3891   2496   5019    780   -957   -966       C  
ATOM   5328  C   HIS D  60      -7.412 -23.104  -1.741  1.00 30.01           C  
ANISOU 5328  C   HIS D  60     3867   2474   5061    570   -865   -860       C  
ATOM   5329  O   HIS D  60      -8.494 -23.694  -1.777  1.00 32.32           O  
ANISOU 5329  O   HIS D  60     4206   2577   5499    463   -859   -871       O  
ATOM   5330  CB  HIS D  60      -6.025 -24.351  -3.425  1.00 33.12           C  
ANISOU 5330  CB  HIS D  60     4201   2951   5432    855  -1039  -1197       C  
ATOM   5331  CG  HIS D  60      -6.078 -23.267  -4.457  1.00 40.20           C  
ANISOU 5331  CG  HIS D  60     4933   4141   6199    810  -1012  -1262       C  
ATOM   5332  ND1 HIS D  60      -5.237 -23.244  -5.548  1.00 45.00           N  
ANISOU 5332  ND1 HIS D  60     5429   4975   6695    936  -1069  -1428       N  
ATOM   5333  CD2 HIS D  60      -6.880 -22.183  -4.578  1.00 39.65           C  
ANISOU 5333  CD2 HIS D  60     4799   4177   6090    663   -935  -1178       C  
ATOM   5334  CE1 HIS D  60      -5.508 -22.184  -6.285  1.00 42.33           C  
ANISOU 5334  CE1 HIS D  60     4973   4863   6247    857  -1023  -1424       C  
ATOM   5335  NE2 HIS D  60      -6.508 -21.529  -5.728  1.00 37.23           N  
ANISOU 5335  NE2 HIS D  60     4359   4137   5648    701   -946  -1276       N  
ATOM   5336  N   ILE D  61      -7.302 -21.798  -1.515  1.00 27.68           N  
ANISOU 5336  N   ILE D  61     3496   2380   4641    513   -796   -771       N  
ATOM   5337  CA  ILE D  61      -8.454 -20.950  -1.287  1.00 29.24           C  
ANISOU 5337  CA  ILE D  61     3663   2590   4858    347   -714   -679       C  
ATOM   5338  C   ILE D  61      -8.767 -20.155  -2.540  1.00 31.01           C  
ANISOU 5338  C   ILE D  61     3759   3009   5017    322   -715   -774       C  
ATOM   5339  O   ILE D  61      -7.869 -19.595  -3.174  1.00 30.25           O  
ANISOU 5339  O   ILE D  61     3590   3113   4791    399   -730   -824       O  
ATOM   5340  CB  ILE D  61      -8.189 -19.985  -0.135  1.00 26.53           C  
ANISOU 5340  CB  ILE D  61     3336   2319   4425    305   -636   -516       C  
ATOM   5341  CG1 ILE D  61      -8.143 -20.755   1.177  1.00 30.71           C  
ANISOU 5341  CG1 ILE D  61     3994   2660   5013    314   -624   -396       C  
ATOM   5342  CG2 ILE D  61      -9.265 -18.894  -0.025  1.00 28.21           C  
ANISOU 5342  CG2 ILE D  61     3497   2589   4633    164   -556   -445       C  
ATOM   5343  CD1 ILE D  61      -7.735 -19.892   2.329  1.00 31.93           C  
ANISOU 5343  CD1 ILE D  61     4156   2914   5062    299   -560   -261       C  
ATOM   5344  N   VAL D  62     -10.039 -20.135  -2.914  1.00 24.75           N  
ANISOU 5344  N   VAL D  62     2933   2169   4304    218   -700   -799       N  
ATOM   5345  CA  VAL D  62     -10.510 -19.182  -3.908  1.00 26.37           C  
ANISOU 5345  CA  VAL D  62     3025   2565   4430    193   -689   -844       C  
ATOM   5346  C   VAL D  62     -11.314 -18.114  -3.175  1.00 28.16           C  
ANISOU 5346  C   VAL D  62     3250   2807   4642     85   -603   -701       C  
ATOM   5347  O   VAL D  62     -12.340 -18.401  -2.563  1.00 29.93           O  
ANISOU 5347  O   VAL D  62     3498   2904   4969    -12   -571   -660       O  
ATOM   5348  CB  VAL D  62     -11.364 -19.850  -4.993  1.00 25.18           C  
ANISOU 5348  CB  VAL D  62     2809   2403   4356    180   -747  -1007       C  
ATOM   5349  CG1 VAL D  62     -11.902 -18.793  -5.969  1.00 32.82           C  
ANISOU 5349  CG1 VAL D  62     3663   3589   5219    173   -737  -1029       C  
ATOM   5350  CG2 VAL D  62     -10.560 -20.912  -5.728  1.00 29.81           C  
ANISOU 5350  CG2 VAL D  62     3396   2973   4959    300   -839  -1173       C  
ATOM   5351  N   ALA D  63     -10.838 -16.878  -3.225  1.00 22.81           N  
ANISOU 5351  N   ALA D  63     2542   2285   3837    100   -562   -631       N  
ATOM   5352  CA  ALA D  63     -11.523 -15.772  -2.569  1.00 21.50           C  
ANISOU 5352  CA  ALA D  63     2380   2135   3654     21   -487   -512       C  
ATOM   5353  C   ALA D  63     -12.394 -15.059  -3.592  1.00 29.64           C  
ANISOU 5353  C   ALA D  63     3331   3281   4650     16   -492   -550       C  
ATOM   5354  O   ALA D  63     -11.894 -14.551  -4.606  1.00 29.45           O  
ANISOU 5354  O   ALA D  63     3263   3405   4520     76   -514   -584       O  
ATOM   5355  CB  ALA D  63     -10.520 -14.816  -1.976  1.00 22.11           C  
ANISOU 5355  CB  ALA D  63     2484   2289   3628     33   -439   -420       C  
ATOM   5356  N   LEU D  64     -13.693 -15.020  -3.311  1.00 26.29           N  
ANISOU 5356  N   LEU D  64     2883   2805   4300    -52   -471   -540       N  
ATOM   5357  CA  LEU D  64     -14.692 -14.483  -4.225  1.00 24.57           C  
ANISOU 5357  CA  LEU D  64     2581   2699   4055    -41   -488   -589       C  
ATOM   5358  C   LEU D  64     -15.193 -13.130  -3.705  1.00 25.36           C  
ANISOU 5358  C   LEU D  64     2690   2838   4108    -55   -425   -475       C  
ATOM   5359  O   LEU D  64     -15.847 -13.069  -2.671  1.00 27.17           O  
ANISOU 5359  O   LEU D  64     2933   2989   4399   -122   -378   -424       O  
ATOM   5360  CB  LEU D  64     -15.865 -15.464  -4.308  1.00 30.42           C  
ANISOU 5360  CB  LEU D  64     3268   3373   4919   -106   -514   -690       C  
ATOM   5361  CG  LEU D  64     -16.468 -15.810  -5.660  1.00 40.97           C  
ANISOU 5361  CG  LEU D  64     4497   4824   6246    -66   -585   -845       C  
ATOM   5362  CD1 LEU D  64     -15.390 -16.435  -6.524  1.00 43.89           C  
ANISOU 5362  CD1 LEU D  64     4872   5231   6575     16   -649   -940       C  
ATOM   5363  CD2 LEU D  64     -17.645 -16.781  -5.497  1.00 39.79           C  
ANISOU 5363  CD2 LEU D  64     4292   4589   6237   -171   -596   -949       C  
ATOM   5364  N   CYS D  65     -14.895 -12.052  -4.424  1.00 23.61           N  
ANISOU 5364  N   CYS D  65     2463   2734   3772     10   -424   -437       N  
ATOM   5365  CA  CYS D  65     -15.330 -10.723  -4.013  1.00 24.96           C  
ANISOU 5365  CA  CYS D  65     2661   2918   3904     14   -373   -337       C  
ATOM   5366  C   CYS D  65     -16.727 -10.432  -4.554  1.00 24.97           C  
ANISOU 5366  C   CYS D  65     2586   2992   3911     52   -398   -379       C  
ATOM   5367  O   CYS D  65     -16.960 -10.503  -5.770  1.00 25.16           O  
ANISOU 5367  O   CYS D  65     2549   3133   3877    121   -454   -443       O  
ATOM   5368  CB  CYS D  65     -14.351  -9.682  -4.539  1.00 27.62           C  
ANISOU 5368  CB  CYS D  65     3048   3323   4122     57   -355   -263       C  
ATOM   5369  SG  CYS D  65     -14.791  -7.979  -4.165  1.00 27.18           S  
ANISOU 5369  SG  CYS D  65     3055   3246   4026     73   -298   -144       S  
ATOM   5370  N   VAL D  66     -17.662 -10.127  -3.658  1.00 25.38           N  
ANISOU 5370  N   VAL D  66     2624   2998   4019     16   -360   -355       N  
ATOM   5371  CA  VAL D  66     -18.988  -9.690  -4.074  1.00 22.69           C  
ANISOU 5371  CA  VAL D  66     2200   2752   3670     70   -382   -397       C  
ATOM   5372  C   VAL D  66     -19.013  -8.175  -4.332  1.00 23.63           C  
ANISOU 5372  C   VAL D  66     2372   2910   3695    173   -369   -304       C  
ATOM   5373  O   VAL D  66     -19.139  -7.377  -3.402  1.00 22.26           O  
ANISOU 5373  O   VAL D  66     2252   2670   3537    165   -317   -236       O  
ATOM   5374  CB  VAL D  66     -20.048 -10.073  -3.043  1.00 26.16           C  
ANISOU 5374  CB  VAL D  66     2581   3155   4204    -12   -346   -429       C  
ATOM   5375  CG1 VAL D  66     -21.430  -9.733  -3.581  1.00 31.08           C  
ANISOU 5375  CG1 VAL D  66     3084   3914   4809     52   -380   -505       C  
ATOM   5376  CG2 VAL D  66     -19.971 -11.566  -2.745  1.00 25.01           C  
ANISOU 5376  CG2 VAL D  66     2415   2929   4159   -129   -350   -496       C  
ATOM   5377  N   LEU D  67     -18.874  -7.793  -5.601  1.00 26.38           N  
ANISOU 5377  N   LEU D  67     2715   3363   3946    271   -417   -300       N  
ATOM   5378  CA  LEU D  67     -18.854  -6.383  -6.023  1.00 23.96           C  
ANISOU 5378  CA  LEU D  67     2484   3077   3545    376   -409   -193       C  
ATOM   5379  C   LEU D  67     -20.234  -5.762  -5.863  1.00 28.54           C  
ANISOU 5379  C   LEU D  67     3013   3701   4132    467   -425   -210       C  
ATOM   5380  O   LEU D  67     -21.211  -6.503  -5.780  1.00 27.29           O  
ANISOU 5380  O   LEU D  67     2728   3616   4027    452   -453   -325       O  
ATOM   5381  CB  LEU D  67     -18.437  -6.316  -7.497  1.00 26.83           C  
ANISOU 5381  CB  LEU D  67     2840   3569   3785    459   -459   -183       C  
ATOM   5382  CG  LEU D  67     -16.991  -6.666  -7.817  1.00 30.76           C  
ANISOU 5382  CG  LEU D  67     3385   4063   4239    396   -442   -158       C  
ATOM   5383  CD1 LEU D  67     -16.807  -6.704  -9.329  1.00 37.05           C  
ANISOU 5383  CD1 LEU D  67     4141   5036   4900    486   -496   -172       C  
ATOM   5384  CD2 LEU D  67     -16.057  -5.655  -7.171  1.00 31.46           C  
ANISOU 5384  CD2 LEU D  67     3607   4034   4312    344   -366    -25       C  
ATOM   5385  N   LYS D  68     -20.335  -4.427  -5.802  1.00 25.84           N  
ANISOU 5385  N   LYS D  68     2763   3312   3741    560   -406   -108       N  
ATOM   5386  CA  LYS D  68     -19.178  -3.531  -5.706  1.00 27.27           C  
ANISOU 5386  CA  LYS D  68     3101   3377   3885    536   -355     23       C  
ATOM   5387  C   LYS D  68     -18.803  -3.314  -4.250  1.00 27.90           C  
ANISOU 5387  C   LYS D  68     3238   3310   4052    431   -284     39       C  
ATOM   5388  O   LYS D  68     -17.647  -3.082  -3.938  1.00 27.36           O  
ANISOU 5388  O   LYS D  68     3257   3158   3979    347   -237     98       O  
ATOM   5389  CB  LYS D  68     -19.486  -2.154  -6.308  1.00 24.17           C  
ANISOU 5389  CB  LYS D  68     2805   2968   3410    681   -367    131       C  
ATOM   5390  CG  LYS D  68     -19.882  -2.120  -7.768  1.00 26.56           C  
ANISOU 5390  CG  LYS D  68     3068   3431   3591    819   -438    144       C  
ATOM   5391  CD  LYS D  68     -20.290  -0.680  -8.108  1.00 30.06           C  
ANISOU 5391  CD  LYS D  68     3636   3819   3969    978   -445    271       C  
ATOM   5392  CE  LYS D  68     -20.774  -0.522  -9.525  1.00 33.59           C  
ANISOU 5392  CE  LYS D  68     4052   4438   4272   1147   -520    305       C  
ATOM   5393  NZ  LYS D  68     -21.028   0.916  -9.761  1.00 34.56           N  
ANISOU 5393  NZ  LYS D  68     4335   4461   4337   1300   -520    458       N  
ATOM   5394  N   GLY D  69     -19.795  -3.382  -3.364  1.00 26.41           N  
ANISOU 5394  N   GLY D  69     2984   3117   3932    438   -276    -23       N  
ATOM   5395  CA  GLY D  69     -19.610  -2.983  -1.981  1.00 26.77           C  
ANISOU 5395  CA  GLY D  69     3079   3053   4039    370   -212    -11       C  
ATOM   5396  C   GLY D  69     -18.592  -3.818  -1.228  1.00 23.69           C  
ANISOU 5396  C   GLY D  69     2699   2613   3689    221   -170    -15       C  
ATOM   5397  O   GLY D  69     -18.011  -3.359  -0.228  1.00 25.11           O  
ANISOU 5397  O   GLY D  69     2944   2707   3888    162   -115     13       O  
ATOM   5398  N   GLY D  70     -18.380  -5.050  -1.688  1.00 21.45           N  
ANISOU 5398  N   GLY D  70     2350   2387   3414    170   -200    -61       N  
ATOM   5399  CA  GLY D  70     -17.409  -5.925  -1.051  1.00 21.26           C  
ANISOU 5399  CA  GLY D  70     2341   2316   3421     58   -174    -63       C  
ATOM   5400  C   GLY D  70     -15.948  -5.585  -1.300  1.00 24.46           C  
ANISOU 5400  C   GLY D  70     2832   2691   3771     30   -156     -7       C  
ATOM   5401  O   GLY D  70     -15.078  -6.149  -0.640  1.00 24.67           O  
ANISOU 5401  O   GLY D  70     2874   2689   3813    -43   -134     -9       O  
ATOM   5402  N   TYR D  71     -15.666  -4.664  -2.222  1.00 24.47           N  
ANISOU 5402  N   TYR D  71     2887   2709   3701     86   -163     47       N  
ATOM   5403  CA  TYR D  71     -14.303  -4.546  -2.757  1.00 25.04           C  
ANISOU 5403  CA  TYR D  71     3009   2801   3706     45   -150     87       C  
ATOM   5404  C   TYR D  71     -13.246  -4.106  -1.745  1.00 23.50           C  
ANISOU 5404  C   TYR D  71     2875   2535   3517    -48    -88    114       C  
ATOM   5405  O   TYR D  71     -12.116  -4.589  -1.777  1.00 22.55           O  
ANISOU 5405  O   TYR D  71     2746   2458   3365   -103    -81    100       O  
ATOM   5406  CB  TYR D  71     -14.256  -3.677  -4.038  1.00 24.98           C  
ANISOU 5406  CB  TYR D  71     3048   2837   3604    113   -163    158       C  
ATOM   5407  CG  TYR D  71     -13.756  -2.254  -3.845  1.00 28.06           C  
ANISOU 5407  CG  TYR D  71     3563   3129   3969     86   -103    257       C  
ATOM   5408  CD1 TYR D  71     -12.391  -1.961  -3.856  1.00 26.18           C  
ANISOU 5408  CD1 TYR D  71     3374   2888   3686    -17    -54    294       C  
ATOM   5409  CD2 TYR D  71     -14.649  -1.200  -3.680  1.00 27.90           C  
ANISOU 5409  CD2 TYR D  71     3610   3021   3972    163    -98    303       C  
ATOM   5410  CE1 TYR D  71     -11.934  -0.667  -3.674  1.00 29.87           C  
ANISOU 5410  CE1 TYR D  71     3957   3248   4143    -70      7    375       C  
ATOM   5411  CE2 TYR D  71     -14.197   0.108  -3.503  1.00 29.51           C  
ANISOU 5411  CE2 TYR D  71     3946   3096   4169    135    -45    388       C  
ATOM   5412  CZ  TYR D  71     -12.839   0.360  -3.503  1.00 31.44           C  
ANISOU 5412  CZ  TYR D  71     4241   3324   4379      4     11    425       C  
ATOM   5413  OH  TYR D  71     -12.378   1.644  -3.348  1.00 31.95           O  
ANISOU 5413  OH  TYR D  71     4441   3251   4449    -52     70    501       O  
ATOM   5414  N   LYS D  72     -13.592  -3.186  -0.859  1.00 20.37           N  
ANISOU 5414  N   LYS D  72     2533   2050   3159    -57    -46    136       N  
ATOM   5415  CA  LYS D  72     -12.610  -2.690   0.103  1.00 24.33           C  
ANISOU 5415  CA  LYS D  72     3082   2499   3661   -147     11    141       C  
ATOM   5416  C   LYS D  72     -12.324  -3.732   1.161  1.00 24.05           C  
ANISOU 5416  C   LYS D  72     2988   2492   3656   -193     13     88       C  
ATOM   5417  O   LYS D  72     -11.169  -3.994   1.492  1.00 21.99           O  
ANISOU 5417  O   LYS D  72     2726   2266   3364   -253     29     74       O  
ATOM   5418  CB  LYS D  72     -13.077  -1.383   0.773  1.00 25.32           C  
ANISOU 5418  CB  LYS D  72     3283   2516   3822   -136     51    158       C  
ATOM   5419  CG  LYS D  72     -12.435  -0.146   0.205  1.00 39.02           C  
ANISOU 5419  CG  LYS D  72     5127   4177   5523   -167     85    224       C  
ATOM   5420  CD  LYS D  72     -10.925  -0.321   0.143  1.00 47.38           C  
ANISOU 5420  CD  LYS D  72     6182   5290   6530   -288    119    222       C  
ATOM   5421  CE  LYS D  72     -10.212   0.681   1.010  1.00 54.18           C  
ANISOU 5421  CE  LYS D  72     7108   6066   7413   -390    182    203       C  
ATOM   5422  NZ  LYS D  72      -8.780   0.299   1.159  1.00 58.24           N  
ANISOU 5422  NZ  LYS D  72     7574   6681   7873   -506    209    167       N  
ATOM   5423  N   PHE D  73     -13.378  -4.313   1.711  1.00 22.24           N  
ANISOU 5423  N   PHE D  73     2710   2257   3481   -163     -1     61       N  
ATOM   5424  CA  PHE D  73     -13.202  -5.347   2.726  1.00 23.13           C  
ANISOU 5424  CA  PHE D  73     2784   2385   3619   -205      5     36       C  
ATOM   5425  C   PHE D  73     -12.406  -6.500   2.123  1.00 25.57           C  
ANISOU 5425  C   PHE D  73     3069   2736   3909   -209    -36     21       C  
ATOM   5426  O   PHE D  73     -11.523  -7.067   2.772  1.00 23.64           O  
ANISOU 5426  O   PHE D  73     2827   2508   3648   -237    -31     15       O  
ATOM   5427  CB  PHE D  73     -14.569  -5.808   3.232  1.00 21.95           C  
ANISOU 5427  CB  PHE D  73     2581   2231   3527   -190      4     19       C  
ATOM   5428  CG  PHE D  73     -14.498  -6.851   4.314  1.00 22.72           C  
ANISOU 5428  CG  PHE D  73     2656   2332   3646   -241     21     21       C  
ATOM   5429  CD1 PHE D  73     -13.674  -6.676   5.429  1.00 19.85           C  
ANISOU 5429  CD1 PHE D  73     2320   1975   3245   -275     58     36       C  
ATOM   5430  CD2 PHE D  73     -15.273  -7.998   4.230  1.00 21.59           C  
ANISOU 5430  CD2 PHE D  73     2463   2184   3554   -258      0     11       C  
ATOM   5431  CE1 PHE D  73     -13.632  -7.633   6.425  1.00 23.04           C  
ANISOU 5431  CE1 PHE D  73     2714   2389   3653   -306     71     60       C  
ATOM   5432  CE2 PHE D  73     -15.233  -8.958   5.222  1.00 23.44           C  
ANISOU 5432  CE2 PHE D  73     2698   2400   3808   -310     22     38       C  
ATOM   5433  CZ  PHE D  73     -14.410  -8.776   6.321  1.00 22.92           C  
ANISOU 5433  CZ  PHE D  73     2669   2346   3691   -324     56     73       C  
ATOM   5434  N   PHE D  74     -12.710  -6.829   0.864  1.00 22.17           N  
ANISOU 5434  N   PHE D  74     2614   2337   3475   -166    -82      5       N  
ATOM   5435  CA  PHE D  74     -12.006  -7.883   0.139  1.00 19.50           C  
ANISOU 5435  CA  PHE D  74     2247   2046   3116   -152   -129    -34       C  
ATOM   5436  C   PHE D  74     -10.516  -7.565   0.011  1.00 22.99           C  
ANISOU 5436  C   PHE D  74     2710   2546   3480   -173   -114    -28       C  
ATOM   5437  O   PHE D  74      -9.673  -8.412   0.323  1.00 23.18           O  
ANISOU 5437  O   PHE D  74     2719   2597   3493   -171   -132    -61       O  
ATOM   5438  CB  PHE D  74     -12.666  -8.101  -1.247  1.00 17.41           C  
ANISOU 5438  CB  PHE D  74     1939   1831   2844    -95   -181    -67       C  
ATOM   5439  CG  PHE D  74     -11.968  -9.128  -2.134  1.00 24.03           C  
ANISOU 5439  CG  PHE D  74     2740   2734   3656    -66   -236   -132       C  
ATOM   5440  CD1 PHE D  74     -12.249 -10.490  -2.019  1.00 23.02           C  
ANISOU 5440  CD1 PHE D  74     2580   2563   3601    -62   -279   -200       C  
ATOM   5441  CD2 PHE D  74     -11.083  -8.713  -3.127  1.00 24.09           C  
ANISOU 5441  CD2 PHE D  74     2745   2844   3565    -43   -243   -130       C  
ATOM   5442  CE1 PHE D  74     -11.637 -11.429  -2.866  1.00 25.49           C  
ANISOU 5442  CE1 PHE D  74     2861   2926   3897    -18   -338   -283       C  
ATOM   5443  CE2 PHE D  74     -10.459  -9.638  -3.971  1.00 27.71           C  
ANISOU 5443  CE2 PHE D  74     3154   3387   3987     -2   -296   -210       C  
ATOM   5444  CZ  PHE D  74     -10.742 -10.998  -3.847  1.00 24.66           C  
ANISOU 5444  CZ  PHE D  74     2737   2949   3682     21   -349   -296       C  
ATOM   5445  N   ALA D  75     -10.180  -6.360  -0.447  1.00 22.51           N  
ANISOU 5445  N   ALA D  75     2683   2507   3363   -194    -80     11       N  
ATOM   5446  CA  ALA D  75      -8.770  -6.031  -0.684  1.00 23.42           C  
ANISOU 5446  CA  ALA D  75     2800   2701   3396   -240    -57      8       C  
ATOM   5447  C   ALA D  75      -8.007  -6.102   0.626  1.00 24.57           C  
ANISOU 5447  C   ALA D  75     2946   2845   3546   -288    -27    -14       C  
ATOM   5448  O   ALA D  75      -6.885  -6.610   0.682  1.00 20.32           O  
ANISOU 5448  O   ALA D  75     2368   2398   2953   -293    -38    -57       O  
ATOM   5449  CB  ALA D  75      -8.619  -4.650  -1.288  1.00 21.64           C  
ANISOU 5449  CB  ALA D  75     2631   2470   3123   -282    -10     71       C  
ATOM   5450  N   ASP D  76      -8.613  -5.571   1.680  1.00 21.08           N  
ANISOU 5450  N   ASP D  76     2538   2320   3153   -311      7      6       N  
ATOM   5451  CA  ASP D  76      -7.938  -5.477   2.977  1.00 21.72           C  
ANISOU 5451  CA  ASP D  76     2614   2420   3219   -354     38    -18       C  
ATOM   5452  C   ASP D  76      -7.814  -6.824   3.671  1.00 20.66           C  
ANISOU 5452  C   ASP D  76     2448   2309   3095   -306      0    -36       C  
ATOM   5453  O   ASP D  76      -6.752  -7.157   4.207  1.00 21.49           O  
ANISOU 5453  O   ASP D  76     2527   2493   3144   -305     -4    -68       O  
ATOM   5454  CB  ASP D  76      -8.667  -4.476   3.883  1.00 24.64           C  
ANISOU 5454  CB  ASP D  76     3025   2708   3631   -383     85     -5       C  
ATOM   5455  CG  ASP D  76      -8.477  -3.048   3.439  1.00 28.69           C  
ANISOU 5455  CG  ASP D  76     3594   3173   4134   -439    128      9       C  
ATOM   5456  OD1 ASP D  76      -7.526  -2.779   2.676  1.00 31.13           O  
ANISOU 5456  OD1 ASP D  76     3905   3535   4389   -488    139     12       O  
ATOM   5457  OD2 ASP D  76      -9.279  -2.191   3.856  1.00 28.14           O  
ANISOU 5457  OD2 ASP D  76     3570   3011   4110   -433    153     17       O  
ATOM   5458  N   LEU D  77      -8.902  -7.588   3.676  1.00 21.63           N  
ANISOU 5458  N   LEU D  77     2572   2361   3283   -266    -26    -16       N  
ATOM   5459  CA  LEU D  77      -8.887  -8.931   4.252  1.00 22.05           C  
ANISOU 5459  CA  LEU D  77     2620   2397   3360   -228    -59    -13       C  
ATOM   5460  C   LEU D  77      -7.838  -9.778   3.551  1.00 21.20           C  
ANISOU 5460  C   LEU D  77     2493   2349   3215   -175   -113    -57       C  
ATOM   5461  O   LEU D  77      -7.054 -10.481   4.205  1.00 22.69           O  
ANISOU 5461  O   LEU D  77     2681   2569   3370   -133   -134    -65       O  
ATOM   5462  CB  LEU D  77     -10.260  -9.608   4.125  1.00 22.36           C  
ANISOU 5462  CB  LEU D  77     2660   2348   3488   -223    -73      7       C  
ATOM   5463  CG  LEU D  77     -10.371 -11.018   4.729  1.00 25.38           C  
ANISOU 5463  CG  LEU D  77     3061   2671   3912   -205    -98     29       C  
ATOM   5464  CD1 LEU D  77     -10.102 -11.008   6.237  1.00 25.94           C  
ANISOU 5464  CD1 LEU D  77     3156   2757   3944   -218    -58     82       C  
ATOM   5465  CD2 LEU D  77     -11.744 -11.625   4.440  1.00 25.00           C  
ANISOU 5465  CD2 LEU D  77     3001   2541   3958   -234   -104     32       C  
ATOM   5466  N   LEU D  78      -7.804  -9.721   2.222  1.00 21.07           N  
ANISOU 5466  N   LEU D  78     2453   2364   3189   -159   -140    -90       N  
ATOM   5467  CA  LEU D  78      -6.783 -10.479   1.499  1.00 21.47           C  
ANISOU 5467  CA  LEU D  78     2468   2498   3190    -99   -192   -153       C  
ATOM   5468  C   LEU D  78      -5.361 -10.008   1.804  1.00 22.48           C  
ANISOU 5468  C   LEU D  78     2564   2761   3217   -112   -172   -183       C  
ATOM   5469  O   LEU D  78      -4.432 -10.831   1.880  1.00 24.30           O  
ANISOU 5469  O   LEU D  78     2764   3064   3406    -40   -216   -236       O  
ATOM   5470  CB  LEU D  78      -7.034 -10.503  -0.020  1.00 20.48           C  
ANISOU 5470  CB  LEU D  78     2312   2415   3055    -76   -224   -192       C  
ATOM   5471  CG  LEU D  78      -7.721 -11.758  -0.530  1.00 28.25           C  
ANISOU 5471  CG  LEU D  78     3289   3328   4116    -16   -289   -240       C  
ATOM   5472  CD1 LEU D  78      -9.067 -11.911   0.163  1.00 24.85           C  
ANISOU 5472  CD1 LEU D  78     2894   2761   3788    -56   -271   -191       C  
ATOM   5473  CD2 LEU D  78      -7.886 -11.702  -2.050  1.00 31.23           C  
ANISOU 5473  CD2 LEU D  78     3618   3791   4457     15   -323   -296       C  
ATOM   5474  N   ASP D  79      -5.171  -8.705   1.989  1.00 20.89           N  
ANISOU 5474  N   ASP D  79     2366   2594   2979   -201   -108   -159       N  
ATOM   5475  CA  ASP D  79      -3.834  -8.204   2.307  1.00 18.87           C  
ANISOU 5475  CA  ASP D  79     2063   2477   2629   -243    -81   -204       C  
ATOM   5476  C   ASP D  79      -3.372  -8.723   3.663  1.00 23.17           C  
ANISOU 5476  C   ASP D  79     2600   3048   3157   -201    -94   -221       C  
ATOM   5477  O   ASP D  79      -2.203  -9.039   3.851  1.00 19.72           O  
ANISOU 5477  O   ASP D  79     2102   2752   2638   -164   -115   -284       O  
ATOM   5478  CB  ASP D  79      -3.797  -6.674   2.293  1.00 24.95           C  
ANISOU 5478  CB  ASP D  79     2855   3242   3383   -367     -4   -179       C  
ATOM   5479  CG  ASP D  79      -3.603  -6.107   0.892  1.00 31.78           C  
ANISOU 5479  CG  ASP D  79     3714   4157   4205   -411     14   -164       C  
ATOM   5480  OD1 ASP D  79      -3.402  -6.905  -0.050  1.00 32.71           O  
ANISOU 5480  OD1 ASP D  79     3789   4351   4290   -343    -34   -194       O  
ATOM   5481  OD2 ASP D  79      -3.636  -4.862   0.742  1.00 29.00           O  
ANISOU 5481  OD2 ASP D  79     3405   3767   3849   -513     77   -124       O  
ATOM   5482  N   TYR D  80      -4.288  -8.803   4.621  1.00 21.37           N  
ANISOU 5482  N   TYR D  80     2423   2706   2991   -199    -81   -164       N  
ATOM   5483  CA  TYR D  80      -3.923  -9.353   5.922  1.00 20.85           C  
ANISOU 5483  CA  TYR D  80     2357   2673   2892   -148    -93   -160       C  
ATOM   5484  C   TYR D  80      -3.627 -10.847   5.809  1.00 21.72           C  
ANISOU 5484  C   TYR D  80     2477   2771   3005    -21   -168   -161       C  
ATOM   5485  O   TYR D  80      -2.703 -11.362   6.447  1.00 21.96           O  
ANISOU 5485  O   TYR D  80     2484   2898   2962     59   -201   -187       O  
ATOM   5486  CB  TYR D  80      -5.030  -9.099   6.953  1.00 20.81           C  
ANISOU 5486  CB  TYR D  80     2401   2567   2940   -181    -54    -93       C  
ATOM   5487  CG  TYR D  80      -4.985  -7.722   7.572  1.00 22.03           C  
ANISOU 5487  CG  TYR D  80     2543   2760   3069   -272     11   -119       C  
ATOM   5488  CD1 TYR D  80      -3.936  -7.358   8.410  1.00 23.60           C  
ANISOU 5488  CD1 TYR D  80     2693   3098   3178   -286     23   -180       C  
ATOM   5489  CD2 TYR D  80      -5.983  -6.778   7.315  1.00 24.51           C  
ANISOU 5489  CD2 TYR D  80     2890   2974   3449   -337     54    -98       C  
ATOM   5490  CE1 TYR D  80      -3.877  -6.092   8.988  1.00 28.03           C  
ANISOU 5490  CE1 TYR D  80     3241   3683   3725   -379     81   -228       C  
ATOM   5491  CE2 TYR D  80      -5.934  -5.507   7.898  1.00 23.76           C  
ANISOU 5491  CE2 TYR D  80     2797   2888   3342   -412    108   -136       C  
ATOM   5492  CZ  TYR D  80      -4.876  -5.177   8.729  1.00 26.33           C  
ANISOU 5492  CZ  TYR D  80     3077   3339   3589   -441    123   -206       C  
ATOM   5493  OH  TYR D  80      -4.814  -3.929   9.317  1.00 26.92           O  
ANISOU 5493  OH  TYR D  80     3153   3414   3663   -524    176   -266       O  
ATOM   5494  N   ILE D  81      -4.402 -11.553   4.999  1.00 20.69           N  
ANISOU 5494  N   ILE D  81     2382   2523   2958      7   -201   -143       N  
ATOM   5495  CA  ILE D  81      -4.125 -12.983   4.762  1.00 22.17           C  
ANISOU 5495  CA  ILE D  81     2591   2665   3167    127   -278   -162       C  
ATOM   5496  C   ILE D  81      -2.769 -13.180   4.070  1.00 21.27           C  
ANISOU 5496  C   ILE D  81     2404   2715   2962    206   -325   -265       C  
ATOM   5497  O   ILE D  81      -1.988 -14.055   4.460  1.00 25.44           O  
ANISOU 5497  O   ILE D  81     2933   3283   3449    329   -381   -293       O  
ATOM   5498  CB  ILE D  81      -5.258 -13.646   3.942  1.00 27.76           C  
ANISOU 5498  CB  ILE D  81     3338   3217   3990    121   -303   -152       C  
ATOM   5499  CG1 ILE D  81      -6.503 -13.822   4.813  1.00 28.68           C  
ANISOU 5499  CG1 ILE D  81     3519   3188   4191     62   -265    -56       C  
ATOM   5500  CG2 ILE D  81      -4.813 -14.998   3.383  1.00 27.65           C  
ANISOU 5500  CG2 ILE D  81     3341   3161   4004    243   -387   -212       C  
ATOM   5501  CD1 ILE D  81      -7.772 -14.101   4.008  1.00 31.99           C  
ANISOU 5501  CD1 ILE D  81     3946   3492   4719     14   -270    -62       C  
ATOM   5502  N   LYS D  82      -2.466 -12.364   3.056  1.00 22.80           N  
ANISOU 5502  N   LYS D  82     2533   3016   3113    141   -300   -319       N  
ATOM   5503  CA  LYS D  82      -1.141 -12.427   2.410  1.00 24.62           C  
ANISOU 5503  CA  LYS D  82     2670   3447   3237    193   -328   -423       C  
ATOM   5504  C   LYS D  82       0.002 -12.171   3.392  1.00 24.59           C  
ANISOU 5504  C   LYS D  82     2609   3605   3130    211   -320   -460       C  
ATOM   5505  O   LYS D  82       1.055 -12.823   3.341  1.00 26.43           O  
ANISOU 5505  O   LYS D  82     2778   3980   3284    330   -377   -545       O  
ATOM   5506  CB  LYS D  82      -1.057 -11.441   1.243  1.00 26.32           C  
ANISOU 5506  CB  LYS D  82     2832   3759   3411     88   -282   -446       C  
ATOM   5507  CG  LYS D  82      -1.746 -11.968  -0.023  1.00 31.15           C  
ANISOU 5507  CG  LYS D  82     3453   4310   4072    128   -321   -464       C  
ATOM   5508  CD  LYS D  82      -2.476 -10.862  -0.771  1.00 35.22           C  
ANISOU 5508  CD  LYS D  82     3984   4804   4595     12   -261   -404       C  
ATOM   5509  CE  LYS D  82      -1.525  -9.769  -1.194  1.00 36.77           C  
ANISOU 5509  CE  LYS D  82     4119   5176   4677    -86   -199   -415       C  
ATOM   5510  NZ  LYS D  82      -2.260  -8.673  -1.894  1.00 38.77           N  
ANISOU 5510  NZ  LYS D  82     4415   5377   4937   -186   -141   -332       N  
ATOM   5511  N   ALA D  83      -0.207 -11.219   4.296  1.00 20.74           N  
ANISOU 5511  N   ALA D  83     2135   3109   2636    105   -254   -412       N  
ATOM   5512  CA  ALA D  83       0.804 -10.917   5.301  1.00 23.17           C  
ANISOU 5512  CA  ALA D  83     2378   3583   2843    112   -245   -461       C  
