HEADER    SIGNALING PROTEIN                       02-MAY-17   5XJM              
TITLE     COMPLEX STRUCTURE OF ANGIOTENSIN II TYPE 2 RECEPTOR WITH FAB          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE-2 ANGIOTENSIN II RECEPTOR,SOLUBLE CYTOCHROME B562,    
COMPND   3 TYPE-2 ANGIOTENSIN II RECEPTOR;                                      
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 35-242,UNP RESIDUES 246-346;                  
COMPND   6 SYNONYM: ANGIOTENSIN II TYPE-2 RECEPTOR,AT2,CYTOCHROME B-562,        
COMPND   7 ANGIOTENSIN II TYPE-2 RECEPTOR,AT2;                                  
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: FABH;                                                      
COMPND  12 CHAIN: H;                                                            
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: FABL;                                                      
COMPND  15 CHAIN: L;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: SAR1, ILE8-ANGIOTENSIN II;                                 
COMPND  19 CHAIN: B;                                                            
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: AGTR2, CYBC;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_TAXID: 10090;                                               
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_TAXID: 9606                                                 
KEYWDS    CLASS A GPCR, REGULATE HUMAN BLOOD PRESSURE, ANGIOTENSIN RECEPTORS,   
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ASADA,S.HORITA,T.SHIMAMURA,S.IWATA                                  
REVDAT   3   25-JUL-18 5XJM    1       JRNL                                     
REVDAT   2   18-JUL-18 5XJM    1       JRNL                                     
REVDAT   1   11-JUL-18 5XJM    0                                                
JRNL        AUTH   H.ASADA,S.HORITA,K.HIRATA,M.SHIROISHI,Y.SHIIMURA,H.IWANARI,  
JRNL        AUTH 2 T.HAMAKUBO,T.SHIMAMURA,N.NOMURA,O.KUSANO-ARAI,T.UEMURA,      
JRNL        AUTH 3 C.SUNO,T.KOBAYASHI,S.IWATA                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN ANGIOTENSIN II TYPE 2         
JRNL        TITL 2 RECEPTOR BOUND TO AN ANGIOTENSIN II ANALOG                   
JRNL        REF    NAT. STRUCT. MOL. BIOL.       V.  25   570 2018              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   29967536                                                     
JRNL        DOI    10.1038/S41594-018-0079-8                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 22033                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 48.3918 -  7.7025    0.99     1590   158  0.2277 0.2686        
REMARK   3     2  7.7025 -  6.1176    1.00     1458   145  0.2643 0.2611        
REMARK   3     3  6.1176 -  5.3454    1.00     1469   147  0.2270 0.2750        
REMARK   3     4  5.3454 -  4.8572    1.00     1430   143  0.1947 0.2473        
REMARK   3     5  4.8572 -  4.5093    1.00     1451   146  0.1789 0.2476        
REMARK   3     6  4.5093 -  4.2436    1.00     1429   142  0.1980 0.2163        
REMARK   3     7  4.2436 -  4.0312    1.00     1390   139  0.2072 0.2646        
REMARK   3     8  4.0312 -  3.8558    1.00     1441   143  0.2152 0.2983        
REMARK   3     9  3.8558 -  3.7074    1.00     1362   136  0.2430 0.3393        
REMARK   3    10  3.7074 -  3.5795    1.00     1450   144  0.2475 0.2919        
REMARK   3    11  3.5795 -  3.4676    1.00     1358   137  0.2437 0.3073        
REMARK   3    12  3.4676 -  3.3685    1.00     1433   143  0.2494 0.2940        
REMARK   3    13  3.3685 -  3.2799    1.00     1354   133  0.2627 0.3145        
REMARK   3    14  3.2799 -  3.1999    1.00     1420   142  0.2843 0.3172        
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)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.92                          
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      :  0.002           6505                                  
REMARK   3   ANGLE     :  0.520           8864                                  
REMARK   3   CHIRALITY :  0.038           1010                                  
REMARK   3   PLANARITY :  0.004           1104                                  
REMARK   3   DIHEDRAL  : 12.071           3850                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 35 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5905  25.4183   7.0986              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2403 T22:   1.5293                                     
REMARK   3      T33:   1.6361 T12:   0.1733                                     
REMARK   3      T13:  -0.1119 T23:   0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4799 L22:   1.0089                                     
REMARK   3      L33:   0.6751 L12:  -0.7148                                     
REMARK   3      L13:  -0.2479 L23:   0.0458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1023 S12:   0.0531 S13:   0.4351                       
REMARK   3      S21:  -0.0704 S22:  -0.0464 S23:   0.4152                       
REMARK   3      S31:  -0.2545 S32:  -0.5628 S33:   0.0151                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   45.893   19.506   17.964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2343 T22:   1.5460                                     
REMARK   3      T33:   1.7547 T12:   0.2351                                     
REMARK   3      T13:   0.0788 T23:   0.0356                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4132 L22:   0.2684                                     
REMARK   3      L33:   0.2715 L12:  -0.2185                                     
REMARK   3      L13:  -0.6734 L23:   0.1404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0050 S12:  -0.2729 S13:  -0.2871                       
REMARK   3      S21:   0.3043 S22:   0.1360 S23:   0.5412                       
REMARK   3      S31:   0.1533 S32:  -0.1696 S33:   0.1493                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 84 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  80.7259  16.9679  -8.3929              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2837 T22:   0.5640                                     
REMARK   3      T33:   0.3915 T12:   0.1380                                     
REMARK   3      T13:  -0.1173 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3950 L22:   1.6166                                     
REMARK   3      L33:   0.5564 L12:  -0.4135                                     
REMARK   3      L13:  -0.4650 L23:  -0.0889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0681 S12:   0.2437 S13:   0.0222                       
REMARK   3      S21:  -0.5791 S22:  -0.1894 S23:   0.6229                       
REMARK   3      S31:  -0.1264 S32:  -0.7588 S33:  -0.0735                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 85 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  84.7518  13.9075  -4.8115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2576 T22:   0.3183                                     
REMARK   3      T33:   0.2507 T12:   0.1466                                     
REMARK   3      T13:  -0.1939 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0793 L22:   2.3350                                     
REMARK   3      L33:   7.8547 L12:   1.6229                                     
REMARK   3      L13:  -3.8799 L23:  -1.7101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1533 S12:   0.0380 S13:   0.0597                       
REMARK   3      S21:  -0.4649 S22:  -0.2269 S23:   0.5319                       
REMARK   3      S31:  -0.0770 S32:  -0.3395 S33:  -0.0177                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 108.1095  -2.8119 -18.8423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2659 T22:   0.4238                                     
REMARK   3      T33:   0.0412 T12:   0.0088                                     
REMARK   3      T13:   0.0087 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5659 L22:   3.9333                                     
REMARK   3      L33:   3.1125 L12:   0.0733                                     
REMARK   3      L13:   1.2624 L23:  -1.6933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1722 S12:   0.2748 S13:  -0.1830                       
REMARK   3      S21:  -0.1927 S22:  -0.1602 S23:  -0.1922                       
REMARK   3      S31:   0.1620 S32:  -0.1652 S33:  -0.0503                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 163 THROUGH 220 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 105.9974  -7.1247 -17.6726              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2699 T22:   0.3608                                     
REMARK   3      T33:   0.1733 T12:   0.0285                                     
REMARK   3      T13:  -0.0122 T23:  -0.2243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9352 L22:   3.5271                                     
REMARK   3      L33:   3.0199 L12:  -1.0723                                     
REMARK   3      L13:   0.3170 L23:  -0.6349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3329 S12:   0.5598 S13:  -0.2308                       
REMARK   3      S21:  -0.3230 S22:  -0.1855 S23:   0.0823                       
REMARK   3      S31:   0.2767 S32:  -0.3247 S33:   0.0938                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  98.7637   9.0754  12.6065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1731 T22:   0.1560                                     
REMARK   3      T33:   0.1603 T12:  -0.0064                                     
REMARK   3      T13:  -0.0420 T23:  -0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0545 L22:   4.1766                                     
REMARK   3      L33:   2.7869 L12:   0.9949                                     
REMARK   3      L13:  -0.3561 L23:   1.1143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:  -0.1776 S13:  -0.1826                       
REMARK   3      S21:   0.2792 S22:   0.1260 S23:  -0.4621                       
REMARK   3      S31:   0.2038 S32:  -0.1538 S33:  -0.2027                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 74 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  88.0382   9.2319  12.5622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0960 T22:   0.4037                                     
REMARK   3      T33:   0.1811 T12:  -0.0200                                     
REMARK   3      T13:   0.0799 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8500 L22:   1.6439                                     
REMARK   3      L33:   2.5868 L12:   0.3650                                     
REMARK   3      L13:  -0.2520 L23:   0.6276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0252 S12:  -0.2281 S13:   0.1514                       
REMARK   3      S21:   0.1758 S22:   0.0783 S23:   0.3180                       
REMARK   3      S31:   0.3657 S32:  -0.6325 S33:   0.0789                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 75 THROUGH 90 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  91.8751   4.8426  10.1778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1250 T22:   0.4221                                     
REMARK   3      T33:   0.1704 T12:  -0.1010                                     
REMARK   3      T13:  -0.0886 T23:   0.0511                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1373 L22:   2.7674                                     
REMARK   3      L33:   3.9421 L12:  -1.1670                                     
REMARK   3      L13:   0.0011 L23:   0.8874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0898 S12:  -0.2796 S13:   0.0289                       
REMARK   3      S21:  -0.0241 S22:   0.0946 S23:   0.2546                       
REMARK   3      S31:   0.6406 S32:  -0.0275 S33:  -0.2373                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 142 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 108.8797   1.0659  -4.7133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2670 T22:   0.2303                                     
REMARK   3      T33:   0.0104 T12:   0.0538                                     
REMARK   3      T13:   0.0254 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4184 L22:   0.3948                                     
REMARK   3      L33:   0.2198 L12:   0.0791                                     
REMARK   3      L13:  -0.0601 L23:   0.0016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0782 S12:   0.1089 S13:   0.0471                       
REMARK   3      S21:   0.0031 S22:  -0.0269 S23:   0.0081                       
REMARK   3      S31:   0.2228 S32:  -0.1740 S33:  -0.0091                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 143 THROUGH 173 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 116.2380   1.3068  -5.6379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2163 T22:   0.1238                                     
REMARK   3      T33:   0.0053 T12:   0.0057                                     
REMARK   3      T13:  -0.0480 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6767 L22:   1.8074                                     
REMARK   3      L33:   5.1696 L12:   1.1939                                     
REMARK   3      L13:  -3.8915 L23:  -1.8792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0383 S12:   0.1254 S13:   0.1287                       
REMARK   3      S21:  -0.1909 S22:  -0.0312 S23:   0.0073                       
REMARK   3      S31:  -0.0363 S32:  -0.2637 S33:   0.0274                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 174 THROUGH 186 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 121.9182   3.3303 -19.2364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3724 T22:   0.2794                                     
REMARK   3      T33:   0.0667 T12:   0.0399                                     
REMARK   3      T13:   0.0877 T23:   0.0943                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2336 L22:   1.3988                                     
REMARK   3      L33:   2.0370 L12:   0.3356                                     
REMARK   3      L13:  -1.0620 L23:  -0.2620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1354 S12:   0.2688 S13:   0.1615                       
REMARK   3      S21:  -0.3082 S22:  -0.0825 S23:  -0.1573                       
REMARK   3      S31:  -0.2147 S32:   0.1185 S33:  -0.0332                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 187 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 126.8369  -3.6899  -9.0790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2054 T22:   0.0208                                     
REMARK   3      T33:   0.1581 T12:   0.0998                                     
REMARK   3      T13:  -0.0322 T23:   0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8277 L22:   1.1182                                     
REMARK   3      L33:   2.0743 L12:  -0.3139                                     
REMARK   3      L13:  -0.3834 L23:   0.8527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1386 S12:   0.2221 S13:  -0.0472                       
REMARK   3      S21:   0.0225 S22:  -0.0098 S23:  -0.1819                       
REMARK   3      S31:  -0.1344 S32:   0.1120 S33:  -0.1345                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 8 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  59.8374  22.4997  13.6093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3457 T22:   1.3568                                     
REMARK   3      T33:   1.3769 T12:  -0.1118                                     
REMARK   3      T13:  -0.0002 T23:  -0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6152 L22:   4.2889                                     
REMARK   3      L33:   3.2824 L12:   1.9675                                     
REMARK   3      L13:  -2.3425 L23:   0.0616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2075 S12:  -0.2597 S13:  -0.1080                       
REMARK   3      S21:  -0.0410 S22:   0.1845 S23:   0.0328                       
REMARK   3      S31:  -0.1049 S32:  -0.1736 S33:   0.0661                       
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 5XJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003643.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22033                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.386                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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         : 1.610                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4YAY, 1M6T                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 34%(V/V) PEG 300, 0.1 M HEPES PH 7.0,    
REMARK 280  0.5%(V/V) TACSIMATE (PH7.0), LIPIDIC CUBIC PHASE, TEMPERATURE       
REMARK 280  293.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      232.69500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.32500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      232.69500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.32500            
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: 7160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, B                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    34                                                      
REMARK 465     PRO A  1046                                                      
REMARK 465     LYS A  1047                                                      
REMARK 465     LEU A  1048                                                      
REMARK 465     GLU A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     LYS A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     PRO A  1056                                                      
REMARK 465     GLU A  1057                                                      
REMARK 465     MET A  1058                                                      
REMARK 465     LYS A  1059                                                      
REMARK 465     VAL A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASN A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     PHE A   325                                                      
REMARK 465     GLN A   326                                                      
REMARK 465     GLN A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     LEU A   329                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     PHE A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     VAL A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     ILE A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     TRP A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     GLN A   341                                                      
REMARK 465     GLY A   342                                                      
REMARK 465     LYS A   343                                                      
REMARK 465     ARG A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     SER A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     ASN A   348                                                      
REMARK 465     LEU A   349                                                      
REMARK 465     TYR A   350                                                      
REMARK 465     PHE A   351                                                      
REMARK 465     GLN A   352                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  73      -60.37     61.62                                   
REMARK 500    LYS A  76       70.18     59.39                                   
REMARK 500    ARG A 107       74.47     57.80                                   
REMARK 500    PRO A 149        2.08    -68.15                                   
REMARK 500    SER A 152       44.00   -142.79                                   
REMARK 500    LYS A 203       53.71   -118.78                                   
REMARK 500    PHE A 220      -48.88   -157.00                                   
REMARK 500    ALA A1020      115.61   -163.31                                   
REMARK 500    ASP A1021       79.21   -117.41                                   
REMARK 500    LYS A1042       86.74    -69.39                                   
REMARK 500    ALA A1043       77.91   -157.48                                   
REMARK 500    VAL H  48      -62.67   -100.67                                   
REMARK 500    ARG H  67      -51.63   -123.02                                   
REMARK 500    TYR H 101       83.90   -161.59                                   
REMARK 500    TYR H 102      -39.86     66.24                                   
REMARK 500    CYS H 135     -158.20   -107.17                                   
REMARK 500    PHE H 153      133.13   -171.67                                   
REMARK 500    PRO H 154     -165.66    -74.74                                   
REMARK 500    SER H 163     -146.88   -124.09                                   
REMARK 500    LEU H 166     -154.17     57.68                                   
REMARK 500    THR H 194      -72.32    -80.72                                   
REMARK 500    LEU H 217       76.05     58.04                                   
REMARK 500    LEU L  46      -61.05    -97.95                                   
REMARK 500    THR L  50      -52.77     63.66                                   
REMARK 500    ALA L  83     -161.21   -161.12                                   
REMARK 500    ASN L 137       75.40     55.47                                   
REMARK 500    ASN L 189      -50.33   -127.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5XLI   RELATED DB: PDB                                   
REMARK 900 5XLI IS SAME PROTEIN AS BOTH FABH AND FABL OF 5XJM.                  