ATOM   5513  C   ALA D  83       1.081 -12.147   6.180  1.00 28.87           C  
ANISOU 5513  C   ALA D  83     3129   4299   3541    290   -320   -446       C  
ATOM   5514  O   ALA D  83       2.237 -12.435   6.522  1.00 28.51           O  
ANISOU 5514  O   ALA D  83     3003   4444   3386    387   -361   -526       O  
ATOM   5515  CB  ALA D  83       0.381  -9.719   6.146  1.00 26.31           C  
ANISOU 5515  CB  ALA D  83     2794   3949   3253    -29   -165   -423       C  
ATOM   5516  N   LEU D  84       0.024 -12.867   6.548  1.00 25.21           N  
ANISOU 5516  N   LEU D  84     2780   3623   3175    334   -337   -341       N  
ATOM   5517  CA  LEU D  84       0.195 -14.097   7.326  1.00 26.22           C  
ANISOU 5517  CA  LEU D  84     2970   3701   3292    501   -405   -296       C  
ATOM   5518  C   LEU D  84       0.973 -15.121   6.505  1.00 29.72           C  
ANISOU 5518  C   LEU D  84     3390   4187   3716    661   -495   -381       C  
ATOM   5519  O   LEU D  84       1.880 -15.805   7.009  1.00 31.14           O  
ANISOU 5519  O   LEU D  84     3553   4466   3812    828   -561   -414       O  
ATOM   5520  CB  LEU D  84      -1.174 -14.676   7.716  1.00 26.80           C  
ANISOU 5520  CB  LEU D  84     3174   3520   3487    480   -392   -162       C  
ATOM   5521  CG  LEU D  84      -1.979 -13.900   8.752  1.00 28.61           C  
ANISOU 5521  CG  LEU D  84     3430   3718   3723    364   -314    -75       C  
ATOM   5522  CD1 LEU D  84      -3.326 -14.539   8.978  1.00 28.11           C  
ANISOU 5522  CD1 LEU D  84     3474   3430   3776    332   -297     44       C  
ATOM   5523  CD2 LEU D  84      -1.217 -13.875  10.046  1.00 27.53           C  
ANISOU 5523  CD2 LEU D  84     3269   3730   3460    438   -320    -63       C  
ATOM   5524  N   ASN D  85       0.628 -15.219   5.228  1.00 28.34           N  
ANISOU 5524  N   ASN D  85     3207   3951   3608    627   -503   -427       N  
ATOM   5525  CA  ASN D  85       1.197 -16.257   4.372  1.00 28.75           C  
ANISOU 5525  CA  ASN D  85     3243   4021   3658    784   -592   -522       C  
ATOM   5526  C   ASN D  85       2.661 -16.064   4.002  1.00 34.25           C  
ANISOU 5526  C   ASN D  85     3793   5012   4209    861   -621   -666       C  
ATOM   5527  O   ASN D  85       3.335 -17.024   3.623  1.00 39.83           O  
ANISOU 5527  O   ASN D  85     4477   5768   4886   1044   -709   -757       O  
ATOM   5528  CB  ASN D  85       0.365 -16.397   3.089  1.00 29.97           C  
ANISOU 5528  CB  ASN D  85     3416   4055   3915    725   -592   -547       C  
ATOM   5529  CG  ASN D  85      -0.732 -17.443   3.203  1.00 43.89           C  
ANISOU 5529  CG  ASN D  85     5316   5532   5828    759   -626   -474       C  
ATOM   5530  OD1 ASN D  85      -0.533 -18.609   2.867  1.00 52.33           O  
ANISOU 5530  OD1 ASN D  85     6430   6512   6942    902   -709   -530       O  
ATOM   5531  ND2 ASN D  85      -1.902 -17.027   3.658  1.00 45.79           N  
ANISOU 5531  ND2 ASN D  85     5620   5628   6149    622   -561   -361       N  
ATOM   5532  N   ARG D  86       3.156 -14.831   4.060  1.00 30.35           N  
ANISOU 5532  N   ARG D  86     3201   4183   4147    102    -70    -31       N  
ATOM   5533  CA  ARG D  86       4.558 -14.601   3.724  1.00 31.74           C  
ANISOU 5533  CA  ARG D  86     3200   4523   4337    181    -81   -222       C  
ATOM   5534  C   ARG D  86       5.406 -14.481   4.981  1.00 33.93           C  
ANISOU 5534  C   ARG D  86     3440   4894   4557    154   -207    -90       C  
ATOM   5535  O   ARG D  86       6.599 -14.194   4.914  1.00 35.90           O  
ANISOU 5535  O   ARG D  86     3522   5334   4784    191   -222   -228       O  
ATOM   5536  CB  ARG D  86       4.735 -13.377   2.812  1.00 31.92           C  
ANISOU 5536  CB  ARG D  86     3208   4759   4161     59    133   -386       C  
ATOM   5537  CG  ARG D  86       4.333 -12.059   3.451  1.00 32.58           C  
ANISOU 5537  CG  ARG D  86     3453   4915   4011   -121    237   -262       C  
ATOM   5538  CD  ARG D  86       4.654 -10.858   2.565  1.00 30.91           C  
ANISOU 5538  CD  ARG D  86     3270   4853   3621   -277    355   -383       C  
ATOM   5539  NE  ARG D  86       4.185  -9.641   3.209  1.00 31.24           N  
ANISOU 5539  NE  ARG D  86     3496   4868   3505   -405    395   -289       N  
ATOM   5540  CZ  ARG D  86       3.017  -9.067   2.952  1.00 31.82           C  
ANISOU 5540  CZ  ARG D  86     3723   4798   3570   -423    431   -259       C  
ATOM   5541  NH1 ARG D  86       2.221  -9.589   2.030  1.00 28.63           N  
ANISOU 5541  NH1 ARG D  86     3316   4292   3271   -362    443   -277       N  
ATOM   5542  NH2 ARG D  86       2.656  -7.972   3.613  1.00 27.98           N  
ANISOU 5542  NH2 ARG D  86     3377   4271   2982   -489    436   -241       N  
ATOM   5543  N   ASN D  87       4.791 -14.716   6.134  1.00 31.18           N  
ANISOU 5543  N   ASN D  87     3231   4460   4158     52   -303    176       N  
ATOM   5544  CA  ASN D  87       5.536 -14.654   7.384  1.00 37.60           C  
ANISOU 5544  CA  ASN D  87     4024   5377   4887    -21   -448    336       C  
ATOM   5545  C   ASN D  87       5.401 -15.923   8.221  1.00 39.65           C  
ANISOU 5545  C   ASN D  87     4345   5423   5299    -18   -770    599       C  
ATOM   5546  O   ASN D  87       5.863 -15.978   9.351  1.00 41.51           O  
ANISOU 5546  O   ASN D  87     4596   5733   5443   -131   -938    800       O  
ATOM   5547  CB  ASN D  87       5.151 -13.403   8.173  1.00 35.80           C  
ANISOU 5547  CB  ASN D  87     3905   5356   4341   -250   -263    401       C  
ATOM   5548  CG  ASN D  87       5.721 -12.133   7.550  1.00 36.62           C  
ANISOU 5548  CG  ASN D  87     3968   5635   4310   -280    -70    187       C  
ATOM   5549  OD1 ASN D  87       6.938 -11.948   7.517  1.00 36.66           O  
ANISOU 5549  OD1 ASN D  87     3836   5789   4303   -262   -119    104       O  
ATOM   5550  ND2 ASN D  87       4.847 -11.263   7.044  1.00 32.10           N  
ANISOU 5550  ND2 ASN D  87     3512   5045   3640   -344    115    105       N  
ATOM   5551  N   SER D  88       4.780 -16.945   7.637  1.00 41.42           N  
ANISOU 5551  N   SER D  88     4621   5371   5747     81   -887    610       N  
ATOM   5552  CA  SER D  88       4.671 -18.253   8.279  1.00 45.64           C  
ANISOU 5552  CA  SER D  88     5254   5616   6470     69  -1269    873       C  
ATOM   5553  C   SER D  88       5.500 -19.308   7.541  1.00 46.45           C  
ANISOU 5553  C   SER D  88     5228   5432   6990    412  -1550    681       C  
ATOM   5554  O   SER D  88       5.862 -19.125   6.375  1.00 44.23           O  
ANISOU 5554  O   SER D  88     4776   5209   6818    622  -1380    316       O  
ATOM   5555  CB  SER D  88       3.213 -18.694   8.344  1.00 48.32           C  
ANISOU 5555  CB  SER D  88     5787   5837   6736   -140  -1245   1063       C  
ATOM   5556  OG  SER D  88       2.706 -18.940   7.045  1.00 55.38           O  
ANISOU 5556  OG  SER D  88     6660   6588   7793     15  -1121    834       O  
ATOM   5557  N   ASP D  89       5.787 -20.409   8.231  1.00 43.69           N  
ANISOU 5557  N   ASP D  89     4955   4778   6866    450  -2003    914       N  
ATOM   5558  CA  ASP D  89       6.631 -21.483   7.700  1.00 54.49           C  
ANISOU 5558  CA  ASP D  89     6192   5814   8698    828  -2364    707       C  
ATOM   5559  C   ASP D  89       6.064 -22.117   6.431  1.00 60.49           C  
ANISOU 5559  C   ASP D  89     6959   6331   9694   1003  -2308    429       C  
ATOM   5560  O   ASP D  89       6.791 -22.355   5.461  1.00 63.81           O  
ANISOU 5560  O   ASP D  89     7137   6741  10368   1338  -2300     -9       O  
ATOM   5561  CB  ASP D  89       6.832 -22.570   8.759  1.00 55.60           C  
ANISOU 5561  CB  ASP D  89     6499   5578   9047    788  -2948   1092       C  
ATOM   5562  CG  ASP D  89       7.609 -22.073   9.964  1.00 62.50           C  
ANISOU 5562  CG  ASP D  89     7325   6693   9730    650  -3074   1335       C  
ATOM   5563  OD1 ASP D  89       8.220 -20.985   9.868  1.00 56.57           O  
ANISOU 5563  OD1 ASP D  89     6365   6361   8769    677  -2740   1122       O  
ATOM   5564  OD2 ASP D  89       7.612 -22.772  11.002  1.00 69.34           O  
ANISOU 5564  OD2 ASP D  89     8389   7353  10607    455  -3455   1715       O  
ATOM   5565  N   ARG D  90       4.769 -22.408   6.452  1.00 57.51           N  
ANISOU 5565  N   ARG D  90     6837   5804   9212    752  -2271    660       N  
ATOM   5566  CA  ARG D  90       4.112 -22.997   5.295  1.00 59.88           C  
ANISOU 5566  CA  ARG D  90     7173   5884   9695    858  -2216    432       C  
ATOM   5567  C   ARG D  90       2.884 -22.169   4.938  1.00 56.45           C  
ANISOU 5567  C   ARG D  90     6823   5718   8906    580  -1782    483       C  
ATOM   5568  O   ARG D  90       2.293 -21.510   5.796  1.00 61.18           O  
ANISOU 5568  O   ARG D  90     7523   6542   9179    281  -1642    768       O  
ATOM   5569  CB  ARG D  90       3.748 -24.462   5.556  1.00 66.96           C  
ANISOU 5569  CB  ARG D  90     8303   6222  10916    858  -2726    648       C  
ATOM   5570  CG  ARG D  90       4.911 -25.297   6.098  1.00 77.46           C  
ANISOU 5570  CG  ARG D  90     9587   7304  12539   1067  -3161    622       C  
ATOM   5571  CD  ARG D  90       5.274 -26.457   5.175  1.00 86.08           C  
ANISOU 5571  CD  ARG D  90    10630   8086  13991   1341  -3334    213       C  
ATOM   5572  NE  ARG D  90       5.806 -26.008   3.890  1.00 85.92           N  
ANISOU 5572  NE  ARG D  90    10292   8318  14033   1648  -3005   -355       N  
ATOM   5573  CZ  ARG D  90       5.968 -26.796   2.828  1.00 87.87           C  
ANISOU 5573  CZ  ARG D  90    10453   8434  14499   1847  -3031   -783       C  
ATOM   5574  NH1 ARG D  90       5.635 -28.078   2.889  1.00 87.51           N  
ANISOU 5574  NH1 ARG D  90    10615   7953  14683   1821  -3402   -712       N  
ATOM   5575  NH2 ARG D  90       6.456 -26.297   1.700  1.00 88.89           N  
ANISOU 5575  NH2 ARG D  90    10283   8909  14581   2025  -2693  -1280       N  
ATOM   5576  N   SER D  91       2.515 -22.190   3.665  1.00 48.42           N  
ANISOU 5576  N   SER D  91     5743   4701   7955    686  -1579    175       N  
ATOM   5577  CA  SER D  91       1.455 -21.329   3.165  1.00 41.06           C  
ANISOU 5577  CA  SER D  91     4848   4027   6727    482  -1193    174       C  
ATOM   5578  C   SER D  91       0.696 -22.067   2.071  1.00 42.71           C  
ANISOU 5578  C   SER D  91     5115   4026   7088    511  -1198     19       C  
ATOM   5579  O   SER D  91       1.159 -23.104   1.593  1.00 43.99           O  
ANISOU 5579  O   SER D  91     5253   3879   7580    727  -1452   -177       O  
ATOM   5580  CB  SER D  91       2.065 -20.055   2.591  1.00 36.60           C  
ANISOU 5580  CB  SER D  91     4089   3842   5975    546   -856    -88       C  
ATOM   5581  OG  SER D  91       2.927 -20.366   1.517  1.00 46.05           O  
ANISOU 5581  OG  SER D  91     5085   5044   7367    792   -856   -490       O  
ATOM   5582  N   ILE D  92      -0.457 -21.530   1.670  1.00 35.41           N  
ANISOU 5582  N   ILE D  92     4250   3267   5938    311   -938     77       N  
ATOM   5583  CA  ILE D  92      -1.248 -22.132   0.590  1.00 34.46           C  
ANISOU 5583  CA  ILE D  92     4178   3003   5914    296   -917    -63       C  
ATOM   5584  C   ILE D  92      -1.545 -21.127  -0.518  1.00 28.93           C  
ANISOU 5584  C   ILE D  92     3361   2610   5021    279   -566   -286       C  
ATOM   5585  O   ILE D  92      -1.692 -19.936  -0.259  1.00 27.75           O  
ANISOU 5585  O   ILE D  92     3177   2741   4626    187   -351   -209       O  
ATOM   5586  CB  ILE D  92      -2.588 -22.735   1.093  1.00 54.22           C  
ANISOU 5586  CB  ILE D  92     6887   5367   8348     10  -1030    270       C  
ATOM   5587  CG1 ILE D  92      -3.120 -21.943   2.286  1.00 55.10           C  
ANISOU 5587  CG1 ILE D  92     7028   5759   8148   -237   -914    580       C  
ATOM   5588  CG2 ILE D  92      -2.432 -24.216   1.438  1.00 58.19           C  
ANISOU 5588  CG2 ILE D  92     7562   5396   9151     21  -1475    394       C  
ATOM   5589  CD1 ILE D  92      -3.874 -20.697   1.908  1.00 53.85           C  
ANISOU 5589  CD1 ILE D  92     6769   5962   7728   -307   -551    501       C  
ATOM   5590  N   PRO D  93      -1.629 -21.607  -1.767  1.00 34.49           N  
ANISOU 5590  N   PRO D  93     4018   3249   5838    351   -540   -569       N  
ATOM   5591  CA  PRO D  93      -1.971 -20.644  -2.816  1.00 34.29           C  
ANISOU 5591  CA  PRO D  93     3910   3525   5593    264   -251   -718       C  
ATOM   5592  C   PRO D  93      -3.400 -20.130  -2.668  1.00 28.17           C  
ANISOU 5592  C   PRO D  93     3245   2832   4624     45   -142   -455       C  
ATOM   5593  O   PRO D  93      -4.272 -20.822  -2.133  1.00 28.06           O  
ANISOU 5593  O   PRO D  93     3351   2657   4653    -69   -267   -242       O  
ATOM   5594  CB  PRO D  93      -1.810 -21.451  -4.113  1.00 40.62           C  
ANISOU 5594  CB  PRO D  93     4641   4249   6544    346   -277  -1077       C  
ATOM   5595  CG  PRO D  93      -1.806 -22.898  -3.686  1.00 44.46           C  
ANISOU 5595  CG  PRO D  93     5234   4303   7356    461   -600  -1062       C  
ATOM   5596  CD  PRO D  93      -1.208 -22.909  -2.310  1.00 41.41           C  
ANISOU 5596  CD  PRO D  93     4886   3806   7041    533   -778   -820       C  
ATOM   5597  N   MET D  94      -3.619 -18.904  -3.121  1.00 24.96           N  
ANISOU 5597  N   MET D  94     2791   2689   4006    -25     61   -475       N  
ATOM   5598  CA  MET D  94      -4.943 -18.312  -3.131  1.00 24.76           C  
ANISOU 5598  CA  MET D  94     2814   2761   3832   -171    148   -305       C  
ATOM   5599  C   MET D  94      -5.169 -17.708  -4.507  1.00 29.52           C  
ANISOU 5599  C   MET D  94     3379   3507   4331   -231    255   -452       C  
ATOM   5600  O   MET D  94      -4.288 -17.039  -5.046  1.00 25.66           O  
ANISOU 5600  O   MET D  94     2834   3158   3757   -222    324   -595       O  
ATOM   5601  CB  MET D  94      -5.045 -17.215  -2.064  1.00 26.15           C  
ANISOU 5601  CB  MET D  94     2989   3081   3865   -186    219   -146       C  
ATOM   5602  CG  MET D  94      -6.405 -16.496  -2.037  1.00 30.55           C  
ANISOU 5602  CG  MET D  94     3539   3767   4303   -274    295    -48       C  
ATOM   5603  SD  MET D  94      -6.622 -15.514  -0.540  1.00 42.31           S  
ANISOU 5603  SD  MET D  94     5000   5416   5662   -274    355     61       S  
ATOM   5604  CE  MET D  94      -4.992 -14.769  -0.372  1.00 45.58           C  
ANISOU 5604  CE  MET D  94     5434   5830   6054   -177    371    -26       C  
ATOM   5605  N   THR D  95      -6.330 -17.968  -5.092  1.00 26.31           N  
ANISOU 5605  N   THR D  95     3000   3092   3906   -338    250   -404       N  
ATOM   5606  CA  THR D  95      -6.681 -17.322  -6.349  1.00 26.25           C  
ANISOU 5606  CA  THR D  95     2972   3230   3772   -439    311   -482       C  
ATOM   5607  C   THR D  95      -7.876 -16.430  -6.066  1.00 27.39           C  
ANISOU 5607  C   THR D  95     3123   3451   3833   -481    315   -292       C  
ATOM   5608  O   THR D  95      -8.515 -16.552  -5.010  1.00 24.48           O  
ANISOU 5608  O   THR D  95     2741   3066   3494   -455    304   -158       O  
ATOM   5609  CB  THR D  95      -7.014 -18.326  -7.463  1.00 28.82           C  
ANISOU 5609  CB  THR D  95     3297   3512   4144   -527    280   -634       C  
ATOM   5610  OG1 THR D  95      -7.942 -19.297  -6.968  1.00 32.36           O  
ANISOU 5610  OG1 THR D  95     3798   3794   4703   -561    192   -510       O  
ATOM   5611  CG2 THR D  95      -5.734 -19.033  -7.963  1.00 31.98           C  
ANISOU 5611  CG2 THR D  95     3633   3889   4629   -448    282   -945       C  
ATOM   5612  N   VAL D  96      -8.185 -15.527  -6.993  1.00 28.25           N  
ANISOU 5612  N   VAL D  96     3238   3664   3832   -559    308   -291       N  
ATOM   5613  CA  VAL D  96      -9.289 -14.597  -6.749  1.00 28.36           C  
ANISOU 5613  CA  VAL D  96     3234   3720   3824   -534    259   -157       C  
ATOM   5614  C   VAL D  96     -10.271 -14.543  -7.916  1.00 30.72           C  
ANISOU 5614  C   VAL D  96     3519   4073   4080   -653    180   -126       C  
ATOM   5615  O   VAL D  96      -9.909 -14.810  -9.061  1.00 30.70           O  
ANISOU 5615  O   VAL D  96     3553   4113   3998   -801    171   -201       O  
ATOM   5616  CB  VAL D  96      -8.791 -13.166  -6.423  1.00 32.88           C  
ANISOU 5616  CB  VAL D  96     3854   4294   4344   -466    229   -127       C  
ATOM   5617  CG1 VAL D  96      -7.803 -13.187  -5.287  1.00 33.61           C  
ANISOU 5617  CG1 VAL D  96     3953   4365   4453   -375    304   -156       C  
ATOM   5618  CG2 VAL D  96      -8.162 -12.523  -7.640  1.00 36.44           C  
ANISOU 5618  CG2 VAL D  96     4390   4786   4668   -624    167   -145       C  
ATOM   5619  N   ASP D  97     -11.524 -14.217  -7.607  1.00 26.05           N  
ANISOU 5619  N   ASP D  97     2845   3524   3530   -599    122    -42       N  
ATOM   5620  CA  ASP D  97     -12.507 -13.932  -8.638  1.00 27.97           C  
ANISOU 5620  CA  ASP D  97     3055   3825   3745   -684     -1     12       C  
ATOM   5621  C   ASP D  97     -13.465 -12.867  -8.108  1.00 27.35           C  
ANISOU 5621  C   ASP D  97     2872   3774   3747   -510   -110     55       C  
ATOM   5622  O   ASP D  97     -13.476 -12.554  -6.905  1.00 30.51           O  
ANISOU 5622  O   ASP D  97     3201   4191   4201   -351    -45      9       O  
ATOM   5623  CB  ASP D  97     -13.259 -15.194  -9.068  1.00 31.91           C  
ANISOU 5623  CB  ASP D  97     3498   4383   4244   -825     24      2       C  
ATOM   5624  CG  ASP D  97     -13.837 -15.082 -10.483  1.00 41.10           C  
ANISOU 5624  CG  ASP D  97     4671   5618   5326   -993    -96     36       C  
ATOM   5625  OD1 ASP D  97     -13.579 -14.056 -11.175  1.00 34.19           O  
ANISOU 5625  OD1 ASP D  97     3867   4740   4383  -1030   -218     91       O  
ATOM   5626  OD2 ASP D  97     -14.546 -16.023 -10.902  1.00 44.77           O  
ANISOU 5626  OD2 ASP D  97     5090   6141   5778  -1128    -93     26       O  
ATOM   5627  N   PHE D  98     -14.239 -12.303  -9.021  1.00 25.49           N  
ANISOU 5627  N   PHE D  98     2616   3550   3519   -540   -296    119       N  
ATOM   5628  CA  PHE D  98     -15.162 -11.223  -8.711  1.00 29.60           C  
ANISOU 5628  CA  PHE D  98     3020   4059   4169   -326   -474    115       C  
ATOM   5629  C   PHE D  98     -16.503 -11.521  -9.338  1.00 37.22           C  
ANISOU 5629  C   PHE D  98     3815   5161   5165   -362   -589    148       C  
ATOM   5630  O   PHE D  98     -16.593 -11.829 -10.530  1.00 38.63           O  
ANISOU 5630  O   PHE D  98     4074   5349   5254   -575   -683    248       O  
ATOM   5631  CB  PHE D  98     -14.629  -9.907  -9.271  1.00 26.67           C  
ANISOU 5631  CB  PHE D  98     2837   3483   3815   -308   -714    197       C  
ATOM   5632  CG  PHE D  98     -13.274  -9.555  -8.769  1.00 27.35           C  
ANISOU 5632  CG  PHE D  98     3089   3464   3840   -324   -615    174       C  
ATOM   5633  CD1 PHE D  98     -12.134 -10.090  -9.368  1.00 24.13           C  
ANISOU 5633  CD1 PHE D  98     2818   3094   3255   -572   -499    200       C  
ATOM   5634  CD2 PHE D  98     -13.125  -8.686  -7.689  1.00 26.21           C  
ANISOU 5634  CD2 PHE D  98     2935   3217   3806    -91   -637     85       C  
ATOM   5635  CE1 PHE D  98     -10.880  -9.779  -8.899  1.00 23.16           C  
ANISOU 5635  CE1 PHE D  98     2804   2926   3068   -591   -410    165       C  
ATOM   5636  CE2 PHE D  98     -11.876  -8.376  -7.211  1.00 26.08           C  
ANISOU 5636  CE2 PHE D  98     3066   3126   3718   -131   -550     71       C  
ATOM   5637  CZ  PHE D  98     -10.745  -8.920  -7.812  1.00 25.31           C  
ANISOU 5637  CZ  PHE D  98     3090   3083   3443   -383   -439    124       C  
ATOM   5638  N   ILE D  99     -17.554 -11.430  -8.540  1.00 28.85           N  
ANISOU 5638  N   ILE D  99     2494   4262   4207   -178   -579     43       N  
ATOM   5639  CA  ILE D  99     -18.893 -11.597  -9.070  1.00 36.44           C  
ANISOU 5639  CA  ILE D  99     3237   5402   5209   -188   -708     51       C  
ATOM   5640  C   ILE D  99     -19.784 -10.452  -8.624  1.00 33.66           C  
ANISOU 5640  C   ILE D  99     2645   5084   5059    154   -907    -92       C  
ATOM   5641  O   ILE D  99     -19.476  -9.734  -7.674  1.00 33.85           O  
ANISOU 5641  O   ILE D  99     2639   5045   5176    385   -877   -242       O  
ATOM   5642  CB  ILE D  99     -19.504 -12.926  -8.630  1.00 44.10           C  
ANISOU 5642  CB  ILE D  99     4035   6647   6073   -366   -491     19       C  
ATOM   5643  CG1 ILE D  99     -19.623 -12.970  -7.109  1.00 44.05           C  
ANISOU 5643  CG1 ILE D  99     3848   6825   6065   -250   -302   -129       C  
ATOM   5644  CG2 ILE D  99     -18.669 -14.100  -9.157  1.00 39.89           C  
ANISOU 5644  CG2 ILE D  99     3745   6011   5401   -661   -360    117       C  
ATOM   5645  CD1 ILE D  99     -20.203 -14.255  -6.593  1.00 49.69           C  
ANISOU 5645  CD1 ILE D  99     4427   7817   6637   -506   -128   -111       C  
ATOM   5646  N   ARG D 100     -20.883 -10.265  -9.330  1.00 36.14           N  
ANISOU 5646  N   ARG D 100     2781   5495   5458    198  -1135    -72       N  
ATOM   5647  CA  ARG D 100     -21.874  -9.316  -8.885  1.00 45.80           C  
ANISOU 5647  CA  ARG D 100     3693   6793   6915    569  -1339   -279       C  
ATOM   5648  C   ARG D 100     -23.196 -10.044  -8.950  1.00 47.27           C  
ANISOU 5648  C   ARG D 100     3502   7396   7064    505  -1290   -354       C  
ATOM   5649  O   ARG D 100     -23.383 -10.907  -9.805  1.00 47.52           O  
ANISOU 5649  O   ARG D 100     3604   7506   6946    194  -1273   -167       O  
ATOM   5650  CB  ARG D 100     -21.874  -8.070  -9.766  1.00 52.77           C  
ANISOU 5650  CB  ARG D 100     4738   7310   8002    741  -1802   -169       C  
ATOM   5651  CG  ARG D 100     -22.826  -6.989  -9.290  1.00 64.62           C  
ANISOU 5651  CG  ARG D 100     5928   8796   9830   1211  -2086   -438       C  
ATOM   5652  CD  ARG D 100     -22.336  -5.614  -9.687  1.00 70.05           C  
ANISOU 5652  CD  ARG D 100     6907   8964  10745   1408  -2530   -350       C  
ATOM   5653  NE  ARG D 100     -23.361  -4.606  -9.451  1.00 78.10           N  
ANISOU 5653  NE  ARG D 100     7733   9904  12038   1806  -2771   -588       N  
ATOM   5654  CZ  ARG D 100     -23.496  -3.500 -10.172  1.00 84.43           C  
ANISOU 5654  CZ  ARG D 100     8782  10278  13017   1902  -3206   -460       C  
ATOM   5655  NH1 ARG D 100     -22.662  -3.255 -11.175  1.00 84.71           N  
ANISOU 5655  NH1 ARG D 100     9246   9972  12970   1606  -3472    -76       N  
ATOM   5656  NH2 ARG D 100     -24.465  -2.638  -9.893  1.00 89.73           N  
ANISOU 5656  NH2 ARG D 100     9279  10882  13931   2248  -3377   -721       N  
ATOM   5657  N   LEU D 101     -24.087  -9.734  -8.017  1.00 44.13           N  
ANISOU 5657  N   LEU D 101     2685   7308   6774    769  -1248   -659       N  
ATOM   5658  CA  LEU D 101     -25.410 -10.335  -8.011  1.00 52.93           C  
ANISOU 5658  CA  LEU D 101     3371   8904   7837    700  -1206   -769       C  
ATOM   5659  C   LEU D 101     -26.381  -9.270  -8.470  1.00 59.29           C  
ANISOU 5659  C   LEU D 101     4005   9614   8907   1050  -1557   -868       C  
ATOM   5660  O   LEU D 101     -26.382  -8.162  -7.932  1.00 65.40           O  
ANISOU 5660  O   LEU D 101     4787  10188   9874   1407  -1656  -1066       O  
ATOM   5661  CB  LEU D 101     -25.777 -10.847  -6.616  1.00 53.76           C  
ANISOU 5661  CB  LEU D 101     3271   9391   7763    621   -824   -979       C  
ATOM   5662  CG  LEU D 101     -24.991 -12.028  -6.040  1.00 55.75           C  
ANISOU 5662  CG  LEU D 101     3687   9758   7738    229   -499   -845       C  
ATOM   5663  CD1 LEU D 101     -24.249 -12.785  -7.107  1.00 55.95           C  
ANISOU 5663  CD1 LEU D 101     4097   9483   7678    -69   -539   -514       C  
ATOM   5664  CD2 LEU D 101     -24.010 -11.558  -5.018  1.00 54.34           C  
ANISOU 5664  CD2 LEU D 101     3630   9453   7565    365   -359   -960       C  
ATOM   5665  N   LYS D 102     -27.192  -9.591  -9.472  1.00 55.26           N  
ANISOU 5665  N   LYS D 102     3391   9214   8393    922  -1747   -716       N  
ATOM   5666  CA  LYS D 102     -28.083  -8.603 -10.061  1.00 60.79           C  
ANISOU 5666  CA  LYS D 102     3986   9779   9334   1220  -2117   -735       C  
ATOM   5667  C   LYS D 102     -29.533  -8.889  -9.714  1.00 68.07           C  
ANISOU 5667  C   LYS D 102     4488  11137  10238   1255  -2001   -928       C  
ATOM   5668  O   LYS D 102     -29.999 -10.025  -9.809  1.00 61.91           O  
ANISOU 5668  O   LYS D 102     3578  10703   9242    909  -1800   -860       O  
ATOM   5669  CB  LYS D 102     -27.900  -8.557 -11.578  1.00 56.71           C  
ANISOU 5669  CB  LYS D 102     3706   9017   8826   1049  -2502   -385       C  
ATOM   5670  CG  LYS D 102     -28.797  -7.572 -12.314  1.00 68.97           C  
ANISOU 5670  CG  LYS D 102     5207  10412  10585   1304  -2917   -336       C  
ATOM   5671  CD  LYS D 102     -28.330  -7.428 -13.758  1.00 71.06           C  
ANISOU 5671  CD  LYS D 102     5856  10361  10784   1057  -3277     46       C  
ATOM   5672  CE  LYS D 102     -29.348  -6.701 -14.622  1.00 78.94           C  
ANISOU 5672  CE  LYS D 102     6787  11283  11924   1215  -3679    134       C  
ATOM   5673  NZ  LYS D 102     -28.912  -6.663 -16.050  1.00 79.82           N  
ANISOU 5673  NZ  LYS D 102     7308  11128  11892    863  -3976    525       N  
ATOM   5674  N   SER D 103     -30.237  -7.842  -9.308  1.00 56.51           N  
ANISOU 5674  N   SER D 103     6625   7855   6992    282  -2705   -865       N  
ATOM   5675  CA  SER D 103     -31.639  -7.952  -8.946  1.00 66.62           C  
ANISOU 5675  CA  SER D 103     7849   9554   7910    432  -2590   -799       C  
ATOM   5676  C   SER D 103     -32.506  -7.563 -10.134  1.00 71.74           C  
ANISOU 5676  C   SER D 103     8544  10372   8343    414  -2636   -656       C  
ATOM   5677  O   SER D 103     -32.274  -6.539 -10.778  1.00 76.91           O  
ANISOU 5677  O   SER D 103     9313  10795   9116    528  -2834   -656       O  
ATOM   5678  CB  SER D 103     -31.946  -7.053  -7.747  1.00 72.20           C  
ANISOU 5678  CB  SER D 103     8600  10200   8634    841  -2691   -924       C  
ATOM   5679  OG  SER D 103     -32.713  -7.739  -6.775  1.00 75.18           O  
ANISOU 5679  OG  SER D 103     8847  10919   8799    938  -2515   -859       O  
ATOM   5680  N   TYR D 104     -33.492  -8.403 -10.434  1.00 71.72           N  
ANISOU 5680  N   TYR D 104     8469  10699   8081    245  -2507   -488       N  
ATOM   5681  CA  TYR D 104     -34.487  -8.089 -11.447  1.00 73.41           C  
ANISOU 5681  CA  TYR D 104     8731  11080   8080    234  -2553   -335       C  
ATOM   5682  C   TYR D 104     -35.852  -7.981 -10.777  1.00 76.56           C  
ANISOU 5682  C   TYR D 104     9028  11698   8364    403  -2530   -197       C  
ATOM   5683  O   TYR D 104     -36.291  -8.911 -10.092  1.00 74.79           O  
ANISOU 5683  O   TYR D 104     8691  11565   8160    340  -2467   -124       O  
ATOM   5684  CB  TYR D 104     -34.538  -9.174 -12.525  1.00 69.79           C  
ANISOU 5684  CB  TYR D 104     8370  10642   7504    -81  -2539   -267       C  
ATOM   5685  CG  TYR D 104     -33.220  -9.470 -13.212  1.00 66.64           C  
ANISOU 5685  CG  TYR D 104     8072  10104   7145   -194  -2525   -403       C  
ATOM   5686  CD1 TYR D 104     -32.272 -10.300 -12.614  1.00 65.13           C  
ANISOU 5686  CD1 TYR D 104     7850   9769   7127   -328  -2442   -520       C  
ATOM   5687  CD2 TYR D 104     -32.937  -8.949 -14.471  1.00 65.27           C  
ANISOU 5687  CD2 TYR D 104     8089   9788   6922   -168  -2466   -303       C  
ATOM   5688  CE1 TYR D 104     -31.075 -10.586 -13.240  1.00 62.21           C  
ANISOU 5688  CE1 TYR D 104     7641   9099   6897   -437  -2258   -501       C  
ATOM   5689  CE2 TYR D 104     -31.744  -9.234 -15.112  1.00 64.78           C  
ANISOU 5689  CE2 TYR D 104     8172   9449   6993   -261  -2237   -236       C  
ATOM   5690  CZ  TYR D 104     -30.815 -10.052 -14.490  1.00 61.79           C  
ANISOU 5690  CZ  TYR D 104     7761   8928   6790   -387  -2132   -331       C  
ATOM   5691  OH  TYR D 104     -29.622 -10.341 -15.115  1.00 58.32           O  
ANISOU 5691  OH  TYR D 104     7434   8274   6449   -418  -1877   -211       O  
ATOM   5692  N   ASP D 112     -35.993 -11.721  -7.689  1.00 83.13           N  
ANISOU 5692  N   ASP D 112     9413  12696   9478    186  -2265    -69       N  
ATOM   5693  CA  ASP D 112     -35.160 -12.550  -8.559  1.00 82.98           C  
ANISOU 5693  CA  ASP D 112     9545  12413   9571   -117  -2306   -177       C  
ATOM   5694  C   ASP D 112     -33.715 -12.056  -8.594  1.00 82.62           C  
ANISOU 5694  C   ASP D 112     9627  12160   9604   -182  -2269   -330       C  
ATOM   5695  O   ASP D 112     -33.459 -10.877  -8.841  1.00 86.73           O  
ANISOU 5695  O   ASP D 112    10189  12687  10076    -52  -2293   -396       O  
ATOM   5696  CB  ASP D 112     -35.738 -12.597  -9.962  1.00 83.88           C  
ANISOU 5696  CB  ASP D 112     9771  12526   9573   -218  -2402   -171       C  
ATOM   5697  N   ILE D 113     -32.775 -12.970  -8.369  1.00 76.01           N  
ANISOU 5697  N   ILE D 113     8817  11159   8904   -348  -2204   -408       N  
ATOM   5698  CA  ILE D 113     -31.376 -12.601  -8.188  1.00 69.28           C  
ANISOU 5698  CA  ILE D 113     7991  10184   8147   -391  -2110   -557       C  