DBREF  5XJM A   35   242  UNP    P50052   AGTR2_HUMAN     35    242             
DBREF  5XJM A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  5XJM A  246   346  UNP    P50052   AGTR2_HUMAN    246    346             
DBREF  5XJM H    1   220  PDB    5XJM     5XJM             1    220             
DBREF  5XJM L    1   212  PDB    5XJM     5XJM             1    212             
DBREF  5XJM B    1     8  PDB    5XJM     5XJM             1      8             
SEQADV 5XJM GLY A   34  UNP  P50052              EXPRESSION TAG                 
SEQADV 5XJM TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 5XJM ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 5XJM LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 5XJM GLU A  347  UNP  P50052              EXPRESSION TAG                 
SEQADV 5XJM ASN A  348  UNP  P50052              EXPRESSION TAG                 
SEQADV 5XJM LEU A  349  UNP  P50052              EXPRESSION TAG                 
SEQADV 5XJM TYR A  350  UNP  P50052              EXPRESSION TAG                 
SEQADV 5XJM PHE A  351  UNP  P50052              EXPRESSION TAG                 
SEQADV 5XJM GLN A  352  UNP  P50052              EXPRESSION TAG                 
SEQRES   1 A  422  GLY CYS SER GLN LYS PRO SER ASP LYS HIS LEU ASP ALA          
SEQRES   2 A  422  ILE PRO ILE LEU TYR TYR ILE ILE PHE VAL ILE GLY PHE          
SEQRES   3 A  422  LEU VAL ASN ILE VAL VAL VAL THR LEU PHE CYS CYS GLN          
SEQRES   4 A  422  LYS GLY PRO LYS LYS VAL SER SER ILE TYR ILE PHE ASN          
SEQRES   5 A  422  LEU ALA VAL ALA ASP LEU LEU LEU LEU ALA THR LEU PRO          
SEQRES   6 A  422  LEU TRP ALA THR TYR TYR SER TYR ARG TYR ASP TRP LEU          
SEQRES   7 A  422  PHE GLY PRO VAL MET CYS LYS VAL PHE GLY SER PHE LEU          
SEQRES   8 A  422  THR LEU ASN MET PHE ALA SER ILE PHE PHE ILE THR CYS          
SEQRES   9 A  422  MET SER VAL ASP ARG TYR GLN SER VAL ILE TYR PRO PHE          
SEQRES  10 A  422  LEU SER GLN ARG ARG ASN PRO TRP GLN ALA SER TYR ILE          
SEQRES  11 A  422  VAL PRO LEU VAL TRP CYS MET ALA CYS LEU SER SER LEU          
SEQRES  12 A  422  PRO THR PHE TYR PHE ARG ASP VAL ARG THR ILE GLU TYR          
SEQRES  13 A  422  LEU GLY VAL ASN ALA CYS ILE MET ALA PHE PRO PRO GLU          
SEQRES  14 A  422  LYS TYR ALA GLN TRP SER ALA GLY ILE ALA LEU MET LYS          
SEQRES  15 A  422  ASN ILE LEU GLY PHE ILE ILE PRO LEU ILE PHE ILE ALA          
SEQRES  16 A  422  THR CYS TYR PHE GLY ILE ARG LYS HIS LEU LEU LYS THR          
SEQRES  17 A  422  ASN ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP          
SEQRES  18 A  422  ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN          
SEQRES  19 A  422  VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU          
SEQRES  20 A  422  ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS          
SEQRES  21 A  422  SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY          
SEQRES  22 A  422  PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS          
SEQRES  23 A  422  LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA          
SEQRES  24 A  422  ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN          
SEQRES  25 A  422  LYS TYR LEU LYS ASN ARG ILE THR ARG ASP GLN VAL LEU          
SEQRES  26 A  422  LYS MET ALA ALA ALA VAL VAL LEU ALA PHE ILE ILE CYS          
SEQRES  27 A  422  TRP LEU PRO PHE HIS VAL LEU THR PHE LEU ASP ALA LEU          
SEQRES  28 A  422  ALA TRP MET GLY VAL ILE ASN SER CYS GLU VAL ILE ALA          
SEQRES  29 A  422  VAL ILE ASP LEU ALA LEU PRO PHE ALA ILE LEU LEU GLY          
SEQRES  30 A  422  PHE THR ASN SER CYS VAL ASN PRO PHE LEU TYR CYS PHE          
SEQRES  31 A  422  VAL GLY ASN ARG PHE GLN GLN LYS LEU ARG SER VAL PHE          
SEQRES  32 A  422  ARG VAL PRO ILE THR TRP LEU GLN GLY LYS ARG GLU SER          
SEQRES  33 A  422  GLU ASN LEU TYR PHE GLN                                      
SEQRES   1 H  220  ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  220  PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  220  PHE THR PHE SER GLY PHE GLY MET HIS TRP VAL ARG GLN          
SEQRES   4 H  220  ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER          
SEQRES   5 H  220  SER GLY SER SER LEU ILE TYR TYR ALA ASP THR VAL LYS          
SEQRES   6 H  220  GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR          
SEQRES   7 H  220  LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  220  ALA MET TYR PHE CYS ALA THR SER LEU TYR TYR GLY THR          
SEQRES   9 H  220  PRO TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 H  220  VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO          
SEQRES  11 H  220  LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL          
SEQRES  12 H  220  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER          
SEQRES  13 H  220  VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER          
SEQRES  14 H  220  VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR          
SEQRES  15 H  220  THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP          
SEQRES  16 H  220  PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA          
SEQRES  17 H  220  SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER              
SEQRES   1 L  212  ASP ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA          
SEQRES   2 L  212  SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER          
SEQRES   3 L  212  SER SER VAL THR TYR MET TYR TRP TYR GLN GLN LYS PRO          
SEQRES   4 L  212  GLY SER SER PRO ARG LEU LEU ILE TYR ASP THR SER ASN          
SEQRES   5 L  212  LEU ALA SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY          
SEQRES   6 L  212  SER GLY THR SER TYR SER LEU THR ILE SER ARG MET GLU          
SEQRES   7 L  212  ALA GLU ASP ALA ALA THR PHE TYR CYS GLN GLN TRP SER          
SEQRES   8 L  212  SER TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU          
SEQRES   9 L  212  LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE          
SEQRES  10 L  212  PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER          
SEQRES  11 L  212  VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE          
SEQRES  12 L  212  ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN          
SEQRES  13 L  212  GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP          
SEQRES  14 L  212  SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS          
SEQRES  15 L  212  ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA          
SEQRES  16 L  212  THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE          
SEQRES  17 L  212  ASN ARG ASN GLU                                              
SEQRES   1 B    8  SAR ARG VAL TYR ILE HIS PRO ILE                              
HET    SAR  B   1       5                                                       
HETNAM     SAR SARCOSINE                                                        
FORMUL   4  SAR    C3 H7 N O2                                                   
HELIX    1 AA1 ALA A   46  LYS A   73  1                                  28    
HELIX    2 AA2 VAL A   78  TYR A  106  1                                  29    
HELIX    3 AA3 GLY A  113  TYR A  148  1                                  36    
HELIX    4 AA4 ARG A  154  PHE A  181  1                                  28    
HELIX    5 AA5 PRO A  200  GLU A  202  5                                   3    
HELIX    6 AA6 LYS A  203  PHE A  220  1                                  18    
HELIX    7 AA7 PHE A  220  LYS A 1019  1                                  42    
HELIX    8 AA8 ASN A 1022  ALA A 1040  1                                  19    
HELIX    9 AA9 PHE A 1061  ASN A 1080  1                                  20    
HELIX   10 AB1 VAL A 1084  ALA A 1100  1                                  17    
HELIX   11 AB2 ILE A 1102  MET A  284  1                                  44    
HELIX   12 AB3 SER A  289  CYS A  319  1                                  31    
HELIX   13 AB4 THR H   28  PHE H   32  5                                   5    
HELIX   14 AB5 ARG H   87  THR H   91  5                                   5    
HELIX   15 AB6 GLU L   78  ALA L   82  5                                   5    
HELIX   16 AB7 SER L  120  GLY L  127  1                                   8    
HELIX   17 AB8 LYS L  182  ARG L  187  1                                   6    
SHEET    1 AA1 2 ARG A 182  ILE A 187  0                                        
SHEET    2 AA1 2 VAL A 192  MET A 197 -1  O  ALA A 194   N  ARG A 185           
SHEET    1 AA2 4 GLN H   3  SER H   7  0                                        
SHEET    2 AA2 4 SER H  17  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3 AA2 4 THR H  78  THR H  84 -1  O  LEU H  81   N  LEU H  20           
SHEET    4 AA2 4 PHE H  68  ASP H  73 -1  N  THR H  69   O  GLN H  82           
SHEET    1 AA3 6 GLY H  10  VAL H  12  0                                        
SHEET    2 AA3 6 THR H 114  VAL H 118  1  O  THR H 117   N  GLY H  10           
SHEET    3 AA3 6 ALA H  92  ALA H  97 -1  N  TYR H  94   O  THR H 114           
SHEET    4 AA3 6 MET H  34  GLN H  39 -1  N  VAL H  37   O  PHE H  95           
SHEET    5 AA3 6 LEU H  45  ILE H  51 -1  O  VAL H  48   N  TRP H  36           
SHEET    6 AA3 6 ILE H  58  TYR H  60 -1  O  TYR H  59   N  TYR H  50           
SHEET    1 AA4 4 SER H 127  LEU H 131  0                                        
SHEET    2 AA4 4 VAL H 143  TYR H 152 -1  O  LEU H 148   N  TYR H 129           
SHEET    3 AA4 4 LEU H 181  VAL H 190 -1  O  TYR H 182   N  TYR H 152           
SHEET    4 AA4 4 SER H 169  THR H 172 -1  N  HIS H 171   O  SER H 187           
SHEET    1 AA5 4 SER H 127  LEU H 131  0                                        
SHEET    2 AA5 4 VAL H 143  TYR H 152 -1  O  LEU H 148   N  TYR H 129           
SHEET    3 AA5 4 LEU H 181  VAL H 190 -1  O  TYR H 182   N  TYR H 152           
SHEET    4 AA5 4 LEU H 176  GLN H 178 -1  N  GLN H 178   O  LEU H 181           
SHEET    1 AA6 3 THR H 158  ASN H 162  0                                        
SHEET    2 AA6 3 THR H 201  HIS H 206 -1  O  THR H 201   N  ASN H 162           
SHEET    3 AA6 3 THR H 211  LYS H 215 -1  O  THR H 211   N  HIS H 206           
SHEET    1 AA7 4 LEU L   4  SER L   7  0                                        
SHEET    2 AA7 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3 AA7 4 SER L  69  ILE L  74 -1  O  ILE L  74   N  VAL L  19           
SHEET    4 AA7 4 PHE L  61  SER L  66 -1  N  SER L  66   O  SER L  69           
SHEET    1 AA8 6 ILE L  10  ALA L  13  0                                        
SHEET    2 AA8 6 THR L 101  LEU L 105  1  O  GLU L 104   N  MET L  11           
SHEET    3 AA8 6 THR L  84  TRP L  90 -1  N  PHE L  85   O  THR L 101           
SHEET    4 AA8 6 TYR L  31  GLN L  37 -1  N  TYR L  31   O  TRP L  90           
SHEET    5 AA8 6 ARG L  44  TYR L  48 -1  O  LEU L  46   N  TRP L  34           
SHEET    6 AA8 6 ASN L  52  LEU L  53 -1  O  ASN L  52   N  TYR L  48           
SHEET    1 AA9 4 ILE L  10  ALA L  13  0                                        
SHEET    2 AA9 4 THR L 101  LEU L 105  1  O  GLU L 104   N  MET L  11           
SHEET    3 AA9 4 THR L  84  TRP L  90 -1  N  PHE L  85   O  THR L 101           
SHEET    4 AA9 4 THR L  96  PHE L  97 -1  O  THR L  96   N  GLN L  89           
SHEET    1 AB1 4 THR L 113  PHE L 117  0                                        
SHEET    2 AB1 4 GLY L 128  PHE L 138 -1  O  PHE L 134   N  SER L 115           
SHEET    3 AB1 4 TYR L 172  THR L 181 -1  O  TYR L 172   N  PHE L 138           
SHEET    4 AB1 4 VAL L 158  TRP L 162 -1  N  SER L 161   O  SER L 175           
SHEET    1 AB2 4 SER L 152  ARG L 154  0                                        
SHEET    2 AB2 4 ILE L 143  ILE L 149 -1  N  TRP L 147   O  ARG L 154           
SHEET    3 AB2 4 SER L 190  HIS L 197 -1  O  THR L 196   N  ASN L 144           
SHEET    4 AB2 4 ILE L 204  ASN L 209 -1  O  PHE L 208   N  TYR L 191           
SSBOND   1 CYS A   35    CYS A  290                          1555   1555  2.03  
SSBOND   2 CYS A  117    CYS A  195                          1555   1555  2.03  
SSBOND   3 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND   4 CYS H  147    CYS H  202                          1555   1555  2.03  
SSBOND   5 CYS L   23    CYS L   87                          1555   1555  2.04  
SSBOND   6 CYS L  133    CYS L  193                          1555   1555  2.03  
LINK         C   SAR B   1                 N   ARG B   2     1555   1555  1.33  
CISPEP   1 PHE H  153    PRO H  154          0        -1.92                     
CISPEP   2 TRP H  195    PRO H  196          0         1.26                     
CISPEP   3 SER L    7    PRO L    8          0        -1.16                     
CISPEP   4 TYR L   93    PRO L   94          0         5.63                     
CISPEP   5 TYR L  139    PRO L  140          0         1.04                     
CRYST1  465.390   48.650   55.700  90.00  90.00  90.00 P 21 21 2     4          
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      0.002149  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020555  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017953        0.00000                         
ATOM      1  N   CYS A  35      74.593   9.269  24.116  1.00 99.48           N  
ANISOU    1  N   CYS A  35     6965  15825  15009    181   -803   -385       N  
ATOM      2  CA  CYS A  35      73.171   9.255  23.796  1.00117.23           C  
ANISOU    2  CA  CYS A  35     9191  18053  17298    176   -755   -326       C  
ATOM      3  C   CYS A  35      72.942   9.710  22.358  1.00122.72           C  
ANISOU    3  C   CYS A  35     9906  18596  18124    109   -769   -217       C  
ATOM      4  O   CYS A  35      72.232   9.056  21.593  1.00120.47           O  
ANISOU    4  O   CYS A  35     9646  18245  17884     70   -744   -127       O  
ATOM      5  CB  CYS A  35      72.392  10.152  24.765  1.00129.16           C  
ANISOU    5  CB  CYS A  35    10629  19663  18783    252   -738   -437       C  
ATOM      6  SG  CYS A  35      70.630   9.744  24.980  1.00138.11           S  
ANISOU    6  SG  CYS A  35    11721  20850  19904    276   -660   -391       S  
ATOM      7  N   SER A  36      73.560  10.834  21.998  1.00125.81           N  
ANISOU    7  N   SER A  36    10285  18947  18572    102   -806   -236       N  
ATOM      8  CA  SER A  36      73.308  11.462  20.707  1.00116.40           C  
ANISOU    8  CA  SER A  36     9097  17664  17467     57   -811   -130       C  
ATOM      9  C   SER A  36      73.857  10.602  19.574  1.00113.90           C  
ANISOU    9  C   SER A  36     8844  17256  17176    -10   -821      0       C  
ATOM     10  O   SER A  36      75.066  10.358  19.494  1.00104.93           O  
ANISOU   10  O   SER A  36     7741  16106  16022    -30   -846     -2       O  
ATOM     11  CB  SER A  36      73.928  12.856  20.668  1.00106.27           C  
ANISOU   11  CB  SER A  36     7780  16383  16215     70   -838   -208       C  
ATOM     12  OG  SER A  36      75.338  12.790  20.789  1.00113.17           O  
ANISOU   12  OG  SER A  36     8678  17247  17073     53   -873   -251       O  
ATOM     13  N   GLN A  37      72.963  10.142  18.704  1.00116.96           N  
ANISOU   13  N   GLN A  37     9291  17561  17588    -36   -797     73       N  
ATOM     14  CA  GLN A  37      73.312   9.440  17.479  1.00107.42           C  
ANISOU   14  CA  GLN A  37     8187  16221  16406    -86   -802    138       C  
ATOM     15  C   GLN A  37      72.500  10.037  16.340  1.00116.35           C  
ANISOU   15  C   GLN A  37     9342  17307  17560    -99   -794    228       C  
ATOM     16  O   GLN A  37      71.618  10.874  16.553  1.00120.56           O  
ANISOU   16  O   GLN A  37     9811  17934  18062    -71   -779    241       O  
ATOM     17  CB  GLN A  37      73.046   7.932  17.595  1.00 94.03           C  
ANISOU   17  CB  GLN A  37     6525  14487  14713    -95   -786     62       C  
ATOM     18  CG  GLN A  37      73.866   7.235  18.663  1.00 91.72           C  
ANISOU   18  CG  GLN A  37     6206  14296  14347    -79   -788     21       C  
ATOM     19  CD  GLN A  37      75.344   7.229  18.341  1.00106.57           C  
ANISOU   19  CD  GLN A  37     8134  16134  16223    -99   -820     35       C  
ATOM     20  OE1 GLN A  37      75.736   7.139  17.178  1.00118.42           O  
ANISOU   20  OE1 GLN A  37     9711  17515  17770   -131   -828     54       O  
ATOM     21  NE2 GLN A  37      76.175   7.331  19.372  1.00107.11           N  
ANISOU   21  NE2 GLN A  37     8150  16304  16242    -71   -839      1       N  
ATOM     22  N   LYS A  38      72.800   9.608  15.118  1.00112.56           N  
ANISOU   22  N   LYS A  38     8943  16664  17159   -128   -807    231       N  
ATOM     23  CA  LYS A  38      71.969  10.037  14.002  1.00109.98           C  
ANISOU   23  CA  LYS A  38     8633  16177  16978   -110   -814     99       C  
ATOM     24  C   LYS A  38      70.719   9.164  13.956  1.00 96.19           C  
ANISOU   24  C   LYS A  38     6874  14525  15147    -90   -791   -189       C  
ATOM     25  O   LYS A  38      70.811   7.951  13.724  1.00 82.01           O  
ANISOU   25  O   LYS A  38     5112  12798  13251   -119   -783   -204       O  
ATOM     26  CB  LYS A  38      72.738   9.985  12.676  1.00109.66           C  
ANISOU   26  CB  LYS A  38     8623  16742  16300    -93   -758   -367       C  
ATOM     27  CG  LYS A  38      73.436   8.668  12.366  1.00 99.67           C  
ANISOU   27  CG  LYS A  38     7420  15209  15240   -122   -784   -367       C  
ATOM     28  CD  LYS A  38      73.975   8.668  10.943  1.00 87.88           C  
ANISOU   28  CD  LYS A  38     5946  13801  13642   -140   -784   -298       C  
ATOM     29  CE  LYS A  38      74.589   7.328  10.578  1.00 97.30           C  