ATOM   5699  C   ILE D 113     -30.417 -13.588  -8.874  1.00 60.99           C  
ANISOU 5699  C   ILE D 113     7064   8949   7162   -655  -2047   -626       C  
ATOM   5700  O   ILE D 113     -30.508 -14.800  -8.665  1.00 62.99           O  
ANISOU 5700  O   ILE D 113     7337   9096   7498   -685  -2023   -637       O  
ATOM   5701  CB  ILE D 113     -31.065 -12.452  -6.677  1.00 71.52           C  
ANISOU 5701  CB  ILE D 113     8154  10492   8527   -165  -2043   -623       C  
ATOM   5702  CG1 ILE D 113     -29.577 -12.204  -6.438  1.00 68.14           C  
ANISOU 5702  CG1 ILE D 113     7770   9796   8323   -163  -2005   -828       C  
ATOM   5703  CG2 ILE D 113     -31.598 -13.641  -5.893  1.00 74.29           C  
ANISOU 5703  CG2 ILE D 113     8392  10948   8886   -203  -1992   -481       C  
ATOM   5704  CD1 ILE D 113     -29.200 -10.772  -6.690  1.00 70.96           C  
ANISOU 5704  CD1 ILE D 113     8208   9916   8836     41  -2186   -967       C  
ATOM   5705  N   LYS D 114     -29.511 -13.063  -9.702  1.00 51.90           N  
ANISOU 5705  N   LYS D 114     5964   7715   6042   -684  -2029   -775       N  
ATOM   5706  CA  LYS D 114     -28.611 -13.902 -10.508  1.00 46.95           C  
ANISOU 5706  CA  LYS D 114     5479   6935   5425   -849  -1981   -864       C  
ATOM   5707  C   LYS D 114     -27.147 -13.444 -10.461  1.00 45.25           C  
ANISOU 5707  C   LYS D 114     5276   6378   5538   -816  -1813   -822       C  
ATOM   5708  O   LYS D 114     -26.859 -12.274 -10.213  1.00 46.99           O  
ANISOU 5708  O   LYS D 114     5417   6428   6009   -694  -1899   -777       O  
ATOM   5709  CB  LYS D 114     -29.094 -13.960 -11.969  1.00 47.49           C  
ANISOU 5709  CB  LYS D 114     5793   7037   5213   -882  -1980   -767       C  
ATOM   5710  CG  LYS D 114     -30.478 -14.595 -12.163  1.00 52.40           C  
ANISOU 5710  CG  LYS D 114     6406   7860   5646   -866  -2087   -766       C  
ATOM   5711  CD  LYS D 114     -30.408 -16.115 -12.088  1.00 54.11           C  
ANISOU 5711  CD  LYS D 114     6692   7992   5875   -967  -2044   -823       C  
ATOM   5712  CE  LYS D 114     -31.784 -16.734 -11.960  1.00 60.22           C  
ANISOU 5712  CE  LYS D 114     7346   8880   6654   -948  -2156   -750       C  
ATOM   5713  NZ  LYS D 114     -31.737 -18.218 -12.132  1.00 64.45           N  
ANISOU 5713  NZ  LYS D 114     7981   9312   7195  -1095  -2194   -786       N  
ATOM   5714  N   VAL D 115     -26.228 -14.376 -10.708  1.00 45.07           N  
ANISOU 5714  N   VAL D 115     5349   6244   5530   -914  -1601   -802       N  
ATOM   5715  CA  VAL D 115     -24.796 -14.071 -10.721  1.00 46.43           C  
ANISOU 5715  CA  VAL D 115     5471   6151   6018   -891  -1400   -656       C  
ATOM   5716  C   VAL D 115     -24.324 -13.505 -12.063  1.00 51.06           C  
ANISOU 5716  C   VAL D 115     6174   6653   6575   -797  -1203   -354       C  
ATOM   5717  O   VAL D 115     -24.561 -14.104 -13.114  1.00 53.43           O  
ANISOU 5717  O   VAL D 115     6717   7079   6503   -730  -1075   -316       O  
ATOM   5718  CB  VAL D 115     -23.957 -15.322 -10.380  1.00 50.69           C  
ANISOU 5718  CB  VAL D 115     6040   6660   6559   -970  -1216   -715       C  
ATOM   5719  CG1 VAL D 115     -22.480 -15.103 -10.713  1.00 52.34           C  
ANISOU 5719  CG1 VAL D 115     6192   6670   7025   -920   -948   -448       C  
ATOM   5720  CG2 VAL D 115     -24.127 -15.679  -8.920  1.00 49.88           C  
ANISOU 5720  CG2 VAL D 115     5740   6617   6594  -1030  -1373   -926       C  
ATOM   5721  N   ILE D 116     -23.661 -12.349 -12.019  1.00 53.53           N  
ANISOU 5721  N   ILE D 116     6313   6744   7283   -767  -1222   -117       N  
ATOM   5722  CA  ILE D 116     -23.103 -11.730 -13.221  1.00 58.38           C  
ANISOU 5722  CA  ILE D 116     6932   7302   7948   -668  -1012    304       C  
ATOM   5723  C   ILE D 116     -21.577 -11.761 -13.171  1.00 62.33           C  
ANISOU 5723  C   ILE D 116     7229   7637   8816   -687   -784    660       C  
ATOM   5724  O   ILE D 116     -20.962 -11.412 -12.154  1.00 60.03           O  
ANISOU 5724  O   ILE D 116     6717   7103   8990   -816   -959    651       O  
ATOM   5725  CB  ILE D 116     -23.608 -10.275 -13.429  1.00 59.86           C  
ANISOU 5725  CB  ILE D 116     7039   7355   8349   -634  -1245    448       C  
ATOM   5726  CG1 ILE D 116     -24.959 -10.268 -14.136  1.00 59.89           C  
ANISOU 5726  CG1 ILE D 116     7256   7618   7880   -540  -1307    303       C  
ATOM   5727  CG2 ILE D 116     -22.629  -9.470 -14.268  1.00 64.45           C  
ANISOU 5727  CG2 ILE D 116     7457   7776   9254   -592  -1070   1018       C  
ATOM   5728  CD1 ILE D 116     -26.070 -10.916 -13.356  1.00 59.46           C  
ANISOU 5728  CD1 ILE D 116     7269   7764   7559   -593  -1521   -116       C  
ATOM   5729  N   GLY D 117     -20.973 -12.207 -14.267  1.00 67.82           N  
ANISOU 5729  N   GLY D 117     8005   8493   9273   -511   -408    988       N  
ATOM   5730  CA  GLY D 117     -19.531 -12.270 -14.370  1.00 70.43           C  
ANISOU 5730  CA  GLY D 117     8095   8770   9896   -465   -125   1452       C  
ATOM   5731  C   GLY D 117     -18.904 -13.396 -13.584  1.00 70.06           C  
ANISOU 5731  C   GLY D 117     8057   8731   9830   -515    -22   1237       C  
ATOM   5732  O   GLY D 117     -19.552 -14.405 -13.287  1.00 68.89           O  
ANISOU 5732  O   GLY D 117     8180   8688   9307   -520    -80    769       O  
ATOM   5733  N   GLY D 118     -17.634 -13.215 -13.237  1.00 67.16           N  
ANISOU 5733  N   GLY D 118     7362   8241   9913   -570    100   1628       N  
ATOM   5734  CA  GLY D 118     -16.879 -14.260 -12.580  1.00 58.68           C  
ANISOU 5734  CA  GLY D 118     6268   7199   8829   -580    254   1510       C  
ATOM   5735  C   GLY D 118     -16.279 -15.193 -13.612  1.00 58.01           C  
ANISOU 5735  C   GLY D 118     6362   7419   8260   -216    734   1768       C  
ATOM   5736  O   GLY D 118     -16.600 -15.117 -14.807  1.00 56.14           O  
ANISOU 5736  O   GLY D 118     6327   7391   7614     72    916   1945       O  
ATOM   5737  N   ASP D 119     -15.382 -16.060 -13.158  1.00 54.34           N  
ANISOU 5737  N   ASP D 119     5843   6996   7807   -163    934   1795       N  
ATOM   5738  CA  ASP D 119     -14.888 -17.133 -13.997  1.00 57.84           C  
ANISOU 5738  CA  ASP D 119     6563   7727   7687    271   1346   1910       C  
ATOM   5739  C   ASP D 119     -16.008 -18.162 -14.114  1.00 55.24           C  
ANISOU 5739  C   ASP D 119     6796   7415   6779    336   1164   1242       C  
ATOM   5740  O   ASP D 119     -16.987 -18.114 -13.359  1.00 45.25           O  
ANISOU 5740  O   ASP D 119     5577   5984   5632      2    786    784       O  
ATOM   5741  CB  ASP D 119     -13.637 -17.780 -13.380  1.00 58.96           C  
ANISOU 5741  CB  ASP D 119     6487   7895   8020    309   1581   2111       C  
ATOM   5742  CG  ASP D 119     -12.452 -16.820 -13.297  1.00 63.31           C  
ANISOU 5742  CG  ASP D 119     6425   8425   9203    219   1717   2880       C  
ATOM   5743  OD1 ASP D 119     -12.499 -15.752 -13.940  1.00 66.86           O  
ANISOU 5743  OD1 ASP D 119     6650   8881   9870    216   1705   3342       O  
ATOM   5744  OD2 ASP D 119     -11.469 -17.143 -12.597  1.00 64.20           O  
ANISOU 5744  OD2 ASP D 119     6261   8508   9624    140   1811   3063       O  
ATOM   5745  N   ASP D 120     -15.879 -19.070 -15.076  1.00 58.99           N  
ANISOU 5745  N   ASP D 120     7693   8092   6629    798   1396   1226       N  
ATOM   5746  CA  ASP D 120     -16.714 -20.255 -15.082  1.00 59.09           C  
ANISOU 5746  CA  ASP D 120     8246   8031   6174    837   1148    622       C  
ATOM   5747  C   ASP D 120     -16.560 -20.866 -13.695  1.00 52.76           C  
ANISOU 5747  C   ASP D 120     7291   7041   5713    475    995    327       C  
ATOM   5748  O   ASP D 120     -15.439 -21.075 -13.224  1.00 54.49           O  
ANISOU 5748  O   ASP D 120     7272   7287   6147    527   1253    564       O  
ATOM   5749  CB  ASP D 120     -16.239 -21.240 -16.147  1.00 68.49           C  
ANISOU 5749  CB  ASP D 120     9934   9405   6684   1472   1399    656       C  
ATOM   5750  CG  ASP D 120     -17.130 -22.460 -16.245  1.00 69.99           C  
ANISOU 5750  CG  ASP D 120    10745   9418   6430   1504   1009     35       C  
ATOM   5751  OD1 ASP D 120     -17.114 -23.286 -15.308  1.00 62.33           O  
ANISOU 5751  OD1 ASP D 120     9802   8257   5624   1247    840   -266       O  
ATOM   5752  OD2 ASP D 120     -17.845 -22.591 -17.261  1.00 74.07           O  
ANISOU 5752  OD2 ASP D 120    11715   9970   6458   1783    832   -127       O  
ATOM   5753  N   LEU D 121     -17.680 -21.128 -13.031  1.00 50.66           N  
ANISOU 5753  N   LEU D 121     7117   6627   5504    125    587   -127       N  
ATOM   5754  CA  LEU D 121     -17.653 -21.514 -11.624  1.00 50.50           C  
ANISOU 5754  CA  LEU D 121     6866   6482   5842   -217    433   -350       C  
ATOM   5755  C   LEU D 121     -17.104 -22.919 -11.384  1.00 46.96           C  
ANISOU 5755  C   LEU D 121     6668   5986   5187    -84    522   -514       C  
ATOM   5756  O   LEU D 121     -16.993 -23.350 -10.239  1.00 45.10           O  
ANISOU 5756  O   LEU D 121     6245   5672   5219   -325    435   -666       O  
ATOM   5757  CB  LEU D 121     -19.038 -21.359 -10.997  1.00 55.14           C  
ANISOU 5757  CB  LEU D 121     7411   7016   6523   -558      9   -673       C  
ATOM   5758  CG  LEU D 121     -19.578 -19.932 -10.900  1.00 58.51           C  
ANISOU 5758  CG  LEU D 121     7551   7466   7214   -695   -121   -560       C  
ATOM   5759  CD1 LEU D 121     -21.009 -19.970 -10.418  1.00 61.71           C  
ANISOU 5759  CD1 LEU D 121     7961   7911   7573   -917   -500   -842       C  
ATOM   5760  CD2 LEU D 121     -18.736 -19.055  -9.980  1.00 56.39           C  
ANISOU 5760  CD2 LEU D 121     6841   7110   7474   -805    -62   -372       C  
ATOM   5761  N   SER D 122     -16.747 -23.623 -12.455  1.00 45.82           N  
ANISOU 5761  N   SER D 122     6970   5897   4542    357    685   -482       N  
ATOM   5762  CA  SER D 122     -16.078 -24.915 -12.322  1.00 48.03           C  
ANISOU 5762  CA  SER D 122     7540   6118   4593    586    786   -609       C  
ATOM   5763  C   SER D 122     -14.680 -24.730 -11.726  1.00 47.15           C  
ANISOU 5763  C   SER D 122     7005   6117   4794    652   1199   -248       C  
ATOM   5764  O   SER D 122     -14.050 -25.697 -11.303  1.00 46.95           O  
ANISOU 5764  O   SER D 122     7088   6049   4700    766   1303   -330       O  
ATOM   5765  CB  SER D 122     -16.011 -25.657 -13.667  1.00 55.32           C  
ANISOU 5765  CB  SER D 122     9119   7077   4825   1178    824   -680       C  
ATOM   5766  OG  SER D 122     -15.295 -24.914 -14.640  1.00 58.61           O  
ANISOU 5766  OG  SER D 122     9454   7782   5035   1638   1246   -221       O  
ATOM   5767  N   THR D 123     -14.206 -23.484 -11.682  1.00 42.89           N  
ANISOU 5767  N   THR D 123     5974   5689   4632    560   1387    173       N  
ATOM   5768  CA  THR D 123     -12.933 -23.168 -11.044  1.00 42.94           C  
ANISOU 5768  CA  THR D 123     5493   5759   5061    524   1674    573       C  
ATOM   5769  C   THR D 123     -13.034 -23.338  -9.531  1.00 38.81           C  
ANISOU 5769  C   THR D 123     4708   5056   4983     81   1431    284       C  
ATOM   5770  O   THR D 123     -12.020 -23.420  -8.842  1.00 42.88           O  
ANISOU 5770  O   THR D 123     4908   5583   5800     46   1599    488       O  
ATOM   5771  CB  THR D 123     -12.494 -21.732 -11.324  1.00 48.01           C  
ANISOU 5771  CB  THR D 123     5655   6475   6111    454   1788   1122       C  
ATOM   5772  OG1 THR D 123     -13.537 -20.836 -10.925  1.00 45.87           O  
ANISOU 5772  OG1 THR D 123     5272   6028   6129     62   1392    887       O  
ATOM   5773  CG2 THR D 123     -12.186 -21.539 -12.804  1.00 49.34           C  
ANISOU 5773  CG2 THR D 123     5979   6917   5849    971   2128   1563       C  
ATOM   5774  N   LEU D 124     -14.261 -23.387  -9.022  1.00 35.96           N  
ANISOU 5774  N   LEU D 124     4453   4566   4642   -218   1041   -148       N  
ATOM   5775  CA  LEU D 124     -14.487 -23.536  -7.583  1.00 32.51           C  
ANISOU 5775  CA  LEU D 124     3767   4034   4551   -552    813   -403       C  
ATOM   5776  C   LEU D 124     -14.410 -24.995  -7.131  1.00 34.64           C  
ANISOU 5776  C   LEU D 124     4276   4265   4621   -517    818   -655       C  
ATOM   5777  O   LEU D 124     -14.216 -25.264  -5.946  1.00 29.95           O  
ANISOU 5777  O   LEU D 124     3438   3647   4295   -698    755   -761       O  
ATOM   5778  CB  LEU D 124     -15.855 -22.973  -7.190  1.00 30.83           C  
ANISOU 5778  CB  LEU D 124     3508   3788   4417   -814    424   -664       C  
ATOM   5779  CG  LEU D 124     -16.016 -21.516  -6.759  1.00 36.79           C  
ANISOU 5779  CG  LEU D 124     3908   4505   5565   -961    253   -561       C  
ATOM   5780  CD1 LEU D 124     -14.969 -20.614  -7.366  1.00 35.69           C  
ANISOU 5780  CD1 LEU D 124     3567   4330   5665   -858    465   -109       C  
ATOM   5781  CD2 LEU D 124     -17.423 -21.024  -7.092  1.00 34.78           C  
ANISOU 5781  CD2 LEU D 124     3777   4291   5147  -1037    -25   -733       C  
ATOM   5782  N   THR D 125     -14.568 -25.924  -8.070  1.00 34.14           N  
ANISOU 5782  N   THR D 125     4713   4176   4082   -255    851   -757       N  
ATOM   5783  CA  THR D 125     -14.617 -27.348  -7.734  1.00 34.19           C  
ANISOU 5783  CA  THR D 125     5027   4060   3903   -227    748  -1016       C  
ATOM   5784  C   THR D 125     -13.359 -27.801  -6.995  1.00 34.62           C  
ANISOU 5784  C   THR D 125     4867   4157   4131   -136   1050   -877       C  
ATOM   5785  O   THR D 125     -12.242 -27.660  -7.501  1.00 36.01           O  
ANISOU 5785  O   THR D 125     5005   4460   4218    194   1429   -564       O  
ATOM   5786  CB  THR D 125     -14.829 -28.219  -8.979  1.00 42.02           C  
ANISOU 5786  CB  THR D 125     6682   4953   4329    144    675  -1154       C  
ATOM   5787  OG1 THR D 125     -16.025 -27.802  -9.650  1.00 38.51           O  
ANISOU 5787  OG1 THR D 125     6425   4467   3741     37    352  -1282       O  
ATOM   5788  CG2 THR D 125     -14.943 -29.696  -8.599  1.00 43.65           C  
ANISOU 5788  CG2 THR D 125     7244   4932   4409    137    447  -1436       C  
ATOM   5789  N   GLY D 126     -13.552 -28.331  -5.789  1.00 34.47           N  
ANISOU 5789  N   GLY D 126     4666   4073   4356   -409    893  -1056       N  
ATOM   5790  CA  GLY D 126     -12.464 -28.899  -5.012  1.00 34.63           C  
ANISOU 5790  CA  GLY D 126     4511   4122   4524   -338   1134   -971       C  
ATOM   5791  C   GLY D 126     -11.623 -27.893  -4.246  1.00 36.37           C  
ANISOU 5791  C   GLY D 126     4164   4462   5191   -447   1303   -717       C  
ATOM   5792  O   GLY D 126     -10.550 -28.248  -3.748  1.00 35.79           O  
ANISOU 5792  O   GLY D 126     3916   4439   5244   -351   1540   -567       O  
ATOM   5793  N   LYS D 127     -12.095 -26.647  -4.146  1.00 29.62           N  
ANISOU 5793  N   LYS D 127     3041   3624   4591   -638   1134   -667       N  
ATOM   5794  CA  LYS D 127     -11.314 -25.587  -3.504  1.00 30.38           C  
ANISOU 5794  CA  LYS D 127     2653   3735   5156   -742   1159   -429       C  
ATOM   5795  C   LYS D 127     -12.018 -25.127  -2.235  1.00 25.24           C  
ANISOU 5795  C   LYS D 127     1849   3056   4683   -922    754   -660       C  
ATOM   5796  O   LYS D 127     -13.211 -25.376  -2.065  1.00 26.71           O  
ANISOU 5796  O   LYS D 127     2195   3272   4681   -979    539   -896       O  
ATOM   5797  CB  LYS D 127     -11.157 -24.383  -4.440  1.00 32.94           C  
ANISOU 5797  CB  LYS D 127     2872   4060   5584   -695   1203    -98       C  
ATOM   5798  CG  LYS D 127     -10.585 -24.707  -5.808  1.00 39.83           C  
ANISOU 5798  CG  LYS D 127     3981   5057   6095   -340   1575    227       C  
ATOM   5799  CD  LYS D 127      -9.193 -25.281  -5.711  1.00 44.11           C  
ANISOU 5799  CD  LYS D 127     4377   5718   6667   -115   1945    558       C  
ATOM   5800  CE  LYS D 127      -8.583 -25.403  -7.106  1.00 54.08           C  
ANISOU 5800  CE  LYS D 127     5815   7195   7537    359   2348    986       C  
ATOM   5801  NZ  LYS D 127      -8.840 -24.163  -7.893  1.00 61.16           N  
ANISOU 5801  NZ  LYS D 127     6546   8128   8563    328   2311   1311       N  
ATOM   5802  N   ASN D 128     -11.279 -24.464  -1.351  1.00 26.96           N  
ANISOU 5802  N   ASN D 128     2890   2900   4454     69   -782   -550       N  
ATOM   5803  CA  ASN D 128     -11.874 -23.798  -0.198  1.00 27.20           C  
ANISOU 5803  CA  ASN D 128     3063   2910   4360    136   -847   -476       C  
ATOM   5804  C   ASN D 128     -12.328 -22.414  -0.631  1.00 27.84           C  
ANISOU 5804  C   ASN D 128     2971   3056   4552    -58   -657   -404       C  
ATOM   5805  O   ASN D 128     -11.506 -21.519  -0.810  1.00 32.19           O  
ANISOU 5805  O   ASN D 128     3275   3613   5343    -89   -623   -586       O  
ATOM   5806  CB  ASN D 128     -10.868 -23.669   0.950  1.00 26.63           C  
ANISOU 5806  CB  ASN D 128     2981   2808   4329    422  -1145   -744       C  
ATOM   5807  CG  ASN D 128     -10.606 -24.993   1.653  1.00 31.72           C  
ANISOU 5807  CG  ASN D 128     3954   3350   4748    721  -1364   -768       C  
ATOM   5808  OD1 ASN D 128     -11.201 -26.009   1.310  1.00 31.08           O  
ANISOU 5808  OD1 ASN D 128     4104   3190   4516    664  -1237   -571       O  
ATOM   5809  ND2 ASN D 128      -9.700 -24.986   2.633  1.00 34.52           N  
ANISOU 5809  ND2 ASN D 128     4343   3691   5082   1072  -1698  -1042       N  
ATOM   5810  N   VAL D 129     -13.629 -22.233  -0.799  1.00 23.40           N  
ANISOU 5810  N   VAL D 129     2533   2520   3838   -179   -515   -173       N  
ATOM   5811  CA  VAL D 129     -14.134 -20.973  -1.343  1.00 21.24           C  
ANISOU 5811  CA  VAL D 129     2147   2297   3627   -313   -345    -88       C  
ATOM   5812  C   VAL D 129     -14.500 -20.007  -0.217  1.00 26.84           C  
ANISOU 5812  C   VAL D 129     2888   2989   4322   -275   -397    -83       C  
ATOM   5813  O   VAL D 129     -15.304 -20.344   0.665  1.00 26.89           O  
ANISOU 5813  O   VAL D 129     3086   2976   4154   -228   -451      2       O  
ATOM   5814  CB  VAL D 129     -15.361 -21.207  -2.236  1.00 24.09           C  
ANISOU 5814  CB  VAL D 129     2579   2727   3848   -412   -214     85       C  
ATOM   5815  CG1 VAL D 129     -15.888 -19.881  -2.792  1.00 22.99           C  
ANISOU 5815  CG1 VAL D 129     2391   2627   3717   -462    -78    174       C  
ATOM   5816  CG2 VAL D 129     -15.009 -22.159  -3.380  1.00 26.23           C  
ANISOU 5816  CG2 VAL D 129     2819   3027   4119   -434   -174     56       C  
ATOM   5817  N   LEU D 130     -13.890 -18.823  -0.240  1.00 24.17           N  
ANISOU 5817  N   LEU D 130     2369   2629   4185   -304   -339   -195       N  
ATOM   5818  CA  LEU D 130     -14.195 -17.743   0.706  1.00 22.80           C  
ANISOU 5818  CA  LEU D 130     2184   2438   4038   -282   -368   -218       C  
ATOM   5819  C   LEU D 130     -14.961 -16.644  -0.032  1.00 21.49           C  
ANISOU 5819  C   LEU D 130     2004   2270   3891   -408   -139    -54       C  
ATOM   5820  O   LEU D 130     -14.395 -15.955  -0.890  1.00 26.12           O  
ANISOU 5820  O   LEU D 130     2486   2790   4649   -483     61    -88       O  
ATOM   5821  CB  LEU D 130     -12.901 -17.138   1.255  1.00 26.38           C  
ANISOU 5821  CB  LEU D 130     2412   2844   4766   -212   -462   -539       C  
ATOM   5822  CG  LEU D 130     -12.826 -16.490   2.652  1.00 35.13           C  
ANISOU 5822  CG  LEU D 130     3508   3952   5887    -75   -653   -705       C  
ATOM   5823  CD1 LEU D 130     -11.962 -15.236   2.630  1.00 33.33           C  
ANISOU 5823  CD1 LEU D 130     2960   3658   6046   -148   -553   -993       C  
ATOM   5824  CD2 LEU D 130     -14.176 -16.234   3.275  1.00 34.29           C  
ANISOU 5824  CD2 LEU D 130     3636   3870   5524    -81   -633   -459       C  
ATOM   5825  N   ILE D 131     -16.237 -16.486   0.301  1.00 20.67           N  
ANISOU 5825  N   ILE D 131     2029   2213   3610   -413   -144    105       N  
ATOM   5826  CA  ILE D 131     -17.053 -15.418  -0.273  1.00 23.39           C  
ANISOU 5826  CA  ILE D 131     2385   2561   3939   -456      8    235       C  
ATOM   5827  C   ILE D 131     -16.920 -14.207   0.635  1.00 22.11           C  
ANISOU 5827  C   ILE D 131     2160   2334   3907   -451     14    160       C  
ATOM   5828  O   ILE D 131     -17.090 -14.324   1.850  1.00 23.71           O  
ANISOU 5828  O   ILE D 131     2392   2557   4061   -399   -134     93       O  
ATOM   5829  CB  ILE D 131     -18.537 -15.839  -0.352  1.00 21.67           C  
ANISOU 5829  CB  ILE D 131     2268   2442   3525   -451    -23    353       C  
ATOM   5830  CG1 ILE D 131     -18.695 -17.024  -1.309  1.00 24.86           C  
ANISOU 5830  CG1 ILE D 131     2698   2912   3837   -459    -27    372       C  
ATOM   5831  CG2 ILE D 131     -19.400 -14.679  -0.818  1.00 26.91           C  
ANISOU 5831  CG2 ILE D 131     2945   3121   4159   -418     61    440       C  
ATOM   5832  CD1 ILE D 131     -20.073 -17.706  -1.267  1.00 28.61           C  
ANISOU 5832  CD1 ILE D 131     3198   3469   4204   -480    -53    368       C  
ATOM   5833  N   VAL D 132     -16.601 -13.052   0.067  1.00 20.36           N  
ANISOU 5833  N   VAL D 132     1887   2008   3840   -492    212    164       N  
ATOM   5834  CA  VAL D 132     -16.397 -11.861   0.870  1.00 22.55           C  
ANISOU 5834  CA  VAL D 132     2074   2197   4299   -506    251     54       C  
ATOM   5835  C   VAL D 132     -17.447 -10.801   0.533  1.00 29.76           C  
ANISOU 5835  C   VAL D 132     3105   3071   5132   -489    386    234       C  
ATOM   5836  O   VAL D 132     -17.518 -10.334  -0.609  1.00 26.63           O  
ANISOU 5836  O   VAL D 132     2827   2585   4708   -474    601    365       O  
ATOM   5837  CB  VAL D 132     -14.992 -11.302   0.652  1.00 23.82           C  
ANISOU 5837  CB  VAL D 132     2049   2202   4799   -579    423   -177       C  
ATOM   5838  CG1 VAL D 132     -14.760 -10.052   1.500  1.00 22.30           C  
ANISOU 5838  CG1 VAL D 132     1761   1931   4780   -567    460   -348       C  
ATOM   5839  CG2 VAL D 132     -13.928 -12.376   0.974  1.00 25.08           C  
ANISOU 5839  CG2 VAL D 132     2060   2419   5049   -541    233   -418       C  
ATOM   5840  N   GLU D 133     -18.222 -10.397   1.543  1.00 24.71           N  
ANISOU 5840  N   GLU D 133     2467   2484   4440   -457    266    226       N  
ATOM   5841  CA  GLU D 133     -19.396  -9.542   1.358  1.00 25.25           C  
ANISOU 5841  CA  GLU D 133     2631   2551   4411   -404    323    365       C  
ATOM   5842  C   GLU D 133     -19.268  -8.294   2.228  1.00 30.01           C  
ANISOU 5842  C   GLU D 133     3160   3046   5198   -422    376    265       C  
ATOM   5843  O   GLU D 133     -18.560  -8.321   3.244  1.00 25.74           O  
ANISOU 5843  O   GLU D 133     2487   2501   4793   -452    277     64       O  
ATOM   5844  CB  GLU D 133     -20.663 -10.355   1.700  1.00 27.31           C  
ANISOU 5844  CB  GLU D 133     2934   2986   4455   -367    157    413       C  
ATOM   5845  CG  GLU D 133     -22.000  -9.648   1.551  1.00 34.50           C  
ANISOU 5845  CG  GLU D 133     3883   3942   5283   -285    156    475       C  
ATOM   5846  CD  GLU D 133     -22.307  -9.251   0.123  1.00 31.27           C  
ANISOU 5846  CD  GLU D 133     3595   3511   4776   -147    228    592       C  
ATOM   5847  OE1 GLU D 133     -21.672  -8.303  -0.369  1.00 29.40           O  
ANISOU 5847  OE1 GLU D 133     3461   3099   4611   -110    408    666       O  
ATOM   5848  OE2 GLU D 133     -23.192  -9.873  -0.506  1.00 32.71           O  
ANISOU 5848  OE2 GLU D 133     3788   3833   4806    -55    121    586       O  
ATOM   5849  N   ASP D 134     -19.903  -7.190   1.823  1.00 28.09           N  
ANISOU 5849  N   ASP D 134     3010   2708   4954   -367    514    374       N  
ATOM   5850  CA  ASP D 134     -19.949  -5.994   2.679  1.00 21.88           C  
ANISOU 5850  CA  ASP D 134     2155   1816   4341   -383    564    276       C  
ATOM   5851  C   ASP D 134     -20.973  -6.126   3.820  1.00 25.12           C  
ANISOU 5851  C   ASP D 134     2529   2389   4626   -347    351    235       C  
ATOM   5852  O   ASP D 134     -20.665  -5.858   4.987  1.00 28.81           O  
ANISOU 5852  O   ASP D 134     2894   2859   5194   -374    270     64       O  
ATOM   5853  CB  ASP D 134     -20.152  -4.698   1.876  1.00 25.85           C  
ANISOU 5853  CB  ASP D 134     2818   2098   4907   -320    833    405       C  
ATOM   5854  CG  ASP D 134     -21.390  -4.729   1.001  1.00 30.59           C  
ANISOU 5854  CG  ASP D 134     3635   2779   5209   -125    774    615       C  
ATOM   5855  OD1 ASP D 134     -21.950  -5.824   0.778  1.00 29.07           O  
ANISOU 5855  OD1 ASP D 134     3425   2803   4818    -84    575    638       O  
ATOM   5856  OD2 ASP D 134     -21.796  -3.650   0.524  1.00 33.55           O  
ANISOU 5856  OD2 ASP D 134     4200   2989   5558     12    924    725       O  
ATOM   5857  N   ILE D 135     -22.183  -6.562   3.501  1.00 28.80           N  
ANISOU 5857  N   ILE D 135     3073   2988   4882   -277    270    347       N  
ATOM   5858  CA  ILE D 135     -23.216  -6.609   4.520  1.00 26.02           C  
ANISOU 5858  CA  ILE D 135     2684   2748   4456   -272    162    283       C  
ATOM   5859  C   ILE D 135     -24.260  -7.679   4.250  1.00 27.70           C  
ANISOU 5859  C   ILE D 135     2906   3117   4501   -264     90    301       C  
ATOM   5860  O   ILE D 135     -24.646  -7.907   3.098  1.00 29.97           O  
ANISOU 5860  O   ILE D 135     3221   3450   4718   -185     80    365       O  
ATOM   5861  CB  ILE D 135     -23.855  -5.198   4.688  1.00 35.17           C  
ANISOU 5861  CB  ILE D 135     3837   3827   5700   -200    220    280       C  
ATOM   5862  CG1 ILE D 135     -24.944  -5.202   5.763  1.00 32.50           C  
ANISOU 5862  CG1 ILE D 135     3440   3599   5309   -209    143    181       C  
ATOM   5863  CG2 ILE D 135     -24.378  -4.669   3.347  1.00 34.53           C  
ANISOU 5863  CG2 ILE D 135     3878   3693   5549    -43    281    419       C  
ATOM   5864  CD1 ILE D 135     -25.277  -3.793   6.247  1.00 33.57           C  
ANISOU 5864  CD1 ILE D 135     3543   3641   5570   -157    188    130       C  
ATOM   5865  N   ILE D 136     -24.685  -8.344   5.327  1.00 24.96           N  
ANISOU 5865  N   ILE D 136     2558   2831   4095   -335     64    216       N  
ATOM   5866  CA  ILE D 136     -25.822  -9.260   5.318  1.00 26.49           C  
ANISOU 5866  CA  ILE D 136     2729   3123   4212   -379     87    160       C  
ATOM   5867  C   ILE D 136     -26.973  -8.528   5.995  1.00 30.57           C  
ANISOU 5867  C   ILE D 136     3170   3665   4782   -373    128     51       C  
ATOM   5868  O   ILE D 136     -26.808  -8.021   7.104  1.00 28.41           O  
ANISOU 5868  O   ILE D 136     2945   3338   4513   -393    160     19       O  
ATOM   5869  CB  ILE D 136     -25.552 -10.512   6.185  1.00 28.97           C  
ANISOU 5869  CB  ILE D 136     3173   3413   4423   -471    140    138       C  
ATOM   5870  CG1 ILE D 136     -24.254 -11.213   5.782  1.00 31.36           C  
ANISOU 5870  CG1 ILE D 136     3550   3682   4684   -454     69    209       C  
ATOM   5871  CG2 ILE D 136     -26.735 -11.498   6.116  1.00 28.35           C  
ANISOU 5871  CG2 ILE D 136     3062   3373   4335   -568    267     44       C  
ATOM   5872  CD1 ILE D 136     -24.179 -11.525   4.333  1.00 30.80           C  
ANISOU 5872  CD1 ILE D 136     3403   3662   4639   -442     46    265       C  
ATOM   5873  N   ASP D 137     -28.133  -8.487   5.348  1.00 30.82           N  
ANISOU 5873  N   ASP D 137     3065   3786   4857   -323    110    -51       N  
ATOM   5874  CA  ASP D 137     -29.313  -7.873   5.943  1.00 33.24           C  
ANISOU 5874  CA  ASP D 137     3247   4127   5254   -317    150   -217       C  
ATOM   5875  C   ASP D 137     -30.395  -8.937   6.095  1.00 35.41           C  
ANISOU 5875  C   ASP D 137     3391   4467   5596   -444    273   -435       C  
ATOM   5876  O   ASP D 137     -30.521  -9.558   7.147  1.00 35.11           O  
ANISOU 5876  O   ASP D 137     3445   4353   5543   -609    481   -477       O  
ATOM   5877  CB  ASP D 137     -29.776  -6.695   5.075  1.00 36.59           C  
ANISOU 5877  CB  ASP D 137     3597   4584   5720    -93      9   -229       C  
ATOM   5878  CG  ASP D 137     -30.913  -5.910   5.695  1.00 40.06           C  
ANISOU 5878  CG  ASP D 137     3890   5056   6275    -52     18   -421       C  
ATOM   5879  OD1 ASP D 137     -31.196  -6.089   6.901  1.00 43.43           O  
ANISOU 5879  OD1 ASP D 137     4295   5458   6750   -221    171   -514       O  
ATOM   5880  OD2 ASP D 137     -31.509  -5.099   4.962  1.00 40.00           O  
ANISOU 5880  OD2 ASP D 137     3823   5087   6288    181   -126   -482       O  
ATOM   5881  N   THR D 138     -31.169  -9.171   5.044  1.00 36.18           N  
ANISOU 5881  N   THR D 138     3294   4683   5769   -351    167   -603       N  
ATOM   5882  CA  THR D 138     -32.163 -10.241   5.094  1.00 36.51           C  
ANISOU 5882  CA  THR D 138     3143   4770   5960   -501    314   -894       C  
ATOM   5883  C   THR D 138     -31.481 -11.603   4.979  1.00 36.28           C  
ANISOU 5883  C   THR D 138     3255   4673   5857   -651    433   -792       C  
ATOM   5884  O   THR D 138     -31.971 -12.598   5.512  1.00 39.29           O  