ANISOU   29  CE  LYS A  38     7194  14904  14872   -172   -796   -253       C  
ATOM     30  NZ  LYS A  38      75.106   7.321   9.181  1.00104.85           N  
ANISOU   30  NZ  LYS A  38     8162  15885  15792   -182   -802   -184       N  
ATOM     31  N   PRO A  39      69.540   9.733  14.196  1.00 90.52           N  
ANISOU   31  N   PRO A  39     6104  13787  14502    -72   -785   -107       N  
ATOM     32  CA  PRO A  39      68.318   8.925  14.181  1.00 89.37           C  
ANISOU   32  CA  PRO A  39     5937  13724  14294    -77   -765   -157       C  
ATOM     33  C   PRO A  39      67.982   8.453  12.776  1.00 87.76           C  
ANISOU   33  C   PRO A  39     5765  13630  13948    -91   -771   -272       C  
ATOM     34  O   PRO A  39      68.436   9.008  11.773  1.00 91.92           O  
ANISOU   34  O   PRO A  39     6310  14257  14358    -81   -780   -324       O  
ATOM     35  CB  PRO A  39      67.251   9.885  14.716  1.00 89.78           C  
ANISOU   35  CB  PRO A  39     5916  13753  14443    -48   -756    -32       C  
ATOM     36  CG  PRO A  39      67.771  11.241  14.373  1.00 81.39           C  
ANISOU   36  CG  PRO A  39     4846  12796  13282    -55   -761    343       C  
ATOM     37  CD  PRO A  39      69.264  11.148  14.501  1.00 66.21           C  
ANISOU   37  CD  PRO A  39     2960  11029  11167    -82   -759    408       C  
ATOM     38  N   SER A  40      67.170   7.397  12.719  1.00 82.09           N  
ANISOU   38  N   SER A  40     5040  12932  13220   -121   -763   -221       N  
ATOM     39  CA  SER A  40      66.742   6.829  11.447  1.00 87.65           C  
ANISOU   39  CA  SER A  40     5761  13688  13853   -143   -783   -218       C  
ATOM     40  C   SER A  40      65.969   7.858  10.632  1.00 87.01           C  
ANISOU   40  C   SER A  40     5644  13659  13755   -106   -801   -251       C  
ATOM     41  O   SER A  40      64.840   8.217  10.984  1.00 74.74           O  
ANISOU   41  O   SER A  40     4037  12115  12247    -85   -792   -267       O  
ATOM     42  CB  SER A  40      65.887   5.580  11.676  1.00 97.89           C  
ANISOU   42  CB  SER A  40     7039  15000  15157   -182   -769   -174       C  
ATOM     43  OG  SER A  40      64.681   5.901  12.349  1.00100.48           O  
ANISOU   43  OG  SER A  40     7300  15334  15542   -164   -747   -176       O  
ATOM     44  N   ASP A  41      66.570   8.341   9.548  1.00 87.04           N  
ANISOU   44  N   ASP A  41     5666  13707  13697    -94   -823   -239       N  
ATOM     45  CA  ASP A  41      65.939   9.332   8.688  1.00 80.38           C  
ANISOU   45  CA  ASP A  41     4777  12928  12834    -52   -842   -224       C  
ATOM     46  C   ASP A  41      65.132   8.709   7.559  1.00 89.59           C  
ANISOU   46  C   ASP A  41     5934  14094  14013    -60   -882   -178       C  
ATOM     47  O   ASP A  41      64.509   9.443   6.785  1.00 94.81           O  
ANISOU   47  O   ASP A  41     6550  14794  14681    -18   -907   -153       O  
ATOM     48  CB  ASP A  41      66.995  10.272   8.099  1.00 65.50           C  
ANISOU   48  CB  ASP A  41     2895  11079  10914    -28   -844   -185       C  
ATOM     49  CG  ASP A  41      67.807   9.620   6.999  1.00 74.92           C  
ANISOU   49  CG  ASP A  41     4129  12235  12103    -50   -870   -127       C  
ATOM     50  OD1 ASP A  41      68.158   8.429   7.138  1.00 80.25           O  
ANISOU   50  OD1 ASP A  41     4853  12868  12768    -93   -872   -132       O  
ATOM     51  OD2 ASP A  41      68.086  10.297   5.987  1.00 74.86           O  
ANISOU   51  OD2 ASP A  41     4095  12239  12111    -18   -887    -64       O  
ATOM     52  N   LYS A  42      65.128   7.381   7.442  1.00 94.97           N  
ANISOU   52  N   LYS A  42     6649  14742  14695   -109   -893   -161       N  
ATOM     53  CA  LYS A  42      64.379   6.693   6.399  1.00 95.21           C  
ANISOU   53  CA  LYS A  42     6664  14786  14725   -121   -937   -129       C  
ATOM     54  C   LYS A  42      62.907   6.508   6.752  1.00 83.20           C  
ANISOU   54  C   LYS A  42     5088  13280  13244   -124   -936   -155       C  
ATOM     55  O   LYS A  42      62.249   5.625   6.189  1.00 77.64           O  
ANISOU   55  O   LYS A  42     4370  12584  12545   -152   -967   -142       O  
ATOM     56  CB  LYS A  42      65.028   5.340   6.095  1.00 97.97           C  
ANISOU   56  CB  LYS A  42     7064  15112  15047   -175   -947   -100       C  
ATOM     57  CG  LYS A  42      66.453   5.455   5.570  1.00 96.99           C  
ANISOU   57  CG  LYS A  42     6987  14976  14887   -170   -952    -67       C  
ATOM     58  CD  LYS A  42      67.050   4.097   5.238  1.00 92.30           C  
ANISOU   58  CD  LYS A  42     6437  14368  14264   -218   -963    -39       C  
ATOM     59  CE  LYS A  42      68.466   4.243   4.699  1.00 86.99           C  
ANISOU   59  CE  LYS A  42     5816  13681  13555   -210   -963      3       C  
ATOM     60  NZ  LYS A  42      69.084   2.928   4.376  1.00 91.00           N  
ANISOU   60  NZ  LYS A  42     6380  14175  14020   -252   -970     39       N  
ATOM     61  N   HIS A  43      62.381   7.321   7.669  1.00 76.70           N  
ANISOU   61  N   HIS A  43     4226  12464  12452    -95   -903   -193       N  
ATOM     62  CA  HIS A  43      60.969   7.282   8.023  1.00 72.80           C  
ANISOU   62  CA  HIS A  43     3669  11987  12006    -91   -897   -214       C  
ATOM     63  C   HIS A  43      60.126   8.239   7.194  1.00 70.06           C  
ANISOU   63  C   HIS A  43     3267  11691  11663    -34   -934   -214       C  
ATOM     64  O   HIS A  43      58.900   8.085   7.153  1.00 74.29           O  
ANISOU   64  O   HIS A  43     3746  12246  12234    -31   -945   -226       O  
ATOM     65  CB  HIS A  43      60.786   7.615   9.507  1.00 68.57           C  
ANISOU   65  CB  HIS A  43     3108  11429  11517    -83   -839   -245       C  
ATOM     66  CG  HIS A  43      60.998   9.062   9.830  1.00 68.55           C  
ANISOU   66  CG  HIS A  43     3085  11450  11509    -22   -826   -282       C  
ATOM     67  ND1 HIS A  43      62.196   9.706   9.607  1.00 71.53           N  
ANISOU   67  ND1 HIS A  43     3502  11845  11829     -4   -829   -284       N  
ATOM     68  CD2 HIS A  43      60.165   9.990  10.357  1.00 71.04           C  
ANISOU   68  CD2 HIS A  43     3338  11797  11857     25   -808   -318       C  
ATOM     69  CE1 HIS A  43      62.092  10.969   9.982  1.00 68.05           C  
ANISOU   69  CE1 HIS A  43     3021  11475  11360     48   -811   -312       C  
ATOM     70  NE2 HIS A  43      60.870  11.166  10.442  1.00 69.76           N  
ANISOU   70  NE2 HIS A  43     3178  11703  11625     70   -798   -339       N  
ATOM     71  N   LEU A  44      60.748   9.220   6.540  1.00 68.11           N  
ANISOU   71  N   LEU A  44     3025  11469  11386     13   -951   -189       N  
ATOM     72  CA  LEU A  44      60.035  10.215   5.753  1.00 68.88           C  
ANISOU   72  CA  LEU A  44     3060  11616  11495     79   -985   -166       C  
ATOM     73  C   LEU A  44      60.032   9.892   4.262  1.00 73.51           C  
ANISOU   73  C   LEU A  44     3645  12206  12078     92  -1054   -109       C  
ATOM     74  O   LEU A  44      59.862  10.796   3.438  1.00 75.41           O  
ANISOU   74  O   LEU A  44     3843  12477  12334    158  -1085    -64       O  
ATOM     75  CB  LEU A  44      60.623  11.606   6.004  1.00 69.01           C  
ANISOU   75  CB  LEU A  44     3059  11663  11500    133   -956   -150       C  
ATOM     76  CG  LEU A  44      62.136  11.807   5.893  1.00 68.30           C  
ANISOU   76  CG  LEU A  44     3020  11550  11383    122   -942   -118       C  
ATOM     77  CD1 LEU A  44      62.545  12.157   4.471  1.00101.05           C  
ANISOU   77  CD1 LEU A  44     7154  15690  15551    160   -986    -36       C  
ATOM     78  CD2 LEU A  44      62.600  12.880   6.865  1.00 68.48           C  
ANISOU   78  CD2 LEU A  44     3022  11606  11390    146   -893   -131       C  
ATOM     79  N   ASP A  45      60.213   8.621   3.899  1.00 75.23           N  
ANISOU   79  N   ASP A  45     3903  12399  12282     37  -1079   -105       N  
ATOM     80  CA  ASP A  45      60.134   8.243   2.492  1.00 81.79           C  
ANISOU   80  CA  ASP A  45     4726  13245  13106     53  -1153    -58       C  
ATOM     81  C   ASP A  45      58.696   8.285   1.990  1.00 81.59           C  
ANISOU   81  C   ASP A  45     4629  13257  13114     82  -1204    -71       C  
ATOM     82  O   ASP A  45      58.433   8.766   0.881  1.00 80.37           O  
ANISOU   82  O   ASP A  45     4436  13135  12966    144  -1266    -27       O  
ATOM     83  CB  ASP A  45      60.734   6.852   2.285  1.00 86.72           C  
ANISOU   83  CB  ASP A  45     5407  13842  13701    -15  -1166    -54       C  
ATOM     84  CG  ASP A  45      62.242   6.841   2.432  1.00 86.52           C  
ANISOU   84  CG  ASP A  45     5447  13787  13641    -30  -1132    -27       C  
ATOM     85  OD1 ASP A  45      62.884   7.841   2.046  1.00 88.02           O  
ANISOU   85  OD1 ASP A  45     5636  13982  13827     21  -1128     15       O  
ATOM     86  OD2 ASP A  45      62.786   5.834   2.931  1.00 85.67           O  
ANISOU   86  OD2 ASP A  45     5389  13648  13514    -91  -1107    -42       O  
ATOM     87  N   ALA A  46      57.754   7.792   2.790  1.00 80.92           N  
ANISOU   87  N   ALA A  46     4519  13169  13056     43  -1181   -125       N  
ATOM     88  CA  ALA A  46      56.348   7.765   2.413  1.00104.02           C  
ANISOU   88  CA  ALA A  46     7371  16130  16023     63  -1226   -146       C  
ATOM     89  C   ALA A  46      55.582   8.998   2.877  1.00122.32           C  
ANISOU   89  C   ALA A  46     9626  18480  18371    126  -1201   -161       C  
ATOM     90  O   ALA A  46      54.363   9.057   2.689  1.00117.74           O  
ANISOU   90  O   ALA A  46     8976  17930  17829    147  -1232   -182       O  
ATOM     91  CB  ALA A  46      55.678   6.504   2.968  1.00115.76           C  
ANISOU   91  CB  ALA A  46     8847  17600  17534    -16  -1211   -191       C  
ATOM     92  N   ILE A  47      56.264   9.977   3.475  1.00 71.52           N  
ANISOU   92  N   ILE A  47     3208  12044  11922    158  -1148   -151       N  
ATOM     93  CA  ILE A  47      55.572  11.182   3.937  1.00 86.69           C  
ANISOU   93  CA  ILE A  47     5065  14005  13867    222  -1122   -163       C  
ATOM     94  C   ILE A  47      54.980  11.987   2.787  1.00 87.81           C  
ANISOU   94  C   ILE A  47     5143  14187  14032    308  -1187   -116       C  
ATOM     95  O   ILE A  47      53.787  12.334   2.857  1.00 74.12           O  
ANISOU   95  O   ILE A  47     3338  12491  12334    345  -1199   -138       O  
ATOM     96  CB  ILE A  47      56.513  12.019   4.831  1.00 71.76           C  
ANISOU   96  CB  ILE A  47     3202  12111  11952    235  -1054   -164       C  
ATOM     97  CG1 ILE A  47      56.670  11.357   6.200  1.00 71.29           C  
ANISOU   97  CG1 ILE A  47     3177  12022  11888    170   -991   -224       C  
ATOM     98  CG2 ILE A  47      55.985  13.430   4.986  1.00 72.73           C  
ANISOU   98  CG2 ILE A  47     3254  12287  12094    318  -1039   -149       C  
ATOM     99  CD1 ILE A  47      55.394  11.320   7.008  1.00 77.86           C  
ANISOU   99  CD1 ILE A  47     3945  12872  12765    171   -963   -272       C  
ATOM    100  N   PRO A  48      55.717  12.318   1.717  1.00 83.69           N  
ANISOU  100  N   PRO A  48     4636  13663  13501    351  -1230    -45       N  
ATOM    101  CA  PRO A  48      55.085  13.075   0.623  1.00 81.91           C  
ANISOU  101  CA  PRO A  48     4339  13475  13309    447  -1296     10       C  
ATOM    102  C   PRO A  48      53.967  12.316  -0.068  1.00 78.92           C  
ANISOU  102  C   PRO A  48     3921  13120  12944    444  -1375    -14       C  
ATOM    103  O   PRO A  48      53.033  12.942  -0.588  1.00 79.72           O  
ANISOU  103  O   PRO A  48     3949  13261  13082    520  -1421      3       O  
ATOM    104  CB  PRO A  48      56.255  13.357  -0.331  1.00 87.56           C  
ANISOU  104  CB  PRO A  48     5094  14167  14006    483  -1316    103       C  
ATOM    105  CG  PRO A  48      57.244  12.289  -0.039  1.00 72.50           C  
ANISOU  105  CG  PRO A  48     3270  12223  12054    391  -1295     78       C  
ATOM    106  CD  PRO A  48      57.142  12.059   1.435  1.00 72.04           C  
ANISOU  106  CD  PRO A  48     3231  12151  11992    325  -1220     -5       C  
ATOM    107  N   ILE A  49      54.032  10.983  -0.088  1.00 84.24           N  
ANISOU  107  N   ILE A  49     4638  13770  13598    359  -1394    -51       N  
ATOM    108  CA  ILE A  49      52.952  10.195  -0.676  1.00 85.74           C  
ANISOU  108  CA  ILE A  49     4784  13978  13813    345  -1469    -81       C  
ATOM    109  C   ILE A  49      51.671  10.379   0.127  1.00 87.22           C  
ANISOU  109  C   ILE A  49     4905  14185  14051    341  -1440   -142       C  
ATOM    110  O   ILE A  49      50.587  10.587  -0.432  1.00 96.55           O  
ANISOU  110  O   ILE A  49     6012  15400  15272    389  -1503   -148       O  
ATOM    111  CB  ILE A  49      53.356   8.712  -0.766  1.00 86.06           C  
ANISOU  111  CB  ILE A  49     4882  13986  13832    250  -1485   -106       C  
ATOM    112  CG1 ILE A  49      54.731   8.572  -1.424  1.00 94.37           C  
ANISOU  112  CG1 ILE A  49     6002  15024  14831    254  -1500    -46       C  
ATOM    113  CG2 ILE A  49      52.311   7.921  -1.538  1.00 77.71           C  
ANISOU  113  CG2 ILE A  49     3772  12946  12809    239  -1578   -132       C  
ATOM    114  CD1 ILE A  49      54.798   9.129  -2.831  1.00102.44           C  
ANISOU  114  CD1 ILE A  49     6991  16088  15844    350  -1589     29       C  
ATOM    115  N   LEU A  50      51.779  10.313   1.457  1.00 79.96           N  
ANISOU  115  N   LEU A  50     4007  13246  13130    289  -1346   -184       N  
ATOM    116  CA  LEU A  50      50.619  10.555   2.309  1.00 76.26           C  
ANISOU  116  CA  LEU A  50     3469  12801  12706    291  -1307   -235       C  
ATOM    117  C   LEU A  50      50.121  11.988   2.165  1.00 77.08           C  
ANISOU  117  C   LEU A  50     3507  12952  12826    396  -1311   -211       C  
ATOM    118  O   LEU A  50      48.908  12.233   2.145  1.00 91.81           O  
ANISOU  118  O   LEU A  50     5292  14856  14738    431  -1332   -236       O  
ATOM    119  CB  LEU A  50      50.965  10.250   3.767  1.00 75.57           C  
ANISOU  119  CB  LEU A  50     3417  12685  12613    227  -1206   -272       C  
ATOM    120  CG  LEU A  50      50.753   8.824   4.288  1.00 75.38           C  
ANISOU  120  CG  LEU A  50     3405  12627  12609    127  -1182   -307       C  
ATOM    121  CD1 LEU A  50      51.506   7.795   3.457  1.00 74.74           C  
ANISOU  121  CD1 LEU A  50     3386  12515  12496     77  -1233   -286       C  
ATOM    122  CD2 LEU A  50      51.163   8.729   5.751  1.00 74.80           C  
ANISOU  122  CD2 LEU A  50     3360  12523  12538     88  -1082   -326       C  
ATOM    123  N   TYR A  51      51.046  12.948   2.062  1.00 76.63           N  
ANISOU  123  N   TYR A  51     3479  12895  12740    450  -1290   -159       N  
ATOM    124  CA  TYR A  51      50.654  14.336   1.833  1.00 77.47           C  
ANISOU  124  CA  TYR A  51     3519  13044  12872    559  -1295   -119       C  
ATOM    125  C   TYR A  51      49.835  14.477   0.556  1.00 90.51           C  
ANISOU  125  C   TYR A  51     5107  14724  14559    631  -1395    -85       C  
ATOM    126  O   TYR A  51      48.830  15.198   0.530  1.00100.61           O  
ANISOU  126  O   TYR A  51     6305  16044  15879    702  -1408    -87       O  
ATOM    127  CB  TYR A  51      51.892  15.231   1.771  1.00 91.64           C  
ANISOU  127  CB  TYR A  51     5349  14820  14648    600  -1261    -53       C  
ATOM    128  CG  TYR A  51      52.255  15.901   3.078  1.00 76.54           C  
ANISOU  128  CG  TYR A  51     3444  12914  12724    592  -1167    -74       C  
ATOM    129  CD1 TYR A  51      51.777  17.168   3.388  1.00 77.39           C  
ANISOU  129  CD1 TYR A  51     3480  13058  12868    677  -1139    -49       C  
ATOM    130  CD2 TYR A  51      53.085  15.273   3.997  1.00 75.49           C  
ANISOU  130  CD2 TYR A  51     3385  12751  12545    506  -1110   -114       C  
ATOM    131  CE1 TYR A  51      52.109  17.787   4.580  1.00 77.29           C  
ANISOU  131  CE1 TYR A  51     3466  13060  12841    675  -1059    -61       C  
ATOM    132  CE2 TYR A  51      53.422  15.884   5.191  1.00 75.32           C  
ANISOU  132  CE2 TYR A  51     3365  12749  12504    506  -1033   -131       C  
ATOM    133  CZ  TYR A  51      52.931  17.140   5.478  1.00 76.20           C  
ANISOU  133  CZ  TYR A  51     3402  12905  12646    589  -1009   -101       C  
ATOM    134  OH  TYR A  51      53.266  17.749   6.666  1.00 76.15           O  
ANISOU  134  OH  TYR A  51     3389  12928  12616    592   -937   -101       O  
ATOM    135  N   TYR A  52      50.247  13.794  -0.515  1.00 80.44           N  
ANISOU  135  N   TYR A  52     3864  13433  13267    620  -1470    -53       N  
ATOM    136  CA  TYR A  52      49.514  13.895  -1.772  1.00 89.95           C  
ANISOU  136  CA  TYR A  52     5009  14671  14499    696  -1579    -17       C  
ATOM    137  C   TYR A  52      48.187  13.147  -1.718  1.00 84.92           C  
ANISOU  137  C   TYR A  52     4315  14047  13904    658  -1623    -89       C  
ATOM    138  O   TYR A  52      47.210  13.585  -2.336  1.00 89.69           O  
ANISOU  138  O   TYR A  52     4840  14687  14551    734  -1692    -77       O  
ATOM    139  CB  TYR A  52      50.374  13.383  -2.927  1.00 85.80           C  
ANISOU  139  CB  TYR A  52     4530  14135  13934    702  -1649     44       C  
ATOM    140  CG  TYR A  52      51.346  14.415  -3.453  1.00 88.56           C  
ANISOU  140  CG  TYR A  52     4894  14485  14269    790  -1636    149       C  
ATOM    141  CD1 TYR A  52      51.015  15.764  -3.462  1.00 84.30           C  
ANISOU  141  CD1 TYR A  52     4305  13959  13765    895  -1612    207       C  
ATOM    142  CD2 TYR A  52      52.595  14.044  -3.933  1.00107.96           C  
ANISOU  142  CD2 TYR A  52     7441  16910  16668    765  -1631    212       C  
ATOM    143  CE1 TYR A  52      51.897  16.714  -3.940  1.00 91.51           C  
ANISOU  143  CE1 TYR A  52     5257  14843  14671    969  -1582    331       C  
ATOM    144  CE2 TYR A  52      53.486  14.987  -4.411  1.00118.29           C  
ANISOU  144  CE2 TYR A  52     8787  18197  17962    838  -1600    334       C  
ATOM    145  CZ  TYR A  52      53.131  16.321  -4.412  1.00110.04           C  
ANISOU  145  CZ  TYR A  52     7689  17154  16967    939  -1574    396       C  
ATOM    146  OH  TYR A  52      54.013  17.264  -4.887  1.00114.99           O  
ANISOU  146  OH  TYR A  52     8346  17742  17604   1011  -1536    528       O  
ATOM    147  N   ILE A  53      48.128  12.029  -0.992  1.00 79.88           N  
ANISOU  147  N   ILE A  53     3710  13378  13264    544  -1585   -157       N  
ATOM    148  CA  ILE A  53      46.866  11.307  -0.842  1.00 80.83           C  
ANISOU  148  CA  ILE A  53     3765  13504  13443    501  -1615   -223       C  
ATOM    149  C   ILE A  53      45.849  12.172  -0.107  1.00 95.15           C  
ANISOU  149  C   ILE A  53     5498  15357  15299    549  -1567   -252       C  
ATOM    150  O   ILE A  53      44.708  12.347  -0.559  1.00 93.22           O  
ANISOU  150  O   ILE A  53     5167  15141  15113    595  -1630   -265       O  
ATOM    151  CB  ILE A  53      47.094   9.966  -0.122  1.00 80.08           C  
ANISOU  151  CB  ILE A  53     3717  13367  13343    373  -1566   -277       C  
ATOM    152  CG1 ILE A  53      47.899   9.014  -1.009  1.00 79.51           C  
ANISOU  152  CG1 ILE A  53     3709  13262  13238    331  -1631   -252       C  
ATOM    153  CG2 ILE A  53      45.767   9.336   0.269  1.00 81.14           C  
ANISOU  153  CG2 ILE A  53     3770  13511  13548    327  -1568   -344       C  
ATOM    154  CD1 ILE A  53      48.232   7.696  -0.345  1.00 78.77           C  
ANISOU  154  CD1 ILE A  53     3663  13129  13138    212  -1581   -296       C  
ATOM    155  N   ILE A  54      46.251  12.733   1.037  1.00 81.06           N  
ANISOU  155  N   ILE A  54     3736  13576  13487    542  -1460   -261       N  
ATOM    156  CA  ILE A  54      45.370  13.640   1.769  1.00 81.90           C  
ANISOU  156  CA  ILE A  54     3766  13729  13624    597  -1410   -282       C  
ATOM    157  C   ILE A  54      45.016  14.844   0.906  1.00 82.87           C  
ANISOU  157  C   ILE A  54     3830  13890  13767    727  -1469   -226       C  
ATOM    158  O   ILE A  54      43.891  15.358   0.960  1.00 84.10           O  
ANISOU  158  O   ILE A  54     3895  14088  13970    785  -1482   -244       O  
ATOM    159  CB  ILE A  54      46.026  14.064   3.097  1.00 81.04           C  
ANISOU  159  CB  ILE A  54     3699  13618  13476    575  -1294   -292       C  
ATOM    160  CG1 ILE A  54      46.320  12.837   3.961  1.00 80.24           C  
ANISOU  160  CG1 ILE A  54     3647  13473  13366    456  -1238   -339       C  
ATOM    161  CG2 ILE A  54      45.138  15.041   3.851  1.00 81.99           C  
ANISOU  161  CG2 ILE A  54     3736  13798  13619    640  -1243   -309       C  
ATOM    162  CD1 ILE A  54      45.087  12.044   4.332  1.00108.07           C  
ANISOU  162  CD1 ILE A  54     7099  17011  16951    406  -1233   -395       C  
ATOM    163  N   PHE A  55      45.963  15.298   0.081  1.00 85.95           N  
ANISOU  163  N   PHE A  55     4264  14265  14127    780  -1505   -151       N  
ATOM    164  CA  PHE A  55      45.712  16.446  -0.784  1.00 91.24           C  
ANISOU  164  CA  PHE A  55     4877  14965  14825    914  -1559    -79       C  
ATOM    165  C   PHE A  55      44.605  16.156  -1.789  1.00100.50           C  
ANISOU  165  C   PHE A  55     5978  16161  16047    957  -1674    -83       C  
ATOM    166  O   PHE A  55      43.674  16.953  -1.948  1.00115.83           O  
ANISOU  166  O   PHE A  55     7834  18140  18037   1049  -1698    -73       O  
ATOM    167  CB  PHE A  55      46.994  16.850  -1.512  1.00 82.70           C  
ANISOU  167  CB  PHE A  55     3853  13859  13711    957  -1572     12       C  
ATOM    168  CG  PHE A  55      46.748  17.536  -2.827  1.00 88.78           C  
ANISOU  168  CG  PHE A  55     4569  14654  14508   1086  -1665    100       C  
ATOM    169  CD1 PHE A  55      46.299  18.845  -2.867  1.00 84.81           C  
ANISOU  169  CD1 PHE A  55     3994  14176  14054   1209  -1651    151       C  
ATOM    170  CD2 PHE A  55      46.960  16.869  -4.023  1.00 85.33           C  
ANISOU  170  CD2 PHE A  55     4152  14220  14049   1094  -1766    138       C  
ATOM    171  CE1 PHE A  55      46.068  19.478  -4.074  1.00 85.94           C  
ANISOU  171  CE1 PHE A  55     4095  14338  14219   1339  -1732    247       C  
ATOM    172  CE2 PHE A  55      46.730  17.496  -5.233  1.00 85.08           C  
ANISOU  172  CE2 PHE A  55     4074  14223  14031   1225  -1853    231       C  
ATOM    173  CZ  PHE A  55      46.285  18.803  -5.258  1.00 86.08           C  
ANISOU  173  CZ  PHE A  55     4146  14364  14197   1346  -1830    294       C  
ATOM    174  N   VAL A  56      44.694  15.023  -2.490  1.00 97.46           N  
ANISOU  174  N   VAL A  56     5622  15752  15655    895  -1751    -95       N  
ATOM    175  CA  VAL A  56      43.716  14.743  -3.536  1.00 98.88           C  
ANISOU  175  CA  VAL A  56     5733  15948  15888    938  -1877    -87       C  
ATOM    176  C   VAL A  56      42.366  14.377  -2.928  1.00 90.32           C  
ANISOU  176  C   VAL A  56     4568  14867  14881    895  -1871   -170       C  
ATOM    177  O   VAL A  56      41.317  14.841  -3.394  1.00 88.47           O  
ANISOU  177  O   VAL A  56     4242  14659  14711    971  -1938   -160       O  
ATOM    178  CB  VAL A  56      44.238  13.650  -4.492  1.00100.01           C  
ANISOU  178  CB  VAL A  56     5928  16068  16005    887  -1968    -66       C  
ATOM    179  CG1 VAL A  56      44.619  12.385  -3.737  1.00 84.60           C  
ANISOU  179  CG1 VAL A  56     4039  14065  14041    739  -1912   -137       C  
ATOM    180  CG2 VAL A  56      43.204  13.345  -5.566  1.00110.90           C  
ANISOU  180  CG2 VAL A  56     7229  17463  17444    927  -2110    -47       C  
ATOM    181  N   ILE A  57      42.364  13.567  -1.867  1.00 86.28           N  
ANISOU  181  N   ILE A  57     4083  14331  14367    778  -1788   -245       N  
ATOM    182  CA  ILE A  57      41.103  13.153  -1.256  1.00 87.26           C  
ANISOU  182  CA  ILE A  57     4123  14462  14568    734  -1773   -319       C  
ATOM    183  C   ILE A  57      40.399  14.351  -0.627  1.00 88.02           C  
ANISOU  183  C   ILE A  57     4146  14617  14681    819  -1715   -327       C  
ATOM    184  O   ILE A  57      39.271  14.698  -0.998  1.00121.53           O  
ANISOU  184  O   ILE A  57     8292  18883  19002    880  -1774   -332       O  
ATOM    185  CB  ILE A  57      41.339  12.034  -0.228  1.00 86.35           C  
ANISOU  185  CB  ILE A  57     4051  14323  14436    599  -1684   -385       C  
ATOM    186  CG1 ILE A  57      41.858  10.774  -0.923  1.00 85.88           C  
ANISOU  186  CG1 ILE A  57     4047  14205  14378    517  -1752   -379       C  
ATOM    187  CG2 ILE A  57      40.058  11.733   0.533  1.00 87.43           C  
ANISOU  187  CG2 ILE A  57     4090  14489  14640    563  -1644   -456       C  
ATOM    188  CD1 ILE A  57      42.070   9.604   0.013  1.00 85.13           C  
ANISOU  188  CD1 ILE A  57     3988  14091  14268    391  -1668   -439       C  
ATOM    189  N   GLY A  58      41.062  15.004   0.330  1.00 87.10           N  
ANISOU  189  N   GLY A  58     4072  14521  14500    827  -1603   -320       N  
ATOM    190  CA  GLY A  58      40.449  16.144   0.990  1.00 87.84           C  
ANISOU  190  CA  GLY A  58     4097  14671  14605    910  -1543   -321       C  
ATOM    191  C   GLY A  58      40.149  17.283   0.036  1.00102.77           C  
ANISOU  191  C   GLY A  58     5935  16586  16527   1052  -1616   -255       C  
ATOM    192  O   GLY A  58      39.144  17.984   0.186  1.00118.47           O  
ANISOU  192  O   GLY A  58     7830  18619  18563   1128  -1615   -264       O  
ATOM    193  N   PHE A  59      41.016  17.485  -0.958  1.00 92.36           N  
ANISOU  193  N   PHE A  59     4669  15241  15181   1097  -1677   -180       N  
ATOM    194  CA  PHE A  59      40.797  18.555  -1.925  1.00 97.60           C  
ANISOU  194  CA  PHE A  59     5282  15927  15873   1244  -1746    -98       C  
ATOM    195  C   PHE A  59      39.556  18.286  -2.765  1.00116.72           C  
ANISOU  195  C   PHE A  59     7615  18362  18372   1283  -1864   -110       C  
ATOM    196  O   PHE A  59      38.725  19.179  -2.964  1.00132.55           O  
ANISOU  196  O   PHE A  59     9533  20402  20427   1393  -1889    -87       O  
ATOM    197  CB  PHE A  59      42.029  18.720  -2.817  1.00100.70           C  
ANISOU  197  CB  PHE A  59     5747  16295  16218   1281  -1782     -6       C  
ATOM    198  CG  PHE A  59      41.964  19.918  -3.724  1.00104.94           C  
ANISOU  198  CG  PHE A  59     6235  16855  16782   1445  -1833     98       C  
ATOM    199  CD1 PHE A  59      42.448  21.147  -3.305  1.00111.89           C  
ANISOU  199  CD1 PHE A  59     7109  17732  17671   1528  -1750    158       C  
ATOM    200  CD2 PHE A  59      41.422  19.816  -4.996  1.00102.21           C  
ANISOU  200  CD2 PHE A  59     5845  16532  16459   1521  -1964    146       C  
ATOM    201  CE1 PHE A  59      42.391  22.251  -4.135  1.00113.84           C  
ANISOU  201  CE1 PHE A  59     7306  17990  17958   1687  -1789    265       C  
ATOM    202  CE2 PHE A  59      41.362  20.917  -5.830  1.00104.97           C  
ANISOU  202  CE2 PHE A  59     6148  16908  16828   1685  -2008    254       C  
ATOM    203  CZ  PHE A  59      41.847  22.136  -5.399  1.00110.29           C  
ANISOU  203  CZ  PHE A  59     6820  17569  17517   1768  -1915    317       C  
ATOM    204  N   LEU A  60      39.413  17.057  -3.269  1.00110.88           N  
ANISOU  204  N   LEU A  60     6890  17587  17652   1194  -1942   -138       N  
ATOM    205  CA  LEU A  60      38.232  16.727  -4.062  1.00104.75           C  
ANISOU  205  CA  LEU A  60     6022  16807  16970   1217  -2065   -134       C  
ATOM    206  C   LEU A  60      36.963  16.800  -3.220  1.00 93.78           C  
ANISOU  206  C   LEU A  60     4536  15429  15667   1199  -2022   -208       C  
ATOM    207  O   LEU A  60      35.928  17.292  -3.686  1.00 95.40           O  
ANISOU  207  O   LEU A  60     4642  15651  15954   1281  -2093   -184       O  
ATOM    208  CB  LEU A  60      38.388  15.341  -4.690  1.00 97.36           C  
ANISOU  208  CB  LEU A  60     5120  15819  16052   1110  -2152   -132       C  
ATOM    209  CG  LEU A  60      38.927  15.286  -6.124  1.00 99.07           C  
ANISOU  209  CG  LEU A  60     5366  16053  16223   1173  -2277    -33       C  
ATOM    210  CD1 LEU A  60      40.296  15.944  -6.238  1.00 91.55           C  
ANISOU  210  CD1 LEU A  60     4504  15123  15157   1233  -2221     16       C  
ATOM    211  CD2 LEU A  60      38.977  13.848  -6.622  1.00 92.74           C  
ANISOU  211  CD2 LEU A  60     4589  15207  15443   1055  -2360    -26       C  
ATOM    212  N   VAL A  61      37.027  16.327  -1.972  1.00 92.94           N  
ANISOU  212  N   VAL A  61     4451  15322  15538   1099  -1905   -292       N  
ATOM    213  CA  VAL A  61      35.854  16.372  -1.099  1.00 93.92           C  
ANISOU  213  CA  VAL A  61     4480  15477  15727   1084  -1850   -363       C  
ATOM    214  C   VAL A  61      35.433  17.816  -0.844  1.00 94.71           C  
ANISOU  214  C   VAL A  61     4519  15645  15821   1220  -1811   -340       C  
ATOM    215  O   VAL A  61      34.261  18.180  -1.008  1.00 96.30           O  
ANISOU  215  O   VAL A  61     4611  15865  16112   1280  -1854   -350       O  
ATOM    216  CB  VAL A  61      36.133  15.625   0.217  1.00 92.83           C  
ANISOU  216  CB  VAL A  61     4383  15356  15533    962  -1721   -440       C  
ATOM    217  CG1 VAL A  61      35.042  15.917   1.235  1.00 93.81           C  
ANISOU  217  CG1 VAL A  61     4408  15554  15684    972  -1640   -500       C  
ATOM    218  CG2 VAL A  61      36.236  14.130  -0.038  1.00 92.49           C  
ANISOU  218  CG2 VAL A  61     4370  15246  15527    834  -1764   -470       C  
ATOM    219  N   ASN A  62      36.386  18.662  -0.443  1.00 93.70           N  
ANISOU  219  N   ASN A  62     4456  15544  15601   1269  -1731   -299       N  
ATOM    220  CA  ASN A  62      36.064  20.060  -0.179  1.00102.29           C  
ANISOU  220  CA  ASN A  62     5488  16685  16693   1401  -1689   -262       C  
ATOM    221  C   ASN A  62      35.606  20.782  -1.439  1.00109.60           C  
ANISOU  221  C   ASN A  62     6354  17608  17680   1537  -1806   -190       C  
ATOM    222  O   ASN A  62      34.797  21.712  -1.360  1.00118.25           O  
ANISOU  222  O   ASN A  62     7362  18743  18824   1646  -1801   -177       O  
ATOM    223  CB  ASN A  62      37.269  20.770   0.438  1.00109.77           C  
ANISOU  223  CB  ASN A  62     6515  17635  17558   1419  -1588   -213       C  
ATOM    224  CG  ASN A  62      37.466  20.415   1.898  1.00115.81           C  
ANISOU  224  CG  ASN A  62     7308  18424  18269   1321  -1462   -270       C  
ATOM    225  OD1 ASN A  62      37.004  21.127   2.789  1.00117.51           O  
ANISOU  225  OD1 ASN A  62     7471  18695  18484   1367  -1382   -276       O  
ATOM    226  ND2 ASN A  62      38.150  19.305   2.150  1.00116.19           N  
ANISOU  226  ND2 ASN A  62     7438  18433  18274   1193  -1444   -304       N  
ATOM    227  N   ILE A  63      36.107  20.372  -2.607  1.00103.45           N  
ANISOU  227  N   ILE A  63     5618  16790  16897   1541  -1911   -134       N  
ATOM    228  CA  ILE A  63      35.605  20.930  -3.858  1.00105.63           C  
ANISOU  228  CA  ILE A  63     5834  17077  17225   1672  -2035    -53       C  
ATOM    229  C   ILE A  63      34.144  20.549  -4.059  1.00113.21           C  
ANISOU  229  C   ILE A  63     6681  18036  18299   1663  -2115    -92       C  
ATOM    230  O   ILE A  63      33.319  21.381  -4.459  1.00100.42           O  
ANISOU  230  O   ILE A  63     4971  16447  16738   1787  -2163    -52       O  
ATOM    231  CB  ILE A  63      36.484  20.475  -5.038  1.00 97.13           C  
ANISOU  231  CB  ILE A  63     4828  15979  16099   1674  -2130     25       C  
ATOM    232  CG1 ILE A  63      37.769  21.304  -5.098  1.00102.14           C  
ANISOU  232  CG1 ILE A  63     5538  16615  16655   1744  -2065    105       C  
ATOM    233  CG2 ILE A  63      35.723  20.578  -6.352  1.00101.85           C  
ANISOU  233  CG2 ILE A  63     5352  16600  16748   1772  -2284     98       C  
ATOM    234  CD1 ILE A  63      37.533  22.781  -5.325  1.00105.65           C  
ANISOU  234  CD1 ILE A  63     5923  17089  17131   1920  -2052    189       C  
ATOM    235  N   VAL A  64      33.796  19.292  -3.767  1.00113.84           N  
ANISOU  235  N   VAL A  64     6757  18070  18428   1518  -2128   -157       N  
ATOM    236  CA  VAL A  64      32.408  18.854  -3.900  1.00108.81           C  
ANISOU  236  CA  VAL A  64     6002  17407  17935   1489  -2199   -168       C  
ATOM    237  C   VAL A  64      31.505  19.636  -2.954  1.00101.17           C  
ANISOU  237  C   VAL A  64     4945  16487  17008   1545  -2112   -232       C  
ATOM    238  O   VAL A  64      30.417  20.081  -3.339  1.00102.94           O  
ANISOU  238  O   VAL A  64     5057  16717  17337   1621  -2178   -199       O  
ATOM    239  CB  VAL A  64      32.301  17.335  -3.662  1.00 99.88           C  
ANISOU  239  CB  VAL A  64     4885  16196  16869   1312  -2211   -195       C  
ATOM    240  CG1 VAL A  64      30.846  16.918  -3.515  1.00101.60           C  
ANISOU  240  CG1 VAL A  64     4967  16368  17267   1262  -2250   -166       C  
ATOM    241  CG2 VAL A  64      32.959  16.574  -4.802  1.00 99.53           C  
ANISOU  241  CG2 VAL A  64     4901  16118  16796   1271  -2326   -101       C  
ATOM    242  N   VAL A  65      31.943  19.830  -1.708  1.00108.08           N  
ANISOU  242  N   VAL A  65     5864  17409  17792   1511  -1962   -308       N  
ATOM    243  CA  VAL A  65      31.109  20.526  -0.730  1.00102.86           C  
ANISOU  243  CA  VAL A  65     5119  16820  17144   1562  -1870   -362       C  
ATOM    244  C   VAL A  65      30.948  21.996  -1.108  1.00101.78           C  
ANISOU  244  C   VAL A  65     4940  16724  17008   1739  -1884   -292       C  
ATOM    245  O   VAL A  65      29.831  22.529  -1.135  1.00104.21           O  
ANISOU  245  O   VAL A  65     5135  17057  17403   1818  -1908   -298       O  
ATOM    246  CB  VAL A  65      31.696  20.369   0.684  1.00105.80           C  
ANISOU  246  CB  VAL A  65     5550  17250  17399   1484  -1710   -420       C  
ATOM    247  CG1 VAL A  65      30.876  21.163   1.689  1.00101.92           C  
ANISOU  247  CG1 VAL A  65     4970  16852  16904   1548  -1613   -449       C  
ATOM    248  CG2 VAL A  65      31.749  18.899   1.074  1.00106.26           C  
ANISOU  248  CG2 VAL A  65     5638  17280  17457   1320  -1692   -488       C  
ATOM    249  N   VAL A  66      32.061  22.672  -1.406  1.00100.83           N  
ANISOU  249  N   VAL A  66     4904  16603  16803   1805  -1866   -217       N  
ATOM    250  CA  VAL A  66      32.005  24.096  -1.731  1.00101.71           C  
ANISOU  250  CA  VAL A  66     4979  16743  16925   1979  -1865   -136       C  