ANISOU 5884  O   THR D 138     3619   4972   6337   -860    703   -945       O  
ATOM   5885  CB  THR D 138     -33.210 -10.118   3.981  1.00 39.63           C  
ANISOU 5885  CB  THR D 138     3229   5340   6487   -312    108  -1208       C  
ATOM   5886  OG1 THR D 138     -32.583 -10.274   2.699  1.00 39.56           O  
ANISOU 5886  OG1 THR D 138     3308   5403   6320   -114   -122  -1070       O  
ATOM   5887  CG2 THR D 138     -33.888  -8.774   4.053  1.00 42.63           C  
ANISOU 5887  CG2 THR D 138     3498   5777   6923   -104    -41  -1317       C  
ATOM   5888  N   GLY D 139     -30.351 -11.642   4.278  1.00 31.55           N  
ANISOU 5888  N   GLY D 139     2811   4078   5100   -548    272   -545       N  
ATOM   5889  CA  GLY D 139     -29.649 -12.902   4.057  1.00 30.02           C  
ANISOU 5889  CA  GLY D 139     2740   3829   4837   -653    342   -457       C  
ATOM   5890  C   GLY D 139     -30.033 -13.572   2.750  1.00 30.21           C  
ANISOU 5890  C   GLY D 139     2584   3979   4918   -590    227   -619       C  
ATOM   5891  O   GLY D 139     -29.474 -14.607   2.386  1.00 34.21           O  
ANISOU 5891  O   GLY D 139     3166   4451   5380   -660    264   -564       O  
ATOM   5892  N   LYS D 140     -30.985 -12.986   2.031  1.00 33.28           N  
ANISOU 5892  N   LYS D 140     2737   4517   5391   -418     57   -848       N  
ATOM   5893  CA  LYS D 140     -31.454 -13.573   0.772  1.00 38.01           C  
ANISOU 5893  CA  LYS D 140     3147   5269   6028   -286   -114  -1082       C  
ATOM   5894  C   LYS D 140     -30.377 -13.616  -0.312  1.00 38.12           C  
ANISOU 5894  C   LYS D 140     3366   5310   5808   -113   -283   -824       C  
ATOM   5895  O   LYS D 140     -30.286 -14.582  -1.073  1.00 40.69           O  
ANISOU 5895  O   LYS D 140     3637   5696   6128   -116   -324   -923       O  
ATOM   5896  CB  LYS D 140     -32.689 -12.829   0.257  1.00 45.73           C  
ANISOU 5896  CB  LYS D 140     3849   6418   7109    -38   -334  -1427       C  
ATOM   5897  CG  LYS D 140     -33.979 -13.152   1.013  1.00 54.79           C  
ANISOU 5897  CG  LYS D 140     4849   7502   8467   -203   -127  -1766       C  
ATOM   5898  CD  LYS D 140     -35.197 -12.562   0.309  1.00 60.61           C  
ANISOU 5898  CD  LYS D 140     5400   8379   9252     84   -380  -2138       C  
ATOM   5899  CE  LYS D 140     -35.610 -11.231   0.914  1.00 63.14           C  
ANISOU 5899  CE  LYS D 140     5700   8700   9591    193   -437  -2128       C  
ATOM   5900  NZ  LYS D 140     -36.542 -11.439   2.058  1.00 67.11           N  
ANISOU 5900  NZ  LYS D 140     6096   9080  10322    -64   -135  -2375       N  
ATOM   5901  N   THR D 141     -29.564 -12.569  -0.387  1.00 38.38           N  
ANISOU 5901  N   THR D 141     3631   5278   5675     23   -339   -521       N  
ATOM   5902  CA  THR D 141     -28.516 -12.514  -1.400  1.00 38.09           C  
ANISOU 5902  CA  THR D 141     3811   5220   5441    166   -410   -286       C  
ATOM   5903  C   THR D 141     -27.536 -13.660  -1.200  1.00 36.65           C  
ANISOU 5903  C   THR D 141     3697   4960   5267    -60   -279   -174       C  
ATOM   5904  O   THR D 141     -27.161 -14.346  -2.148  1.00 36.36           O  
ANISOU 5904  O   THR D 141     3693   4974   5148     -3   -334   -172       O  
ATOM   5905  CB  THR D 141     -27.766 -11.166  -1.372  1.00 36.54           C  
ANISOU 5905  CB  THR D 141     3848   4892   5144    286   -376    -12       C  
ATOM   5906  OG1 THR D 141     -28.714 -10.098  -1.494  1.00 42.89           O  
ANISOU 5906  OG1 THR D 141     4624   5741   5931    523   -497   -109       O  
ATOM   5907  CG2 THR D 141     -26.759 -11.081  -2.511  1.00 39.77           C  
ANISOU 5907  CG2 THR D 141     4497   5239   5375    426   -361    195       C  
ATOM   5908  N   MET D 142     -27.135 -13.888   0.043  1.00 29.59           N  
ANISOU 5908  N   MET D 142     2851   3945   4449   -279   -121    -99       N  
ATOM   5909  CA AMET D 142     -26.148 -14.919   0.345  0.49 28.73           C  
ANISOU 5909  CA AMET D 142     2855   3742   4318   -428    -29      5       C  
ATOM   5910  CA BMET D 142     -26.145 -14.923   0.305  0.51 28.31           C  
ANISOU 5910  CA BMET D 142     2801   3692   4263   -424    -33      5       C  
ATOM   5911  C   MET D 142     -26.712 -16.330   0.189  1.00 26.36           C  
ANISOU 5911  C   MET D 142     2460   3464   4093   -552     46   -180       C  
ATOM   5912  O   MET D 142     -26.034 -17.226  -0.308  1.00 29.17           O  
ANISOU 5912  O   MET D 142     2875   3800   4406   -579     44   -134       O  
ATOM   5913  CB AMET D 142     -25.575 -14.722   1.753  0.49 29.73           C  
ANISOU 5913  CB AMET D 142     3116   3732   4447   -532     71    109       C  
ATOM   5914  CB BMET D 142     -25.454 -14.732   1.659  0.51 29.75           C  
ANISOU 5914  CB BMET D 142     3126   3735   4443   -524     62    123       C  
ATOM   5915  CG AMET D 142     -24.242 -15.408   1.973  0.49 29.14           C  
ANISOU 5915  CG AMET D 142     3194   3565   4313   -563     73    225       C  
ATOM   5916  CG BMET D 142     -24.401 -13.631   1.687  0.51 30.52           C  
ANISOU 5916  CG BMET D 142     3298   3775   4522   -440      8    272       C  
ATOM   5917  SD AMET D 142     -23.111 -15.161   0.584  0.49 37.02           S  
ANISOU 5917  SD AMET D 142     4183   4593   5289   -462    -17    326       S  
ATOM   5918  SD BMET D 142     -22.979 -13.795   0.575  0.51 33.39           S  
ANISOU 5918  SD BMET D 142     3720   4105   4860   -387    -18    384       S  
ATOM   5919  CE AMET D 142     -22.850 -13.389   0.626  0.49 34.97           C  
ANISOU 5919  CE AMET D 142     3927   4284   5077   -370    -10    404       C  
ATOM   5920  CE BMET D 142     -22.777 -15.568   0.485  0.51 40.51           C  
ANISOU 5920  CE BMET D 142     4646   5024   5724   -477    -18    333       C  
ATOM   5921  N   GLN D 143     -27.948 -16.537   0.629  1.00 29.92           N  
ANISOU 5921  N   GLN D 143     2747   3931   4689   -644    149   -421       N  
ATOM   5922  CA  GLN D 143     -28.547 -17.863   0.465  1.00 30.53           C  
ANISOU 5922  CA  GLN D 143     2701   3986   4913   -796    292   -660       C  
ATOM   5923  C   GLN D 143     -28.610 -18.207  -1.019  1.00 36.28           C  
ANISOU 5923  C   GLN D 143     3275   4886   5625   -646     81   -799       C  
ATOM   5924  O   GLN D 143     -28.359 -19.345  -1.416  1.00 38.28           O  
ANISOU 5924  O   GLN D 143     3523   5107   5916   -733    141   -862       O  
ATOM   5925  CB  GLN D 143     -29.922 -17.937   1.124  1.00 42.52           C  
ANISOU 5925  CB  GLN D 143     4053   5471   6632   -913    484   -954       C  
ATOM   5926  CG  GLN D 143     -29.855 -18.387   2.585  1.00 48.58           C  
ANISOU 5926  CG  GLN D 143     5101   5995   7360  -1081    809   -833       C  
ATOM   5927  CD  GLN D 143     -31.213 -18.416   3.255  1.00 56.48           C  
ANISOU 5927  CD  GLN D 143     6018   6932   8510  -1147   1033  -1102       C  
ATOM   5928  OE1 GLN D 143     -32.210 -17.970   2.683  1.00 58.43           O  
ANISOU 5928  OE1 GLN D 143     5974   7320   8909  -1066    916  -1393       O  
ATOM   5929  NE2 GLN D 143     -31.259 -18.940   4.475  1.00 56.83           N  
ANISOU 5929  NE2 GLN D 143     6340   6748   8503  -1266   1360  -1033       N  
ATOM   5930  N   THR D 144     -28.902 -17.196  -1.835  1.00 40.70           N  
ANISOU 5930  N   THR D 144     3759   5611   6094   -383   -168   -835       N  
ATOM   5931  CA  THR D 144     -28.947 -17.349  -3.287  1.00 43.68           C  
ANISOU 5931  CA  THR D 144     4075   6159   6361   -139   -406   -951       C  
ATOM   5932  C   THR D 144     -27.574 -17.711  -3.851  1.00 40.53           C  
ANISOU 5932  C   THR D 144     3923   5701   5776   -124   -400   -656       C  
ATOM   5933  O   THR D 144     -27.431 -18.652  -4.635  1.00 39.92           O  
ANISOU 5933  O   THR D 144     3797   5683   5687   -113   -444   -768       O  
ATOM   5934  CB  THR D 144     -29.417 -16.056  -3.963  1.00 45.09           C  
ANISOU 5934  CB  THR D 144     4272   6472   6386    220   -657   -977       C  
ATOM   5935  OG1 THR D 144     -30.797 -15.834  -3.658  1.00 49.15           O  
ANISOU 5935  OG1 THR D 144     4479   7090   7106    257   -725  -1365       O  
ATOM   5936  CG2 THR D 144     -29.248 -16.149  -5.477  1.00 47.87           C  
ANISOU 5936  CG2 THR D 144     4714   6968   6505    548   -893  -1019       C  
ATOM   5937  N   LEU D 145     -26.564 -16.950  -3.456  1.00 34.03           N  
ANISOU 5937  N   LEU D 145     3329   4758   4841   -126   -338   -326       N  
ATOM   5938  CA  LEU D 145     -25.208 -17.195  -3.927  1.00 34.02           C  
ANISOU 5938  CA  LEU D 145     3518   4685   4725   -128   -300    -98       C  
ATOM   5939  C   LEU D 145     -24.704 -18.569  -3.484  1.00 35.60           C  
ANISOU 5939  C   LEU D 145     3706   4801   5020   -348   -189   -119       C  
ATOM   5940  O   LEU D 145     -24.070 -19.285  -4.261  1.00 37.06           O  
ANISOU 5940  O   LEU D 145     3928   5003   5152   -329   -209   -105       O  
ATOM   5941  CB  LEU D 145     -24.263 -16.096  -3.440  1.00 32.22           C  
ANISOU 5941  CB  LEU D 145     3459   4322   4459   -124   -219    158       C  
ATOM   5942  CG  LEU D 145     -22.825 -16.274  -3.917  1.00 37.00           C  
ANISOU 5942  CG  LEU D 145     4201   4836   5022   -144   -140    318       C  
ATOM   5943  CD1 LEU D 145     -22.787 -16.409  -5.449  1.00 39.54           C  
ANISOU 5943  CD1 LEU D 145     4613   5241   5170     50   -187    314       C  
ATOM   5944  CD2 LEU D 145     -21.965 -15.112  -3.439  1.00 35.93           C  
ANISOU 5944  CD2 LEU D 145     4161   4552   4937   -158    -29    470       C  
ATOM   5945  N   LEU D 146     -25.002 -18.944  -2.243  1.00 26.47           N  
ANISOU 5945  N   LEU D 146     2540   3534   3982   -530    -55   -152       N  
ATOM   5946  CA  LEU D 146     -24.532 -20.223  -1.715  1.00 27.97           C  
ANISOU 5946  CA  LEU D 146     2821   3587   4218   -689     78   -143       C  
ATOM   5947  C   LEU D 146     -25.121 -21.389  -2.509  1.00 32.42           C  
ANISOU 5947  C   LEU D 146     3237   4204   4877   -744    103   -378       C  
ATOM   5948  O   LEU D 146     -24.415 -22.334  -2.858  1.00 31.11           O  
ANISOU 5948  O   LEU D 146     3143   3984   4694   -777    122   -345       O  
ATOM   5949  CB  LEU D 146     -24.862 -20.353  -0.215  1.00 27.45           C  
ANISOU 5949  CB  LEU D 146     2877   3355   4200   -823    265   -125       C  
ATOM   5950  CG  LEU D 146     -23.940 -19.531   0.685  1.00 26.92           C  
ANISOU 5950  CG  LEU D 146     2991   3213   4026   -756    217     81       C  
ATOM   5951  CD1 LEU D 146     -24.414 -19.528   2.119  1.00 28.55           C  
ANISOU 5951  CD1 LEU D 146     3353   3277   4217   -828    386     84       C  
ATOM   5952  CD2 LEU D 146     -22.514 -20.065   0.606  1.00 29.65           C  
ANISOU 5952  CD2 LEU D 146     3478   3492   4297   -698    140    197       C  
ATOM   5953  N   SER D 147     -26.413 -21.306  -2.804  1.00 34.40           N  
ANISOU 5953  N   SER D 147     3248   4564   5258   -742     89   -664       N  
ATOM   5954  CA  SER D 147     -27.099 -22.333  -3.582  1.00 41.28           C  
ANISOU 5954  CA  SER D 147     3894   5507   6282   -784     93   -998       C  
ATOM   5955  C   SER D 147     -26.457 -22.545  -4.963  1.00 40.90           C  
ANISOU 5955  C   SER D 147     3856   5609   6076   -594   -124   -978       C  
ATOM   5956  O   SER D 147     -26.379 -23.669  -5.457  1.00 41.90           O  
ANISOU 5956  O   SER D 147     3913   5723   6284   -665    -86  -1131       O  
ATOM   5957  CB  SER D 147     -28.579 -21.982  -3.734  1.00 48.10           C  
ANISOU 5957  CB  SER D 147     4502   6487   7287   -712     47  -1351       C  
ATOM   5958  OG  SER D 147     -28.756 -20.903  -4.634  1.00 55.46           O  
ANISOU 5958  OG  SER D 147     5316   7665   8091   -423   -279  -1411       O  
ATOM   5959  N   LEU D 148     -25.991 -21.469  -5.583  1.00 37.22           N  
ANISOU 5959  N   LEU D 148     3508   5253   5382   -355   -309   -790       N  
ATOM   5960  CA  LEU D 148     -25.283 -21.595  -6.855  1.00 40.79           C  
ANISOU 5960  CA  LEU D 148     4058   5804   5638   -167   -442   -727       C  
ATOM   5961  C   LEU D 148     -23.912 -22.241  -6.656  1.00 41.74           C  
ANISOU 5961  C   LEU D 148     4349   5770   5739   -308   -310   -492       C  
ATOM   5962  O   LEU D 148     -23.553 -23.202  -7.344  1.00 44.16           O  
ANISOU 5962  O   LEU D 148     4636   6100   6044   -317   -321   -575       O  
ATOM   5963  CB  LEU D 148     -25.113 -20.234  -7.529  1.00 43.65           C  
ANISOU 5963  CB  LEU D 148     4594   6245   5744    129   -573   -561       C  
ATOM   5964  CG  LEU D 148     -24.348 -20.342  -8.846  1.00 45.40           C  
ANISOU 5964  CG  LEU D 148     5001   6523   5725    332   -629   -473       C  
ATOM   5965  CD1 LEU D 148     -25.052 -21.324  -9.763  1.00 46.00           C  
ANISOU 5965  CD1 LEU D 148     4895   6782   5800    448   -802   -829       C  
ATOM   5966  CD2 LEU D 148     -24.251 -19.007  -9.518  1.00 51.14           C  
ANISOU 5966  CD2 LEU D 148     5996   7262   6173    646   -675   -297       C  
ATOM   5967  N   VAL D 149     -23.151 -21.718  -5.702  1.00 33.87           N  
ANISOU 5967  N   VAL D 149     3499   4626   4745   -395   -210   -246       N  
ATOM   5968  CA  VAL D 149     -21.782 -22.175  -5.486  1.00 30.08           C  
ANISOU 5968  CA  VAL D 149     3152   4018   4259   -467   -141    -80       C  
ATOM   5969  C   VAL D 149     -21.690 -23.662  -5.138  1.00 30.54           C  
ANISOU 5969  C   VAL D 149     3205   3974   4426   -611    -64   -176       C  
ATOM   5970  O   VAL D 149     -20.820 -24.374  -5.648  1.00 34.43           O  
ANISOU 5970  O   VAL D 149     3738   4441   4903   -604    -72   -160       O  
ATOM   5971  CB  VAL D 149     -21.079 -21.321  -4.418  1.00 30.60           C  
ANISOU 5971  CB  VAL D 149     3325   3962   4341   -497    -95    101       C  
ATOM   5972  CG1 VAL D 149     -19.774 -21.970  -3.977  1.00 30.34           C  
ANISOU 5972  CG1 VAL D 149     3377   3802   4349   -544    -74    162       C  
ATOM   5973  CG2 VAL D 149     -20.817 -19.912  -4.975  1.00 33.19           C  
ANISOU 5973  CG2 VAL D 149     3698   4329   4585   -364   -104    215       C  
ATOM   5974  N   ARG D 150     -22.593 -24.129  -4.285  1.00 29.26           N  
ANISOU 5974  N   ARG D 150     3013   3722   4381   -742     53   -286       N  
ATOM   5975  CA  ARG D 150     -22.568 -25.517  -3.837  1.00 32.24           C  
ANISOU 5975  CA  ARG D 150     3470   3920   4859   -881    213   -356       C  
ATOM   5976  C   ARG D 150     -22.700 -26.524  -4.974  1.00 36.65           C  
ANISOU 5976  C   ARG D 150     3885   4551   5491   -895    191   -560       C  
ATOM   5977  O   ARG D 150     -22.273 -27.675  -4.859  1.00 35.39           O  
ANISOU 5977  O   ARG D 150     3825   4235   5386   -970    298   -574       O  
ATOM   5978  CB  ARG D 150     -23.659 -25.764  -2.800  1.00 33.18           C  
ANISOU 5978  CB  ARG D 150     3608   3888   5110  -1039    447   -464       C  
ATOM   5979  CG  ARG D 150     -23.326 -25.178  -1.441  1.00 36.79           C  
ANISOU 5979  CG  ARG D 150     4317   4201   5462  -1022    514   -248       C  
ATOM   5980  CD  ARG D 150     -24.033 -25.915  -0.314  1.00 43.40           C  
ANISOU 5980  CD  ARG D 150     5350   4768   6372  -1176    853   -297       C  
ATOM   5981  NE  ARG D 150     -23.590 -25.409   0.980  1.00 49.30           N  
ANISOU 5981  NE  ARG D 150     6411   5380   6941  -1090    882    -83       N  
ATOM   5982  CZ  ARG D 150     -24.182 -24.408   1.623  1.00 55.33           C  
ANISOU 5982  CZ  ARG D 150     7141   6186   7697  -1102    912    -76       C  
ATOM   5983  NH1 ARG D 150     -25.251 -23.828   1.090  1.00 49.64           N  
ANISOU 5983  NH1 ARG D 150     6087   5637   7139  -1175    903   -270       N  
ATOM   5984  NH2 ARG D 150     -23.715 -23.991   2.798  1.00 57.56           N  
ANISOU 5984  NH2 ARG D 150     7722   6354   7794   -992    914     94       N  
ATOM   5985  N   GLN D 151     -23.290 -26.091  -6.077  1.00 37.71           N  
ANISOU 5985  N   GLN D 151     3809   4917   5602   -783     35   -732       N  
ATOM   5986  CA  GLN D 151     -23.506 -26.993  -7.202  1.00 41.22           C  
ANISOU 5986  CA  GLN D 151     4095   5465   6100   -756    -26   -987       C  
ATOM   5987  C   GLN D 151     -22.201 -27.349  -7.899  1.00 39.86           C  
ANISOU 5987  C   GLN D 151     4057   5300   5789   -674    -91   -829       C  
ATOM   5988  O   GLN D 151     -22.150 -28.287  -8.695  1.00 43.22           O  
ANISOU 5988  O   GLN D 151     4397   5765   6258   -673   -112  -1008       O  
ATOM   5989  CB  GLN D 151     -24.500 -26.383  -8.187  1.00 47.29           C  
ANISOU 5989  CB  GLN D 151     4640   6501   6826   -564   -235  -1254       C  
ATOM   5990  CG  GLN D 151     -25.886 -26.193  -7.591  1.00 53.84           C  
ANISOU 5990  CG  GLN D 151     5258   7334   7867   -645   -170  -1524       C  
ATOM   5991  CD  GLN D 151     -26.916 -25.797  -8.625  1.00 67.27           C  
ANISOU 5991  CD  GLN D 151     6764   9280   9515   -372   -412  -1851       C  
ATOM   5992  OE1 GLN D 151     -26.770 -24.780  -9.306  1.00 70.97           O  
ANISOU 5992  OE1 GLN D 151     7263   9958   9745    -96   -680  -1795       O  
ATOM   5993  NE2 GLN D 151     -27.965 -26.605  -8.756  1.00 72.98           N  
ANISOU 5993  NE2 GLN D 151     7317   9965  10446   -400   -309  -2211       N  
ATOM   5994  N   TYR D 152     -21.147 -26.601  -7.587  1.00 33.64           N  
ANISOU 5994  N   TYR D 152     3446   4464   4870   -614   -107   -540       N  
ATOM   5995  CA  TYR D 152     -19.851 -26.796  -8.222  1.00 34.85           C  
ANISOU 5995  CA  TYR D 152     3690   4615   4939   -548   -133   -430       C  
ATOM   5996  C   TYR D 152     -18.922 -27.608  -7.345  1.00 30.99           C  
ANISOU 5996  C   TYR D 152     3317   3917   4541   -640    -60   -345       C  
ATOM   5997  O   TYR D 152     -17.736 -27.738  -7.641  1.00 32.07           O  
ANISOU 5997  O   TYR D 152     3498   4028   4660   -591    -83   -285       O  
ATOM   5998  CB  TYR D 152     -19.234 -25.450  -8.619  1.00 36.62           C  
ANISOU 5998  CB  TYR D 152     4000   4902   5011   -415   -157   -252       C  
ATOM   5999  CG  TYR D 152     -20.029 -24.814  -9.735  1.00 44.76           C  
ANISOU 5999  CG  TYR D 152     5018   6123   5865   -223   -247   -332       C  
ATOM   6000  CD1 TYR D 152     -21.099 -23.970  -9.458  1.00 52.31           C  
ANISOU 6000  CD1 TYR D 152     5934   7152   6788   -148   -318   -367       C  
ATOM   6001  CD2 TYR D 152     -19.754 -25.111 -11.067  1.00 47.75           C  
ANISOU 6001  CD2 TYR D 152     5445   6612   6088    -74   -283   -404       C  
ATOM   6002  CE1 TYR D 152     -21.856 -23.414 -10.478  1.00 58.16           C  
ANISOU 6002  CE1 TYR D 152     6694   8072   7332    113   -461   -478       C  
ATOM   6003  CE2 TYR D 152     -20.501 -24.556 -12.095  1.00 53.10           C  
ANISOU 6003  CE2 TYR D 152     6183   7464   6530    195   -409   -495       C  
ATOM   6004  CZ  TYR D 152     -21.549 -23.705 -11.795  1.00 58.12           C  
ANISOU 6004  CZ  TYR D 152     6787   8172   7124    308   -517   -537       C  
ATOM   6005  OH  TYR D 152     -22.303 -23.150 -12.812  1.00 59.63           O  
ANISOU 6005  OH  TYR D 152     7068   8542   7046    658   -699   -659       O  
ATOM   6006  N   ASN D 153     -19.488 -28.155  -6.274  1.00 29.37           N  
ANISOU 6006  N   ASN D 153     3183   3549   4430   -749     43   -364       N  
ATOM   6007  CA AASN D 153     -18.753 -29.026  -5.359  0.72 29.75           C  
ANISOU 6007  CA AASN D 153     3440   3361   4502   -762    107   -287       C  
ATOM   6008  CA BASN D 153     -18.765 -29.032  -5.355  0.28 30.02           C  
ANISOU 6008  CA BASN D 153     3474   3394   4537   -763    108   -288       C  
ATOM   6009  C   ASN D 153     -17.437 -28.452  -4.871  1.00 31.06           C  
ANISOU 6009  C   ASN D 153     3705   3498   4599   -633    -16   -145       C  
ATOM   6010  O   ASN D 153     -16.382 -29.060  -5.078  1.00 27.70           O  
ANISOU 6010  O   ASN D 153     3312   3022   4190   -559    -83   -169       O  
ATOM   6011  CB AASN D 153     -18.511 -30.388  -6.001  0.72 30.66           C  
ANISOU 6011  CB AASN D 153     3547   3410   4694   -794    150   -416       C  
ATOM   6012  CB BASN D 153     -18.530 -30.397  -6.005  0.28 31.23           C  
ANISOU 6012  CB BASN D 153     3617   3481   4767   -796    152   -419       C  
ATOM   6013  CG AASN D 153     -19.792 -31.131  -6.240  0.72 33.52           C  
ANISOU 6013  CG AASN D 153     3798   3734   5204   -945    313   -635       C  
ATOM   6014  CG BASN D 153     -18.396 -31.518  -4.988  0.28 34.99           C  
ANISOU 6014  CG BASN D 153     4372   3646   5277   -820    304   -382       C  
ATOM   6015  OD1AASN D 153     -20.805 -30.833  -5.608  0.72 38.47           O  
ANISOU 6015  OD1AASN D 153     4410   4308   5897  -1043    445   -681       O  
ATOM   6016  OD1BASN D 153     -18.573 -31.316  -3.785  0.28 38.84           O  
ANISOU 6016  OD1BASN D 153     5092   3966   5701   -801    391   -261       O  
ATOM   6017  ND2AASN D 153     -19.770 -32.094  -7.151  0.72 35.26           N  
ANISOU 6017  ND2AASN D 153     3906   3978   5514   -976    322   -819       N  
ATOM   6018  ND2BASN D 153     -18.100 -32.715  -5.474  0.28 38.16           N  
ANISOU 6018  ND2BASN D 153     4799   3947   5753   -836    354   -483       N  
ATOM   6019  N   PRO D 154     -17.485 -27.270  -4.218  1.00 26.76           N  
ANISOU 6019  N   PRO D 154     3172   2985   4010   -601    -53    -49       N  
ATOM   6020  CA  PRO D 154     -16.239 -26.793  -3.618  1.00 25.68           C  
ANISOU 6020  CA  PRO D 154     3086   2803   3868   -477   -174     -5       C  
ATOM   6021  C   PRO D 154     -15.871 -27.730  -2.476  1.00 26.75           C  
ANISOU 6021  C   PRO D 154     3489   2730   3945   -367   -209      5       C  
ATOM   6022  O   PRO D 154     -16.733 -28.466  -1.989  1.00 28.16           O  
ANISOU 6022  O   PRO D 154     3860   2764   4075   -425    -59     38       O  
ATOM   6023  CB  PRO D 154     -16.615 -25.420  -3.070  1.00 25.72           C  
ANISOU 6023  CB  PRO D 154     3058   2862   3852   -481   -178     67       C  
ATOM   6024  CG  PRO D 154     -18.095 -25.509  -2.784  1.00 26.54           C  
ANISOU 6024  CG  PRO D 154     3205   2958   3923   -584    -57     85       C  
ATOM   6025  CD  PRO D 154     -18.649 -26.444  -3.840  1.00 26.88           C  
ANISOU 6025  CD  PRO D 154     3151   3052   4011   -664      9    -25       C  
ATOM   6026  N   LYS D 155     -14.616 -27.714  -2.047  1.00 29.98           N  
ANISOU 6026  N   LYS D 155     3929   3100   4361   -188   -386    -54       N  
ATOM   6027  CA  LYS D 155     -14.226 -28.532  -0.895  1.00 33.75           C  
ANISOU 6027  CA  LYS D 155     4742   3376   4707     27   -477    -50       C  
ATOM   6028  C   LYS D 155     -14.923 -28.016   0.363  1.00 32.06           C  
ANISOU 6028  C   LYS D 155     4774   3072   4337     77   -428     59       C  
ATOM   6029  O   LYS D 155     -15.319 -28.781   1.244  1.00 32.03           O  
ANISOU 6029  O   LYS D 155     5167   2845   4158    176   -325    144       O  
ATOM   6030  CB  LYS D 155     -12.710 -28.497  -0.713  1.00 36.56           C  
ANISOU 6030  CB  LYS D 155     5015   3752   5124    268   -751   -228       C  
ATOM   6031  CG  LYS D 155     -12.191 -29.238   0.504  1.00 38.38           C  
ANISOU 6031  CG  LYS D 155     5630   3792   5160    614   -938   -260       C  
ATOM   6032  CD  LYS D 155     -10.679 -29.361   0.438  1.00 47.02           C  
ANISOU 6032  CD  LYS D 155     6546   4939   6378    869  -1249   -539       C  
ATOM   6033  CE  LYS D 155     -10.132 -30.152   1.614  1.00 53.47           C  
ANISOU 6033  CE  LYS D 155     7795   5573   6949   1321  -1508   -603       C  
ATOM   6034  NZ  LYS D 155     -10.719 -31.514   1.643  1.00 58.34           N  
ANISOU 6034  NZ  LYS D 155     8855   5940   7371   1346  -1314   -402       N  
ATOM   6035  N   MET D 156     -15.045 -26.698   0.446  1.00 29.03           N  
ANISOU 6035  N   MET D 156     4187   2834   4010     18   -468     56       N  
ATOM   6036  CA  MET D 156     -15.804 -26.050   1.510  1.00 31.43           C  
ANISOU 6036  CA  MET D 156     4664   3088   4191     30   -404    145       C  
ATOM   6037  C   MET D 156     -16.155 -24.660   1.010  1.00 31.44           C  
ANISOU 6037  C   MET D 156     4342   3277   4328   -128   -382    144       C  
ATOM   6038  O   MET D 156     -15.512 -24.130   0.093  1.00 27.89           O  
ANISOU 6038  O   MET D 156     3614   2952   4032   -172   -438     70       O  
ATOM   6039  CB  MET D 156     -15.005 -25.964   2.823  1.00 34.10           C  
ANISOU 6039  CB  MET D 156     5264   3332   4359    355   -629     89       C  
ATOM   6040  CG  MET D 156     -13.961 -24.858   2.859  1.00 36.91           C  
ANISOU 6040  CG  MET D 156     5310   3846   4869    460   -885   -103       C  
ATOM   6041  SD  MET D 156     -13.208 -24.590   4.491  1.00 38.55           S  
ANISOU 6041  SD  MET D 156     5780   3992   4873    890  -1210   -261       S  
ATOM   6042  CE  MET D 156     -12.393 -26.151   4.743  1.00 35.69           C  
ANISOU 6042  CE  MET D 156     5772   3467   4323   1244  -1398   -328       C  
ATOM   6043  N   VAL D 157     -17.200 -24.080   1.578  1.00 27.31           N  
ANISOU 6043  N   VAL D 157     3886   2744   3746   -209   -258    223       N  
ATOM   6044  CA  VAL D 157     -17.546 -22.711   1.241  1.00 24.40           C  
ANISOU 6044  CA  VAL D 157     3270   2522   3479   -306   -252    228       C  
ATOM   6045  C   VAL D 157     -17.903 -21.981   2.528  1.00 28.08           C  
ANISOU 6045  C   VAL D 157     3879   2940   3850   -237   -261    254       C  
ATOM   6046  O   VAL D 157     -18.671 -22.488   3.349  1.00 28.18           O  
ANISOU 6046  O   VAL D 157     4156   2826   3725   -238   -124    314       O  
ATOM   6047  CB  VAL D 157     -18.657 -22.620   0.139  1.00 31.87           C  
ANISOU 6047  CB  VAL D 157     4042   3575   4493   -487   -104    250       C  
ATOM   6048  CG1 VAL D 157     -19.895 -23.421   0.522  1.00 38.83           C  
ANISOU 6048  CG1 VAL D 157     5051   4361   5340   -595     87    243       C  
ATOM   6049  CG2 VAL D 157     -19.002 -21.159  -0.169  1.00 24.38           C  
ANISOU 6049  CG2 VAL D 157     2919   2745   3599   -513   -110    272       C  
ATOM   6050  N   LYS D 158     -17.278 -20.820   2.728  1.00 24.35           N  
ANISOU 6050  N   LYS D 158     3248   2539   3464   -175   -390    187       N  
ATOM   6051  CA  LYS D 158     -17.469 -20.020   3.927  1.00 23.12           C  
ANISOU 6051  CA  LYS D 158     3192   2359   3233    -86   -439    170       C  
ATOM   6052  C   LYS D 158     -17.718 -18.593   3.499  1.00 26.38           C  
ANISOU 6052  C   LYS D 158     3342   2870   3813   -199   -395    164       C  
ATOM   6053  O   LYS D 158     -17.260 -18.174   2.434  1.00 26.14           O  
ANISOU 6053  O   LYS D 158     3093   2892   3945   -271   -367    141       O  
ATOM   6054  CB  LYS D 158     -16.222 -20.037   4.820  1.00 24.88           C  
ANISOU 6054  CB  LYS D 158     3496   2546   3412    183   -700      1       C  
ATOM   6055  CG  LYS D 158     -15.776 -21.402   5.313  1.00 34.82           C  
ANISOU 6055  CG  LYS D 158     5088   3684   4460    403   -800     -6       C  
ATOM   6056  CD  LYS D 158     -16.747 -21.963   6.319  1.00 40.65           C  
ANISOU 6056  CD  LYS D 158     6282   4262   4902    463   -632    152       C  
ATOM   6057  CE  LYS D 158     -16.160 -23.171   7.028  1.00 46.07           C  
ANISOU 6057  CE  LYS D 158     7421   4771   5312    786   -742    148       C  
ATOM   6058  NZ  LYS D 158     -17.121 -23.676   8.033  1.00 50.21           N  
ANISOU 6058  NZ  LYS D 158     8476   5072   5529    839   -473    322       N  
ATOM   6059  N   VAL D 159     -18.436 -17.847   4.330  1.00 21.97           N  
ANISOU 6059  N   VAL D 159     2843   2305   3200   -201   -355    188       N  
ATOM   6060  CA  VAL D 159     -18.748 -16.462   4.009  1.00 21.23           C  
ANISOU 6060  CA  VAL D 159     2543   2272   3251   -284   -304    190       C  
ATOM   6061  C   VAL D 159     -18.198 -15.550   5.087  1.00 24.35           C  
ANISOU 6061  C   VAL D 159     2920   2644   3686   -170   -424     60       C  
ATOM   6062  O   VAL D 159     -18.433 -15.793   6.278  1.00 23.25           O  
ANISOU 6062  O   VAL D 159     3001   2467   3367    -51   -484     39       O  
ATOM   6063  CB  VAL D 159     -20.266 -16.247   3.898  1.00 25.28           C  
ANISOU 6063  CB  VAL D 159     3069   2819   3716   -396   -150    286       C  
ATOM   6064  CG1 VAL D 159     -20.587 -14.776   3.642  1.00 22.93           C  
ANISOU 6064  CG1 VAL D 159     2612   2564   3537   -419   -122    291       C  
ATOM   6065  CG2 VAL D 159     -20.831 -17.130   2.794  1.00 26.70           C  
ANISOU 6065  CG2 VAL D 159     3209   3044   3892   -484    -67    326       C  
ATOM   6066  N   ALA D 160     -17.455 -14.515   4.673  1.00 21.14           N  
ANISOU 6066  N   ALA D 160     2276   2238   3517   -198   -429    -50       N  
ATOM   6067  CA  ALA D 160     -17.029 -13.458   5.586  1.00 23.29           C  
ANISOU 6067  CA  ALA D 160     2455   2491   3905   -123   -516   -230       C  
ATOM   6068  C   ALA D 160     -17.800 -12.210   5.192  1.00 27.05           C  
ANISOU 6068  C   ALA D 160     2837   2950   4492   -252   -334   -130       C  
ATOM   6069  O   ALA D 160     -17.828 -11.826   4.016  1.00 25.00           O  
ANISOU 6069  O   ALA D 160     2495   2660   4346   -353   -168    -36       O  
ATOM   6070  CB  ALA D 160     -15.529 -13.207   5.501  1.00 23.59           C  
ANISOU 6070  CB  ALA D 160     2256   2497   4211    -65   -620   -522       C  
ATOM   6071  N   SER D 161     -18.441 -11.577   6.164  1.00 24.19           N  
ANISOU 6071  N   SER D 161     2530   2594   4065   -214   -360   -147       N  
ATOM   6072  CA  SER D 161     -19.184 -10.358   5.885  1.00 22.99           C  
ANISOU 6072  CA  SER D 161     2301   2417   4017   -298   -212    -72       C  
ATOM   6073  C   SER D 161     -18.714  -9.296   6.850  1.00 26.97           C  
ANISOU 6073  C   SER D 161     2698   2874   4675   -246   -275   -281       C  
ATOM   6074  O   SER D 161     -18.646  -9.543   8.060  1.00 26.68           O  
ANISOU 6074  O   SER D 161     2756   2879   4502   -117   -443   -405       O  
ATOM   6075  CB  SER D 161     -20.699 -10.584   6.043  1.00 23.52           C  
ANISOU 6075  CB  SER D 161     2499   2546   3891   -327   -152     83       C  
ATOM   6076  OG  SER D 161     -21.416  -9.402   5.721  1.00 27.01           O  
ANISOU 6076  OG  SER D 161     2865   2970   4429   -356    -52    131       O  
ATOM   6077  N   LEU D 162     -18.368  -8.118   6.338  1.00 23.13           N  
ANISOU 6077  N   LEU D 162     2046   2280   4462   -324   -123   -338       N  
ATOM   6078  CA  LEU D 162     -17.889  -7.070   7.225  1.00 22.73           C  
ANISOU 6078  CA  LEU D 162     1844   2168   4623   -295   -162   -595       C  
ATOM   6079  C   LEU D 162     -18.945  -6.754   8.273  1.00 26.75           C  
ANISOU 6079  C   LEU D 162     2476   2748   4940   -228   -242   -552       C  
ATOM   6080  O   LEU D 162     -18.628  -6.625   9.461  1.00 23.59           O  
ANISOU 6080  O   LEU D 162     2067   2387   4509   -105   -421   -775       O  
ATOM   6081  CB  LEU D 162     -17.562  -5.785   6.473  1.00 22.71           C  
ANISOU 6081  CB  LEU D 162     1699   1973   4957   -420    119   -628       C  
ATOM   6082  CG  LEU D 162     -17.177  -4.647   7.423  1.00 25.91           C  
ANISOU 6082  CG  LEU D 162     1920   2299   5626   -412    104   -930       C  
ATOM   6083  CD1 LEU D 162     -15.872  -4.953   8.161  1.00 28.10           C  
ANISOU 6083  CD1 LEU D 162     2016   2636   6025   -291   -100  -1330       C  
ATOM   6084  CD2 LEU D 162     -17.086  -3.315   6.696  1.00 29.45           C  
ANISOU 6084  CD2 LEU D 162     2377   2551   6260   -472    457   -874       C  
ATOM   6085  N   LEU D 163     -20.193  -6.633   7.818  1.00 23.81           N  
ANISOU 6085  N   LEU D 163     2213   2395   4438   -283   -117   -305       N  
ATOM   6086  CA  LEU D 163     -21.294  -6.203   8.676  1.00 24.32           C  
ANISOU 6086  CA  LEU D 163     2353   2506   4381   -254   -124   -284       C  
ATOM   6087  C   LEU D 163     -22.440  -7.196   8.609  1.00 24.37           C  
ANISOU 6087  C   LEU D 163     2519   2607   4135   -272    -95   -119       C  
ATOM   6088  O   LEU D 163     -22.719  -7.771   7.553  1.00 23.32           O  
ANISOU 6088  O   LEU D 163     2391   2497   3972   -319    -39     15       O  
ATOM   6089  CB  LEU D 163     -21.810  -4.818   8.253  1.00 26.47           C  
ANISOU 6089  CB  LEU D 163     2537   2682   4837   -294     25   -243       C  
ATOM   6090  CG  LEU D 163     -20.815  -3.661   8.126  1.00 27.28           C  
ANISOU 6090  CG  LEU D 163     2481   2612   5273   -329    126   -405       C  
ATOM   6091  CD1 LEU D 163     -21.507  -2.395   7.628  1.00 29.78           C  
ANISOU 6091  CD1 LEU D 163     2818   2790   5706   -337    317   -297       C  
ATOM   6092  CD2 LEU D 163     -20.104  -3.376   9.441  1.00 29.82           C  
ANISOU 6092  CD2 LEU D 163     2680   2953   5697   -273    -33   -725       C  
ATOM   6093  N   VAL D 164     -23.099  -7.404   9.740  1.00 23.39           N  
ANISOU 6093  N   VAL D 164     2526   2520   3842   -235   -103   -163       N  
ATOM   6094  CA  VAL D 164     -24.334  -8.185   9.770  1.00 24.91           C  
ANISOU 6094  CA  VAL D 164     2831   2754   3880   -300     24    -72       C  
ATOM   6095  C   VAL D 164     -25.345  -7.339  10.507  1.00 29.82           C  
ANISOU 6095  C   VAL D 164     3428   3382   4522   -312    110   -141       C  
ATOM   6096  O   VAL D 164     -25.066  -6.876  11.615  1.00 28.62           O  
ANISOU 6096  O   VAL D 164     3357   3207   4309   -233     63   -245       O  
ATOM   6097  CB  VAL D 164     -24.170  -9.511  10.527  1.00 30.33           C  
ANISOU 6097  CB  VAL D 164     3796   3415   4314   -256     43    -61       C  
ATOM   6098  CG1 VAL D 164     -25.543 -10.135  10.847  1.00 33.54           C  
ANISOU 6098  CG1 VAL D 164     4323   3799   4623   -364    290    -36       C  
ATOM   6099  CG2 VAL D 164     -23.329 -10.474   9.739  1.00 25.74           C  
ANISOU 6099  CG2 VAL D 164     3233   2831   3717   -246    -34      1       C  
ATOM   6100  N   LYS D 165     -26.506  -7.125   9.888  1.00 31.35           N  
ANISOU 6100  N   LYS D 165     3495   3615   4803   -380    209   -124       N  
ATOM   6101  CA  LYS D 165     -27.560  -6.301  10.488  1.00 36.99           C  
ANISOU 6101  CA  LYS D 165     4136   4340   5577   -390    292   -225       C  
ATOM   6102  C   LYS D 165     -28.484  -7.118  11.379  1.00 37.80           C  
ANISOU 6102  C   LYS D 165     4372   4434   5558   -478    500   -301       C  
ATOM   6103  O   LYS D 165     -28.925  -8.210  10.995  1.00 36.80           O  
ANISOU 6103  O   LYS D 165     4272   4306   5404   -570    625   -296       O  
ATOM   6104  CB  LYS D 165     -28.397  -5.614   9.401  1.00 38.93           C  
ANISOU 6104  CB  LYS D 165     4173   4633   5986   -360    268   -234       C  
ATOM   6105  CG  LYS D 165     -28.050  -4.162   9.195  1.00 43.58           C  
ANISOU 6105  CG  LYS D 165     4696   5156   6708   -260    195   -216       C  
ATOM   6106  CD  LYS D 165     -29.056  -3.448   8.291  1.00 41.18           C  
ANISOU 6106  CD  LYS D 165     4273   4879   6494   -144    161   -236       C  
ATOM   6107  CE  LYS D 165     -28.443  -2.163   7.782  1.00 35.99           C  
ANISOU 6107  CE  LYS D 165     3660   4078   5936    -25    145   -141       C  
ATOM   6108  NZ  LYS D 165     -29.331  -1.388   6.882  1.00 31.94           N  
ANISOU 6108  NZ  LYS D 165     3135   3554   5445    182     89   -135       N  
ATOM   6109  N   ARG D 166     -28.770  -6.601  12.573  1.00 42.83           N  
ANISOU 6109  N   ARG D 166     3679   5755   6841   -359   1166   -489       N  
ATOM   6110  CA  ARG D 166     -29.837  -7.167  13.391  1.00 44.72           C  
ANISOU 6110  CA  ARG D 166     3812   6062   7118   -479   1350   -530       C  
ATOM   6111  C   ARG D 166     -31.164  -6.665  12.840  1.00 48.16           C  
ANISOU 6111  C   ARG D 166     3897   6692   7710   -406   1362   -536       C  
ATOM   6112  O   ARG D 166     -31.457  -5.471  12.916  1.00 48.36           O  
ANISOU 6112  O   ARG D 166     3836   6736   7802   -203   1403   -524       O  
ATOM   6113  CB  ARG D 166     -29.704  -6.738  14.853  1.00 44.84           C  
ANISOU 6113  CB  ARG D 166     4002   5968   7068   -447   1549   -549       C  
ATOM   6114  CG  ARG D 166     -28.471  -7.271  15.583  1.00 38.86           C  
ANISOU 6114  CG  ARG D 166     3580   5035   6149   -529   1535   -533       C  
ATOM   6115  CD  ARG D 166     -28.603  -6.997  17.091  1.00 38.13           C  
ANISOU 6115  CD  ARG D 166     3655   4857   5975   -543   1746   -559       C  
ATOM   6116  NE  ARG D 166     -28.558  -5.566  17.380  1.00 36.61           N  
ANISOU 6116  NE  ARG D 166     3486   4628   5795   -356   1794   -569       N  
ATOM   6117  CZ  ARG D 166     -27.438  -4.855  17.431  1.00 39.27           C  
ANISOU 6117  CZ  ARG D 166     4022   4849   6052   -273   1685   -544       C  
ATOM   6118  NH1 ARG D 166     -26.271  -5.449  17.213  1.00 31.49           N  
ANISOU 6118  NH1 ARG D 166     3190   3794   4980   -343   1523   -502       N  
ATOM   6119  NH2 ARG D 166     -27.483  -3.556  17.700  1.00 43.71           N  
ANISOU 6119  NH2 ARG D 166     4626   5361   6620   -120   1744   -560       N  
ATOM   6120  N   THR D 167     -31.962  -7.567  12.278  1.00 53.47           N  
ANISOU 6120  N   THR D 167     4371   7504   8440   -570   1321   -552       N  
ATOM   6121  CA  THR D 167     -33.249  -7.191  11.692  1.00 56.75           C  
ANISOU 6121  CA  THR D 167     4411   8139   9012   -518   1300   -548       C  
ATOM   6122  C   THR D 167     -34.275  -8.305  11.856  1.00 59.12           C  
ANISOU 6122  C   THR D 167     4563   8568   9331   -759   1360   -568       C  
ATOM   6123  O   THR D 167     -33.930  -9.485  11.804  1.00 57.73           O  
ANISOU 6123  O   THR D 167     4526   8330   9080   -990   1342   -599       O  
ATOM   6124  CB  THR D 167     -33.114  -6.819  10.191  1.00 58.58           C  
ANISOU 6124  CB  THR D 167     4538   8449   9271   -426   1033   -504       C  
ATOM   6125  OG1 THR D 167     -34.412  -6.775   9.579  1.00 60.31           O  
ANISOU 6125  OG1 THR D 167     4421   8898   9597   -428    960   -478       O  
ATOM   6126  CG2 THR D 167     -32.259  -7.841   9.460  1.00 56.47           C  
ANISOU 6126  CG2 THR D 167     4472   8102   8883   -596    877   -510       C  
ATOM   6127  N   PRO D 168     -35.546  -7.931  12.073  1.00 63.70           N  
ANISOU 6127  N   PRO D 168     4895   9316   9991   -696   1428   -536       N  
ATOM   6128  CA  PRO D 168     -36.619  -8.931  12.110  1.00 65.66           C  
ANISOU 6128  CA  PRO D 168     4986   9705  10254   -922   1451   -527       C  
ATOM   6129  C   PRO D 168     -36.875  -9.565  10.731  1.00 65.51           C  
ANISOU 6129  C   PRO D 168     4837   9805  10250  -1060   1195   -504       C  
ATOM   6130  O   PRO D 168     -37.408 -10.675  10.657  1.00 62.82           O  
ANISOU 6130  O   PRO D 168     4468   9510   9890  -1316   1185   -513       O  
ATOM   6131  CB  PRO D 168     -37.839  -8.122  12.578  1.00 70.12           C  
ANISOU 6131  CB  PRO D 168     5284  10437  10922   -761   1575   -482       C  
ATOM   6132  CG  PRO D 168     -37.515  -6.694  12.236  1.00 68.57           C  
ANISOU 6132  CG  PRO D 168     5057  10224  10771   -439   1516   -455       C  
ATOM   6133  CD  PRO D 168     -36.030  -6.577  12.401  1.00 64.28           C  
ANISOU 6133  CD  PRO D 168     4843   9440  10141   -415   1511   -504       C  
ATOM   6134  N   ARG D 169     -36.488  -8.868   9.661  1.00 67.32           N  
ANISOU 6134  N   ARG D 169     5013  10063  10502   -902    992   -476       N  
ATOM   6135  CA  ARG D 169     -36.649  -9.367   8.293  1.00 69.27           C  
ANISOU 6135  CA  ARG D 169     5170  10410  10742  -1022    736   -459       C  
ATOM   6136  C   ARG D 169     -35.625 -10.445   7.928  1.00 68.91           C  
ANISOU 6136  C   ARG D 169     5403  10206  10572  -1235    673   -531       C  
ATOM   6137  O   ARG D 169     -35.570 -10.890   6.779  1.00 68.61           O  
ANISOU 6137  O   ARG D 169     5359  10215  10495  -1343    468   -538       O  
ATOM   6138  CB  ARG D 169     -36.524  -8.226   7.278  1.00 71.26           C  
ANISOU 6138  CB  ARG D 169     5307  10732  11037   -773    543   -402       C  
ATOM   6139  CG  ARG D 169     -37.765  -7.368   7.070  1.00 78.90           C  
ANISOU 6139  CG  ARG D 169     5943  11910  12125   -598    503   -303       C  
ATOM   6140  CD  ARG D 169     -37.417  -6.180   6.181  1.00 81.75           C  
ANISOU 6140  CD  ARG D 169     6279  12284  12498   -325    333   -247       C  
ATOM   6141  NE  ARG D 169     -36.144  -5.591   6.590  1.00 81.19           N  
ANISOU 6141  NE  ARG D 169     6483  11990  12375   -179    418   -297       N  
ATOM   6142  CZ  ARG D 169     -35.210  -5.153   5.752  1.00 79.25           C  
ANISOU 6142  CZ  ARG D 169     6375  11649  12086    -83    261   -293       C  
ATOM   6143  NH1 ARG D 169     -35.407  -5.228   4.442  1.00 79.38           N  
ANISOU 6143  NH1 ARG D 169     6298  11780  12083   -110      8   -253       N  
ATOM   6144  NH2 ARG D 169     -34.077  -4.641   6.227  1.00 75.33           N  
ANISOU 6144  NH2 ARG D 169     6123  10940  11558     30    353   -320       N  
ATOM   6145  N   SER D 170     -34.803 -10.847   8.894  1.00 67.13           N  
ANISOU 6145  N   SER D 170     5438   9791  10278  -1287    848   -580       N  
ATOM   6146  CA  SER D 170     -33.782 -11.870   8.662  1.00 65.24           C  
ANISOU 6146  CA  SER D 170     5482   9383   9923  -1464    818   -636       C  
ATOM   6147  C   SER D 170     -34.403 -13.247   8.411  1.00 64.09           C  
ANISOU 6147  C   SER D 170     5369   9262   9721  -1768    790   -661       C  
ATOM   6148  O   SER D 170     -35.295 -13.675   9.144  1.00 63.35           O  
ANISOU 6148  O   SER D 170     5200   9219   9652  -1884    916   -651       O  
ATOM   6149  CB  SER D 170     -32.822 -11.939   9.852  1.00 65.70           C  
ANISOU 6149  CB  SER D 170     5844   9221   9898  -1411    994   -637       C  
ATOM   6150  OG  SER D 170     -31.903 -13.005   9.712  1.00 67.56           O  
ANISOU 6150  OG  SER D 170     6397   9275   9998  -1540    959   -651       O  
ATOM   6151  N   VAL D 171     -33.931 -13.933   7.370  1.00 63.25           N  
ANISOU 6151  N   VAL D 171     5391   9109   9533  -1899    632   -697       N  
ATOM   6152  CA  VAL D 171     -34.407 -15.286   7.069  1.00 64.82           C  
ANISOU 6152  CA  VAL D 171     5686   9286   9657  -2195    600   -731       C  
ATOM   6153  C   VAL D 171     -33.654 -16.295   7.926  1.00 60.63           C  
ANISOU 6153  C   VAL D 171     5502   8514   9021  -2324    770   -766       C  
ATOM   6154  O   VAL D 171     -33.947 -17.494   7.907  1.00 62.43           O  
ANISOU 6154  O   VAL D 171     5881   8666   9172  -2561    789   -794       O  
ATOM   6155  CB  VAL D 171     -34.230 -15.660   5.580  1.00 65.16           C  
ANISOU 6155  CB  VAL D 171     5774   9356   9626  -2295    367   -762       C  
ATOM   6156  CG1 VAL D 171     -34.945 -14.658   4.677  1.00 67.06           C  
ANISOU 6156  CG1 VAL D 171     5694   9829   9956  -2159    171   -711       C  
ATOM   6157  CG2 VAL D 171     -32.742 -15.777   5.224  1.00 62.11           C  
ANISOU 6157  CG2 VAL D 171     5720   8757   9123  -2200    344   -782       C  
ATOM   6158  N   GLY D 172     -32.669 -15.798   8.666  1.00 55.67           N  
ANISOU 6158  N   GLY D 172     5023   7748   8380  -2150    880   -752       N  
ATOM   6159  CA  GLY D 172     -31.939 -16.626   9.601  1.00 55.62           C  
ANISOU 6159  CA  GLY D 172     5356   7508   8269  -2213   1028   -751       C  
ATOM   6160  C   GLY D 172     -30.550 -17.033   9.148  1.00 53.96           C  
ANISOU 6160  C   GLY D 172     5481   7083   7936  -2113    943   -734       C  
ATOM   6161  O   GLY D 172     -29.916 -17.855   9.815  1.00 56.08           O  
ANISOU 6161  O   GLY D 172     6043   7150   8114  -2163   1041   -725       O  
ATOM   6162  N   TYR D 173     -30.067 -16.481   8.031  1.00 44.64           N  
ANISOU 6162  N   TYR D 173     4264   5944   6752  -1968    770   -724       N  
ATOM   6163  CA  TYR D 173     -28.695 -16.788   7.594  1.00 42.40           C  
ANISOU 6163  CA  TYR D 173     4274   5471   6366  -1849    713   -705       C  
ATOM   6164  C   TYR D 173     -27.632 -16.055   8.408  1.00 43.47           C  
ANISOU 6164  C   TYR D 173     4509   5510   6497  -1605    766   -640       C  
ATOM   6165  O   TYR D 173     -27.670 -14.835   8.530  1.00 48.86           O  
ANISOU 6165  O   TYR D 173     5021   6296   7248  -1437    741   -609       O  
ATOM   6166  CB  TYR D 173     -28.445 -16.499   6.101  1.00 40.16           C  
ANISOU 6166  CB  TYR D 173     3955   5248   6055  -1789    529   -716       C  
ATOM   6167  CG  TYR D 173     -26.992 -16.770   5.763  1.00 38.30           C  
ANISOU 6167  CG  TYR D 173     4004   4823   5726  -1648    514   -693       C  
ATOM   6168  CD1 TYR D 173     -26.535 -18.073   5.611  1.00 42.05           C  
ANISOU 6168  CD1 TYR D 173     4764   5112   6102  -1764    560   -727       C  
ATOM   6169  CD2 TYR D 173     -26.070 -15.740   5.656  1.00 38.61           C  
ANISOU 6169  CD2 TYR D 173     4027   4860   5782  -1398    472   -636       C  
ATOM   6170  CE1 TYR D 173     -25.206 -18.343   5.347  1.00 37.94           C  
ANISOU 6170  CE1 TYR D 173     4479   4424   5513  -1610    567   -701       C  
ATOM   6171  CE2 TYR D 173     -24.734 -16.001   5.389  1.00 36.86           C  
ANISOU 6171  CE2 TYR D 173     4028   4486   5492  -1273    473   -610       C  
ATOM   6172  CZ  TYR D 173     -24.320 -17.309   5.234  1.00 37.51           C  
ANISOU 6172  CZ  TYR D 173     4365   4401   5489  -1368    523   -642       C  
ATOM   6173  OH  TYR D 173     -23.009 -17.588   4.973  1.00 37.01           O  
ANISOU 6173  OH  TYR D 173     4496   4193   5372  -1221    540   -612       O  
ATOM   6174  N   LYS D 174     -26.657 -16.798   8.922  1.00 44.68           N  
ANISOU 6174  N   LYS D 174     4948   5462   6565  -1585    827   -617       N  
ATOM   6175  CA  LYS D 174     -25.513 -16.193   9.600  1.00 44.28           C  
ANISOU 6175  CA  LYS D 174     5003   5324   6498  -1371    841   -550       C  
ATOM   6176  C   LYS D 174     -24.214 -16.573   8.891  1.00 33.44           C  
ANISOU 6176  C   LYS D 174     3821   3823   5062  -1254    767   -525       C  
ATOM   6177  O   LYS D 174     -23.994 -17.742   8.569  1.00 36.12           O  
ANISOU 6177  O   LYS D 174     4356   4033   5336  -1346    786   -547       O  
ATOM   6178  CB  LYS D 174     -25.460 -16.622  11.068  1.00 52.13           C  
ANISOU 6178  CB  LYS D 174     6148   6209   7449  -1419    982   -523       C  
ATOM   6179  CG  LYS D 174     -26.646 -16.152  11.902  1.00 57.70           C  
ANISOU 6179  CG  LYS D 174     6675   7036   8214  -1510   1097   -544       C  
ATOM   6180  CD  LYS D 174     -26.646 -16.794  13.287  1.00 62.66           C  
ANISOU 6180  CD  LYS D 174     7505   7536   8766  -1602   1252   -522       C  
ATOM   6181  CE  LYS D 174     -27.880 -16.395  14.094  1.00 67.02           C  
ANISOU 6181  CE  LYS D 174     7881   8211   9372  -1707   1404   -552       C  
ATOM   6182  NZ  LYS D 174     -28.158 -17.344  15.221  1.00 70.68           N  
ANISOU 6182  NZ  LYS D 174     8552   8554   9748  -1885   1573   -545       N  
ATOM   6183  N   PRO D 175     -23.345 -15.583   8.641  1.00 30.94           N  
ANISOU 6183  N   PRO D 175     3452   3536   4766  -1053    695   -480       N  
ATOM   6184  CA  PRO D 175     -22.102 -15.885   7.925  1.00 28.15           C  
ANISOU 6184  CA  PRO D 175     3243   3085   4368   -936    643   -454       C  
ATOM   6185  C   PRO D 175     -21.095 -16.550   8.857  1.00 30.53           C  
ANISOU 6185  C   PRO D 175     3754   3222   4623   -868    702   -396       C  
ATOM   6186  O   PRO D 175     -21.293 -16.568  10.067  1.00 33.16           O  
ANISOU 6186  O   PRO D 175     4125   3527   4948   -900    764   -370       O  
ATOM   6187  CB  PRO D 175     -21.605 -14.503   7.491  1.00 28.92           C  
ANISOU 6187  CB  PRO D 175     3192   3285   4511   -770    561   -418       C  
ATOM   6188  CG  PRO D 175     -22.171 -13.567   8.482  1.00 29.79           C  
ANISOU 6188  CG  PRO D 175     3173   3474   4673   -754    594   -403       C  
ATOM   6189  CD  PRO D 175     -23.494 -14.144   8.916  1.00 29.54           C  
ANISOU 6189  CD  PRO D 175     3087   3480   4656   -933    669   -454       C  
ATOM   6190  N   ASP D 176     -20.028 -17.094   8.293  1.00 29.78           N  
ANISOU 6190  N   ASP D 176     3796   3024   4494   -767    684   -372       N  
ATOM   6191  CA  ASP D 176     -19.054 -17.822   9.083  1.00 30.98           C  
ANISOU 6191  CA  ASP D 176     4141   3023   4609   -679    724   -306       C  
ATOM   6192  C   ASP D 176     -18.103 -16.876   9.796  1.00 31.55           C  
ANISOU 6192  C   ASP D 176     4137   3141   4710   -519    674   -223       C  
ATOM   6193  O   ASP D 176     -17.651 -17.156  10.902  1.00 30.86           O  
ANISOU 6193  O   ASP D 176     4157   2976   4591   -483    688   -159       O  
ATOM   6194  CB  ASP D 176     -18.287 -18.778   8.176  1.00 30.19           C  
ANISOU 6194  CB  ASP D 176     4204   2795   4472   -610    740   -312       C  
ATOM   6195  CG  ASP D 176     -19.203 -19.719   7.442  1.00 35.94           C  
ANISOU 6195  CG  ASP D 176     5043   3463   5151   -795    782   -404       C  
ATOM   6196  OD1 ASP D 176     -19.575 -20.744   8.038  1.00 36.61           O  
ANISOU 6196  OD1 ASP D 176     5312   3411   5187   -909    856   -413       O  
ATOM   6197  OD2 ASP D 176     -19.568 -19.421   6.284  1.00 30.96           O  
ANISOU 6197  OD2 ASP D 176     4327   2919   4517   -842    736   -466       O  
ATOM   6198  N   PHE D 177     -17.819 -15.743   9.160  1.00 25.92           N  
ANISOU 6198  N   PHE D 177     3254   2550   4045   -438    607   -221       N  
ATOM   6199  CA  PHE D 177     -16.926 -14.747   9.738  1.00 25.05           C  
ANISOU 6199  CA  PHE D 177     3068   2490   3960   -318    551   -151       C  
ATOM   6200  C   PHE D 177     -17.630 -13.396   9.695  1.00 29.51           C  
ANISOU 6200  C   PHE D 177     3463   3187   4565   -347    522   -180       C  
ATOM   6201  O   PHE D 177     -18.157 -13.016   8.647  1.00 28.89           O  
ANISOU 6201  O   PHE D 177     3283   3183   4511   -366    500   -226       O  
ATOM   6202  CB  PHE D 177     -15.628 -14.695   8.928  1.00 25.79           C  
ANISOU 6202  CB  PHE D 177     3144   2581   4076   -173    511   -107       C  
ATOM   6203  CG  PHE D 177     -14.948 -16.034   8.785  1.00 28.11           C  
ANISOU 6203  CG  PHE D 177     3600   2738   4343   -107    556    -81       C  
ATOM   6204  CD1 PHE D 177     -14.245 -16.584   9.857  1.00 27.20           C  
ANISOU 6204  CD1 PHE D 177     3589   2536   4209    -36    550      0       C  
ATOM   6205  CD2 PHE D 177     -15.031 -16.750   7.600  1.00 26.34           C  
ANISOU 6205  CD2 PHE D 177     3447   2461   4100   -112    605   -136       C  
ATOM   6206  CE1 PHE D 177     -13.631 -17.815   9.746  1.00 28.69           C  
ANISOU 6206  CE1 PHE D 177     3939   2584   4379     54    596     34       C  
ATOM   6207  CE2 PHE D 177     -14.410 -17.983   7.476  1.00 30.13           C  
ANISOU 6207  CE2 PHE D 177     4105   2788   4553    -33    667   -117       C  
ATOM   6208  CZ  PHE D 177     -13.709 -18.516   8.558  1.00 29.20           C  
ANISOU 6208  CZ  PHE D 177     4080   2581   4435     62    665    -28       C  
ATOM   6209  N   VAL D 178     -17.645 -12.669  10.814  1.00 24.12           N  
ANISOU 6209  N   VAL D 178     2766   2522   3876   -345    521   -153       N  
ATOM   6210  CA  VAL D 178     -18.398 -11.422  10.894  1.00 25.77           C  
ANISOU 6210  CA  VAL D 178     2845   2828   4120   -358    521   -184       C  
ATOM   6211  C   VAL D 178     -17.541 -10.331  11.491  1.00 25.88           C  
ANISOU 6211  C   VAL D 178     2854   2853   4128   -284    469   -134       C  
ATOM   6212  O   VAL D 178     -17.002 -10.509  12.582  1.00 25.87           O  
ANISOU 6212  O   VAL D 178     2959   2796   4075   -288    465    -92       O  
ATOM   6213  CB  VAL D 178     -19.605 -11.575  11.833  1.00 29.45           C  
ANISOU 6213  CB  VAL D 178     3321   3295   4573   -465    615   -225       C  
ATOM   6214  CG1 VAL D 178     -20.422 -10.296  11.852  1.00 28.92           C  
ANISOU 6214  CG1 VAL D 178     3109   3323   4556   -445    633   -258       C  
ATOM   6215  CG2 VAL D 178     -20.461 -12.730  11.422  1.00 38.01           C  
ANISOU 6215  CG2 VAL D 178     4422   4363   5656   -583    669   -273       C  
ATOM   6216  N   GLY D 179     -17.434  -9.191  10.817  1.00 22.96           N  
ANISOU 6216  N   GLY D 179     2379   2548   3796   -230    424   -136       N  
ATOM   6217  CA  GLY D 179     -16.699  -8.080  11.385  1.00 23.47           C  
ANISOU 6217  CA  GLY D 179     2456   2614   3849   -192    379    -98       C  
ATOM   6218  C   GLY D 179     -17.466  -7.448  12.533  1.00 28.13           C  
ANISOU 6218  C   GLY D 179     3090   3189   4410   -233    440   -128       C  
ATOM   6219  O   GLY D 179     -17.025  -7.497  13.690  1.00 24.79           O  
ANISOU 6219  O   GLY D 179     2783   2715   3920   -264    439   -103       O  
ATOM   6220  N   PHE D 180     -18.628  -6.870  12.207  1.00 24.50           N  
ANISOU 6220  N   PHE D 180     2539   2775   3996   -226    496   -180       N  
ATOM   6221  CA  PHE D 180     -19.420  -6.105  13.157  1.00 24.05           C  
ANISOU 6221  CA  PHE D 180     2506   2706   3926   -234    583   -215       C  
ATOM   6222  C   PHE D 180     -20.892  -6.468  13.048  1.00 28.53           C  
ANISOU 6222  C   PHE D 180     2964   3331   4547   -263    682   -270       C  
ATOM   6223  O   PHE D 180     -21.405  -6.695  11.949  1.00 30.33           O  
ANISOU 6223  O   PHE D 180     3058   3630   4836   -252    648   -283       O  
ATOM   6224  CB  PHE D 180     -19.230  -4.604  12.895  1.00 23.77           C  
ANISOU 6224  CB  PHE D 180     2454   2669   3909   -157    552   -211       C  
ATOM   6225  CG  PHE D 180     -17.805  -4.156  12.993  1.00 23.06           C  
ANISOU 6225  CG  PHE D 180     2451   2538   3773   -160    455   -159       C  
ATOM   6226  CD1 PHE D 180     -16.921  -4.337  11.934  1.00 22.39           C  
ANISOU 6226  CD1 PHE D 180     2306   2486   3716   -136    364   -115       C  
ATOM   6227  CD2 PHE D 180     -17.338  -3.562  14.166  1.00 24.14           C  
ANISOU 6227  CD2 PHE D 180     2730   2610   3831   -201    458   -154       C  
ATOM   6228  CE1 PHE D 180     -15.595  -3.935  12.044  1.00 22.91           C  
ANISOU 6228  CE1 PHE D 180     2416   2537   3754   -151    282    -62       C  
ATOM   6229  CE2 PHE D 180     -16.023  -3.160  14.290  1.00 23.37           C  
ANISOU 6229  CE2 PHE D 180     2692   2495   3693   -231    351   -104       C  
ATOM   6230  CZ  PHE D 180     -15.144  -3.336  13.231  1.00 24.21           C  
ANISOU 6230  CZ  PHE D 180     2700   2650   3848   -206    265    -54       C  
ATOM   6231  N   GLU D 181     -21.571  -6.544  14.186  1.00 26.98           N  
ANISOU 6231  N   GLU D 181     2823   3110   4318   -313    805   -302       N  
ATOM   6232  CA  GLU D 181     -23.013  -6.727  14.169  1.00 27.52           C  
ANISOU 6232  CA  GLU D 181     2751   3254   4452   -343    919   -353       C  
ATOM   6233  C   GLU D 181     -23.650  -5.389  14.527  1.00 32.04           C  
ANISOU 6233  C   GLU D 181     3271   3840   5062   -243   1002   -380       C  
ATOM   6234  O   GLU D 181     -23.386  -4.825  15.595  1.00 32.32           O  
ANISOU 6234  O   GLU D 181     3461   3794   5023   -236   1074   -388       O  
ATOM   6235  CB  GLU D 181     -23.447  -7.816  15.150  1.00 29.13           C  
ANISOU 6235  CB  GLU D 181     3045   3424   4600   -475   1037   -371       C  
ATOM   6236  CG  GLU D 181     -24.912  -8.225  14.986  1.00 30.83           C  
ANISOU 6236  CG  GLU D 181     3079   3740   4896   -546   1151   -421       C  
ATOM   6237  CD  GLU D 181     -25.436  -8.944  16.193  1.00 39.17           C  
ANISOU 6237  CD  GLU D 181     4240   4753   5888   -675   1317   -442       C  
ATOM   6238  OE1 GLU D 181     -25.675  -8.265  17.209  1.00 40.98           O  
ANISOU 6238  OE1 GLU D 181     4541   4953   6078   -646   1442   -460       O  
ATOM   6239  OE2 GLU D 181     -25.605 -10.177  16.125  1.00 42.52           O  
ANISOU 6239  OE2 GLU D 181     4702   5162   6291   -812   1332   -443       O  
ATOM   6240  N   ILE D 182     -24.482  -4.871  13.630  1.00 32.28           N  
ANISOU 6240  N   ILE D 182     3100   3967   5198   -161    989   -391       N  
ATOM   6241  CA  ILE D 182     -24.952  -3.494  13.744  1.00 30.63           C  
ANISOU 6241  CA  ILE D 182     2849   3754   5036    -18   1046   -402       C  
ATOM   6242  C   ILE D 182     -26.466  -3.405  13.856  1.00 33.43           C  
ANISOU 6242  C   ILE D 182     2992   4214   5494     22   1180   -440       C  
ATOM   6243  O   ILE D 182     -27.176  -4.343  13.484  1.00 34.28           O  
ANISOU 6243  O   ILE D 182     2938   4431   5655    -71   1182   -452       O  
ATOM   6244  CB  ILE D 182     -24.462  -2.652  12.538  1.00 31.17           C  
ANISOU 6244  CB  ILE D 182     2876   3827   5138     96    896   -359       C  
ATOM   6245  CG1 ILE D 182     -24.972  -3.235  11.218  1.00 37.42           C  
ANISOU 6245  CG1 ILE D 182     3470   4745   6002     87    790   -345       C  
ATOM   6246  CG2 ILE D 182     -22.946  -2.567  12.523  1.00 30.13           C  
ANISOU 6246  CG2 ILE D 182     2933   3600   4916     59    792   -321       C  
ATOM   6247  CD1 ILE D 182     -24.776  -2.291  10.023  1.00 35.27           C  
ANISOU 6247  CD1 ILE D 182     3152   4489   5761    214    663   -299       C  
ATOM   6248  N   PRO D 183     -26.971  -2.271  14.373  1.00 31.59           N  
ANISOU 6248  N   PRO D 183     2760   3950   5291    157   1300   -459       N  
ATOM   6249  CA  PRO D 183     -28.418  -2.043  14.433  1.00 33.69           C  
ANISOU 6249  CA  PRO D 183     2787   4333   5682    238   1437   -487       C  
ATOM   6250  C   PRO D 183     -29.013  -1.917  13.029  1.00 36.12           C  
ANISOU 6250  C   PRO D 183     2826   4784   6112    324   1291   -448       C  
ATOM   6251  O   PRO D 183     -28.271  -1.835  12.053  1.00 36.11           O  
ANISOU 6251  O   PRO D 183     2870   4766   6084    337   1104   -405       O  
ATOM   6252  CB  PRO D 183     -28.528  -0.689  15.142  1.00 41.54           C  
ANISOU 6252  CB  PRO D 183     3899   5218   6666    407   1573   -507       C  
ATOM   6253  CG  PRO D 183     -27.213  -0.481  15.830  1.00 39.00           C  
ANISOU 6253  CG  PRO D 183     3912   4722   6184    335   1541   -509       C  
ATOM   6254  CD  PRO D 183     -26.203  -1.166  14.983  1.00 33.65           C  
ANISOU 6254  CD  PRO D 183     3257   4058   5469    235   1324   -460       C  
ATOM   6255  N   ASP D 184     -30.336  -1.881  12.940  1.00 38.25           N  