ATOM    251  C   VAL A  66      31.178  24.327  -2.990  1.00117.20           C  
ANISOU  251  C   VAL A  66     6859  18693  18978   2082  -2011    -79       C  
ATOM    252  O   VAL A  66      30.376  25.267  -3.058  1.00118.52           O  
ANISOU  252  O   VAL A  66     6937  18892  19204   2211  -2020    -53       O  
ATOM    253  CB  VAL A  66      33.427  24.670  -1.869  1.00100.38           C  
ANISOU  253  CB  VAL A  66     4914  16553  16675   2018  -1819    -52       C  
ATOM    254  CG1 VAL A  66      33.386  26.056  -2.492  1.00101.51           C  
ANISOU  254  CG1 VAL A  66     5014  16699  16855   2207  -1841     56       C  
ATOM    255  CG2 VAL A  66      34.106  24.725  -0.511  1.00100.56           C  
ANISOU  255  CG2 VAL A  66     4993  16589  16626   1942  -1671    -88       C  
ATOM    256  N   THR A  67      31.350  23.472  -4.001  1.00119.79           N  
ANISOU  256  N   THR A  67     7215  18983  19319   2032  -2131    -46       N  
ATOM    257  CA  THR A  67      30.543  23.601  -5.211  1.00122.08           C  
ANISOU  257  CA  THR A  67     7422  19277  19686   2123  -2280     30       C  
ATOM    258  C   THR A  67      29.072  23.302  -4.941  1.00119.70           C  
ANISOU  258  C   THR A  67     6991  18969  19519   2091  -2314    -18       C  
ATOM    259  O   THR A  67      28.194  23.908  -5.569  1.00108.71           O  
ANISOU  259  O   THR A  67     5502  17605  18198   2209  -2396     42       O  
ATOM    260  CB  THR A  67      31.083  22.684  -6.309  1.00120.10           C  
ANISOU  260  CB  THR A  67     7228  19003  19402   2068  -2399     91       C  
ATOM    261  OG1 THR A  67      31.375  21.393  -5.759  1.00126.00           O  
ANISOU  261  OG1 THR A  67     8029  19697  20150   1880  -2367     17       O  
ATOM    262  CG2 THR A  67      32.349  23.272  -6.920  1.00104.04           C  
ANISOU  262  CG2 THR A  67     5289  16988  17255   2160  -2394    177       C  
ATOM    263  N   LEU A  68      28.781  22.381  -4.018  1.00117.34           N  
ANISOU  263  N   LEU A  68     6686  18635  19263   1937  -2251   -112       N  
ATOM    264  CA  LEU A  68      27.395  22.151  -3.623  1.00107.85           C  
ANISOU  264  CA  LEU A  68     5352  17418  18207   1904  -2260   -145       C  
ATOM    265  C   LEU A  68      26.797  23.395  -2.982  1.00108.76           C  
ANISOU  265  C   LEU A  68     5396  17604  18325   2037  -2181   -185       C  
ATOM    266  O   LEU A  68      25.626  23.721  -3.215  1.00134.58           O  
ANISOU  266  O   LEU A  68     8541  20877  21716   2099  -2236   -159       O  
ATOM    267  CB  LEU A  68      27.300  20.958  -2.671  1.00107.02           C  
ANISOU  267  CB  LEU A  68     5258  17262  18142   1722  -2186   -230       C  
ATOM    268  CG  LEU A  68      27.270  19.568  -3.312  1.00107.01           C  
ANISOU  268  CG  LEU A  68     5262  17164  18233   1573  -2285   -133       C  
ATOM    269  CD1 LEU A  68      27.052  18.494  -2.257  1.00106.45           C  
ANISOU  269  CD1 LEU A  68     5184  17029  18232   1407  -2194   -192       C  
ATOM    270  CD2 LEU A  68      26.200  19.495  -4.390  1.00109.15           C  
ANISOU  270  CD2 LEU A  68     5406  17439  18627   1602  -2433     41       C  
ATOM    271  N   PHE A  69      27.584  24.106  -2.169  1.00107.55           N  
ANISOU  271  N   PHE A  69     5315  17508  18042   2080  -2051   -223       N  
ATOM    272  CA  PHE A  69      27.116  25.389  -1.656  1.00110.76           C  
ANISOU  272  CA  PHE A  69     5657  17981  18446   2222  -1979   -220       C  
ATOM    273  C   PHE A  69      26.959  26.407  -2.777  1.00109.80           C  
ANISOU  273  C   PHE A  69     5499  17857  18362   2399  -2075   -109       C  
ATOM    274  O   PHE A  69      26.095  27.286  -2.698  1.00111.36           O  
ANISOU  274  O   PHE A  69     5600  18087  18624   2522  -2071    -97       O  
ATOM    275  CB  PHE A  69      28.068  25.922  -0.585  1.00118.89           C  
ANISOU  275  CB  PHE A  69     6770  19058  19345   2222  -1824   -232       C  
ATOM    276  CG  PHE A  69      27.537  27.123   0.152  1.00125.02           C  
ANISOU  276  CG  PHE A  69     7476  19896  20130   2347  -1734   -225       C  
ATOM    277  CD1 PHE A  69      27.775  28.407  -0.316  1.00127.00           C  
ANISOU  277  CD1 PHE A  69     7722  20137  20395   2516  -1740   -128       C  
ATOM    278  CD2 PHE A  69      26.798  26.968   1.312  1.00108.31           C  
ANISOU  278  CD2 PHE A  69     5294  17848  18012   2302  -1638   -305       C  
ATOM    279  CE1 PHE A  69      27.287  29.510   0.359  1.00109.53           C  
ANISOU  279  CE1 PHE A  69     5444  17966  18208   2635  -1657   -114       C  
ATOM    280  CE2 PHE A  69      26.307  28.068   1.992  1.00110.86           C  
ANISOU  280  CE2 PHE A  69     5551  18228  18344   2422  -1555   -289       C  
ATOM    281  CZ  PHE A  69      26.553  29.339   1.514  1.00109.88           C  
ANISOU  281  CZ  PHE A  69     5425  18078  18246   2587  -1566   -196       C  
ATOM    282  N   CYS A  70      27.782  26.310  -3.823  1.00109.28           N  
ANISOU  282  N   CYS A  70     5508  17762  18251   2424  -2159    -21       N  
ATOM    283  CA  CYS A  70      27.614  27.171  -4.987  1.00119.10           C  
ANISOU  283  CA  CYS A  70     6715  19019  19517   2599  -2259     98       C  
ATOM    284  C   CYS A  70      26.395  26.795  -5.818  1.00132.05           C  
ANISOU  284  C   CYS A  70     8241  20665  21269   2616  -2404    128       C  
ATOM    285  O   CYS A  70      25.974  27.592  -6.664  1.00135.86           O  
ANISOU  285  O   CYS A  70     8665  21181  21775   2778  -2484    220       O  
ATOM    286  CB  CYS A  70      28.870  27.130  -5.860  1.00118.32           C  
ANISOU  286  CB  CYS A  70     6727  18906  19324   2624  -2302    190       C  
ATOM    287  SG  CYS A  70      30.361  27.779  -5.065  1.00121.73           S  
ANISOU  287  SG  CYS A  70     7279  19320  19654   2629  -2142    208       S  
ATOM    288  N   CYS A  71      25.823  25.610  -5.600  1.00141.70           N  
ANISOU  288  N   CYS A  71     9424  21853  22565   2455  -2437     73       N  
ATOM    289  CA  CYS A  71      24.617  25.191  -6.310  1.00141.30           C  
ANISOU  289  CA  CYS A  71     9246  21804  22636   2450  -2569    134       C  
ATOM    290  C   CYS A  71      23.353  25.529  -5.522  1.00136.52           C  
ANISOU  290  C   CYS A  71     8509  21202  22160   2464  -2517     81       C  
ATOM    291  O   CYS A  71      22.466  26.224  -6.028  1.00129.88           O  
ANISOU  291  O   CYS A  71     7562  20402  21384   2594  -2585    139       O  
ATOM    292  CB  CYS A  71      24.678  23.688  -6.608  1.00137.07           C  
ANISOU  292  CB  CYS A  71     8727  21226  22129   2264  -2638    161       C  
ATOM    293  SG  CYS A  71      23.188  23.026  -7.393  1.00136.88           S  
ANISOU  293  SG  CYS A  71     8531  21239  22239   2226  -2788    283       S  
ATOM    294  N   GLN A  72      23.259  25.043  -4.282  1.00142.64           N  
ANISOU  294  N   GLN A  72     9289  21944  22965   2339  -2396    -31       N  
ATOM    295  CA  GLN A  72      22.061  25.262  -3.479  1.00151.65           C  
ANISOU  295  CA  GLN A  72    10301  23092  24225   2343  -2339    -87       C  
ATOM    296  C   GLN A  72      22.042  26.622  -2.793  1.00157.30           C  
ANISOU  296  C   GLN A  72    11010  23886  24873   2500  -2232   -151       C  
ATOM    297  O   GLN A  72      20.965  27.079  -2.393  1.00158.91           O  
ANISOU  297  O   GLN A  72    11092  24115  25170   2558  -2209   -177       O  
ATOM    298  CB  GLN A  72      21.918  24.158  -2.429  1.00153.71           C  
ANISOU  298  CB  GLN A  72    10561  23304  24537   2155  -2250   -173       C  
ATOM    299  CG  GLN A  72      21.542  22.801  -3.002  1.00157.54           C  
ANISOU  299  CG  GLN A  72    11003  23701  25153   1990  -2347    -31       C  
ATOM    300  CD  GLN A  72      21.298  21.762  -1.926  1.00158.07           C  
ANISOU  300  CD  GLN A  72    11054  23700  25307   1813  -2246    -63       C  
ATOM    301  OE1 GLN A  72      21.708  21.932  -0.778  1.00160.22           O  
ANISOU  301  OE1 GLN A  72    11385  24024  25469   1813  -2108   -278       O  
ATOM    302  NE2 GLN A  72      20.622  20.678  -2.292  1.00155.27           N  
ANISOU  302  NE2 GLN A  72    10610  23308  25078   1667  -2301    198       N  
ATOM    303  N   LYS A  73      23.202  27.265  -2.636  1.00152.96           N  
ANISOU  303  N   LYS A  73    10579  23369  24171   2564  -2161   -149       N  
ATOM    304  CA  LYS A  73      23.316  28.596  -2.043  1.00147.44           C  
ANISOU  304  CA  LYS A  73     9877  22731  23412   2712  -2057   -148       C  
ATOM    305  C   LYS A  73      22.829  28.635  -0.598  1.00139.97           C  
ANISOU  305  C   LYS A  73     8884  21846  22451   2668  -1914   -255       C  
ATOM    306  O   LYS A  73      23.599  28.964   0.310  1.00125.47           O  
ANISOU  306  O   LYS A  73     7123  20054  20496   2660  -1784   -270       O  
ATOM    307  CB  LYS A  73      22.560  29.626  -2.888  1.00144.47           C  
ANISOU  307  CB  LYS A  73     9407  22365  23121   2901  -2143    -60       C  
ATOM    308  CG  LYS A  73      23.107  29.790  -4.297  1.00134.29           C  
ANISOU  308  CG  LYS A  73     8165  21052  21805   2985  -2270     67       C  
ATOM    309  CD  LYS A  73      22.313  30.818  -5.085  1.00132.05           C  
ANISOU  309  CD  LYS A  73     7784  20795  21592   3184  -2350    159       C  
ATOM    310  CE  LYS A  73      22.867  30.981  -6.491  1.00127.04           C  
ANISOU  310  CE  LYS A  73     7198  20165  20907   3282  -2473    292       C  
ATOM    311  NZ  LYS A  73      22.085  31.969  -7.284  1.00124.69           N  
ANISOU  311  NZ  LYS A  73     6806  19904  20667   3489  -2553    390       N  
ATOM    312  N   GLY A  74      21.559  28.307  -0.372  1.00142.13           N  
ANISOU  312  N   GLY A  74     9029  22126  22846   2641  -1935   -309       N  
ATOM    313  CA  GLY A  74      20.981  28.386   0.948  1.00138.34           C  
ANISOU  313  CA  GLY A  74     8488  21730  22343   2619  -1802   -402       C  
ATOM    314  C   GLY A  74      20.616  29.812   1.302  1.00139.77           C  
ANISOU  314  C   GLY A  74     8615  21970  22520   2802  -1738   -370       C  
ATOM    315  O   GLY A  74      21.395  30.543   1.923  1.00140.57           O  
ANISOU  315  O   GLY A  74     8790  22110  22511   2859  -1630   -338       O  
ATOM    316  N   PRO A  75      19.412  30.237   0.908  1.00147.23           N  
ANISOU  316  N   PRO A  75     9425  22909  23607   2896  -1805   -361       N  
ATOM    317  CA  PRO A  75      19.024  31.643   1.092  1.00147.87           C  
ANISOU  317  CA  PRO A  75     9450  23030  23703   3089  -1758   -320       C  
ATOM    318  C   PRO A  75      18.899  32.051   2.552  1.00159.98           C  
ANISOU  318  C   PRO A  75    10967  24658  25161   3101  -1588   -375       C  
ATOM    319  O   PRO A  75      17.903  31.736   3.212  1.00165.33           O  
ANISOU  319  O   PRO A  75    11538  25392  25889   3065  -1546   -449       O  
ATOM    320  CB  PRO A  75      17.673  31.729   0.369  1.00133.33           C  
ANISOU  320  CB  PRO A  75     7458  21162  22041   3153  -1876   -304       C  
ATOM    321  CG  PRO A  75      17.145  30.332   0.387  1.00129.02           C  
ANISOU  321  CG  PRO A  75     6860  20578  21582   2968  -1924   -363       C  
ATOM    322  CD  PRO A  75      18.348  29.444   0.269  1.00140.50           C  
ANISOU  322  CD  PRO A  75     8459  21995  22928   2829  -1926   -366       C  
ATOM    323  N   LYS A  76      19.916  32.754   3.057  1.00162.86           N  
ANISOU  323  N   LYS A  76    11431  25034  25415   3154  -1488   -321       N  
ATOM    324  CA  LYS A  76      19.925  33.325   4.404  1.00166.13           C  
ANISOU  324  CA  LYS A  76    11836  25520  25765   3191  -1326   -328       C  
ATOM    325  C   LYS A  76      19.763  32.232   5.467  1.00177.59           C  
ANISOU  325  C   LYS A  76    13280  27053  27143   3024  -1241   -409       C  
ATOM    326  O   LYS A  76      18.739  32.114   6.142  1.00175.67           O  
ANISOU  326  O   LYS A  76    12926  26882  26937   3023  -1190   -466       O  
ATOM    327  CB  LYS A  76      18.842  34.403   4.545  1.00165.13           C  
ANISOU  327  CB  LYS A  76    11584  25418  25740   3364  -1308   -321       C  
ATOM    328  CG  LYS A  76      18.956  35.533   3.533  1.00160.05           C  
ANISOU  328  CG  LYS A  76    10942  24698  25172   3545  -1383   -228       C  
ATOM    329  CD  LYS A  76      17.817  36.528   3.684  1.00159.79           C  
ANISOU  329  CD  LYS A  76    10780  24688  25245   3713  -1366   -226       C  
ATOM    330  CE  LYS A  76      17.917  37.643   2.654  1.00157.79           C  
ANISOU  330  CE  LYS A  76    10527  24358  25067   3902  -1439   -121       C  
ATOM    331  NZ  LYS A  76      16.798  38.618   2.777  1.00151.00           N  
ANISOU  331  NZ  LYS A  76     9542  23516  24315   4074  -1425   -118       N  
ATOM    332  N   LYS A  77      20.820  31.433   5.595  1.00117.47           N  
ANISOU  332  N   LYS A  77     5785  19424  19425   2887  -1223   -405       N  
ATOM    333  CA  LYS A  77      20.891  30.386   6.603  1.00116.52           C  
ANISOU  333  CA  LYS A  77     5680  19373  19219   2729  -1134   -458       C  
ATOM    334  C   LYS A  77      22.171  30.562   7.410  1.00133.62           C  
ANISOU  334  C   LYS A  77     7971  21541  21259   2697  -1023   -392       C  
ATOM    335  O   LYS A  77      23.094  31.271   7.002  1.00130.12           O  
ANISOU  335  O   LYS A  77     7610  21027  20803   2764  -1035   -319       O  
ATOM    336  CB  LYS A  77      20.836  28.987   5.969  1.00115.98           C  
ANISOU  336  CB  LYS A  77     5624  19275  19168   2570  -1230   -523       C  
ATOM    337  CG  LYS A  77      20.391  27.887   6.923  1.00115.85           C  
ANISOU  337  CG  LYS A  77     5566  19344  19110   2428  -1149   -588       C  
ATOM    338  CD  LYS A  77      20.409  26.523   6.255  1.00115.36           C  
ANISOU  338  CD  LYS A  77     5520  19243  19068   2277  -1241   -644       C  
ATOM    339  CE  LYS A  77      19.992  25.433   7.230  1.00115.32           C  
ANISOU  339  CE  LYS A  77     5469  19345  19003   2143  -1146   -691       C  
ATOM    340  NZ  LYS A  77      20.032  24.083   6.606  1.00114.90           N  
ANISOU  340  NZ  LYS A  77     5431  19281  18944   2000  -1225   -737       N  
ATOM    341  N   VAL A  78      22.217  29.907   8.569  1.00132.77           N  
ANISOU  341  N   VAL A  78     7869  21505  21074   2594   -913   -411       N  
ATOM    342  CA  VAL A  78      23.325  30.073   9.504  1.00128.16           C  
ANISOU  342  CA  VAL A  78     7387  20921  20386   2565   -800   -337       C  
ATOM    343  C   VAL A  78      24.328  28.939   9.344  1.00114.49           C  
ANISOU  343  C   VAL A  78     5773  19154  18574   2399   -825   -350       C  
ATOM    344  O   VAL A  78      25.509  29.176   9.066  1.00115.24           O  
ANISOU  344  O   VAL A  78     5980  19179  18629   2393   -835   -293       O  
ATOM    345  CB  VAL A  78      22.815  30.147  10.955  1.00129.30           C  
ANISOU  345  CB  VAL A  78     7469  21159  20500   2575   -655   -324       C  
ATOM    346  CG1 VAL A  78      23.938  30.562  11.893  1.00117.56           C  
ANISOU  346  CG1 VAL A  78     6077  19651  18939   2582   -541   -214       C  
ATOM    347  CG2 VAL A  78      21.640  31.104  11.054  1.00136.08           C  
ANISOU  347  CG2 VAL A  78     8196  22057  21450   2731   -639   -335       C  
ATOM    348  N   SER A  79      23.864  27.699   9.524  1.00113.40           N  
ANISOU  348  N   SER A  79     5605  19053  18428   2263   -833   -428       N  
ATOM    349  CA  SER A  79      24.771  26.556   9.504  1.00112.99           C  
ANISOU  349  CA  SER A  79     5660  18965  18307   2104   -843   -447       C  
ATOM    350  C   SER A  79      25.418  26.366   8.138  1.00117.55           C  
ANISOU  350  C   SER A  79     6315  19446  18902   2084   -976   -449       C  
ATOM    351  O   SER A  79      26.584  25.959   8.057  1.00122.33           O  
ANISOU  351  O   SER A  79     7042  19999  19439   2006   -977   -425       O  
ATOM    352  CB  SER A  79      24.023  25.288   9.917  1.00109.17           C  
ANISOU  352  CB  SER A  79     5111  18524  17845   1973   -824   -530       C  
ATOM    353  OG  SER A  79      22.969  25.001   9.015  1.00110.59           O  
ANISOU  353  OG  SER A  79     5189  18710  18121   1982   -927   -587       O  
ATOM    354  N   SER A  80      24.686  26.655   7.059  1.00119.22           N  
ANISOU  354  N   SER A  80     6456  19628  19213   2159  -1090   -474       N  
ATOM    355  CA  SER A  80      25.241  26.477   5.720  1.00116.65           C  
ANISOU  355  CA  SER A  80     6196  19203  18923   2153  -1223   -465       C  
ATOM    356  C   SER A  80      26.415  27.419   5.476  1.00118.41           C  
ANISOU  356  C   SER A  80     6519  19370  19102   2235  -1211   -374       C  
ATOM    357  O   SER A  80      27.382  27.051   4.797  1.00117.13           O  
ANISOU  357  O   SER A  80     6456  19135  18911   2183  -1269   -352       O  
ATOM    358  CB  SER A  80      24.152  26.689   4.669  1.00115.70           C  
ANISOU  358  CB  SER A  80     5968  19052  18941   2233  -1349   -492       C  
ATOM    359  OG  SER A  80      23.637  28.007   4.726  1.00115.10           O  
ANISOU  359  OG  SER A  80     5821  18999  18913   2402  -1330   -450       O  
ATOM    360  N   ILE A  81      26.350  28.635   6.022  1.00117.72           N  
ANISOU  360  N   ILE A  81     6401  19308  19021   2365  -1134   -316       N  
ATOM    361  CA  ILE A  81      27.447  29.585   5.859  1.00114.56           C  
ANISOU  361  CA  ILE A  81     6081  18840  18607   2447  -1112   -224       C  
ATOM    362  C   ILE A  81      28.697  29.081   6.571  1.00115.03           C  
ANISOU  362  C   ILE A  81     6257  18881  18566   2329  -1035   -200       C  
ATOM    363  O   ILE A  81      29.805  29.125   6.021  1.00115.92           O  
ANISOU  363  O   ILE A  81     6466  18916  18663   2312  -1068   -158       O  
ATOM    364  CB  ILE A  81      27.028  30.977   6.365  1.00114.68           C  
ANISOU  364  CB  ILE A  81     6026  18867  18681   2613  -1039   -171       C  
ATOM    365  CG1 ILE A  81      25.946  31.571   5.461  1.00110.79           C  
ANISOU  365  CG1 ILE A  81     5429  18371  18296   2746  -1132   -180       C  
ATOM    366  CG2 ILE A  81      28.230  31.907   6.438  1.00120.63           C  
ANISOU  366  CG2 ILE A  81     6857  19531  19445   2681   -990    -80       C  
ATOM    367  CD1 ILE A  81      26.414  31.843   4.049  1.00110.78           C  
ANISOU  367  CD1 ILE A  81     5468  18280  18343   2808  -1252   -129       C  
ATOM    368  N   TYR A  82      28.539  28.592   7.803  1.00107.23           N  
ANISOU  368  N   TYR A  82     5261  17967  17516   2250   -932   -221       N  
ATOM    369  CA  TYR A  82      29.683  28.061   8.538  1.00103.49           C  
ANISOU  369  CA  TYR A  82     4894  17478  16950   2138   -861   -194       C  
ATOM    370  C   TYR A  82      30.254  26.825   7.853  1.00102.19           C  
ANISOU  370  C   TYR A  82     4813  17272  16743   1996   -940   -247       C  
ATOM    371  O   TYR A  82      31.474  26.618   7.846  1.00100.65           O  
ANISOU  371  O   TYR A  82     4726  17019  16496   1936   -930   -214       O  
ATOM    372  CB  TYR A  82      29.282  27.742   9.978  1.00103.67           C  
ANISOU  372  CB  TYR A  82     4878  17591  16921   2093   -738   -188       C  
ATOM    373  CG  TYR A  82      29.011  28.963  10.827  1.00104.69           C  
ANISOU  373  CG  TYR A  82     4946  17736  17093   2228   -639   -111       C  
ATOM    374  CD1 TYR A  82      30.038  29.829  11.177  1.00105.59           C  
ANISOU  374  CD1 TYR A  82     5120  17763  17238   2284   -586    -32       C  
ATOM    375  CD2 TYR A  82      27.732  29.244  11.288  1.00109.49           C  
ANISOU  375  CD2 TYR A  82     5433  18428  17739   2300   -598   -128       C  
ATOM    376  CE1 TYR A  82      29.798  30.946  11.953  1.00110.90           C  
ANISOU  376  CE1 TYR A  82     5732  18414  17991   2411   -496     20       C  
ATOM    377  CE2 TYR A  82      27.482  30.359  12.067  1.00112.40           C  
ANISOU  377  CE2 TYR A  82     5746  18796  18164   2430   -504    -59       C  
ATOM    378  CZ  TYR A  82      28.518  31.206  12.397  1.00113.76           C  
ANISOU  378  CZ  TYR A  82     5979  18863  18381   2486   -454     12       C  
ATOM    379  OH  TYR A  82      28.275  32.316  13.172  1.00114.56           O  
ANISOU  379  OH  TYR A  82     6022  18931  18576   2619   -363     55       O  
ATOM    380  N   ILE A  83      29.387  25.991   7.274  1.00102.87           N  
ANISOU  380  N   ILE A  83     4844  17375  16867   1943  -1018   -328       N  
ATOM    381  CA  ILE A  83      29.859  24.839   6.508  1.00101.85           C  
ANISOU  381  CA  ILE A  83     4786  17185  16728   1822  -1103   -374       C  
ATOM    382  C   ILE A  83      30.685  25.304   5.315  1.00104.30           C  
ANISOU  382  C   ILE A  83     5165  17406  17058   1879  -1194   -320       C  
ATOM    383  O   ILE A  83      31.771  24.776   5.041  1.00105.62           O  
ANISOU  383  O   ILE A  83     5439  17514  17177   1800  -1212   -307       O  
ATOM    384  CB  ILE A  83      28.672  23.965   6.065  1.00103.02           C  
ANISOU  384  CB  ILE A  83     4842  17351  16949   1770  -1174   -458       C  
ATOM    385  CG1 ILE A  83      28.082  23.217   7.260  1.00103.24           C  
ANISOU  385  CG1 ILE A  83     4817  17457  16952   1679  -1074   -508       C  
ATOM    386  CG2 ILE A  83      29.099  22.985   4.982  1.00102.31           C  
ANISOU  386  CG2 ILE A  83     4813  17175  16883   1681  -1288   -486       C  
ATOM    387  CD1 ILE A  83      29.018  22.193   7.846  1.00101.56           C  
ANISOU  387  CD1 ILE A  83     4707  17215  16666   1535  -1020   -521       C  
ATOM    388  N   PHE A  84      30.184  26.310   4.595  1.00102.63           N  
ANISOU  388  N   PHE A  84     4889  17181  16923   2024  -1252   -282       N  
ATOM    389  CA  PHE A  84      30.885  26.807   3.415  1.00114.36           C  
ANISOU  389  CA  PHE A  84     6427  18587  18439   2098  -1338   -214       C  
ATOM    390  C   PHE A  84      32.248  27.382   3.782  1.00116.59           C  
ANISOU  390  C   PHE A  84     6805  18824  18670   2108  -1265   -139       C  
ATOM    391  O   PHE A  84      33.263  27.038   3.168  1.00111.48           O  
ANISOU  391  O   PHE A  84     6248  18113  17995   2061  -1306   -110       O  
ATOM    392  CB  PHE A  84      30.030  27.855   2.703  1.00104.24           C  
ANISOU  392  CB  PHE A  84     5048  17304  17256   2267  -1400   -176       C  
ATOM    393  CG  PHE A  84      30.752  28.583   1.608  1.00104.22           C  
ANISOU  393  CG  PHE A  84     5087  17228  17283   2373  -1467    -78       C  
ATOM    394  CD1 PHE A  84      31.022  27.958   0.402  1.00104.00           C  
ANISOU  394  CD1 PHE A  84     5098  17155  17263   2345  -1589    -61       C  
ATOM    395  CD2 PHE A  84      31.159  29.896   1.783  1.00104.53           C  
ANISOU  395  CD2 PHE A  84     5123  17238  17356   2506  -1406      7       C  
ATOM    396  CE1 PHE A  84      31.684  28.628  -0.609  1.00104.09           C  
ANISOU  396  CE1 PHE A  84     5144  17113  17294   2452  -1645     46       C  
ATOM    397  CE2 PHE A  84      31.822  30.570   0.776  1.00104.63           C  
ANISOU  397  CE2 PHE A  84     5168  17180  17408   2610  -1459    108       C  
ATOM    398  CZ  PHE A  84      32.085  29.936  -0.421  1.00104.41           C  
ANISOU  398  CZ  PHE A  84     5178  17126  17367   2585  -1577    132       C  
ATOM    399  N   ASN A  85      32.290  28.260   4.788  1.00113.43           N  
ANISOU  399  N   ASN A  85     6380  18446  18272   2170  -1156   -105       N  
ATOM    400  CA  ASN A  85      33.557  28.868   5.182  1.00111.11           C  
ANISOU  400  CA  ASN A  85     6162  18088  17966   2182  -1087    -36       C  
ATOM    401  C   ASN A  85      34.530  27.825   5.723  1.00108.80           C  
ANISOU  401  C   ASN A  85     5974  17789  17576   2019  -1050    -61       C  
ATOM    402  O   ASN A  85      35.742  27.915   5.489  1.00 97.15           O  
ANISOU  402  O   ASN A  85     4583  16239  16090   1996  -1049    -18       O  
ATOM    403  CB  ASN A  85      33.311  29.965   6.218  1.00106.14           C  
ANISOU  403  CB  ASN A  85     5474  17470  17385   2280   -979     -1       C  
ATOM    404  CG  ASN A  85      32.590  31.164   5.638  1.00112.27           C  
ANISOU  404  CG  ASN A  85     6160  18224  18272   2459  -1010     38       C  
ATOM    405  OD1 ASN A  85      31.477  31.492   6.049  1.00121.82           O  
ANISOU  405  OD1 ASN A  85     7276  19498  19512   2525   -984     14       O  
ATOM    406  ND2 ASN A  85      33.223  31.829   4.680  1.00112.24           N  
ANISOU  406  ND2 ASN A  85     6183  18128  18334   2545  -1061    106       N  
ATOM    407  N   LEU A  86      34.016  26.827   6.445  1.00107.38           N  
ANISOU  407  N   LEU A  86     5785  17683  17332   1910  -1017   -129       N  
ATOM    408  CA  LEU A  86      34.873  25.768   6.969  1.00 96.50           C  
ANISOU  408  CA  LEU A  86     4503  16298  15864   1760   -983   -155       C  
ATOM    409  C   LEU A  86      35.501  24.961   5.837  1.00 95.56           C  
ANISOU  409  C   LEU A  86     4461  16112  15735   1688  -1083   -177       C  
ATOM    410  O   LEU A  86      36.723  24.760   5.801  1.00120.10           O  
ANISOU  410  O   LEU A  86     7668  19163  18801   1632  -1073   -149       O  
ATOM    411  CB  LEU A  86      34.064  24.867   7.902  1.00 96.77           C  
ANISOU  411  CB  LEU A  86     4494  16419  15853   1672   -929   -220       C  
ATOM    412  CG  LEU A  86      34.769  23.689   8.571  1.00 95.32           C  
ANISOU  412  CG  LEU A  86     4397  16233  15588   1521   -886   -254       C  
ATOM    413  CD1 LEU A  86      36.009  24.153   9.310  1.00 94.18           C  
ANISOU  413  CD1 LEU A  86     4332  16063  15389   1518   -809   -173       C  
ATOM    414  CD2 LEU A  86      33.810  22.993   9.520  1.00 96.00           C  
ANISOU  414  CD2 LEU A  86     4414  16398  15663   1464   -823   -312       C  
ATOM    415  N   ALA A  87      34.675  24.498   4.894  1.00 96.41           N  
ANISOU  415  N   ALA A  87     4520  16220  15890   1693  -1183   -221       N  
ATOM    416  CA  ALA A  87      35.197  23.773   3.742  1.00 95.74           C  
ANISOU  416  CA  ALA A  87     4500  16068  15810   1641  -1287   -225       C  
ATOM    417  C   ALA A  87      36.095  24.643   2.874  1.00 95.47           C  
ANISOU  417  C   ALA A  87     4510  15971  15795   1736  -1326   -132       C  
ATOM    418  O   ALA A  87      36.937  24.110   2.142  1.00115.37           O  
ANISOU  418  O   ALA A  87     7108  18436  18292   1687  -1381   -112       O  
ATOM    419  CB  ALA A  87      34.046  23.210   2.908  1.00104.07           C  
ANISOU  419  CB  ALA A  87     5477  17130  16936   1643  -1393   -277       C  
ATOM    420  N   VAL A  88      35.937  25.967   2.936  1.00 96.92           N  
ANISOU  420  N   VAL A  88     4639  16156  16030   1875  -1296    -68       N  
ATOM    421  CA  VAL A  88      36.830  26.859   2.204  1.00110.16           C  
ANISOU  421  CA  VAL A  88     6349  17762  17745   1971  -1316     31       C  
ATOM    422  C   VAL A  88      38.197  26.910   2.876  1.00116.29           C  
ANISOU  422  C   VAL A  88     7215  18488  18480   1905  -1233     59       C  
ATOM    423  O   VAL A  88      39.237  26.817   2.212  1.00120.83           O  
ANISOU  423  O   VAL A  88     7859  19001  19049   1890  -1264    109       O  
ATOM    424  CB  VAL A  88      36.206  28.262   2.079  1.00114.49           C  
ANISOU  424  CB  VAL A  88     6805  18309  18388   2146  -1305     91       C  
ATOM    425  CG1 VAL A  88      37.280  29.303   1.801  1.00118.14           C  
ANISOU  425  CG1 VAL A  88     7298  18683  18908   2236  -1274    194       C  
ATOM    426  CG2 VAL A  88      35.161  28.278   0.974  1.00111.91           C  
ANISOU  426  CG2 VAL A  88     6404  18005  18111   2232  -1420     93       C  
ATOM    427  N   ALA A  89      38.216  27.054   4.204  1.00124.42           N  
ANISOU  427  N   ALA A  89     8240  19547  19485   1868  -1129     34       N  
ATOM    428  CA  ALA A  89      39.482  27.048   4.931  1.00 92.99           C  
ANISOU  428  CA  ALA A  89     4340  15520  15472   1799  -1055     54       C  
ATOM    429  C   ALA A  89      40.225  25.735   4.721  1.00 91.48           C  
ANISOU  429  C   ALA A  89     4250  15319  15190   1653  -1086     15       C  
ATOM    430  O   ALA A  89      41.424  25.726   4.408  1.00123.86           O  
ANISOU  430  O   ALA A  89     8425  19351  19286   1625  -1090     54       O  
ATOM    431  CB  ALA A  89      39.235  27.298   6.419  1.00 93.12           C  
ANISOU  431  CB  ALA A  89     4326  15582  15474   1785   -946     38       C  
ATOM    432  N   ASP A  90      39.523  24.609   4.879  1.00 91.44           N  
ANISOU  432  N   ASP A  90     4242  15371  15129   1561  -1108    -64       N  
ATOM    433  CA  ASP A  90      40.148  23.316   4.617  1.00 90.15           C  
ANISOU  433  CA  ASP A  90     4170  15182  14903   1429  -1142   -107       C  
ATOM    434  C   ASP A  90      40.593  23.205   3.164  1.00 90.02           C  
ANISOU  434  C   ASP A  90     4185  15105  14913   1457  -1245    -67       C  
ATOM    435  O   ASP A  90      41.636  22.609   2.870  1.00 90.55           O  
ANISOU  435  O   ASP A  90     4341  15122  14940   1384  -1259    -57       O  
ATOM    436  CB  ASP A  90      39.186  22.183   4.973  1.00112.89           C  
ANISOU  436  CB  ASP A  90     7020  18111  17763   1339  -1149   -199       C  
ATOM    437  CG  ASP A  90      38.913  22.098   6.460  1.00118.06           C  
ANISOU  437  CG  ASP A  90     7655  18829  18373   1298  -1039   -228       C  
ATOM    438  OD1 ASP A  90      39.512  22.887   7.220  1.00 90.12           O  
ANISOU  438  OD1 ASP A  90     4131  15298  14811   1336   -963   -170       O  
ATOM    439  OD2 ASP A  90      38.100  21.242   6.869  1.00128.47           O  
ANISOU  439  OD2 ASP A  90     8936  20184  19693   1231  -1029   -299       O  
ATOM    440  N   LEU A  91      39.821  23.785   2.242  1.00 91.36           N  
ANISOU  440  N   LEU A  91     4281  15283  15150   1570  -1319    -35       N  
ATOM    441  CA  LEU A  91      40.183  23.727   0.829  1.00 91.46           C  
ANISOU  441  CA  LEU A  91     4314  15252  15183   1616  -1422     23       C  
ATOM    442  C   LEU A  91      41.481  24.478   0.558  1.00 94.55           C  
ANISOU  442  C   LEU A  91     4757  15582  15585   1666  -1394    119       C  
ATOM    443  O   LEU A  91      42.299  24.044  -0.262  1.00 95.27           O  
ANISOU  443  O   LEU A  91     4910  15635  15652   1641  -1445    159       O  
ATOM    444  CB  LEU A  91      39.046  24.288  -0.025  1.00 93.24           C  
ANISOU  444  CB  LEU A  91     4440  15505  15480   1744  -1505     48       C  
ATOM    445  CG  LEU A  91      39.242  24.246  -1.540  1.00 99.23           C  
ANISOU  445  CG  LEU A  91     5207  16240  16257   1812  -1624    122       C  
ATOM    446  CD1 LEU A  91      39.484  22.820  -2.009  1.00 92.87           C  
ANISOU  446  CD1 LEU A  91     4462  15420  15404   1687  -1693     74       C  
ATOM    447  CD2 LEU A  91      38.040  24.851  -2.250  1.00 95.60           C  
ANISOU  447  CD2 LEU A  91     4642  15813  15868   1946  -1704    148       C  
ATOM    448  N   LEU A  92      41.688  25.609   1.236  1.00 91.02           N  
ANISOU  448  N   LEU A  92     4280  15118  15185   1737  -1311    159       N  
ATOM    449  CA  LEU A  92      42.936  26.347   1.070  1.00 90.45           C  
ANISOU  449  CA  LEU A  92     4265  14952  15150   1771  -1271    253       C  
ATOM    450  C   LEU A  92      44.098  25.620   1.739  1.00 88.78           C  
ANISOU  450  C   LEU A  92     4146  14716  14871   1634  -1220    218       C  
ATOM    451  O   LEU A  92      45.221  25.618   1.218  1.00 87.96           O  
ANISOU  451  O   LEU A  92     4127  14529  14766   1614  -1222    286       O  
ATOM    452  CB  LEU A  92      42.786  27.760   1.630  1.00 91.39           C  
ANISOU  452  CB  LEU A  92     4339  15019  15367   1878  -1194    308       C  
ATOM    453  CG  LEU A  92      41.686  28.619   1.004  1.00 93.20           C  
ANISOU  453  CG  LEU A  92     4479  15262  15673   2030  -1235    355       C  
ATOM    454  CD1 LEU A  92      41.575  29.955   1.720  1.00 94.09           C  
ANISOU  454  CD1 LEU A  92     4549  15307  15893   2126  -1146    394       C  
ATOM    455  CD2 LEU A  92      41.940  28.822  -0.482  1.00 93.71           C  
ANISOU  455  CD2 LEU A  92     4574  15273  15759   2111  -1314    467       C  
ATOM    456  N   LEU A  93      43.845  25.000   2.894  1.00 88.20           N  
ANISOU  456  N   LEU A  93     4077  14699  14735   1538  -1166    128       N  
ATOM    457  CA  LEU A  93      44.869  24.202   3.562  1.00 87.46           C  
ANISOU  457  CA  LEU A  93     4078  14586  14565   1407  -1122     94       C  
ATOM    458  C   LEU A  93      45.364  23.080   2.653  1.00 94.49           C  
ANISOU  458  C   LEU A  93     5043  15455  15402   1329  -1194     83       C  
ATOM    459  O   LEU A  93      46.564  22.972   2.355  1.00 90.06           O  
ANISOU  459  O   LEU A  93     4550  14839  14831   1298  -1192    122       O  
ATOM    460  CB  LEU A  93      44.301  23.639   4.866  1.00 86.50           C  
ANISOU  460  CB  LEU A  93     3954  14532  14380   1328  -1057     17       C  
ATOM    461  CG  LEU A  93      45.236  22.941   5.852  1.00 85.13           C  
ANISOU  461  CG  LEU A  93     3865  14352  14126   1209   -995    -13       C  
ATOM    462  CD1 LEU A  93      46.102  23.954   6.575  1.00 90.53           C  
ANISOU  462  CD1 LEU A  93     4548  14993  14856   1248   -924     40       C  
ATOM    463  CD2 LEU A  93      44.430  22.121   6.842  1.00 85.21           C  
ANISOU  463  CD2 LEU A  93     3864  14442  14071   1138   -953    -83       C  
ATOM    464  N   LEU A  94      44.439  22.233   2.194  1.00 99.27           N  
ANISOU  464  N   LEU A  94     5631  16100  15987   1300  -1260     30       N  
ATOM    465  CA  LEU A  94      44.801  21.166   1.268  1.00103.74           C  
ANISOU  465  CA  LEU A  94     6256  16640  16520   1237  -1339     23       C  
ATOM    466  C   LEU A  94      45.366  21.724  -0.031  1.00100.40           C  
ANISOU  466  C   LEU A  94     5833  16183  16132   1332  -1405    126       C  
ATOM    467  O   LEU A  94      46.156  21.052  -0.703  1.00 91.88           O  
ANISOU  467  O   LEU A  94     4819  15075  15018   1287  -1447    149       O  
ATOM    468  CB  LEU A  94      43.583  20.284   0.997  1.00104.46           C  
ANISOU  468  CB  LEU A  94     6304  16768  16618   1203  -1403    -48       C  
ATOM    469  CG  LEU A  94      42.980  19.644   2.250  1.00 96.83           C  
ANISOU  469  CG  LEU A  94     5328  15834  15630   1110  -1334   -141       C  
ATOM    470  CD1 LEU A  94      41.473  19.533   2.130  1.00100.86           C  
ANISOU  470  CD1 LEU A  94     5738  16391  16194   1140  -1375   -189       C  
ATOM    471  CD2 LEU A  94      43.594  18.278   2.505  1.00 86.71           C  
ANISOU  471  CD2 LEU A  94     4131  14512  14301    972  -1325   -192       C  