ANISOU 6255  N   ASP D 184     2819   5202   6512    382   1375   -460       N  
ATOM   6256  CA  ASP D 184     -31.018  -1.684  11.665  1.00 45.49           C  
ANISOU 6256  CA  ASP D 184     3465   6275   7546    475   1223   -416       C  
ATOM   6257  C   ASP D 184     -31.014  -0.198  11.305  1.00 43.91           C  
ANISOU 6257  C   ASP D 184     3284   6013   7389    740   1193   -372       C  
ATOM   6258  O   ASP D 184     -32.053   0.463  11.349  1.00 44.21           O  
ANISOU 6258  O   ASP D 184     3116   6131   7549    916   1279   -362       O  
ATOM   6259  CB  ASP D 184     -32.452  -2.219  11.739  1.00 49.25           C  
ANISOU 6259  CB  ASP D 184     3603   6954   8155    428   1314   -437       C  
ATOM   6260  CG  ASP D 184     -33.134  -2.283  10.377  1.00 58.20           C  
ANISOU 6260  CG  ASP D 184     4446   8278   9390    464   1109   -388       C  
ATOM   6261  OD1 ASP D 184     -32.463  -2.056   9.347  1.00 60.50           O  
ANISOU 6261  OD1 ASP D 184     4826   8533   9626    503    900   -341       O  
ATOM   6262  OD2 ASP D 184     -34.349  -2.575  10.343  1.00 65.52           O  
ANISOU 6262  OD2 ASP D 184     5102   9397  10395    437   1137   -381       O  
ATOM   6263  N   LYS D 185     -29.826   0.311  10.983  1.00 37.82           N  
ANISOU 6263  N   LYS D 185     2765   5090   6514    765   1083   -343       N  
ATOM   6264  CA  LYS D 185     -29.625   1.691  10.544  1.00 43.85           C  
ANISOU 6264  CA  LYS D 185     3613   5758   7290    984   1036   -295       C  
ATOM   6265  C   LYS D 185     -28.976   1.639   9.165  1.00 40.90           C  
ANISOU 6265  C   LYS D 185     3259   5405   6877    963    795   -231       C  
ATOM   6266  O   LYS D 185     -28.251   0.692   8.866  1.00 35.92           O  
ANISOU 6266  O   LYS D 185     2694   4786   6169    779    705   -239       O  
ATOM   6267  CB  LYS D 185     -28.666   2.419  11.491  1.00 47.34           C  
ANISOU 6267  CB  LYS D 185     4388   5979   7621    993   1140   -323       C  
ATOM   6268  CG  LYS D 185     -29.219   2.767  12.863  1.00 55.01           C  
ANISOU 6268  CG  LYS D 185     5420   6884   8598   1045   1394   -388       C  
ATOM   6269  CD  LYS D 185     -28.143   3.475  13.697  1.00 54.16           C  
ANISOU 6269  CD  LYS D 185     5681   6550   8346   1016   1452   -416       C  
ATOM   6270  CE  LYS D 185     -28.741   4.196  14.903  1.00 58.48           C  
ANISOU 6270  CE  LYS D 185     6338   6994   8888   1126   1709   -480       C  
ATOM   6271  NZ  LYS D 185     -28.314   3.592  16.198  1.00 58.66           N  
ANISOU 6271  NZ  LYS D 185     6562   6949   8777    937   1832   -545       N  
ATOM   6272  N   PHE D 186     -29.217   2.643   8.323  1.00 40.56           N  
ANISOU 6272  N   PHE D 186     3180   5356   6876   1157    701   -165       N  
ATOM   6273  CA  PHE D 186     -28.575   2.648   7.011  1.00 38.57           C  
ANISOU 6273  CA  PHE D 186     2981   5110   6562   1132    487   -102       C  
ATOM   6274  C   PHE D 186     -27.183   3.252   7.107  1.00 34.03           C  
ANISOU 6274  C   PHE D 186     2723   4337   5868   1102    480    -90       C  
ATOM   6275  O   PHE D 186     -27.025   4.400   7.528  1.00 39.59           O  
ANISOU 6275  O   PHE D 186     3583   4894   6565   1235    559    -78       O  
ATOM   6276  CB  PHE D 186     -29.404   3.389   5.951  1.00 42.34           C  
ANISOU 6276  CB  PHE D 186     3297   5675   7117   1336    359    -19       C  
ATOM   6277  CG  PHE D 186     -28.998   3.043   4.542  1.00 42.90           C  
ANISOU 6277  CG  PHE D 186     3377   5810   7115   1265    134     37       C  
ATOM   6278  CD1 PHE D 186     -27.914   3.670   3.943  1.00 40.52           C  
ANISOU 6278  CD1 PHE D 186     3328   5364   6705   1277     61     85       C  
ATOM   6279  CD2 PHE D 186     -29.684   2.064   3.830  1.00 46.16           C  
ANISOU 6279  CD2 PHE D 186     3560   6424   7555   1161      6     37       C  
ATOM   6280  CE1 PHE D 186     -27.517   3.332   2.646  1.00 39.75           C  
ANISOU 6280  CE1 PHE D 186     3261   5318   6523   1204   -121    133       C  
ATOM   6281  CE2 PHE D 186     -29.303   1.721   2.544  1.00 46.86           C  
ANISOU 6281  CE2 PHE D 186     3695   6560   7552   1083   -190     78       C  
ATOM   6282  CZ  PHE D 186     -28.212   2.356   1.947  1.00 43.24           C  
ANISOU 6282  CZ  PHE D 186     3497   5953   6980   1113   -246    127       C  
ATOM   6283  N   VAL D 187     -26.178   2.477   6.713  1.00 31.39           N  
ANISOU 6283  N   VAL D 187     2484   3999   5444    925    393    -92       N  
ATOM   6284  CA  VAL D 187     -24.789   2.925   6.807  1.00 30.77           C  
ANISOU 6284  CA  VAL D 187     2665   3765   5263    865    383    -79       C  
ATOM   6285  C   VAL D 187     -24.122   2.990   5.444  1.00 35.07           C  
ANISOU 6285  C   VAL D 187     3259   4319   5748    845    227    -15       C  
ATOM   6286  O   VAL D 187     -24.526   2.303   4.514  1.00 32.45           O  
ANISOU 6286  O   VAL D 187     2791   4114   5423    816    121      0       O  
ATOM   6287  CB  VAL D 187     -23.969   2.025   7.750  1.00 30.90           C  
ANISOU 6287  CB  VAL D 187     2775   3746   5218    682    448   -134       C  
ATOM   6288  CG1 VAL D 187     -24.538   2.096   9.160  1.00 33.61           C  
ANISOU 6288  CG1 VAL D 187     3131   4053   5587    695    617   -194       C  
ATOM   6289  CG2 VAL D 187     -23.971   0.584   7.248  1.00 31.00           C  
ANISOU 6289  CG2 VAL D 187     2671   3882   5225    545    379   -149       C  
ATOM   6290  N   VAL D 188     -23.095   3.820   5.329  1.00 32.17           N  
ANISOU 6290  N   VAL D 188     3098   3813   5311    844    219     19       N  
ATOM   6291  CA  VAL D 188     -22.363   3.963   4.075  1.00 28.37           C  
ANISOU 6291  CA  VAL D 188     2691   3327   4761    815    102     82       C  
ATOM   6292  C   VAL D 188     -20.890   4.098   4.410  1.00 28.11           C  
ANISOU 6292  C   VAL D 188     2840   3188   4653    684    134     80       C  
ATOM   6293  O   VAL D 188     -20.538   4.200   5.584  1.00 27.00           O  
ANISOU 6293  O   VAL D 188     2774   2976   4510    632    222     38       O  
ATOM   6294  CB  VAL D 188     -22.822   5.226   3.295  1.00 29.94           C  
ANISOU 6294  CB  VAL D 188     2946   3466   4963    991     46    160       C  
ATOM   6295  CG1 VAL D 188     -24.262   5.093   2.818  1.00 31.53           C  
ANISOU 6295  CG1 VAL D 188     2930   3804   5246   1132    -22    180       C  
ATOM   6296  CG2 VAL D 188     -22.657   6.485   4.161  1.00 30.68           C  
ANISOU 6296  CG2 VAL D 188     3220   3377   5060   1076    154    159       C  
ATOM   6297  N   GLY D 189     -20.033   4.094   3.391  1.00 27.24           N  
ANISOU 6297  N   GLY D 189     2797   3076   4477    624     64    129       N  
ATOM   6298  CA  GLY D 189     -18.599   4.229   3.598  1.00 26.42           C  
ANISOU 6298  CA  GLY D 189     2823   2899   4315    496     90    138       C  
ATOM   6299  C   GLY D 189     -17.877   2.894   3.530  1.00 25.21           C  
ANISOU 6299  C   GLY D 189     2596   2835   4147    372     84    112       C  
ATOM   6300  O   GLY D 189     -18.519   1.842   3.614  1.00 26.70           O  
ANISOU 6300  O   GLY D 189     2663   3115   4367    368     78     71       O  
ATOM   6301  N   TYR D 190     -16.553   2.932   3.397  1.00 27.77           N  
ANISOU 6301  N   TYR D 190     2991   3132   4429    271     92    139       N  
ATOM   6302  CA  TYR D 190     -15.752   1.711   3.233  1.00 28.09           C  
ANISOU 6302  CA  TYR D 190     2965   3247   4462    185     95    127       C  
ATOM   6303  C   TYR D 190     -16.352   0.850   2.118  1.00 27.05           C  
ANISOU 6303  C   TYR D 190     2764   3201   4313    217     57    118       C  
ATOM   6304  O   TYR D 190     -16.522  -0.366   2.265  1.00 25.72           O  
ANISOU 6304  O   TYR D 190     2524   3090   4158    187     65     75       O  
ATOM   6305  CB  TYR D 190     -15.676   0.936   4.548  1.00 22.66           C  
ANISOU 6305  CB  TYR D 190     2234   2569   3807    138    129     79       C  
ATOM   6306  CG  TYR D 190     -14.580  -0.114   4.591  1.00 23.68           C  
ANISOU 6306  CG  TYR D 190     2324   2742   3930     65    136     85       C  
ATOM   6307  CD1 TYR D 190     -13.238   0.255   4.576  1.00 28.32           C  
ANISOU 6307  CD1 TYR D 190     2936   3319   4504     -2    137    130       C  
ATOM   6308  CD2 TYR D 190     -14.885  -1.467   4.652  1.00 22.03           C  
ANISOU 6308  CD2 TYR D 190     2052   2583   3735     64    146     50       C  
ATOM   6309  CE1 TYR D 190     -12.225  -0.703   4.621  1.00 27.89           C  
ANISOU 6309  CE1 TYR D 190     2819   3316   4463    -38    147    146       C  
ATOM   6310  CE2 TYR D 190     -13.880  -2.429   4.711  1.00 21.92           C  
ANISOU 6310  CE2 TYR D 190     2016   2592   3721     30    162     62       C  
ATOM   6311  CZ  TYR D 190     -12.557  -2.042   4.692  1.00 25.72           C  
ANISOU 6311  CZ  TYR D 190     2497   3074   4202     -6    161    113       C  
ATOM   6312  OH  TYR D 190     -11.542  -2.987   4.749  1.00 25.65           O  
ANISOU 6312  OH  TYR D 190     2438   3097   4209    -11    179    136       O  
ATOM   6313  N   ALA D 191     -16.674   1.519   1.005  1.00 25.56           N  
ANISOU 6313  N   ALA D 191     2622   3008   4080    271      9    162       N  
ATOM   6314  CA  ALA D 191     -17.222   0.915  -0.222  1.00 24.51           C  
ANISOU 6314  CA  ALA D 191     2463   2952   3899    289    -52    163       C  
ATOM   6315  C   ALA D 191     -18.721   0.660  -0.214  1.00 25.99           C  
ANISOU 6315  C   ALA D 191     2541   3208   4124    355   -120    135       C  
ATOM   6316  O   ALA D 191     -19.304   0.439  -1.266  1.00 29.13           O  
ANISOU 6316  O   ALA D 191     2926   3671   4473    371   -204    148       O  
ATOM   6317  CB  ALA D 191     -16.428  -0.352  -0.661  1.00 23.96           C  
ANISOU 6317  CB  ALA D 191     2387   2926   3791    205    -15    134       C  
ATOM   6318  N   LEU D 192     -19.357   0.715   0.954  1.00 26.27           N  
ANISOU 6318  N   LEU D 192     2499   3239   4244    385    -83     99       N  
ATOM   6319  CA  LEU D 192     -20.824   0.673   0.992  1.00 26.06           C  
ANISOU 6319  CA  LEU D 192     2338   3291   4274    460   -133     83       C  
ATOM   6320  C   LEU D 192     -21.441   1.992   0.503  1.00 31.93           C  
ANISOU 6320  C   LEU D 192     3103   4007   5024    608   -193    151       C  
ATOM   6321  O   LEU D 192     -20.973   3.081   0.870  1.00 29.98           O  
ANISOU 6321  O   LEU D 192     2976   3640   4774    662   -145    185       O  
ATOM   6322  CB  LEU D 192     -21.343   0.343   2.388  1.00 27.85           C  
ANISOU 6322  CB  LEU D 192     2477   3520   4584    451    -46     25       C  
ATOM   6323  CG  LEU D 192     -21.181  -1.112   2.842  1.00 32.39           C  
ANISOU 6323  CG  LEU D 192     3009   4139   5160    322     -5    -37       C  
ATOM   6324  CD1 LEU D 192     -19.792  -1.359   3.380  1.00 31.99           C  
ANISOU 6324  CD1 LEU D 192     3077   4006   5073    251     55    -38       C  
ATOM   6325  CD2 LEU D 192     -22.233  -1.495   3.883  1.00 34.71           C  
ANISOU 6325  CD2 LEU D 192     3181   4476   5530    316     59    -89       C  
ATOM   6326  N   ASP D 193     -22.507   1.898  -0.294  1.00 28.72           N  
ANISOU 6326  N   ASP D 193     2585   3704   4622    670   -305    173       N  
ATOM   6327  CA  ASP D 193     -23.041   3.077  -0.974  1.00 30.29           C  
ANISOU 6327  CA  ASP D 193     2817   3880   4811    829   -390    259       C  
ATOM   6328  C   ASP D 193     -24.474   3.454  -0.623  1.00 33.28           C  
ANISOU 6328  C   ASP D 193     3009   4335   5303    984   -423    271       C  
ATOM   6329  O   ASP D 193     -25.230   2.681  -0.038  1.00 34.08           O  
ANISOU 6329  O   ASP D 193     2919   4543   5485    946   -397    210       O  
ATOM   6330  CB  ASP D 193     -22.983   2.905  -2.491  1.00 31.01           C  
ANISOU 6330  CB  ASP D 193     2968   4030   4786    802   -531    312       C  
ATOM   6331  CG  ASP D 193     -24.043   1.952  -3.002  1.00 33.15           C  
ANISOU 6331  CG  ASP D 193     3056   4474   5064    762   -653    284       C  
ATOM   6332  OD1 ASP D 193     -24.086   0.813  -2.504  1.00 33.85           O  
ANISOU 6332  OD1 ASP D 193     3054   4622   5184    633   -602    199       O  
ATOM   6333  OD2 ASP D 193     -24.837   2.338  -3.890  1.00 35.68           O  
ANISOU 6333  OD2 ASP D 193     3330   4872   5356    851   -808    351       O  
ATOM   6334  N   TYR D 194     -24.825   4.670  -1.012  1.00 33.46           N  
ANISOU 6334  N   TYR D 194     3091   4294   5329   1163   -473    356       N  
ATOM   6335  CA  TYR D 194     -26.202   5.093  -1.116  1.00 35.68           C  
ANISOU 6335  CA  TYR D 194     3182   4670   5705   1350   -550    401       C  
ATOM   6336  C   TYR D 194     -26.296   5.666  -2.515  1.00 38.78           C  
ANISOU 6336  C   TYR D 194     3664   5069   6001   1437   -728    512       C  
ATOM   6337  O   TYR D 194     -25.660   6.678  -2.804  1.00 39.47           O  
ANISOU 6337  O   TYR D 194     3985   4993   6020   1509   -711    579       O  
ATOM   6338  CB  TYR D 194     -26.503   6.163  -0.074  1.00 36.46           C  
ANISOU 6338  CB  TYR D 194     3310   4641   5902   1530   -412    405       C  
ATOM   6339  CG  TYR D 194     -27.865   6.790  -0.205  1.00 39.16           C  
ANISOU 6339  CG  TYR D 194     3463   5060   6355   1778   -472    469       C  
ATOM   6340  CD1 TYR D 194     -29.008   6.089   0.146  1.00 44.10           C  
ANISOU 6340  CD1 TYR D 194     3769   5883   7105   1794   -478    430       C  
ATOM   6341  CD2 TYR D 194     -28.003   8.091  -0.649  1.00 40.89           C  
ANISOU 6341  CD2 TYR D 194     3821   5153   6563   2001   -514    573       C  
ATOM   6342  CE1 TYR D 194     -30.256   6.667   0.038  1.00 47.94           C  
ANISOU 6342  CE1 TYR D 194     4039   6462   7712   2035   -530    495       C  
ATOM   6343  CE2 TYR D 194     -29.243   8.680  -0.760  1.00 49.88           C  
ANISOU 6343  CE2 TYR D 194     4774   6362   7815   2264   -569    643       C  
ATOM   6344  CZ  TYR D 194     -30.367   7.963  -0.413  1.00 51.60           C  
ANISOU 6344  CZ  TYR D 194     4636   6801   8170   2285   -578    605       C  
ATOM   6345  OH  TYR D 194     -31.608   8.550  -0.522  1.00 58.57           O  
ANISOU 6345  OH  TYR D 194     5293   7777   9186   2560   -632    682       O  
ATOM   6346  N   ASN D 195     -27.062   5.005  -3.380  1.00 38.31           N  
ANISOU 6346  N   ASN D 195     3441   5195   5922   1409   -901    531       N  
ATOM   6347  CA  ASN D 195     -27.146   5.374  -4.793  1.00 39.82           C  
ANISOU 6347  CA  ASN D 195     3732   5411   5986   1458  -1096    635       C  
ATOM   6348  C   ASN D 195     -25.790   5.644  -5.448  1.00 38.59           C  
ANISOU 6348  C   ASN D 195     3899   5101   5661   1357  -1062    662       C  
ATOM   6349  O   ASN D 195     -25.621   6.650  -6.149  1.00 39.86           O  
ANISOU 6349  O   ASN D 195     4245   5161   5739   1472  -1125    770       O  
ATOM   6350  CB  ASN D 195     -28.086   6.565  -4.993  1.00 53.04           C  
ANISOU 6350  CB  ASN D 195     5346   7077   7728   1743  -1191    754       C  
ATOM   6351  CG  ASN D 195     -29.505   6.247  -4.598  1.00 60.79           C  
ANISOU 6351  CG  ASN D 195     5963   8260   8875   1846  -1253    745       C  
ATOM   6352  OD1 ASN D 195     -29.982   5.140  -4.829  1.00 62.94           O  
ANISOU 6352  OD1 ASN D 195     6037   8726   9152   1688  -1344    690       O  
ATOM   6353  ND2 ASN D 195     -30.189   7.213  -3.988  1.00 63.15           N  
ANISOU 6353  ND2 ASN D 195     6171   8510   9312   2107  -1191    795       N  
ATOM   6354  N   GLU D 196     -24.841   4.746  -5.185  1.00 37.03           N  
ANISOU 6354  N   GLU D 196     3763   4887   5421   1148   -950    569       N  
ATOM   6355  CA  GLU D 196     -23.493   4.765  -5.772  1.00 35.25           C  
ANISOU 6355  CA  GLU D 196     3793   4551   5051   1023   -890    578       C  
ATOM   6356  C   GLU D 196     -22.545   5.771  -5.110  1.00 36.49           C  
ANISOU 6356  C   GLU D 196     4126   4512   5225   1053   -737    599       C  
ATOM   6357  O   GLU D 196     -21.336   5.744  -5.345  1.00 34.96           O  
ANISOU 6357  O   GLU D 196     4100   4239   4946    927   -651    594       O  
ATOM   6358  CB  GLU D 196     -23.543   4.950  -7.295  1.00 37.82           C  
ANISOU 6358  CB  GLU D 196     4260   4904   5205   1026  -1051    665       C  
ATOM   6359  CG  GLU D 196     -24.234   3.792  -8.023  1.00 37.58           C  
ANISOU 6359  CG  GLU D 196     4105   5060   5115    925  -1202    625       C  
ATOM   6360  CD  GLU D 196     -23.543   2.463  -7.782  1.00 38.66           C  
ANISOU 6360  CD  GLU D 196     4236   5222   5230    716  -1089    502       C  
ATOM   6361  OE1 GLU D 196     -22.325   2.465  -7.552  1.00 37.10           O  
ANISOU 6361  OE1 GLU D 196     4184   4909   5003    645   -929    477       O  
ATOM   6362  OE2 GLU D 196     -24.217   1.416  -7.828  1.00 47.68           O  
ANISOU 6362  OE2 GLU D 196     5230   6499   6387    623  -1162    435       O  
ATOM   6363  N   TYR D 197     -23.095   6.638  -4.267  1.00 35.09           N  
ANISOU 6363  N   TYR D 197     3908   4264   5161   1211   -694    617       N  
ATOM   6364  CA  TYR D 197     -22.282   7.595  -3.534  1.00 34.56           C  
ANISOU 6364  CA  TYR D 197     4022   4003   5107   1220   -551    624       C  
ATOM   6365  C   TYR D 197     -21.771   7.037  -2.206  1.00 32.70           C  
ANISOU 6365  C   TYR D 197     3718   3755   4952   1103   -403    515       C  
ATOM   6366  O   TYR D 197     -22.272   6.021  -1.722  1.00 32.04           O  
ANISOU 6366  O   TYR D 197     3436   3800   4938   1060   -399    441       O  
ATOM   6367  CB  TYR D 197     -23.073   8.871  -3.298  1.00 36.52           C  
ANISOU 6367  CB  TYR D 197     4318   4142   5414   1456   -563    697       C  
ATOM   6368  CG  TYR D 197     -23.252   9.676  -4.553  1.00 47.33           C  
ANISOU 6368  CG  TYR D 197     5848   5459   6678   1570   -695    828       C  
ATOM   6369  CD1 TYR D 197     -22.315  10.629  -4.921  1.00 48.27           C  
ANISOU 6369  CD1 TYR D 197     6268   5383   6689   1534   -642    894       C  
ATOM   6370  CD2 TYR D 197     -24.351   9.477  -5.380  1.00 51.73           C  
ANISOU 6370  CD2 TYR D 197     6260   6165   7232   1699   -881    892       C  
ATOM   6371  CE1 TYR D 197     -22.470  11.371  -6.073  1.00 54.19           C  
ANISOU 6371  CE1 TYR D 197     7198   6069   7323   1635   -757   1024       C  
ATOM   6372  CE2 TYR D 197     -24.514  10.213  -6.538  1.00 55.10           C  
ANISOU 6372  CE2 TYR D 197     6853   6541   7542   1808  -1020   1025       C  
ATOM   6373  CZ  TYR D 197     -23.571  11.158  -6.878  1.00 56.75           C  
ANISOU 6373  CZ  TYR D 197     7388   6537   7636   1780   -951   1092       C  
ATOM   6374  OH  TYR D 197     -23.727  11.895  -8.029  1.00 60.78           O  
ANISOU 6374  OH  TYR D 197     8097   6984   8015   1885  -1084   1233       O  
ATOM   6375  N   PHE D 198     -20.765   7.707  -1.644  1.00 32.08           N  
ANISOU 6375  N   PHE D 198     3818   3520   4852   1037   -291    512       N  
ATOM   6376  CA  PHE D 198     -20.170   7.360  -0.345  1.00 30.63           C  
ANISOU 6376  CA  PHE D 198     3611   3305   4723    924   -167    424       C  
ATOM   6377  C   PHE D 198     -19.248   6.162  -0.361  1.00 28.92           C  
ANISOU 6377  C   PHE D 198     3334   3179   4477    735   -144    371       C  
ATOM   6378  O   PHE D 198     -18.789   5.725   0.695  1.00 27.84           O  
ANISOU 6378  O   PHE D 198     3160   3036   4381    646    -66    307       O  
ATOM   6379  CB  PHE D 198     -21.236   7.185   0.746  1.00 30.91           C  
ANISOU 6379  CB  PHE D 198     3490   3378   4875   1027   -121    363       C  
ATOM   6380  CG  PHE D 198     -22.070   8.405   0.968  1.00 32.78           C  
ANISOU 6380  CG  PHE D 198     3791   3506   5159   1239   -102    406       C  
ATOM   6381  CD1 PHE D 198     -21.556   9.492   1.658  1.00 35.64           C  
ANISOU 6381  CD1 PHE D 198     4373   3666   5502   1251      0    406       C  
ATOM   6382  CD2 PHE D 198     -23.368   8.467   0.488  1.00 42.25           C  
ANISOU 6382  CD2 PHE D 198     4830   4802   6421   1427   -187    448       C  
ATOM   6383  CE1 PHE D 198     -22.325  10.634   1.869  1.00 39.76           C  
ANISOU 6383  CE1 PHE D 198     4986   4057   6064   1468     37    444       C  
ATOM   6384  CE2 PHE D 198     -24.146   9.598   0.688  1.00 47.82           C  
ANISOU 6384  CE2 PHE D 198     5585   5403   7183   1660   -161    497       C  
ATOM   6385  CZ  PHE D 198     -23.621  10.686   1.380  1.00 46.96           C  
ANISOU 6385  CZ  PHE D 198     5726   5064   7051   1690    -38    493       C  
ATOM   6386  N   ARG D 199     -18.969   5.605  -1.538  1.00 28.87           N  
ANISOU 6386  N   ARG D 199     3328   3249   4392    679   -209    399       N  
ATOM   6387  CA  ARG D 199     -18.018   4.502  -1.555  1.00 27.51           C  
ANISOU 6387  CA  ARG D 199     3117   3141   4196    524   -162    351       C  
ATOM   6388  C   ARG D 199     -16.607   5.007  -1.264  1.00 30.61           C  
ANISOU 6388  C   ARG D 199     3630   3438   4560    412    -73    369       C  
ATOM   6389  O   ARG D 199     -15.791   4.272  -0.700  1.00 27.77           O  
ANISOU 6389  O   ARG D 199     3212   3114   4227    307    -14    326       O  
ATOM   6390  CB  ARG D 199     -18.034   3.748  -2.878  1.00 29.54           C  
ANISOU 6390  CB  ARG D 199     3371   3489   4362    488   -229    364       C  
ATOM   6391  CG  ARG D 199     -19.354   3.059  -3.198  1.00 31.91           C  
ANISOU 6391  CG  ARG D 199     3532   3910   4681    547   -336    338       C  
ATOM   6392  CD  ARG D 199     -19.147   1.990  -4.254  1.00 28.43           C  
ANISOU 6392  CD  ARG D 199     3107   3553   4141    454   -376    315       C  
ATOM   6393  NE  ARG D 199     -20.384   1.641  -4.949  1.00 29.69           N  
ANISOU 6393  NE  ARG D 199     3186   3822   4273    493   -522    318       N  
ATOM   6394  CZ  ARG D 199     -21.224   0.695  -4.538  1.00 31.80           C  
ANISOU 6394  CZ  ARG D 199     3288   4191   4605    459   -558    249       C  
ATOM   6395  NH1 ARG D 199     -20.957   0.010  -3.433  1.00 30.30           N  
ANISOU 6395  NH1 ARG D 199     3022   3989   4502    399   -448    177       N  
ATOM   6396  NH2 ARG D 199     -22.319   0.429  -5.239  1.00 31.13           N  
ANISOU 6396  NH2 ARG D 199     3118   4220   4490    472   -709    258       N  
ATOM   6397  N   ASP D 200     -16.347   6.259  -1.645  1.00 28.09           N  
ANISOU 6397  N   ASP D 200     3479   3002   4190    434    -69    439       N  
ATOM   6398  CA  ASP D 200     -15.028   6.884  -1.518  1.00 29.69           C  
ANISOU 6398  CA  ASP D 200     3805   3117   4358    301      8    468       C  
ATOM   6399  C   ASP D 200     -14.860   7.536  -0.144  1.00 32.01           C  
ANISOU 6399  C   ASP D 200     4142   3310   4710    273     57    435       C  
ATOM   6400  O   ASP D 200     -14.601   8.733  -0.029  1.00 33.84           O  
ANISOU 6400  O   ASP D 200     4551   3397   4910    255     83    474       O  
ATOM   6401  CB  ASP D 200     -14.817   7.931  -2.623  1.00 29.55           C  
ANISOU 6401  CB  ASP D 200     3986   3003   4240    310     -2    562       C  
ATOM   6402  CG  ASP D 200     -15.955   8.941  -2.697  1.00 33.67           C  
ANISOU 6402  CG  ASP D 200     4612   3421   4761    487    -65    609       C  
ATOM   6403  OD1 ASP D 200     -17.111   8.536  -2.460  1.00 31.07           O  
ANISOU 6403  OD1 ASP D 200     4149   3162   4494    625   -129    579       O  
ATOM   6404  OD2 ASP D 200     -15.695  10.137  -2.986  1.00 32.20           O  
ANISOU 6404  OD2 ASP D 200     4639   3080   4515    490    -45    680       O  
ATOM   6405  N   LEU D 201     -15.025   6.731   0.895  1.00 28.78           N  
ANISOU 6405  N   LEU D 201     3597   2966   4371    260     70    361       N  
ATOM   6406  CA  LEU D 201     -14.994   7.197   2.278  1.00 32.31           C  
ANISOU 6406  CA  LEU D 201     4092   3329   4856    233    112    317       C  
ATOM   6407  C   LEU D 201     -14.443   6.031   3.060  1.00 32.42           C  
ANISOU 6407  C   LEU D 201     3966   3445   4905    135    125    263       C  
ATOM   6408  O   LEU D 201     -14.897   4.906   2.863  1.00 32.25           O  
ANISOU 6408  O   LEU D 201     3804   3536   4913    176    106    235       O  
ATOM   6409  CB  LEU D 201     -16.410   7.549   2.733  1.00 33.72           C  
ANISOU 6409  CB  LEU D 201     4267   3464   5080    407    112    291       C  
ATOM   6410  CG  LEU D 201     -16.702   7.848   4.196  1.00 35.44           C  
ANISOU 6410  CG  LEU D 201     4530   3605   5332    414    177    227       C  
ATOM   6411  CD1 LEU D 201     -15.941   9.086   4.641  1.00 32.50           C  
ANISOU 6411  CD1 LEU D 201     4389   3056   4903    325    217    241       C  
ATOM   6412  CD2 LEU D 201     -18.205   8.052   4.377  1.00 35.57           C  
ANISOU 6412  CD2 LEU D 201     4490   3615   5408    617    195    210       C  
ATOM   6413  N   ASN D 202     -13.454   6.271   3.923  1.00 30.75           N  
ANISOU 6413  N   ASN D 202     3802   3196   4686     -1    146    254       N  
ATOM   6414  CA AASN D 202     -12.766   5.179   4.613  0.51 30.41           C  
ANISOU 6414  CA AASN D 202     3632   3252   4670    -89    140    224       C  
ATOM   6415  CA BASN D 202     -12.776   5.165   4.600  0.49 30.37           C  
ANISOU 6415  CA BASN D 202     3625   3249   4666    -87    140    224       C  
ATOM   6416  C   ASN D 202     -13.515   4.645   5.833  1.00 29.49           C  
ANISOU 6416  C   ASN D 202     3482   3141   4583    -47    149    159       C  
ATOM   6417  O   ASN D 202     -13.378   3.471   6.199  1.00 29.84           O  
ANISOU 6417  O   ASN D 202     3413   3274   4651    -64    141    137       O  
ATOM   6418  CB AASN D 202     -11.354   5.610   5.019  0.51 33.37           C  
ANISOU 6418  CB AASN D 202     4043   3613   5024   -262    135    253       C  
ATOM   6419  CB BASN D 202     -11.309   5.506   4.932  0.49 33.25           C  
ANISOU 6419  CB BASN D 202     4013   3611   5011   -261    134    256       C  
ATOM   6420  CG AASN D 202     -10.271   4.775   4.360  0.51 37.07           C  
ANISOU 6420  CG AASN D 202     4367   4206   5512   -326    136    292       C  
ATOM   6421  CG BASN D 202     -11.175   6.640   5.940  0.49 32.61           C  
ANISOU 6421  CG BASN D 202     4099   3399   4892   -348    134    238       C  
ATOM   6422  OD1AASN D 202     -10.542   3.957   3.474  0.51 41.01           O  
ANISOU 6422  OD1AASN D 202     4783   4778   6022   -243    152    295       O  
ATOM   6423  OD1BASN D 202     -12.082   7.459   6.093  0.49 33.05           O  
ANISOU 6423  OD1BASN D 202     4297   3333   4929   -262    161    218       O  
ATOM   6424  ND2AASN D 202      -9.028   4.979   4.793  0.51 40.05           N  
ANISOU 6424  ND2AASN D 202     4713   4612   5892   -476    122    320       N  
ATOM   6425  ND2BASN D 202     -10.030   6.696   6.628  0.49 28.51           N  
ANISOU 6425  ND2BASN D 202     3570   2904   4360   -518    101    248       N  
ATOM   6426  N   HIS D 203     -14.305   5.508   6.465  1.00 27.61           N  
ANISOU 6426  N   HIS D 203     3359   2795   4336     12    180    130       N  
ATOM   6427  CA  HIS D 203     -15.069   5.111   7.644  1.00 27.00           C  
ANISOU 6427  CA  HIS D 203     3272   2713   4276     49    219     65       C  
ATOM   6428  C   HIS D 203     -16.456   4.634   7.249  1.00 29.41           C  
ANISOU 6428  C   HIS D 203     3462   3077   4637    201    241     44       C  
ATOM   6429  O   HIS D 203     -16.988   5.034   6.206  1.00 31.08           O  
ANISOU 6429  O   HIS D 203     3654   3293   4864    301    218     79       O  
ATOM   6430  CB  HIS D 203     -15.263   6.300   8.594  1.00 27.42           C  
ANISOU 6430  CB  HIS D 203     3521   2611   4286     42    271     34       C  
ATOM   6431  CG  HIS D 203     -14.011   7.052   8.913  1.00 27.01           C  
ANISOU 6431  CG  HIS D 203     3614   2482   4169   -127    239     54       C  
ATOM   6432  ND1 HIS D 203     -12.963   6.499   9.623  1.00 26.39           N  
ANISOU 6432  ND1 HIS D 203     3502   2465   4061   -287    186     54       N  
ATOM   6433  CD2 HIS D 203     -13.649   8.330   8.641  1.00 27.83           C  
ANISOU 6433  CD2 HIS D 203     3897   2449   4227   -173    248     79       C  
ATOM   6434  CE1 HIS D 203     -12.005   7.400   9.757  1.00 27.33           C  
ANISOU 6434  CE1 HIS D 203     3749   2510   4125   -438    154     75       C  
ATOM   6435  NE2 HIS D 203     -12.396   8.517   9.176  1.00 28.18           N  
ANISOU 6435  NE2 HIS D 203     4000   2488   4219   -382    199     87       N  
ATOM   6436  N   VAL D 204     -17.070   3.824   8.102  1.00 25.16           N  
ANISOU 6436  N   VAL D 204     2853   2585   4123    210    281     -9       N  
ATOM   6437  CA  VAL D 204     -18.497   3.538   7.962  1.00 29.15           C  
ANISOU 6437  CA  VAL D 204     3243   3144   4688    336    318    -37       C  
ATOM   6438  C   VAL D 204     -19.257   4.604   8.736  1.00 31.40           C  
ANISOU 6438  C   VAL D 204     3630   3320   4982    433    408    -67       C  
ATOM   6439  O   VAL D 204     -18.963   4.876   9.901  1.00 28.10           O  
ANISOU 6439  O   VAL D 204     3343   2818   4516    370    471   -107       O  
ATOM   6440  CB  VAL D 204     -18.859   2.122   8.450  1.00 27.28           C  
ANISOU 6440  CB  VAL D 204     2884   3007   4475    286    339    -79       C  