ATOM    472  N   ALA A  95      44.981  22.950  -0.396  1.00103.99           N  
ANISOU  472  N   ALA A  95     6212  16642  16658   1471  -1411    195       N  
ATOM    473  CA  ALA A  95      45.580  23.592  -1.561  1.00105.40           C  
ANISOU  473  CA  ALA A  95     6429  16757  16863   1563  -1447    333       C  
ATOM    474  C   ALA A  95      47.047  23.922  -1.323  1.00 86.31           C  
ANISOU  474  C   ALA A  95     4102  14248  14445   1527  -1372    402       C  
ATOM    475  O   ALA A  95      47.840  23.929  -2.272  1.00 86.11           O  
ANISOU  475  O   ALA A  95     4135  14172  14411   1551  -1399    502       O  
ATOM    476  CB  ALA A  95      44.800  24.855  -1.926  1.00 98.82           C  
ANISOU  476  CB  ALA A  95     5517  15920  16111   1718  -1453    409       C  
ATOM    477  N   THR A  96      47.429  24.197  -0.075  1.00 98.50           N  
ANISOU  477  N   THR A  96     5654  15771  15999   1474  -1279    354       N  
ATOM    478  CA  THR A  96      48.826  24.435   0.260  1.00 91.72           C  
ANISOU  478  CA  THR A  96     4876  14820  15153   1426  -1213    400       C  
ATOM    479  C   THR A  96      49.585  23.162   0.613  1.00 89.55           C  
ANISOU  479  C   THR A  96     4679  14564  14781   1285  -1212    327       C  
ATOM    480  O   THR A  96      50.809  23.217   0.770  1.00 88.97           O  
ANISOU  480  O   THR A  96     4676  14417  14709   1239  -1169    362       O  
ATOM    481  CB  THR A  96      48.940  25.424   1.426  1.00 98.74           C  
ANISOU  481  CB  THR A  96     5735  15665  16115   1445  -1120    389       C  
ATOM    482  OG1 THR A  96      47.984  25.089   2.439  1.00115.40           O  
ANISOU  482  OG1 THR A  96     7786  17880  18183   1414  -1101    281       O  
ATOM    483  CG2 THR A  96      48.695  26.844   0.945  1.00102.32           C  
ANISOU  483  CG2 THR A  96     6139  16036  16700   1588  -1104    495       C  
ATOM    484  N   LEU A  97      48.896  22.027   0.744  1.00 90.95           N  
ANISOU  484  N   LEU A  97     4842  14826  14890   1216  -1255    226       N  
ATOM    485  CA  LEU A  97      49.592  20.768   1.010  1.00 81.53           C  
ANISOU  485  CA  LEU A  97     3724  13635  13619   1088  -1255    162       C  
ATOM    486  C   LEU A  97      50.666  20.394  -0.014  1.00 91.32           C  
ANISOU  486  C   LEU A  97     5049  14813  14835   1072  -1293    239       C  
ATOM    487  O   LEU A  97      51.744  19.941   0.413  1.00 95.59           O  
ANISOU  487  O   LEU A  97     5666  15318  15338    989  -1252    226       O  
ATOM    488  CB  LEU A  97      48.573  19.628   1.134  1.00 81.66           C  
ANISOU  488  CB  LEU A  97     3732  13703  13595   1021  -1295     67       C  
ATOM    489  CG  LEU A  97      47.833  19.528   2.466  1.00 81.82           C  
ANISOU  489  CG  LEU A  97     3727  13763  13598    976  -1227    -13       C  
ATOM    490  CD1 LEU A  97      47.214  18.150   2.624  1.00 81.63           C  
ANISOU  490  CD1 LEU A  97     3723  13750  13545    877  -1251    -98       C  
ATOM    491  CD2 LEU A  97      48.774  19.835   3.613  1.00 80.94           C  
ANISOU  491  CD2 LEU A  97     3662  13636  13457    934  -1134    -16       C  
ATOM    492  N   PRO A  98      50.455  20.519  -1.335  1.00 81.60           N  
ANISOU  492  N   PRO A  98     3808  13577  13617   1150  -1369    323       N  
ATOM    493  CA  PRO A  98      51.478  20.018  -2.276  1.00 85.69           C  
ANISOU  493  CA  PRO A  98     4408  14057  14094   1130  -1402    399       C  
ATOM    494  C   PRO A  98      52.855  20.633  -2.089  1.00 92.50           C  
ANISOU  494  C   PRO A  98     5334  14832  14981   1123  -1326    479       C  
ATOM    495  O   PRO A  98      53.864  19.936  -2.265  1.00 79.24           O  
ANISOU  495  O   PRO A  98     3730  13123  13252   1053  -1322    489       O  
ATOM    496  CB  PRO A  98      50.887  20.369  -3.649  1.00 82.24           C  
ANISOU  496  CB  PRO A  98     3932  13646  13671   1250  -1488    495       C  
ATOM    497  CG  PRO A  98      49.430  20.403  -3.426  1.00 85.55           C  
ANISOU  497  CG  PRO A  98     4257  14131  14117   1283  -1529    417       C  
ATOM    498  CD  PRO A  98      49.247  20.972  -2.052  1.00 84.45           C  
ANISOU  498  CD  PRO A  98     4085  13984  14017   1257  -1436    350       C  
ATOM    499  N   LEU A  99      52.932  21.920  -1.744  1.00 96.32           N  
ANISOU  499  N   LEU A  99     5782  15261  15552   1194  -1266    537       N  
ATOM    500  CA  LEU A  99      54.234  22.546  -1.534  1.00 81.07           C  
ANISOU  500  CA  LEU A  99     3901  13226  13676   1182  -1193    608       C  
ATOM    501  C   LEU A  99      54.977  21.892  -0.377  1.00 79.01           C  
ANISOU  501  C   LEU A  99     3693  12962  13367   1055  -1143    504       C  
ATOM    502  O   LEU A  99      56.199  21.713  -0.436  1.00 78.19           O  
ANISOU  502  O   LEU A  99     3655  12796  13258   1005  -1114    538       O  
ATOM    503  CB  LEU A  99      54.068  24.044  -1.286  1.00 82.65           C  
ANISOU  503  CB  LEU A  99     4044  13353  14008   1279  -1138    674       C  
ATOM    504  CG  LEU A  99      53.542  24.870  -2.461  1.00 89.93           C  
ANISOU  504  CG  LEU A  99     4920  14256  14994   1423  -1171    808       C  
ATOM    505  CD1 LEU A  99      53.490  26.344  -2.094  1.00 90.42           C  
ANISOU  505  CD1 LEU A  99     4931  14216  15208   1510  -1102    868       C  
ATOM    506  CD2 LEU A  99      54.400  24.651  -3.698  1.00 87.62           C  
ANISOU  506  CD2 LEU A  99     4683  13931  14676   1449  -1196    939       C  
ATOM    507  N   TRP A 100      54.255  21.524   0.683  1.00 78.86           N  
ANISOU  507  N   TRP A 100     3641  13014  13309   1007  -1129    383       N  
ATOM    508  CA  TRP A 100      54.893  20.841   1.801  1.00 78.71           C  
ANISOU  508  CA  TRP A 100     3669  13009  13229    896  -1083    292       C  
ATOM    509  C   TRP A 100      55.212  19.391   1.462  1.00 84.79           C  
ANISOU  509  C   TRP A 100     4505  13808  13905    807  -1125    246       C  
ATOM    510  O   TRP A 100      56.164  18.823   2.011  1.00 83.64           O  
ANISOU  510  O   TRP A 100     4422  13642  13714    724  -1093    211       O  
ATOM    511  CB  TRP A 100      54.007  20.927   3.042  1.00 78.00           C  
ANISOU  511  CB  TRP A 100     3518  12995  13124    884  -1048    198       C  
ATOM    512  CG  TRP A 100      53.688  22.337   3.425  1.00 79.03           C  
ANISOU  512  CG  TRP A 100     3583  13088  13356    973  -1005    241       C  
ATOM    513  CD1 TRP A 100      52.483  22.965   3.311  1.00 94.70           C  
ANISOU  513  CD1 TRP A 100     5483  15109  15388   1061  -1019    248       C  
ATOM    514  CD2 TRP A 100      54.595  23.304   3.967  1.00 79.04           C  
ANISOU  514  CD2 TRP A 100     3596  12992  13445    986   -944    278       C  
ATOM    515  NE1 TRP A 100      52.580  24.260   3.758  1.00 94.41           N  
ANISOU  515  NE1 TRP A 100     5407  15000  15464   1131   -966    290       N  
ATOM    516  CE2 TRP A 100      53.867  24.494   4.165  1.00 87.32           C  
ANISOU  516  CE2 TRP A 100     4565  14010  14601   1084   -921    305       C  
ATOM    517  CE3 TRP A 100      55.950  23.278   4.309  1.00 78.20           C  
ANISOU  517  CE3 TRP A 100     3553  12810  13349    925   -908    285       C  
ATOM    518  CZ2 TRP A 100      54.448  25.646   4.690  1.00 85.94           C  
ANISOU  518  CZ2 TRP A 100     4376  13718  14560   1120   -863    330       C  
ATOM    519  CZ3 TRP A 100      56.526  24.424   4.828  1.00 78.67           C  
ANISOU  519  CZ3 TRP A 100     3594  12759  13538    957   -856    308       C  
ATOM    520  CH2 TRP A 100      55.775  25.591   5.014  1.00 84.18           C  
ANISOU  520  CH2 TRP A 100     4214  13414  14357   1052   -834    326       C  
ATOM    521  N   ALA A 101      54.435  18.778   0.565  1.00 77.13           N  
ANISOU  521  N   ALA A 101     3516  12877  12912    826  -1201    245       N  
ATOM    522  CA  ALA A 101      54.810  17.466   0.048  1.00 76.35           C  
ANISOU  522  CA  ALA A 101     3479  12781  12748    753  -1247    222       C  
ATOM    523  C   ALA A 101      56.148  17.538  -0.679  1.00 75.78           C  
ANISOU  523  C   ALA A 101     3481  12643  12668    755  -1242    322       C  
ATOM    524  O   ALA A 101      57.027  16.690  -0.479  1.00 74.72           O  
ANISOU  524  O   ALA A 101     3418  12488  12484    672  -1228    294       O  
ATOM    525  CB  ALA A 101      53.718  16.933  -0.878  1.00112.38           C  
ANISOU  525  CB  ALA A 101     7998  17393  17308    786  -1339    214       C  
ATOM    526  N   THR A 102      56.320  18.556  -1.527  1.00 87.24           N  
ANISOU  526  N   THR A 102     4913  14058  14175    853  -1247    446       N  
ATOM    527  CA  THR A 102      57.612  18.782  -2.164  1.00 85.68           C  
ANISOU  527  CA  THR A 102     4775  13792  13989    863  -1226    556       C  
ATOM    528  C   THR A 102      58.688  19.105  -1.136  1.00 75.36           C  
ANISOU  528  C   THR A 102     3505  12419  12711    800  -1142    529       C  
ATOM    529  O   THR A 102      59.860  18.764  -1.332  1.00 74.61           O  
ANISOU  529  O   THR A 102     3473  12277  12597    756  -1122    566       O  
ATOM    530  CB  THR A 102      57.501  19.912  -3.189  1.00 77.38           C  
ANISOU  530  CB  THR A 102     3683  12707  13009    992  -1234    705       C  
ATOM    531  OG1 THR A 102      56.351  19.697  -4.017  1.00 99.34           O  
ANISOU  531  OG1 THR A 102     6418  15566  15759   1060  -1319    716       O  
ATOM    532  CG2 THR A 102      58.742  19.964  -4.069  1.00 77.13           C  
ANISOU  532  CG2 THR A 102     3708  12619  12981   1008  -1219    835       C  
ATOM    533  N   TYR A 103      58.308  19.756  -0.033  1.00 75.59           N  
ANISOU  533  N   TYR A 103     3490  12447  12784    799  -1095    466       N  
ATOM    534  CA  TYR A 103      59.271  20.060   1.020  1.00 79.24           C  
ANISOU  534  CA  TYR A 103     3978  12857  13271    743  -1025    430       C  
ATOM    535  C   TYR A 103      59.798  18.787   1.669  1.00 79.14           C  
ANISOU  535  C   TYR A 103     4030  12886  13153    632  -1022    334       C  
ATOM    536  O   TYR A 103      61.005  18.653   1.903  1.00 72.98           O  
ANISOU  536  O   TYR A 103     3305  12057  12368    582   -990    342       O  
ATOM    537  CB  TYR A 103      58.626  20.970   2.064  1.00 95.58           C  
ANISOU  537  CB  TYR A 103     5980  14936  15400    774   -984    382       C  
ATOM    538  CG  TYR A 103      59.571  21.477   3.130  1.00 87.41           C  
ANISOU  538  CG  TYR A 103     4959  13843  14411    733   -920    353       C  
ATOM    539  CD1 TYR A 103      60.524  22.441   2.836  1.00 75.60           C  
ANISOU  539  CD1 TYR A 103     3467  12217  13041    764   -885    434       C  
ATOM    540  CD2 TYR A 103      59.494  21.008   4.435  1.00 74.76           C  
ANISOU  540  CD2 TYR A 103     3358  12313  12735    669   -895    249       C  
ATOM    541  CE1 TYR A 103      61.382  22.916   3.806  1.00 75.42           C  
ANISOU  541  CE1 TYR A 103     3450  12128  13079    725   -835    395       C  
ATOM    542  CE2 TYR A 103      60.349  21.477   5.413  1.00 74.58           C  
ANISOU  542  CE2 TYR A 103     3342  12242  12751    639   -846    226       C  
ATOM    543  CZ  TYR A 103      61.291  22.431   5.091  1.00 74.91           C  
ANISOU  543  CZ  TYR A 103     3389  12145  12929    664   -821    289       C  
ATOM    544  OH  TYR A 103      62.146  22.907   6.056  1.00 79.86           O  
ANISOU  544  OH  TYR A 103     4017  12709  13616    633   -781    250       O  
ATOM    545  N   TYR A 104      58.908  17.838   1.967  1.00 83.29           N  
ANISOU  545  N   TYR A 104     4547  13495  13606    594  -1054    243       N  
ATOM    546  CA  TYR A 104      59.349  16.565   2.522  1.00 83.28           C  
ANISOU  546  CA  TYR A 104     4604  13515  13522    495  -1049    159       C  
ATOM    547  C   TYR A 104      60.006  15.674   1.476  1.00 80.93           C  
ANISOU  547  C   TYR A 104     4374  13186  13189    467  -1091    206       C  
ATOM    548  O   TYR A 104      60.730  14.742   1.844  1.00 70.96           O  
ANISOU  548  O   TYR A 104     3173  11912  11875    390  -1079    162       O  
ATOM    549  CB  TYR A 104      58.174  15.831   3.169  1.00 72.61           C  
ANISOU  549  CB  TYR A 104     3214  12237  12137    463  -1061     55       C  
ATOM    550  CG  TYR A 104      57.855  16.305   4.570  1.00 72.79           C  
ANISOU  550  CG  TYR A 104     3218  12291  12148    454   -998      2       C  
ATOM    551  CD1 TYR A 104      56.839  17.222   4.801  1.00 73.82           C  
ANISOU  551  CD1 TYR A 104     3266  12463  12321    523   -990      8       C  
ATOM    552  CD2 TYR A 104      58.574  15.835   5.661  1.00 78.94           C  
ANISOU  552  CD2 TYR A 104     4057  13066  12871    385   -949    -47       C  
ATOM    553  CE1 TYR A 104      56.546  17.655   6.081  1.00 88.77           C  
ANISOU  553  CE1 TYR A 104     5134  14397  14197    522   -932    -25       C  
ATOM    554  CE2 TYR A 104      58.290  16.263   6.943  1.00 77.16           C  
ANISOU  554  CE2 TYR A 104     3807  12889  12621    387   -895    -80       C  
ATOM    555  CZ  TYR A 104      57.275  17.173   7.148  1.00 86.11           C  
ANISOU  555  CZ  TYR A 104     4856  14068  13794    455   -886    -63       C  
ATOM    556  OH  TYR A 104      56.990  17.601   8.424  1.00 97.91           O  
ANISOU  556  OH  TYR A 104     6318  15621  15261    462   -832    -70       O  
ATOM    557  N   SER A 105      59.773  15.936   0.188  1.00 82.61           N  
ANISOU  557  N   SER A 105     4573  13389  13424    534  -1141    301       N  
ATOM    558  CA  SER A 105      60.422  15.141  -0.851  1.00 78.20           C  
ANISOU  558  CA  SER A 105     4074  12815  12823    519  -1182    361       C  
ATOM    559  C   SER A 105      61.921  15.411  -0.904  1.00 71.49           C  
ANISOU  559  C   SER A 105     3281  11898  11984    502  -1133    427       C  
ATOM    560  O   SER A 105      62.721  14.478  -1.042  1.00 70.66           O  
ANISOU  560  O   SER A 105     3241  11783  11825    443  -1136    421       O  
ATOM    561  CB  SER A 105      59.777  15.421  -2.207  1.00 73.11           C  
ANISOU  561  CB  SER A 105     3392  12197  12191    611  -1250    455       C  
ATOM    562  OG  SER A 105      58.417  15.023  -2.216  1.00 91.49           O  
ANISOU  562  OG  SER A 105     5666  14586  14509    619  -1305    384       O  
ATOM    563  N   TYR A 106      62.321  16.677  -0.795  1.00 84.19           N  
ANISOU  563  N   TYR A 106     4861  13452  13674    552  -1086    492       N  
ATOM    564  CA  TYR A 106      63.726  17.062  -0.827  1.00 83.22           C  
ANISOU  564  CA  TYR A 106     4778  13251  13591    537  -1035    557       C  
ATOM    565  C   TYR A 106      64.386  17.014   0.545  1.00 70.84           C  
ANISOU  565  C   TYR A 106     3231  11666  12018    461   -983    459       C  
ATOM    566  O   TYR A 106      65.512  17.500   0.692  1.00 78.62           O  
ANISOU  566  O   TYR A 106     4235  12580  13056    448   -938    497       O  
ATOM    567  CB  TYR A 106      63.877  18.463  -1.424  1.00 72.59           C  
ANISOU  567  CB  TYR A 106     3384  11831  12366    629  -1007    685       C  
ATOM    568  CG  TYR A 106      63.613  18.525  -2.910  1.00 73.32           C  
ANISOU  568  CG  TYR A 106     3465  11938  12454    716  -1051    819       C  
ATOM    569  CD1 TYR A 106      64.615  18.226  -3.824  1.00 73.11           C  
ANISOU  569  CD1 TYR A 106     3482  11885  12410    722  -1046    926       C  
ATOM    570  CD2 TYR A 106      62.365  18.883  -3.401  1.00 79.60           C  
ANISOU  570  CD2 TYR A 106     4202  12784  13256    798  -1097    843       C  
ATOM    571  CE1 TYR A 106      64.381  18.280  -5.183  1.00 73.89           C  
ANISOU  571  CE1 TYR A 106     3569  12018  12489    814  -1086   1058       C  
ATOM    572  CE2 TYR A 106      62.121  18.941  -4.760  1.00 80.79           C  
ANISOU  572  CE2 TYR A 106     4342  12966  13389    888  -1144    969       C  
ATOM    573  CZ  TYR A 106      63.134  18.638  -5.646  1.00 77.19           C  
ANISOU  573  CZ  TYR A 106     3932  12492  12906    898  -1137   1079       C  
ATOM    574  OH  TYR A 106      62.900  18.693  -7.001  1.00 86.73           O  
ANISOU  574  OH  TYR A 106     5127  13749  14077   1001  -1182   1212       O  
ATOM    575  N   ARG A 107      63.710  16.444   1.545  1.00 70.52           N  
ANISOU  575  N   ARG A 107     3183  11694  11917    415   -986    337       N  
ATOM    576  CA  ARG A 107      64.229  16.301   2.905  1.00 69.93           C  
ANISOU  576  CA  ARG A 107     3124  11633  11813    351   -942    244       C  
ATOM    577  C   ARG A 107      64.599  17.665   3.498  1.00 70.51           C  
ANISOU  577  C   ARG A 107     3153  11656  11982    384   -895    268       C  
ATOM    578  O   ARG A 107      65.766  18.041   3.619  1.00 70.31           O  
ANISOU  578  O   ARG A 107     3151  11561  12004    365   -864    297       O  
ATOM    579  CB  ARG A 107      65.417  15.331   2.938  1.00 68.90           C  
ANISOU  579  CB  ARG A 107     3072  11483  11624    281   -935    229       C  
ATOM    580  CG  ARG A 107      65.100  13.970   2.339  1.00 68.41           C  
ANISOU  580  CG  ARG A 107     3053  11447  11493    248   -981    212       C  
ATOM    581  CD  ARG A 107      65.809  12.850   3.079  1.00 78.85           C  
ANISOU  581  CD  ARG A 107     4436  12773  12752    168   -966    137       C  
ATOM    582  NE  ARG A 107      65.343  11.538   2.636  1.00 67.11           N  