ATOM   6441  CG1 VAL D 204     -20.377   1.944   8.552  1.00 30.71           C  
ANISOU 6441  CG1 VAL D 204     3192   3499   4977    387    398   -114       C  
ATOM   6442  CG2 VAL D 204     -18.273   1.093   7.506  1.00 23.54           C  
ANISOU 6442  CG2 VAL D 204     2324   2623   3997    228    264    -52       C  
ATOM   6443  N   CYS D 205     -20.216   5.239   8.081  1.00 29.65           N  
ANISOU 6443  N   CYS D 205     3361   3093   4811    593    414    -45       N  
ATOM   6444  CA  CYS D 205     -20.871   6.383   8.681  1.00 30.16           C  
ANISOU 6444  CA  CYS D 205     3541   3030   4887    722    512    -64       C  
ATOM   6445  C   CYS D 205     -22.377   6.264   8.540  1.00 34.96           C  
ANISOU 6445  C   CYS D 205     3961   3724   5597    900    559    -73       C  
ATOM   6446  O   CYS D 205     -22.869   5.472   7.742  1.00 32.68           O  
ANISOU 6446  O   CYS D 205     3467   3588   5359    914    481    -51       O  
ATOM   6447  CB  CYS D 205     -20.373   7.667   8.034  1.00 31.68           C  
ANISOU 6447  CB  CYS D 205     3916   3082   5039    767    477     -7       C  
ATOM   6448  N   VAL D 206     -23.108   7.052   9.316  1.00 34.64           N  
ANISOU 6448  N   VAL D 206     3988   3588   5585   1032    691   -107       N  
ATOM   6449  CA  VAL D 206     -24.537   7.203   9.080  1.00 41.30           C  
ANISOU 6449  CA  VAL D 206     4637   4511   6544   1242    739    -98       C  
ATOM   6450  C   VAL D 206     -24.747   8.483   8.272  1.00 39.58           C  
ANISOU 6450  C   VAL D 206     4513   4184   6343   1438    698    -24       C  
ATOM   6451  O   VAL D 206     -24.123   9.509   8.545  1.00 42.07           O  
ANISOU 6451  O   VAL D 206     5100   4297   6586   1444    741    -21       O  
ATOM   6452  CB  VAL D 206     -25.347   7.223  10.396  1.00 45.73           C  
ANISOU 6452  CB  VAL D 206     5185   5048   7143   1301    939   -177       C  
ATOM   6453  CG1 VAL D 206     -25.288   5.872  11.076  1.00 42.65           C  
ANISOU 6453  CG1 VAL D 206     4691   4778   6736   1115    972   -234       C  
ATOM   6454  CG2 VAL D 206     -24.805   8.278  11.336  1.00 51.70           C  
ANISOU 6454  CG2 VAL D 206     6265   5572   7806   1303   1059   -218       C  
ATOM   6455  N   ILE D 207     -25.611   8.421   7.266  1.00 48.19           N  
ANISOU 6455  N   ILE D 207     5392   5400   7517   1587    602     41       N  
ATOM   6456  CA  ILE D 207     -25.821   9.555   6.358  1.00 50.11           C  
ANISOU 6456  CA  ILE D 207     5722   5548   7767   1785    532    134       C  
ATOM   6457  C   ILE D 207     -26.881  10.543   6.879  1.00 58.08           C  
ANISOU 6457  C   ILE D 207     6736   6464   8868   2065    671    136       C  
ATOM   6458  O   ILE D 207     -27.867  10.134   7.488  1.00 65.64           O  
ANISOU 6458  O   ILE D 207     7474   7536   9929   2149    775     90       O  
ATOM   6459  CB  ILE D 207     -26.123   9.033   4.925  1.00 67.82           C  
ANISOU 6459  CB  ILE D 207     7769   7969  10029   1802    330    216       C  
ATOM   6460  CG1 ILE D 207     -26.883  10.060   4.089  1.00 70.84           C  
ANISOU 6460  CG1 ILE D 207     8146   8314  10458   2074    256    321       C  
ATOM   6461  CG2 ILE D 207     -26.891   7.714   4.980  1.00 66.95           C  
ANISOU 6461  CG2 ILE D 207     7337   8104   9998   1731    302    173       C  
ATOM   6462  CD1 ILE D 207     -27.193   9.567   2.692  1.00 72.62           C  
ANISOU 6462  CD1 ILE D 207     8203   8716  10674   2078     39    404       C  
ATOM   6463  N   SER D 208     -26.658  11.842   6.668  1.00 55.99           N  
ANISOU 6463  N   SER D 208     6731   5980   8564   2208    691    187       N  
ATOM   6464  CA  SER D 208     -27.537  12.877   7.216  1.00 61.45           C  
ANISOU 6464  CA  SER D 208     7488   6530   9329   2492    850    186       C  
ATOM   6465  C   SER D 208     -28.819  13.042   6.406  1.00 65.54           C  
ANISOU 6465  C   SER D 208     7725   7190   9989   2788    771    281       C  
ATOM   6466  O   SER D 208     -28.989  12.414   5.360  1.00 65.97           O  
ANISOU 6466  O   SER D 208     7564   7440  10061   2751    572    349       O  
ATOM   6467  CB  SER D 208     -26.809  14.222   7.301  1.00 61.51           C  
ANISOU 6467  CB  SER D 208     7919   6221   9233   2531    906    206       C  
ATOM   6468  OG  SER D 208     -26.704  14.841   6.033  1.00 61.86           O  
ANISOU 6468  OG  SER D 208     8038   6213   9254   2639    748    333       O  
ATOM   6469  N   GLU D 209     -29.723  13.885   6.900  1.00 71.30           N  
ANISOU 6469  N   GLU D 209     8463   7836  10792   3038    903    270       N  
ATOM   6470  CA  GLU D 209     -30.948  14.206   6.176  1.00 72.80           C  
ANISOU 6470  CA  GLU D 209     8405   8171  11084   3260    780    338       C  
ATOM   6471  C   GLU D 209     -30.632  14.969   4.896  1.00 72.47           C  
ANISOU 6471  C   GLU D 209     8522   8027  10986   3358    586    475       C  
ATOM   6472  O   GLU D 209     -31.163  14.655   3.830  1.00 75.03           O  
ANISOU 6472  O   GLU D 209     8614   8537  11356   3420    378    564       O  
ATOM   6473  CB  GLU D 209     -31.911  15.009   7.059  1.00 80.02           C  
ANISOU 6473  CB  GLU D 209     9325   9014  12067   3451    958    274       C  
ATOM   6474  CG  GLU D 209     -32.477  14.215   8.226  1.00 82.66           C  
ANISOU 6474  CG  GLU D 209     9455   9494  12459   3375   1143    152       C  
ATOM   6475  CD  GLU D 209     -33.098  12.889   7.796  1.00 84.78           C  
ANISOU 6475  CD  GLU D 209     9289  10104  12820   3280   1021    157       C  
ATOM   6476  OE1 GLU D 209     -32.975  11.901   8.552  1.00 81.38           O  
ANISOU 6476  OE1 GLU D 209     8763   9776  12384   3091   1132     75       O  
ATOM   6477  OE2 GLU D 209     -33.717  12.835   6.710  1.00 88.87           O  
ANISOU 6477  OE2 GLU D 209     9578  10781  13407   3377    812    243       O  
ATOM   6478  N   THR D 210     -29.763  15.969   5.019  1.00 70.85           N  
ANISOU 6478  N   THR D 210     8731   7522  10666   3348    653    487       N  
ATOM   6479  CA  THR D 210     -29.237  16.698   3.871  1.00 75.72           C  
ANISOU 6479  CA  THR D 210     9574   8002  11192   3387    496    615       C  
ATOM   6480  C   THR D 210     -28.691  15.731   2.820  1.00 74.44           C  
ANISOU 6480  C   THR D 210     9288   8013  10984   3250    302    692       C  
ATOM   6481  O   THR D 210     -28.882  15.929   1.620  1.00 76.77           O  
ANISOU 6481  O   THR D 210     9557   8360  11250   3331    107    813       O  
ATOM   6482  CB  THR D 210     -28.115  17.662   4.302  1.00 77.98           C  
ANISOU 6482  CB  THR D 210    10342   7951  11338   3283    618    590       C  
ATOM   6483  OG1 THR D 210     -28.671  18.707   5.107  1.00 82.90           O  
ANISOU 6483  OG1 THR D 210    11115   8400  11984   3431    778    536       O  
ATOM   6484  CG2 THR D 210     -27.417  18.274   3.090  1.00 78.69           C  
ANISOU 6484  CG2 THR D 210    10679   7908  11313   3260    464    721       C  
ATOM   6485  N   GLY D 211     -28.038  14.671   3.287  1.00 68.99           N  
ANISOU 6485  N   GLY D 211     8521   7432  10261   2974    336    598       N  
ATOM   6486  CA  GLY D 211     -27.394  13.704   2.413  1.00 66.02           C  
ANISOU 6486  CA  GLY D 211     8054   7228   9804   2721    157    616       C  
ATOM   6487  C   GLY D 211     -28.318  12.753   1.668  1.00 61.78           C  
ANISOU 6487  C   GLY D 211     7131   6996   9347   2764    -12    655       C  
ATOM   6488  O   GLY D 211     -28.136  12.519   0.468  1.00 57.56           O  
ANISOU 6488  O   GLY D 211     6585   6548   8736   2712   -207    738       O  
ATOM   6489  N   LYS D 212     -29.294  12.189   2.377  1.00 61.94           N  
ANISOU 6489  N   LYS D 212     6845   7181   9509   2835     67    594       N  
ATOM   6490  CA  LYS D 212     -30.244  11.262   1.767  1.00 63.66           C  
ANISOU 6490  CA  LYS D 212     6674   7701   9813   2848    -88    622       C  
ATOM   6491  C   LYS D 212     -31.054  11.967   0.693  1.00 61.49           C  
ANISOU 6491  C   LYS D 212     6320   7471   9574   3118   -272    768       C  
ATOM   6492  O   LYS D 212     -31.357  11.391  -0.346  1.00 61.37           O  
ANISOU 6492  O   LYS D 212     6130   7653   9534   3076   -494    835       O  
ATOM   6493  CB  LYS D 212     -31.179  10.664   2.821  1.00 66.77           C  
ANISOU 6493  CB  LYS D 212     6763   8246  10361   2877     64    531       C  
ATOM   6494  CG  LYS D 212     -30.903   9.200   3.139  1.00 68.15           C  
ANISOU 6494  CG  LYS D 212     6788   8592  10514   2559     67    428       C  
ATOM   6495  CD  LYS D 212     -31.931   8.638   4.117  1.00 72.95           C  
ANISOU 6495  CD  LYS D 212     7091   9355  11272   2587    222    352       C  
ATOM   6496  CE  LYS D 212     -33.358   8.937   3.670  1.00 77.72           C  
ANISOU 6496  CE  LYS D 212     7424  10137  11968   2774    117    380       C  
ATOM   6497  NZ  LYS D 212     -34.379   8.236   4.506  1.00 80.62           N  
ANISOU 6497  NZ  LYS D 212     7502  10700  12430   2714    239    277       N  
ATOM   6498  N   ALA D 213     -31.387  13.223   0.958  1.00 61.16           N  
ANISOU 6498  N   ALA D 213     6449   7232   9559   3324   -196    785       N  
ATOM   6499  CA  ALA D 213     -32.150  14.045   0.029  1.00 65.01           C  
ANISOU 6499  CA  ALA D 213     6916   7712  10072   3534   -368    900       C  
ATOM   6500  C   ALA D 213     -31.334  14.371  -1.219  1.00 68.45           C  
ANISOU 6500  C   ALA D 213     7611   8054  10344   3505   -547   1035       C  
ATOM   6501  O   ALA D 213     -31.832  14.314  -2.345  1.00 71.00           O  
ANISOU 6501  O   ALA D 213     7823   8507  10649   3560   -783   1143       O  
ATOM   6502  CB  ALA D 213     -32.578  15.334   0.722  1.00 63.23           C  
ANISOU 6502  CB  ALA D 213     6852   7262   9911   3750   -207    883       C  
ATOM   6503  N   LYS D 214     -30.075  14.724  -0.984  1.00 64.91           N  
ANISOU 6503  N   LYS D 214     7523   7373   9767   3406   -430   1026       N  
ATOM   6504  CA  LYS D 214     -29.154  15.202  -2.003  1.00 64.38           C  
ANISOU 6504  CA  LYS D 214     7783   7156   9522   3365   -540   1138       C  
ATOM   6505  C   LYS D 214     -28.841  14.111  -3.018  1.00 63.15           C  
ANISOU 6505  C   LYS D 214     7504   7225   9264   3133   -739   1152       C  
ATOM   6506  O   LYS D 214     -28.725  14.378  -4.217  1.00 64.68           O  
ANISOU 6506  O   LYS D 214     7824   7413   9337   3159   -920   1273       O  
ATOM   6507  CB  LYS D 214     -27.868  15.639  -1.303  1.00 65.00           C  
ANISOU 6507  CB  LYS D 214     8225   6968   9502   3175   -346   1060       C  
ATOM   6508  CG  LYS D 214     -26.880  16.470  -2.098  1.00 67.25           C  
ANISOU 6508  CG  LYS D 214     8916   7025   9613   3100   -389   1150       C  
ATOM   6509  CD  LYS D 214     -25.909  17.104  -1.107  1.00 68.85           C  
ANISOU 6509  CD  LYS D 214     9436   6957   9768   2960   -171   1063       C  
ATOM   6510  CE  LYS D 214     -24.672  17.689  -1.752  1.00 69.16           C  
ANISOU 6510  CE  LYS D 214     9848   6799   9630   2765   -183   1119       C  
ATOM   6511  NZ  LYS D 214     -23.704  18.120  -0.698  1.00 67.81           N  
ANISOU 6511  NZ  LYS D 214     9929   6416   9420   2568     10   1015       N  
ATOM   6512  N   TYR D 215     -28.707  12.880  -2.531  1.00 58.99           N  
ANISOU 6512  N   TYR D 215     6758   6882   8774   2898   -697   1025       N  
ATOM   6513  CA  TYR D 215     -28.277  11.769  -3.373  1.00 55.57           C  
ANISOU 6513  CA  TYR D 215     6254   6629   8233   2640   -844   1007       C  
ATOM   6514  C   TYR D 215     -29.407  10.822  -3.766  1.00 55.94           C  
ANISOU 6514  C   TYR D 215     5912   6981   8361   2659  -1011   1010       C  
ATOM   6515  O   TYR D 215     -29.201   9.891  -4.539  1.00 56.76           O  
ANISOU 6515  O   TYR D 215     5962   7236   8369   2458  -1149    996       O  
ATOM   6516  CB  TYR D 215     -27.115  11.024  -2.709  1.00 53.53           C  
ANISOU 6516  CB  TYR D 215     6085   6331   7923   2332   -694    874       C  
ATOM   6517  CG  TYR D 215     -25.905  11.914  -2.540  1.00 53.02           C  
ANISOU 6517  CG  TYR D 215     6394   5995   7754   2262   -574    884       C  
ATOM   6518  CD1 TYR D 215     -25.230  12.404  -3.652  1.00 56.21           C  
ANISOU 6518  CD1 TYR D 215     7051   6302   8003   2218   -666    982       C  
ATOM   6519  CD2 TYR D 215     -25.455  12.289  -1.277  1.00 50.15           C  
ANISOU 6519  CD2 TYR D 215     6143   5474   7439   2226   -371    798       C  
ATOM   6520  CE1 TYR D 215     -24.135  13.234  -3.520  1.00 55.95           C  
ANISOU 6520  CE1 TYR D 215     7350   6030   7880   2128   -553    996       C  
ATOM   6521  CE2 TYR D 215     -24.350  13.118  -1.130  1.00 50.60           C  
ANISOU 6521  CE2 TYR D 215     6538   5291   7397   2131   -277    807       C  
ATOM   6522  CZ  TYR D 215     -23.698  13.589  -2.259  1.00 52.95           C  
ANISOU 6522  CZ  TYR D 215     7059   5503   7555   2079   -366    907       C  
ATOM   6523  OH  TYR D 215     -22.607  14.417  -2.138  1.00 50.48           O  
ANISOU 6523  OH  TYR D 215     7072   4961   7148   1958   -268    919       O  
ATOM   6524  N   LYS D 216     -30.594  11.083  -3.231  1.00 62.01           N  
ANISOU 6524  N   LYS D 216     6418   7837   9306   2896   -990   1026       N  
ATOM   6525  CA  LYS D 216     -31.803  10.330  -3.552  1.00 71.40           C  
ANISOU 6525  CA  LYS D 216     7199   9330  10599   2934  -1152   1042       C  
ATOM   6526  C   LYS D 216     -32.000  10.209  -5.057  1.00 77.34           C  
ANISOU 6526  C   LYS D 216     7956  10207  11223   2925  -1454   1161       C  
ATOM   6527  O   LYS D 216     -31.826  11.184  -5.791  1.00 79.09           O  
ANISOU 6527  O   LYS D 216     8413  10286  11351   3091  -1550   1291       O  
ATOM   6528  CB  LYS D 216     -33.023  11.036  -2.950  1.00 77.33           C  
ANISOU 6528  CB  LYS D 216     7760  10079  11543   3172  -1090   1034       C  
ATOM   6529  CG  LYS D 216     -34.351  10.306  -3.113  1.00 82.46           C  
ANISOU 6529  CG  LYS D 216     7991  11017  12323   3144  -1227    998       C  
ATOM   6530  CD  LYS D 216     -34.555   9.256  -2.030  1.00 83.20           C  
ANISOU 6530  CD  LYS D 216     7853  11252  12507   2968  -1051    840       C  
ATOM   6531  CE  LYS D 216     -35.909   8.577  -2.172  1.00 86.38           C  
ANISOU 6531  CE  LYS D 216     7854  11934  13034   2928  -1173    794       C  
ATOM   6532  NZ  LYS D 216     -37.035   9.553  -2.143  1.00 90.53           N  
ANISOU 6532  NZ  LYS D 216     8247  12443  13709   3201  -1199    834       N  
ATOM   6533  N   ALA D 217     -32.360   9.010  -5.508  1.00 80.59           N  
ANISOU 6533  N   ALA D 217     8135  10871  11615   2719  -1601   1115       N  
ATOM   6534  CA  ALA D 217     -32.677   8.768  -6.913  1.00 84.79           C  
ANISOU 6534  CA  ALA D 217     8648  11554  12013   2684  -1906   1215       C  
ATOM   6535  C   ALA D 217     -33.687   9.784  -7.438  1.00 91.06           C  
ANISOU 6535  C   ALA D 217     9373  12340  12884   2954  -2069   1354       C  
ATOM   6536  O   ALA D 217     -34.549  10.258  -6.698  1.00 94.64           O  
ANISOU 6536  O   ALA D 217     9643  12772  13546   3108  -1973   1323       O  
ATOM   6537  CB  ALA D 217     -33.204   7.358  -7.095  1.00 84.21           C  
ANISOU 6537  CB  ALA D 217     8282  11761  11953   2434  -2023   1129       C  
ATOM   6538  OXT ALA D 217     -33.663  10.157  -8.610  1.00 93.91           O  
ANISOU 6538  OXT ALA D 217     9890  12693  13099   2993  -2287   1487       O  
TER    6539      ALA D 217                                                      
HETATM 6540  OAD 3L7 A 301      22.653  12.169  14.376  1.00 60.75           O  
HETATM 6541  PBA 3L7 A 301      22.534  11.057  15.525  1.00 66.65           P  
HETATM 6542  OAE 3L7 A 301      21.468  10.018  15.123  1.00 61.34           O  
HETATM 6543  OAB 3L7 A 301      22.136  11.700  16.830  1.00 58.23           O  
HETATM 6544  CAP 3L7 A 301      24.163  10.139  15.725  1.00 73.28           C  
HETATM 6545  CAK 3L7 A 301      25.461  10.764  15.216  1.00 72.85           C  
HETATM 6546  OAU 3L7 A 301      26.627  10.207  15.682  1.00 69.45           O  
HETATM 6547  CAJ 3L7 A 301      27.165   9.126  15.052  1.00 59.88           C  
HETATM 6548  CAL 3L7 A 301      27.517   9.287  13.579  1.00 49.95           C  
HETATM 6549  NAY 3L7 A 301      27.521   8.046  12.781  1.00 42.66           N  
HETATM 6550  CAN 3L7 A 301      28.860   7.450  12.701  1.00 39.28           C  
HETATM 6551  CAQ 3L7 A 301      28.877   5.945  12.648  1.00 37.42           C  
HETATM 6552  PBB 3L7 A 301      30.472   5.138  12.617  1.00 45.66           P  
HETATM 6553  OAF 3L7 A 301      31.444   5.868  11.684  1.00 46.18           O  
HETATM 6554  OAG 3L7 A 301      31.063   5.124  14.091  1.00 51.22           O  
HETATM 6555  OAC 3L7 A 301      30.306   3.744  12.188  1.00 42.01           O  
HETATM 6556  CAM 3L7 A 301      27.017   8.334  11.416  1.00 39.77           C  
HETATM 6557  CAO 3L7 A 301      27.744   9.349  10.621  1.00 38.15           C  
HETATM 6558  N9  3L7 A 301      27.558   9.108   9.137  1.00 42.15           N  
HETATM 6559  C4  3L7 A 301      26.435   9.513   8.408  1.00 39.09           C  
HETATM 6560  N3  3L7 A 301      25.257  10.231   8.767  1.00 36.41           N  
HETATM 6561  C2  3L7 A 301      24.329  10.487   7.820  1.00 40.80           C  
HETATM 6562  N1  3L7 A 301      24.520  10.071   6.534  1.00 39.93           N  
HETATM 6563  C6  3L7 A 301      25.627   9.382   6.116  1.00 42.00           C  
HETATM 6564  O6  3L7 A 301      25.771   8.997   4.853  1.00 42.39           O  
HETATM 6565  C5  3L7 A 301      26.645   9.085   7.113  1.00 42.28           C  
HETATM 6566  N7  3L7 A 301      27.882   8.418   7.071  1.00 45.38           N  
HETATM 6567  C8  3L7 A 301      28.403   8.442   8.315  1.00 43.08           C  
HETATM 6568 MG    MG A 302      23.579   6.214  14.654  1.00 28.55          MG  
HETATM 6569 MG    MG A 303      23.966  13.164  12.618  1.00 45.81          MG  
HETATM 6570  OADA3L7 B 301      -7.444 -14.766 -20.104  0.35 62.45           O  
HETATM 6571  OADB3L7 B 301      -5.877  -9.820 -14.863  0.55 31.21           O  
HETATM 6572  PBAA3L7 B 301      -8.048 -13.499 -19.456  0.35 62.55           P  
HETATM 6573  PBAB3L7 B 301      -6.583 -10.638 -15.957  0.55 31.96           P  
HETATM 6574  OAEA3L7 B 301      -9.602 -13.726 -19.163  0.35 51.89           O  
HETATM 6575  OAEB3L7 B 301      -5.851 -12.043 -16.110  0.55 27.34           O  
HETATM 6576  OABA3L7 B 301      -7.334 -13.212 -18.170  0.35 60.85           O  
HETATM 6577  OABB3L7 B 301      -8.017 -10.850 -15.568  0.55 26.80           O  
HETATM 6578  CAPA3L7 B 301      -7.846 -12.053 -20.635  0.35 43.17           C  
HETATM 6579  CAPB3L7 B 301      -6.516  -9.708 -17.589  0.55 35.50           C  
HETATM 6580  CAKA3L7 B 301      -6.430 -11.544 -20.876  0.35 42.94           C  
HETATM 6581  CAKB3L7 B 301      -5.877  -8.323 -17.600  0.55 39.18           C  
HETATM 6582  OAUA3L7 B 301      -5.986 -10.517 -20.087  0.35 43.07           O  
HETATM 6583  OAUB3L7 B 301      -6.301  -7.458 -18.576  0.55 42.73           O  
HETATM 6584  CAJA3L7 B 301      -4.772  -9.960 -20.340  0.35 40.10           C  
HETATM 6585  CAJB3L7 B 301      -5.369  -6.713 -19.234  0.55 42.67           C  
HETATM 6586  CALA3L7 B 301      -4.538  -8.558 -19.802  0.35 40.88           C  
HETATM 6587  CALB3L7 B 301      -3.936  -7.213 -19.143  0.55 41.21           C  
HETATM 6588  NAYA3L7 B 301      -3.223  -7.935 -20.077  0.35 40.19           N  
HETATM 6589  NAYB3L7 B 301      -3.467  -8.156 -20.185  0.55 40.45           N  
HETATM 6590  CANA3L7 B 301      -3.043  -7.637 -21.512  0.35 38.92           C  
HETATM 6591  CANB3L7 B 301      -3.605  -7.510 -21.490  0.55 38.42           C  
HETATM 6592  CAQA3L7 B 301      -2.829  -6.174 -21.874  0.35 38.79           C  
HETATM 6593  CAQB3L7 B 301      -2.627  -6.398 -21.801  0.55 38.50           C  
HETATM 6594  PBBA3L7 B 301      -2.669  -5.630 -23.586  0.35 35.23           P  
HETATM 6595  PBBB3L7 B 301      -2.795  -5.672 -23.428  0.55 36.74           P  
HETATM 6596  OAFA3L7 B 301      -1.673  -6.490 -24.362  0.35 32.70           O  
HETATM 6597  OAFB3L7 B 301      -1.938  -6.460 -24.422  0.55 33.00           O  
HETATM 6598  OAGA3L7 B 301      -4.047  -5.660 -24.359  0.35 40.07           O  
HETATM 6599  OAGB3L7 B 301      -4.311  -5.728 -23.872  0.55 37.73           O  
HETATM 6600  OACA3L7 B 301      -2.166  -4.254 -23.590  0.35 32.06           O  
HETATM 6601  OACB3L7 B 301      -2.322  -4.285 -23.400  0.55 33.25           O  
HETATM 6602  CAMA3L7 B 301      -2.168  -8.840 -19.551  0.35 38.93           C  
HETATM 6603  CAMB3L7 B 301      -2.025  -8.377 -19.946  0.55 38.94           C  
HETATM 6604  CAOA3L7 B 301      -1.288  -9.538 -20.520  0.35 37.75           C  
HETATM 6605  CAOB3L7 B 301      -1.352  -9.612 -20.420  0.55 37.66           C  
HETATM 6606  N9 A3L7 B 301       0.191  -9.435 -20.198  0.35 36.62           N  
HETATM 6607  N9 B3L7 B 301       0.134  -9.508 -20.140  0.55 36.82           N  
HETATM 6608  C4 A3L7 B 301       0.767  -9.824 -18.978  0.35 35.52           C  
HETATM 6609  C4 B3L7 B 301       0.738  -9.871 -18.924  0.55 35.64           C  
HETATM 6610  N3 A3L7 B 301       0.220 -10.399 -17.797  0.35 33.86           N  
HETATM 6611  N3 B3L7 B 301       0.222 -10.440 -17.727  0.55 33.86           N  
HETATM 6612  C2 A3L7 B 301       1.044 -10.679 -16.758  0.35 33.32           C  
HETATM 6613  C2 B3L7 B 301       1.074 -10.701 -16.703  0.55 33.35           C  
HETATM 6614  N1 A3L7 B 301       2.377 -10.423 -16.835  0.35 31.94           N  
HETATM 6615  N1 B3L7 B 301       2.403 -10.432 -16.814  0.55 31.38           N  
HETATM 6616  C6 A3L7 B 301       2.974  -9.873 -17.938  0.35 33.16           C  
HETATM 6617  C6 B3L7 B 301       2.969  -9.886 -17.935  0.55 33.20           C  
HETATM 6618  O6 A3L7 B 301       4.284  -9.633 -17.976  0.35 32.91           O  
HETATM 6619  O6 B3L7 B 301       4.274  -9.630 -18.012  0.55 32.82           O  
HETATM 6620  C5 A3L7 B 301       2.115  -9.557 -19.074  0.35 34.73           C  
HETATM 6621  C5 B3L7 B 301       2.080  -9.591 -19.053  0.55 34.33           C  
HETATM 6622  N7 A3L7 B 301       2.345  -9.002 -20.342  0.35 37.28           N  
HETATM 6623  N7 B3L7 B 301       2.278  -9.046 -20.332  0.55 37.76           N  
HETATM 6624  C8 A3L7 B 301       1.164  -8.941 -20.992  0.35 37.40           C  
HETATM 6625  C8 B3L7 B 301       1.082  -9.002 -20.957  0.55 37.38           C  
HETATM 6626 MG    MG B 302      -5.210  -5.329 -17.495  1.00 75.02          MG  
HETATM 6627 MG    MG B 303      -3.838 -12.735 -16.918  1.00 36.82          MG  
HETATM 6628  OAD 3L7 C 301       7.098   7.277  29.693  0.76 32.84           O  
HETATM 6629  PBA 3L7 C 301       8.003   6.646  30.843  0.76 42.99           P  
HETATM 6630  OAE 3L7 C 301       9.433   6.342  30.358  0.76 39.61           O  
HETATM 6631  OAB 3L7 C 301       7.368   5.365  31.307  0.76 45.48           O  
HETATM 6632  CAP 3L7 C 301       8.121   7.875  32.272  0.76 51.46           C  
HETATM 6633  CAK 3L7 C 301       6.815   8.492  32.781  0.76 53.49           C  
HETATM 6634  OAU 3L7 C 301       6.778   9.137  33.991  0.76 52.28           O  
HETATM 6635  CAJ 3L7 C 301       5.689   9.889  34.322  0.76 46.21           C  
HETATM 6636  CAL 3L7 C 301       4.344   9.192  34.486  0.76 38.41           C  
HETATM 6637  NAY 3L7 C 301       3.165   9.912  33.952  0.76 38.50           N  
HETATM 6638  CAN 3L7 C 301       2.703  10.972  34.866  0.76 38.99           C  
HETATM 6639  CAQ 3L7 C 301       1.721  11.988  34.315  0.76 37.56           C  
HETATM 6640  PBB 3L7 C 301       1.206  13.332  35.388  0.76 29.00           P  
HETATM 6641  OAF 3L7 C 301       0.301  14.203  34.646  0.76 23.38           O  
HETATM 6642  OAG 3L7 C 301       2.459  14.134  35.895  0.76 30.40           O  
HETATM 6643  OAC 3L7 C 301       0.461  12.792  36.618  0.76 32.35           O  
HETATM 6644  CAM 3L7 C 301       2.064   8.943  33.723  0.76 38.34           C  
HETATM 6645  CAO 3L7 C 301       1.745   7.929  34.768  0.76 32.21           C  
HETATM 6646  N9  3L7 C 301       0.362   7.355  34.526  0.76 32.63           N  
HETATM 6647  C4  3L7 C 301       0.091   6.254  33.709  0.76 31.75           C  
HETATM 6648  N3  3L7 C 301       0.940   5.393  32.973  0.76 30.79           N  
HETATM 6649  C2  3L7 C 301       0.377   4.376  32.279  0.76 28.89           C  
HETATM 6650  N1  3L7 C 301      -0.969   4.183  32.269  0.76 27.45           N  
HETATM 6651  C6  3L7 C 301      -1.851   4.972  32.963  0.76 29.01           C  
HETATM 6652  O6  3L7 C 301      -3.171   4.753  32.937  0.76 28.01           O  
HETATM 6653  C5  3L7 C 301      -1.274   6.072  33.721  0.76 32.09           C  
HETATM 6654  N7  3L7 C 301      -1.823   7.074  34.529  0.76 33.26           N  
HETATM 6655  C8  3L7 C 301      -0.813   7.834  34.991  0.76 33.04           C  
HETATM 6656 MG    MG C 302       4.650  10.536  29.631  1.00 27.57          MG  
HETATM 6657 MG    MG C 303       5.548   4.520  32.837  1.00 41.66          MG  
HETATM 6658  OAD 3L7 D 301     -23.450  -3.557  -5.767  1.00 80.13           O  
HETATM 6659  PBA 3L7 D 301     -23.548  -3.063  -4.356  1.00 81.70           P  
HETATM 6660  OAE 3L7 D 301     -23.594  -1.466  -4.354  1.00115.71           O  
HETATM 6661  OAB 3L7 D 301     -22.311  -3.544  -3.571  1.00 79.26           O  
HETATM 6662  CAP 3L7 D 301     -25.105  -3.719  -3.525  1.00 78.09           C  
HETATM 6663  CAK 3L7 D 301     -25.603  -5.119  -3.877  1.00 76.52           C  
HETATM 6664  OAU 3L7 D 301     -26.950  -5.349  -3.762  1.00 74.40           O  
HETATM 6665  CAJ 3L7 D 301     -27.439  -6.041  -2.691  1.00 68.27           C  
HETATM 6666  CAL 3L7 D 301     -27.919  -5.258  -1.476  1.00 60.41           C  
HETATM 6667  NAY 3L7 D 301     -27.586  -5.819  -0.145  1.00 54.55           N  
HETATM 6668  CAN 3L7 D 301     -28.666  -6.675   0.377  1.00 52.51           C  
HETATM 6669  CAQ 3L7 D 301     -28.264  -7.882   1.198  1.00 50.36           C  
HETATM 6670  PBB 3L7 D 301     -29.549  -8.981   1.821  1.00 45.20           P  
HETATM 6671  OAF 3L7 D 301     -29.977  -9.959   0.648  1.00 40.70           O  
HETATM 6672  OAG 3L7 D 301     -30.756  -8.181   2.323  1.00 41.87           O  
HETATM 6673  OAC 3L7 D 301     -28.994  -9.755   2.951  1.00 37.63           O  
HETATM 6674  CAM 3L7 D 301     -27.324  -4.709   0.805  1.00 52.48           C  
HETATM 6675  CAO 3L7 D 301     -28.260  -3.555   0.847  1.00 48.58           C  
HETATM 6676  N9  3L7 D 301     -28.212  -2.863   2.197  1.00 43.31           N  
HETATM 6677  C4  3L7 D 301     -27.370  -1.791   2.508  1.00 42.40           C  
HETATM 6678  N3  3L7 D 301     -26.423  -1.071   1.739  1.00 39.74           N  
HETATM 6679  C2  3L7 D 301     -25.747  -0.053   2.331  1.00 41.42           C  
HETATM 6680  N1  3L7 D 301     -25.962   0.280   3.630  1.00 37.89           N  
HETATM 6681  C6  3L7 D 301     -26.863  -0.375   4.431  1.00 40.68           C  
HETATM 6682  O6  3L7 D 301     -27.071  -0.031   5.698  1.00 37.04           O  
HETATM 6683  C5  3L7 D 301     -27.607  -1.472   3.827  1.00 42.29           C  
HETATM 6684  N7  3L7 D 301     -28.586  -2.351   4.305  1.00 41.39           N  
HETATM 6685  C8  3L7 D 301     -28.925  -3.180   3.298  1.00 40.50           C  
HETATM 6686 MG    MG D 302     -23.121  -6.852  -1.000  1.00 26.21          MG  
HETATM 6687 MG    MG D 303     -25.740  -0.547  -2.907  1.00 45.21          MG  
HETATM 6688  O   HOH A 401       8.285  12.435   3.609  1.00 26.92           O  
HETATM 6689  O   HOH A 402      15.858   5.506  11.235  1.00 26.44           O  
HETATM 6690  O   HOH A 403       7.968  -9.955   9.122  1.00 31.00           O  
HETATM 6691  O   HOH A 404      15.153  17.070  10.439  1.00 37.46           O  
HETATM 6692  O   HOH A 405       8.043   9.541  12.387  1.00 31.36           O  
HETATM 6693  O   HOH A 406       9.452  -7.993   2.006  1.00 28.91           O  
HETATM 6694  O   HOH A 407       5.285  -2.739   1.644  1.00 34.85           O  
HETATM 6695  O   HOH A 408       2.520  -3.775  14.955  1.00 34.48           O  
HETATM 6696  O   HOH A 409      21.818  -7.596  -3.050  1.00 36.85           O  
HETATM 6697  O   HOH A 410       7.847   4.557   8.277  1.00 39.70           O  
HETATM 6698  O   HOH A 411      26.827   3.052  14.226  1.00 40.20           O  
HETATM 6699  O   HOH A 412      29.274   2.203  14.147  1.00 35.93           O  
HETATM 6700  O   HOH A 413      17.013   3.268  30.713  1.00 55.05           O  
HETATM 6701  O   HOH A 414      16.313  16.919  13.791  1.00 38.84           O  
HETATM 6702  O   HOH A 415       7.180   0.493  17.200  1.00 35.11           O  
HETATM 6703  O   HOH A 416      31.129  -0.010   7.421  1.00 45.01           O  
HETATM 6704  O   HOH A 417       2.613  -8.212  19.409  1.00 38.95           O  
HETATM 6705  O   HOH A 418      21.781   7.104  15.752  1.00 34.65           O  
HETATM 6706  O   HOH A 419       6.589  -6.816   1.984  1.00 40.18           O  
HETATM 6707  O   HOH A 420      10.213 -15.289   2.395  1.00 37.44           O  
HETATM 6708  O   HOH A 421      13.357  15.745 -12.744  1.00 48.12           O  
HETATM 6709  O   HOH A 422       5.914  -8.693  10.295  1.00 28.72           O  
HETATM 6710  O   HOH A 423       5.084  -0.291  20.682  1.00 39.43           O  
HETATM 6711  O   HOH A 424      31.852  -2.928  34.185  1.00 41.21           O  
HETATM 6712  O   HOH A 425      17.140 -11.431   4.702  1.00 39.12           O  
HETATM 6713  O   HOH A 426      25.446   6.113  13.118  1.00 42.19           O  
HETATM 6714  O   HOH A 427      15.894  14.239  -9.052  1.00 43.14           O  
HETATM 6715  O   HOH A 428       4.949  -4.655   4.467  1.00 41.01           O  
HETATM 6716  O   HOH A 429       6.155  18.339  -2.900  1.00 46.46           O  
HETATM 6717  O   HOH A 430      19.572 -11.545   4.541  1.00 46.34           O  
HETATM 6718  O   HOH A 431      20.186  -4.324  -5.176  1.00 56.18           O  
HETATM 6719  O   HOH A 432      33.206  -3.142  21.297  1.00 47.60           O  
HETATM 6720  O   HOH A 433      27.421  -7.322   8.447  1.00 52.95           O  
HETATM 6721  O   HOH A 434      27.635  -7.378  16.483  1.00 49.57           O  
HETATM 6722  O   HOH A 435      18.166   0.252  -8.440  1.00 48.88           O  
HETATM 6723  O   HOH A 436       7.555  17.406  -9.004  1.00 51.35           O  
HETATM 6724  O   HOH A 437      13.530   0.212  -9.954  1.00 46.42           O  
HETATM 6725  O   HOH A 438      10.765 -15.830  12.300  1.00 43.22           O  
HETATM 6726  O   HOH A 439      20.020  -2.143  -5.767  1.00 43.23           O  
HETATM 6727  O   HOH A 440       8.457  16.597   5.965  1.00 38.55           O  
HETATM 6728  O   HOH A 441      28.295  12.437  -1.042  1.00 46.97           O  
HETATM 6729  O   HOH A 442      23.608  -8.043  -5.331  1.00 57.06           O  
HETATM 6730  O   HOH A 443       9.737 -11.251  30.633  1.00 53.54           O  
HETATM 6731  O   HOH A 444      23.721   8.443  19.042  1.00 48.84           O  
HETATM 6732  O   HOH A 445      35.050   2.827  19.371  1.00 54.81           O  
HETATM 6733  O   HOH A 446      17.138 -17.212  22.969  1.00 38.19           O  
HETATM 6734  O   HOH A 447      16.555 -17.159  20.348  1.00 40.45           O  
HETATM 6735  O   HOH A 448      21.574  10.133  11.630  1.00 40.78           O  
HETATM 6736  O   HOH A 449      24.783   6.915  16.371  1.00 42.43           O  
HETATM 6737  O   HOH A 450      23.355   8.260  13.669  1.00 40.58           O  
HETATM 6738  O   HOH A 451      24.751  13.628  10.173  1.00 49.38           O  
HETATM 6739  O   HOH A 452      24.162  10.678  11.479  1.00 50.24           O  
HETATM 6740  O   HOH A 453       4.747  -0.719   5.120  1.00 72.45           O  
HETATM 6741  O   HOH B 401      -3.756  -2.392 -23.030  1.00 38.23           O  
HETATM 6742  O   HOH B 402      -9.729   1.810  -2.340  1.00 32.81           O  
HETATM 6743  O   HOH B 403       2.823 -11.238  -0.455  1.00 26.30           O  
HETATM 6744  O   HOH B 404      -1.231  -3.104  -1.421  1.00 32.12           O  
HETATM 6745  O   HOH B 405      -3.512 -15.975  -7.485  1.00 32.23           O  
HETATM 6746  O   HOH B 406      12.191 -14.926   0.735  1.00 31.05           O  
HETATM 6747  O   HOH B 407      14.259 -16.922   1.917  1.00 32.08           O  
HETATM 6748  O   HOH B 408       2.453  -5.878   1.347  1.00 44.12           O  
HETATM 6749  O   HOH B 409      -3.066  -4.242  -9.497  1.00 28.32           O  
HETATM 6750  O   HOH B 410      12.831   7.003 -14.408  1.00 35.79           O  
HETATM 6751  O   HOH B 411      19.476  -8.130  -4.396  1.00 40.84           O  
HETATM 6752  O   HOH B 412       1.545  11.184 -13.507  1.00 39.76           O  
HETATM 6753  O   HOH B 413      -2.326  10.455  -0.829  1.00 31.18           O  
HETATM 6754  O   HOH B 414      -3.151  -9.335 -14.781  1.00 48.25           O  
HETATM 6755  O   HOH B 415       8.639  15.702  -6.127  1.00 35.93           O  
HETATM 6756  O   HOH B 416       0.227 -15.213  -0.342  1.00 36.38           O  
HETATM 6757  O   HOH B 417       5.824   3.873   1.367  1.00 39.14           O  
HETATM 6758  O   HOH B 418       6.192   8.869  -3.008  1.00 38.33           O  
HETATM 6759  O   HOH B 419       6.677  16.070  -4.487  1.00 37.09           O  
HETATM 6760  O   HOH B 420     -11.778  10.939   1.622  1.00 39.84           O  
HETATM 6761  O   HOH B 421      -1.571 -13.722 -17.150  1.00 37.71           O  
HETATM 6762  O   HOH B 422       4.799  11.651 -11.555  1.00 41.31           O  
HETATM 6763  O   HOH B 423      -7.575   6.340   2.416  1.00 37.62           O  
HETATM 6764  O   HOH B 424       7.615 -22.814  -5.182  1.00 54.16           O  
HETATM 6765  O   HOH B 425       5.071 -11.366  -0.776  1.00 39.89           O  
HETATM 6766  O   HOH B 426      -3.118 -24.925  -6.408  1.00 55.77           O  
HETATM 6767  O   HOH B 427       4.804 -23.843   1.242  1.00 49.16           O  
HETATM 6768  O   HOH B 428      -3.239   5.472   1.876  1.00 48.08           O  
HETATM 6769  O   HOH B 429      -0.614 -13.446 -19.983  1.00 44.52           O  
HETATM 6770  O   HOH B 430      -0.661  -8.881 -24.121  1.00 46.32           O  
HETATM 6771  O   HOH B 431      -2.867   3.446   0.941  1.00 57.86           O  
HETATM 6772  O   HOH B 432      -1.913 -16.951  -0.407  1.00 47.25           O  
HETATM 6773  O   HOH B 433       2.771   7.918 -20.720  1.00 53.73           O  
HETATM 6774  O   HOH B 434      -1.660 -11.369 -24.025  1.00 57.55           O  
HETATM 6775  O   HOH B 435      12.561  -4.765 -23.088  1.00 47.25           O  
HETATM 6776  O   HOH B 436     -16.157 -10.593 -12.696  1.00 66.01           O  
HETATM 6777  O   HOH B 437      11.168   8.860 -15.647  1.00 47.90           O  
HETATM 6778  O   HOH B 438       5.787   7.417  -0.077  1.00 61.28           O  
HETATM 6779  O   HOH B 439       2.854   9.225 -15.411  1.00 42.17           O  
HETATM 6780  O   HOH B 440      12.353   9.221 -18.555  1.00 52.30           O  
HETATM 6781  O   HOH B 441      -1.525 -16.322 -17.882  1.00 44.43           O  
HETATM 6782  O   HOH B 442     -12.228  -7.454 -27.862  1.00 68.46           O  
HETATM 6783  O   HOH B 443      16.218   0.437 -20.785  1.00 52.72           O  
HETATM 6784  O   HOH B 444      16.255   0.046 -13.476  1.00 38.85           O  
HETATM 6785  O   HOH B 445      11.320 -22.724   0.362  1.00 62.53           O  
HETATM 6786  O   HOH B 446      -2.539 -10.786 -16.969  1.00 37.23           O  
HETATM 6787  O   HOH B 447      -4.640 -14.523 -16.855  1.00 41.20           O  
HETATM 6788  O   HOH B 448      -4.091 -12.701 -19.169  1.00 44.51           O  
HETATM 6789  O   HOH C 401      -0.720  11.582  -2.648  1.00 35.45           O  
HETATM 6790  O   HOH C 402       1.635  15.962  33.011  1.00 34.96           O  
HETATM 6791  O   HOH C 403       2.813   6.511  22.406  1.00 34.91           O  
HETATM 6792  O   HOH C 404      -5.163  10.541  38.929  1.00 44.85           O  
HETATM 6793  O   HOH C 405       3.050  10.694  31.284  1.00 32.10           O  
HETATM 6794  O   HOH C 406       4.693   9.655   6.385  1.00 38.94           O  
HETATM 6795  O   HOH C 407       2.570  14.206  31.073  1.00 38.56           O  
HETATM 6796  O   HOH C 408      -3.653  14.581   8.560  1.00 37.52           O  
HETATM 6797  O   HOH C 409     -14.122  16.562  10.177  1.00 34.83           O  
HETATM 6798  O   HOH C 410      -7.275 -12.382  21.429  1.00 38.57           O  
HETATM 6799  O   HOH C 411       6.548   9.696  28.325  1.00 35.13           O  
HETATM 6800  O   HOH C 412       3.720   3.362  33.995  1.00 41.27           O  
HETATM 6801  O   HOH C 413      -0.163  10.390  37.550  1.00 44.89           O  
HETATM 6802  O   HOH C 414       7.056  14.930   4.000  1.00 36.81           O  
HETATM 6803  O   HOH C 415       2.481   4.827  35.892  1.00 46.81           O  
HETATM 6804  O   HOH C 416     -14.101  19.608  11.498  1.00 48.24           O  
HETATM 6805  O   HOH C 417      -6.981   4.232   9.656  1.00 39.96           O  
HETATM 6806  O   HOH C 418       3.169  13.347  38.128  1.00 45.87           O  
HETATM 6807  O   HOH C 419      -7.308  18.439  20.543  1.00 39.67           O  
HETATM 6808  O   HOH C 420      -4.916   6.929   8.288  1.00 43.07           O  
HETATM 6809  O   HOH C 421       3.857   5.917  32.232  1.00 38.33           O  
HETATM 6810  O   HOH C 422      -9.222   9.218  39.865  1.00 42.85           O  
HETATM 6811  O   HOH C 423       0.677 -14.588  20.041  1.00 46.44           O  
HETATM 6812  O   HOH C 424       4.464  -8.197  21.195  1.00 38.98           O  
HETATM 6813  O   HOH C 425     -12.387  16.686   8.286  1.00 45.27           O  
HETATM 6814  O   HOH C 426      -9.396  10.443  10.624  1.00 36.27           O  
HETATM 6815  O   HOH C 427      -6.860  19.362  17.887  1.00 38.18           O  
HETATM 6816  O   HOH C 428     -17.161   6.029  25.009  1.00 55.16           O  
HETATM 6817  O   HOH C 429       0.573  -5.969  19.114  1.00 36.33           O  
HETATM 6818  O   HOH C 430     -19.731   7.780  24.217  1.00 56.89           O  
HETATM 6819  O   HOH C 431     -16.141  12.919  21.751  1.00 42.49           O  
HETATM 6820  O   HOH C 432      10.873   2.374  34.640  1.00 61.69           O  
HETATM 6821  O   HOH C 433      11.619  33.828  22.456  1.00 54.18           O  
HETATM 6822  O   HOH C 434       1.579   2.478  15.064  1.00 33.13           O  
HETATM 6823  O   HOH C 435      -1.854  -6.265  19.906  1.00 39.76           O  
HETATM 6824  O   HOH C 436       4.295   1.589  35.741  1.00 47.42           O  
HETATM 6825  O   HOH C 437      -1.529  13.027   7.233  1.00 41.62           O  
HETATM 6826  O   HOH C 438       5.162   5.721  35.219  1.00 57.38           O  
HETATM 6827  O   HOH C 439       3.332 -16.913  24.752  1.00 53.04           O  
HETATM 6828  O   HOH C 440      10.201  10.638  30.798  1.00 46.98           O  
HETATM 6829  O   HOH C 441       4.486  25.097  34.091  1.00 50.52           O  
HETATM 6830  O   HOH C 442       0.645  23.994   3.676  1.00 64.08           O  
HETATM 6831  O   HOH C 443      -9.780  17.547  16.498  1.00 48.77           O  
HETATM 6832  O   HOH C 444      -2.493 -14.174  19.509  1.00 44.26           O  
HETATM 6833  O   HOH C 445       9.887  -1.063  28.028  1.00 46.58           O  
HETATM 6834  O   HOH C 446       4.872  20.001  -0.319  1.00 75.11           O  
HETATM 6835  O   HOH C 447      18.298  12.100  23.921  1.00 55.46           O  
HETATM 6836  O   HOH C 448       6.007  11.907  30.780  1.00 43.65           O  
HETATM 6837  O   HOH C 449       8.209  11.052  31.886  1.00 58.64           O  
HETATM 6838  O   HOH C 450       5.937   9.684  30.549  1.00 57.32           O  
HETATM 6839  O   HOH C 451       4.537   8.021  30.284  1.00 38.58           O  
HETATM 6840  O   HOH C 452       6.895   3.469  34.081  1.00 60.93           O  
HETATM 6841  O   HOH C 453       6.953   5.881  33.941  1.00 81.26           O  
HETATM 6842  O   HOH D 401     -23.433  -4.534  -1.203  1.00 37.81           O  
HETATM 6843  O   HOH D 402     -18.933   6.530  -4.292  1.00 33.33           O  
HETATM 6844  O   HOH D 403     -15.950  -3.272   1.572  1.00 29.54           O  
HETATM 6845  O   HOH D 404      -5.664  -7.416  -1.515  1.00 29.90           O  
HETATM 6846  O   HOH D 405     -27.223 -11.794   2.109  1.00 30.50           O  
HETATM 6847  O   HOH D 406     -19.911   3.947  -6.880  1.00 33.94           O  
HETATM 6848  O   HOH D 407      -8.761 -27.419   4.266  1.00 35.75           O  
HETATM 6849  O   HOH D 408      -4.755  -0.751  12.922  1.00 37.43           O  
HETATM 6850  O   HOH D 409       1.831 -13.506   0.831  1.00 37.34           O  
HETATM 6851  O   HOH D 410     -24.925  -6.879   0.361  1.00 43.00           O  
HETATM 6852  O   HOH D 411      -6.541  -6.758  15.826  1.00 36.26           O  
HETATM 6853  O   HOH D 412     -11.917   9.022   3.464  1.00 29.81           O  
HETATM 6854  O   HOH D 413     -16.675 -14.010  13.222  1.00 35.07           O  
HETATM 6855  O   HOH D 414       5.445 -18.660   3.707  1.00 38.79           O  
HETATM 6856  O   HOH D 415     -18.451 -25.781   3.562  1.00 41.71           O  
HETATM 6857  O   HOH D 416      -2.247 -10.334   9.034  1.00 31.96           O  
HETATM 6858  O   HOH D 417      -8.564   0.450   3.729  1.00 43.74           O  
HETATM 6859  O   HOH D 418     -12.764 -13.000  16.178  1.00 46.54           O  
HETATM 6860  O   HOH D 419      -6.726 -15.625  -9.362  1.00 35.98           O  
HETATM 6861  O   HOH D 420      -8.489 -25.785   6.150  1.00 39.61           O  
HETATM 6862  O   HOH D 421     -25.324 -10.073   1.328  1.00 38.09           O  
HETATM 6863  O   HOH D 422      -0.145  -8.007   2.246  1.00 37.08           O  
HETATM 6864  O   HOH D 423     -18.973  -7.216  20.875  1.00 40.13           O  
HETATM 6865  O   HOH D 424      -3.845 -11.568  10.929  1.00 34.88           O  
HETATM 6866  O   HOH D 425     -26.783   0.697  -1.277  1.00 42.87           O  
HETATM 6867  O   HOH D 426       4.283 -20.579  10.894  1.00 52.54           O  
HETATM 6868  O   HOH D 427      -3.620  -3.940  11.752  1.00 45.34           O  
HETATM 6869  O   HOH D 428     -14.152 -15.122  13.142  1.00 38.76           O  
HETATM 6870  O   HOH D 429     -26.789 -19.632   8.406  1.00 47.29           O  
HETATM 6871  O   HOH D 430      -5.281 -13.132  19.782  1.00 47.94           O  
HETATM 6872  O   HOH D 431     -28.672   2.806  -2.242  1.00 47.44           O  
HETATM 6873  O   HOH D 432     -32.010  -8.850  -0.845  1.00 47.67           O  
HETATM 6874  O   HOH D 433     -13.025  10.720  -0.588  1.00 38.55           O  
HETATM 6875  O   HOH D 434     -28.803 -21.421   0.040  1.00 45.18           O  
HETATM 6876  O   HOH D 435     -28.145  -3.223  21.441  1.00 58.47           O  
HETATM 6877  O   HOH D 436     -22.403 -15.423  12.456  1.00 51.31           O  
HETATM 6878  O   HOH D 437     -31.748  -2.602   5.676  1.00 56.07           O  
HETATM 6879  O   HOH D 438     -22.188 -20.045   5.413  1.00 47.48           O  
HETATM 6880  O   HOH D 439     -31.600   4.619   8.440  1.00 52.41           O  
HETATM 6881  O   HOH D 440      -4.673 -23.669   8.606  1.00 55.66           O  
HETATM 6882  O   HOH D 441     -19.172  18.673  15.915  1.00 49.55           O  
HETATM 6883  O   HOH D 442     -24.281 -21.451 -13.546  1.00 55.78           O  
HETATM 6884  O   HOH D 443      -0.294  -5.429   1.187  1.00 51.06           O  
HETATM 6885  O   HOH D 444     -23.913 -13.482  12.955  1.00 53.07           O  
HETATM 6886  O   HOH D 445     -21.686  -6.298  -2.486  1.00 36.64           O  
HETATM 6887  O   HOH D 446     -26.329   0.263  -5.030  1.00 53.49           O  
HETATM 6888  O   HOH D 447     -24.178  -7.868  -2.229  1.00 49.33           O  
CONECT  910 6568                                                                
CONECT  911 6568                                                                
CONECT  918 6568                                                                
CONECT 1385 6569                                                                
CONECT 2539 6626                                                                
CONECT 2540 6626                                                                
CONECT 2542 6626                                                                
CONECT 2551 6626                                                                
CONECT 3021 6627                                                                
CONECT 4172 6656                                                                
CONECT 4180 6656                                                                
CONECT 4653 6657                                                                
CONECT 5847 6686                                                                
CONECT 5855 6686                                                                
CONECT 6332 6687                                                                
CONECT 6540 6541 6569                                                           
CONECT 6541 6540 6542 6543 6544                                                 
CONECT 6542 6541                                                                
CONECT 6543 6541                                                                
CONECT 6544 6541 6545                                                           
CONECT 6545 6544 6546                                                           
CONECT 6546 6545 6547                                                           
CONECT 6547 6546 6548                                                           
CONECT 6548 6547 6549                                                           
CONECT 6549 6548 6550 6556                                                      
CONECT 6550 6549 6551                                                           
CONECT 6551 6550 6552                                                           
CONECT 6552 6551 6553 6554 6555                                                 
CONECT 6553 6552                                                                
CONECT 6554 6552                                                                
CONECT 6555 6552                                                                
CONECT 6556 6549 6557                                                           
CONECT 6557 6556 6558                                                           
CONECT 6558 6557 6559 6567                                                      
CONECT 6559 6558 6560 6565                                                      
CONECT 6560 6559 6561                                                           
CONECT 6561 6560 6562                                                           
CONECT 6562 6561 6563                                                           
CONECT 6563 6562 6564 6565                                                      
CONECT 6564 6563                                                                
CONECT 6565 6559 6563 6566                                                      
CONECT 6566 6565 6567                                                           
CONECT 6567 6558 6566                                                           
CONECT 6568  910  911  918 6705                                                 
CONECT 6568 6713 6736 6737                                                      
CONECT 6569 1385 6540 6738 6739                                                 
CONECT 6570 6572                                                                
CONECT 6571 6573                                                                
CONECT 6572 6570 6574 6576 6578                                                 
CONECT 6573 6571 6575 6577 6579                                                 
CONECT 6574 6572                                                                
CONECT 6575 6573 6627                                                           
CONECT 6576 6572                                                                
CONECT 6577 6573                                                                
CONECT 6578 6572 6580                                                           
CONECT 6579 6573 6581                                                           
CONECT 6580 6578 6582                                                           
CONECT 6581 6579 6583                                                           
CONECT 6582 6580 6584                                                           
CONECT 6583 6581 6585 6626                                                      
CONECT 6584 6582 6586                                                           
CONECT 6585 6583 6587                                                           
CONECT 6586 6584 6588                                                           
CONECT 6587 6585 6589                                                           
CONECT 6588 6586 6590 6602                                                      
CONECT 6589 6587 6591 6603                                                      
CONECT 6590 6588 6592                                                           
CONECT 6591 6589 6593                                                           
CONECT 6592 6590 6594                                                           
CONECT 6593 6591 6595                                                           
CONECT 6594 6592 6596 6598 6600                                                 
CONECT 6595 6593 6597 6599 6601                                                 
CONECT 6596 6594                                                                
CONECT 6597 6595                                                                
CONECT 6598 6594                                                                
CONECT 6599 6595                                                                
CONECT 6600 6594                                                                
CONECT 6601 6595                                                                
CONECT 6602 6588 6604                                                           
CONECT 6603 6589 6605                                                           
CONECT 6604 6602 6606                                                           
CONECT 6605 6603 6607                                                           
CONECT 6606 6604 6608 6624                                                      
CONECT 6607 6605 6609 6625                                                      
CONECT 6608 6606 6610 6620                                                      
CONECT 6609 6607 6611 6621                                                      
CONECT 6610 6608 6612                                                           
CONECT 6611 6609 6613                                                           
CONECT 6612 6610 6614                                                           
CONECT 6613 6611 6615                                                           
CONECT 6614 6612 6616                                                           
CONECT 6615 6613 6617                                                           
CONECT 6616 6614 6618 6620                                                      
CONECT 6617 6615 6619 6621                                                      
CONECT 6618 6616                                                                
CONECT 6619 6617                                                                
CONECT 6620 6608 6616 6622                                                      
CONECT 6621 6609 6617 6623                                                      
CONECT 6622 6620 6624                                                           
CONECT 6623 6621 6625                                                           
CONECT 6624 6606 6622                                                           
CONECT 6625 6607 6623                                                           
CONECT 6626 2539 2540 2542 2551                                                 
CONECT 6626 6583                                                                
CONECT 6627 3021 6575 6761 6786                                                 
CONECT 6627 6787 6788                                                           
CONECT 6628 6629                                                                
CONECT 6629 6628 6630 6631 6632                                                 
CONECT 6630 6629                                                                
CONECT 6631 6629 6657                                                           
CONECT 6632 6629 6633                                                           
CONECT 6633 6632 6634                                                           
CONECT 6634 6633 6635                                                           
CONECT 6635 6634 6636                                                           
CONECT 6636 6635 6637                                                           
CONECT 6637 6636 6638 6644                                                      
CONECT 6638 6637 6639                                                           
CONECT 6639 6638 6640                                                           
CONECT 6640 6639 6641 6642 6643                                                 
CONECT 6641 6640                                                                
CONECT 6642 6640                                                                
CONECT 6643 6640                                                                
CONECT 6644 6637 6645                                                           
CONECT 6645 6644 6646                                                           
CONECT 6646 6645 6647 6655                                                      
CONECT 6647 6646 6648 6653                                                      
CONECT 6648 6647 6649                                                           
CONECT 6649 6648 6650                                                           
CONECT 6650 6649 6651                                                           
CONECT 6651 6650 6652 6653                                                      
CONECT 6652 6651                                                                
CONECT 6653 6647 6651 6654                                                      
CONECT 6654 6653 6655                                                           
CONECT 6655 6646 6654                                                           
CONECT 6656 4172 4180 6793 6799                                                 
CONECT 6656 6836 6838 6839                                                      
CONECT 6657 4653 6631 6800 6809                                                 
CONECT 6657 6826 6840 6841                                                      
CONECT 6658 6659                                                                
CONECT 6659 6658 6660 6661 6662                                                 
CONECT 6660 6659 6687                                                           
CONECT 6661 6659                                                                
CONECT 6662 6659 6663                                                           
CONECT 6663 6662 6664                                                           
CONECT 6664 6663 6665                                                           
CONECT 6665 6664 6666                                                           
CONECT 6666 6665 6667                                                           
CONECT 6667 6666 6668 6674                                                      
CONECT 6668 6667 6669                                                           
CONECT 6669 6668 6670                                                           
CONECT 6670 6669 6671 6672 6673                                                 
CONECT 6671 6670                                                                
CONECT 6672 6670                                                                
CONECT 6673 6670                                                                
CONECT 6674 6667 6675                                                           
CONECT 6675 6674 6676                                                           
CONECT 6676 6675 6677 6685                                                      
CONECT 6677 6676 6678 6683                                                      
CONECT 6678 6677 6679                                                           
CONECT 6679 6678 6680                                                           
CONECT 6680 6679 6681                                                           
CONECT 6681 6680 6682 6683                                                      
CONECT 6682 6681                                                                
CONECT 6683 6677 6681 6684                                                      
CONECT 6684 6683 6685                                                           
CONECT 6685 6676 6684                                                           
CONECT 6686 5847 5855 6842 6851                                                 
CONECT 6686 6886 6888                                                           
CONECT 6687 6332 6660 6866 6887                                                 
CONECT 6705 6568                                                                
CONECT 6713 6568                                                                
CONECT 6736 6568                                                                
CONECT 6737 6568                                                                
CONECT 6738 6569                                                                
CONECT 6739 6569                                                                
CONECT 6761 6627                                                                
CONECT 6786 6627                                                                
CONECT 6787 6627                                                                
CONECT 6788 6627                                                                
CONECT 6793 6656                                                                
CONECT 6799 6656                                                                
CONECT 6800 6657                                                                
CONECT 6809 6657                                                                
CONECT 6826 6657                                                                
CONECT 6836 6656                                                                
CONECT 6838 6656                                                                
CONECT 6839 6656                                                                
CONECT 6840 6657                                                                
CONECT 6841 6657                                                                
CONECT 6842 6686                                                                
CONECT 6851 6686                                                                
CONECT 6866 6687                                                                
CONECT 6886 6686                                                                
CONECT 6887 6687                                                                
CONECT 6888 6686                                                                
MASTER      991    0   12   29   38    0   36    6 6682    4  195   68          
END