ANISOU  582  NE  ARG A 107     2980  11296  11222    134  -1008    117       N  
ATOM    583  CZ  ARG A 107      65.524  10.411   3.316  1.00 66.45           C  
ANISOU  583  CZ  ARG A 107     2935  11210  11102     69   -999     49       C  
ATOM    584  NH1 ARG A 107      65.066   9.264   2.835  1.00 66.31           N  
ANISOU  584  NH1 ARG A 107     2939  11191  11064     40  -1038     47       N  
ATOM    585  NH2 ARG A 107      66.160  10.432   4.478  1.00 68.85           N  
ANISOU  585  NH2 ARG A 107     3258  11508  11393     37   -953    -10       N  
ATOM    586  N   TYR A 108      63.546  18.400   3.857  1.00 71.33           N  
ANISOU  586  N   TYR A 108     3188  11788  12127    435   -892    254       N  
ATOM    587  CA  TYR A 108      63.600  19.672   4.573  1.00 72.06           C  
ANISOU  587  CA  TYR A 108     3226  11832  12323    471   -851    259       C  
ATOM    588  C   TYR A 108      64.268  20.790   3.785  1.00 72.73           C  
ANISOU  588  C   TYR A 108     3295  11778  12559    524   -832    364       C  
ATOM    589  O   TYR A 108      64.554  21.848   4.358  1.00 73.35           O  
ANISOU  589  O   TYR A 108     3334  11775  12759    545   -795    361       O  
ATOM    590  CB  TYR A 108      64.298  19.523   5.931  1.00 71.58           C  
ANISOU  590  CB  TYR A 108     3178  11795  12223    410   -818    184       C  
ATOM    591  CG  TYR A 108      63.555  18.631   6.899  1.00 71.21           C  
ANISOU  591  CG  TYR A 108     3126  11885  12045    373   -821     98       C  
ATOM    592  CD1 TYR A 108      62.171  18.527   6.854  1.00 74.25           C  
ANISOU  592  CD1 TYR A 108     3463  12343  12406    407   -837     77       C  
ATOM    593  CD2 TYR A 108      64.237  17.889   7.853  1.00 81.76           C  
ANISOU  593  CD2 TYR A 108     4498  13277  13289    306   -805     47       C  
ATOM    594  CE1 TYR A 108      61.486  17.712   7.736  1.00 71.48           C  
ANISOU  594  CE1 TYR A 108     3120  12089  11951    370   -829     10       C  
ATOM    595  CE2 TYR A 108      63.561  17.071   8.739  1.00 81.76           C  
ANISOU  595  CE2 TYR A 108     4520  13367  13177    275   -796     -6       C  
ATOM    596  CZ  TYR A 108      62.186  16.986   8.676  1.00 70.76           C  
ANISOU  596  CZ  TYR A 108     3095  12020  11772    304   -804    -24       C  
ATOM    597  OH  TYR A 108      61.510  16.173   9.556  1.00 82.58           O  
ANISOU  597  OH  TYR A 108     4616  13585  13175    273   -785    -74       O  
ATOM    598  N   ASP A 109      64.508  20.606   2.489  1.00 72.74           N  
ANISOU  598  N   ASP A 109     3322  11743  12571    551   -853    461       N  
ATOM    599  CA  ASP A 109      65.155  21.625   1.668  1.00 73.46           C  
ANISOU  599  CA  ASP A 109     3396  11705  12812    607   -824    584       C  
ATOM    600  C   ASP A 109      64.083  22.466   0.981  1.00 74.66           C  
ANISOU  600  C   ASP A 109     3482  11843  13042    712   -837    662       C  
ATOM    601  O   ASP A 109      63.345  21.967   0.125  1.00 77.10           O  
ANISOU  601  O   ASP A 109     3792  12224  13277    750   -886    703       O  
ATOM    602  CB  ASP A 109      66.088  20.982   0.646  1.00 72.93           C  
ANISOU  602  CB  ASP A 109     3387  11615  12707    588   -832    670       C  
ATOM    603  CG  ASP A 109      67.040  21.982   0.019  1.00 73.61           C  
ANISOU  603  CG  ASP A 109     3456  11559  12954    627   -782    794       C  
ATOM    604  OD1 ASP A 109      67.101  23.130   0.506  1.00 75.64           O  
ANISOU  604  OD1 ASP A 109     3660  11717  13361    654   -740    793       O  
ATOM    605  OD2 ASP A 109      67.726  21.621  -0.959  1.00 73.43           O  
ANISOU  605  OD2 ASP A 109     3468  11517  12916    634   -780    896       O  
ATOM    606  N   TRP A 110      64.000  23.741   1.354  1.00 75.63           N  
ANISOU  606  N   TRP A 110     3546  11868  13322    762   -795    678       N  
ATOM    607  CA  TRP A 110      63.051  24.670   0.754  1.00 76.90           C  
ANISOU  607  CA  TRP A 110     3641  12000  13579    872   -798    759       C  
ATOM    608  C   TRP A 110      63.731  25.427  -0.379  1.00 92.57           C  
ANISOU  608  C   TRP A 110     5617  13857  15698    938   -764    925       C  
ATOM    609  O   TRP A 110      64.780  26.048  -0.178  1.00 98.01           O  
ANISOU  609  O   TRP A 110     6305  14413  16521    916   -708    950       O  
ATOM    610  CB  TRP A 110      62.515  25.644   1.804  1.00 77.67           C  
ANISOU  610  CB  TRP A 110     3673  12053  13783    898   -766    685       C  
ATOM    611  CG  TRP A 110      61.465  26.584   1.288  1.00 79.02           C  
ANISOU  611  CG  TRP A 110     3774  12198  14051   1015   -768    757       C  
ATOM    612  CD1 TRP A 110      61.668  27.811   0.727  1.00 80.24           C  
ANISOU  612  CD1 TRP A 110     3886  12205  14397   1101   -724    871       C  
ATOM    613  CD2 TRP A 110      60.047  26.374   1.292  1.00 79.39           C  
ANISOU  613  CD2 TRP A 110     3782  12366  14015   1064   -811    724       C  
ATOM    614  NE1 TRP A 110      60.465  28.377   0.379  1.00 81.91           N  
ANISOU  614  NE1 TRP A 110     4037  12443  14640   1206   -740    913       N  
ATOM    615  CE2 TRP A 110      59.455  27.515   0.715  1.00 87.36           C  
ANISOU  615  CE2 TRP A 110     4729  13301  15163   1184   -796    820       C  
ATOM    616  CE3 TRP A 110      59.221  25.333   1.726  1.00 78.73           C  
ANISOU  616  CE3 TRP A 110     3708  12442  13764   1018   -858    623       C  
ATOM    617  CZ2 TRP A 110      58.076  27.643   0.561  1.00 88.93           C  
ANISOU  617  CZ2 TRP A 110     4874  13588  15328   1260   -833    814       C  
ATOM    618  CZ3 TRP A 110      57.853  25.461   1.572  1.00 79.51           C  
ANISOU  618  CZ3 TRP A 110     3749  12622  13840   1088   -891    615       C  
ATOM    619  CH2 TRP A 110      57.294  26.608   0.995  1.00 80.92           C  
ANISOU  619  CH2 TRP A 110     3865  12732  14148   1208   -881    707       C  
ATOM    620  N   LEU A 111      63.131  25.376  -1.569  1.00 92.32           N  
ANISOU  620  N   LEU A 111     5574  13869  15633   1023   -798   1041       N  
ATOM    621  CA  LEU A 111      63.722  25.968  -2.764  1.00 93.36           C  
ANISOU  621  CA  LEU A 111     5700  13908  15863   1100   -764   1226       C  
ATOM    622  C   LEU A 111      62.853  27.058  -3.380  1.00 90.77           C  
ANISOU  622  C   LEU A 111     5304  13538  15645   1237   -753   1340       C  
ATOM    623  O   LEU A 111      63.138  27.503  -4.499  1.00 81.48           O  
ANISOU  623  O   LEU A 111     4121  12311  14527   1326   -727   1516       O  
ATOM    624  CB  LEU A 111      64.007  24.878  -3.804  1.00 93.84           C  
ANISOU  624  CB  LEU A 111     5818  14063  15772   1094   -810   1296       C  
ATOM    625  CG  LEU A 111      62.803  24.094  -4.338  1.00 80.16           C  
ANISOU  625  CG  LEU A 111     4086  12489  13884   1132   -900   1274       C  
ATOM    626  CD1 LEU A 111      62.396  24.584  -5.722  1.00 79.74           C  
ANISOU  626  CD1 LEU A 111     4003  12447  13847   1272   -916   1454       C  
ATOM    627  CD2 LEU A 111      63.092  22.600  -4.357  1.00 77.13           C  
ANISOU  627  CD2 LEU A 111     3771  12207  13329   1038   -952   1192       C  
ATOM    628  N   PHE A 112      61.813  27.510  -2.681  1.00 96.55           N  
ANISOU  628  N   PHE A 112     5986  14294  16406   1265   -766   1253       N  
ATOM    629  CA  PHE A 112      60.857  28.456  -3.241  1.00 82.63           C  
ANISOU  629  CA  PHE A 112     4159  12509  14728   1401   -764   1350       C  
ATOM    630  C   PHE A 112      61.097  29.897  -2.807  1.00 92.92           C  
ANISOU  630  C   PHE A 112     5406  13628  16270   1450   -680   1384       C  
ATOM    631  O   PHE A 112      60.477  30.804  -3.371  1.00 85.19           O  
ANISOU  631  O   PHE A 112     4378  12601  15391   1575   -662   1494       O  
ATOM    632  CB  PHE A 112      59.430  28.038  -2.869  1.00 82.65           C  
ANISOU  632  CB  PHE A 112     4131  12657  14613   1417   -834   1241       C  
ATOM    633  CG  PHE A 112      59.008  26.733  -3.480  1.00 81.92           C  
ANISOU  633  CG  PHE A 112     4079  12729  14319   1391   -920   1218       C  
ATOM    634  CD1 PHE A 112      59.276  26.460  -4.811  1.00 82.21           C  
ANISOU  634  CD1 PHE A 112     4142  12792  14303   1451   -948   1361       C  
ATOM    635  CD2 PHE A 112      58.356  25.775  -2.722  1.00 81.05           C  
ANISOU  635  CD2 PHE A 112     3977  12741  14077   1309   -970   1056       C  
ATOM    636  CE1 PHE A 112      58.893  25.260  -5.378  1.00 81.66           C  
ANISOU  636  CE1 PHE A 112     4106  12863  14060   1428  -1034   1329       C  
ATOM    637  CE2 PHE A 112      57.972  24.571  -3.284  1.00 80.50           C  
ANISOU  637  CE2 PHE A 112     3940  12799  13850   1281  -1048   1026       C  
ATOM    638  CZ  PHE A 112      58.241  24.314  -4.614  1.00 80.81           C  
ANISOU  638  CZ  PHE A 112     4004  12857  13844   1339  -1085   1156       C  
ATOM    639  N   GLY A 113      61.972  30.131  -1.833  1.00 88.42           N  
ANISOU  639  N   GLY A 113     4844  12954  15799   1360   -632   1290       N  
ATOM    640  CA  GLY A 113      62.296  31.474  -1.416  1.00 87.41           C  
ANISOU  640  CA  GLY A 113     4662  12632  15919   1396   -554   1307       C  
ATOM    641  C   GLY A 113      61.677  31.847  -0.085  1.00 88.29           C  
ANISOU  641  C   GLY A 113     4732  12742  16072   1373   -556   1136       C  
ATOM    642  O   GLY A 113      60.761  31.184   0.412  1.00 96.97           O  
ANISOU  642  O   GLY A 113     5833  14001  17010   1355   -613   1032       O  
ATOM    643  N   PRO A 114      62.175  32.929   0.523  1.00 87.25           N  
ANISOU  643  N   PRO A 114     4558  12426  16168   1376   -491   1103       N  
ATOM    644  CA  PRO A 114      61.637  33.331   1.834  1.00 98.97           C  
ANISOU  644  CA  PRO A 114     5999  13904  17699   1361   -491    934       C  
ATOM    645  C   PRO A 114      60.211  33.845   1.766  1.00105.32           C  
ANISOU  645  C   PRO A 114     6746  14758  18511   1474   -505    949       C  
ATOM    646  O   PRO A 114      59.429  33.608   2.697  1.00116.70           O  
ANISOU  646  O   PRO A 114     8169  16304  19867   1460   -533    815       O  
ATOM    647  CB  PRO A 114      62.615  34.425   2.293  1.00106.47           C  
ANISOU  647  CB  PRO A 114     6915  14619  18921   1345   -418    906       C  
ATOM    648  CG  PRO A 114      63.843  34.241   1.443  1.00105.86           C  
ANISOU  648  CG  PRO A 114     6877  14459  18886   1306   -386   1029       C  
ATOM    649  CD  PRO A 114      63.340  33.735   0.129  1.00 96.76           C  
ANISOU  649  CD  PRO A 114     5751  13420  17594   1377   -413   1200       C  
ATOM    650  N   VAL A 115      59.849  34.549   0.690  1.00102.47           N  
ANISOU  650  N   VAL A 115     6356  14329  18248   1594   -481   1116       N  
ATOM    651  CA  VAL A 115      58.502  35.104   0.579  1.00104.84           C  
ANISOU  651  CA  VAL A 115     6599  14672  18563   1713   -494   1137       C  
ATOM    652  C   VAL A 115      57.465  33.988   0.559  1.00103.97           C  
ANISOU  652  C   VAL A 115     6506  14806  18193   1700   -580   1082       C  
ATOM    653  O   VAL A 115      56.417  34.080   1.211  1.00105.73           O  
ANISOU  653  O   VAL A 115     6685  15109  18380   1730   -599    990       O  
ATOM    654  CB  VAL A 115      58.394  36.002  -0.667  1.00 96.68           C  
ANISOU  654  CB  VAL A 115     5540  13526  17667   1851   -451   1348       C  
ATOM    655  CG1 VAL A 115      57.006  36.616  -0.763  1.00 91.94           C  
ANISOU  655  CG1 VAL A 115     4881  12968  17085   1982   -465   1369       C  
ATOM    656  CG2 VAL A 115      59.459  37.087  -0.633  1.00 94.10           C  
ANISOU  656  CG2 VAL A 115     5193  12941  17619   1855   -354   1404       C  
ATOM    657  N   MET A 116      57.743  32.911  -0.179  1.00 97.27           N  
ANISOU  657  N   MET A 116     5716  14075  17169   1655   -630   1134       N  
ATOM    658  CA  MET A 116      56.814  31.787  -0.217  1.00 94.06           C  
ANISOU  658  CA  MET A 116     5322  13884  16531   1631   -712   1069       C  
ATOM    659  C   MET A 116      56.778  31.045   1.114  1.00 95.17           C  
ANISOU  659  C   MET A 116     5479  14117  16566   1513   -725    883       C  
ATOM    660  O   MET A 116      55.734  30.501   1.491  1.00 94.12           O  
ANISOU  660  O   MET A 116     5324  14132  16306   1511   -767    803       O  
ATOM    661  CB  MET A 116      57.189  30.835  -1.352  1.00 97.86           C  
ANISOU  661  CB  MET A 116     5863  14449  16870   1613   -761   1163       C  
ATOM    662  CG  MET A 116      57.406  31.525  -2.691  1.00105.40           C  
ANISOU  662  CG  MET A 116     6811  15319  17917   1733   -739   1369       C  
ATOM    663  SD  MET A 116      55.986  32.497  -3.228  1.00110.41           S  
ANISOU  663  SD  MET A 116     7368  15966  18616   1910   -751   1456       S  
ATOM    664  CE  MET A 116      56.619  33.220  -4.740  1.00107.52           C  
ANISOU  664  CE  MET A 116     7015  15488  18351   2038   -704   1718       C  
ATOM    665  N   CYS A 117      57.901  31.010   1.834  1.00 84.53           N  
ANISOU  665  N   CYS A 117     4166  12685  15268   1419   -686    819       N  
ATOM    666  CA  CYS A 117      57.916  30.410   3.166  1.00 83.61           C  
ANISOU  666  CA  CYS A 117     4062  12649  15056   1323   -690    655       C  
ATOM    667  C   CYS A 117      57.012  31.185   4.118  1.00 84.59           C  
ANISOU  667  C   CYS A 117     4113  12765  15261   1379   -666    572       C  
ATOM    668  O   CYS A 117      56.216  30.595   4.859  1.00 84.23           O  
ANISOU  668  O   CYS A 117     4053  12865  15085   1354   -688    479       O  
ATOM    669  CB  CYS A 117      59.357  30.352   3.683  1.00 95.45           C  
ANISOU  669  CB  CYS A 117     5608  14047  16611   1227   -656    611       C  
ATOM    670  SG  CYS A 117      59.603  29.853   5.413  1.00 90.10           S  
ANISOU  670  SG  CYS A 117     4943  13437  15853   1125   -650    423       S  
ATOM    671  N   LYS A 118      57.109  32.518   4.093  1.00 85.93           N  
ANISOU  671  N   LYS A 118     4233  12760  15656   1459   -616    608       N  
ATOM    672  CA  LYS A 118      56.232  33.355   4.907  1.00 87.05           C  
ANISOU  672  CA  LYS A 118     4302  12878  15897   1529   -591    533       C  
ATOM    673  C   LYS A 118      54.770  33.162   4.519  1.00 87.56           C  
ANISOU  673  C   LYS A 118     4324  13088  15855   1610   -629    566       C  
ATOM    674  O   LYS A 118      53.929  32.809   5.356  1.00 88.67           O  
ANISOU  674  O   LYS A 118     4436  13356  15900   1601   -641    469       O  
ATOM    675  CB  LYS A 118      56.627  34.826   4.756  1.00 90.15           C  
ANISOU  675  CB  LYS A 118     4650  13036  16569   1608   -529    579       C  
ATOM    676  CG  LYS A 118      57.887  35.237   5.495  1.00 89.98           C  
ANISOU  676  CG  LYS A 118     4640  12852  16694   1534   -487    492       C  
ATOM    677  CD  LYS A 118      57.549  36.090   6.710  1.00 89.67           C  
ANISOU  677  CD  LYS A 118     4540  12736  16795   1566   -454    346       C  
ATOM    678  CE  LYS A 118      58.804  36.637   7.372  1.00 89.65           C  
ANISOU  678  CE  LYS A 118     4539  12551  16975   1504   -419    248       C  
ATOM    679  NZ  LYS A 118      58.486  37.403   8.609  1.00 91.11           N  
ANISOU  679  NZ  LYS A 118     4663  12668  17286   1536   -396     79       N  
ATOM    680  N   VAL A 119      54.454  33.388   3.241  1.00 88.20           N  
ANISOU  680  N   VAL A 119     4398  13157  15955   1695   -649    707       N  
ATOM    681  CA  VAL A 119      53.061  33.416   2.800  1.00 94.66           C  
ANISOU  681  CA  VAL A 119     5165  14091  16710   1792   -688    741       C  
ATOM    682  C   VAL A 119      52.406  32.053   2.977  1.00 87.93           C  
ANISOU  682  C   VAL A 119     4331  13459  15621   1720   -752    665       C  
ATOM    683  O   VAL A 119      51.272  31.953   3.459  1.00 94.41           O  
ANISOU  683  O   VAL A 119     5097  14392  16384   1750   -767    601       O  
ATOM    684  CB  VAL A 119      52.977  33.900   1.340  1.00 98.59           C  
ANISOU  684  CB  VAL A 119     5659  14531  17268   1902   -700    917       C  
ATOM    685  CG1 VAL A 119      51.558  33.753   0.809  1.00 90.75           C  
ANISOU  685  CG1 VAL A 119     4618  13682  16181   1996   -759    944       C  
ATOM    686  CG2 VAL A 119      53.442  35.344   1.234  1.00 94.49           C  
ANISOU  686  CG2 VAL A 119     5110  13785  17006   1987   -622    997       C  
ATOM    687  N   PHE A 120      53.102  30.983   2.594  1.00 86.61           N  
ANISOU  687  N   PHE A 120     4234  13350  15322   1624   -787    671       N  
ATOM    688  CA  PHE A 120      52.485  29.663   2.642  1.00 85.70           C  
ANISOU  688  CA  PHE A 120     4136  13426  15002   1557   -847    603       C  
ATOM    689  C   PHE A 120      52.535  29.048   4.036  1.00 84.81           C  
ANISOU  689  C   PHE A 120     4032  13390  14804   1455   -822    468       C  
ATOM    690  O   PHE A 120      51.647  28.264   4.390  1.00 97.58           O  
ANISOU  690  O   PHE A 120     5625  15158  16292   1427   -850    401       O  
ATOM    691  CB  PHE A 120      53.143  28.738   1.618  1.00 84.78           C  
ANISOU  691  CB  PHE A 120     4090  13337  14784   1505   -896    662       C  
ATOM    692  CG  PHE A 120      52.789  29.071   0.196  1.00 90.13           C  
ANISOU  692  CG  PHE A 120     4754  14001  15490   1615   -939    797       C  
ATOM    693  CD1 PHE A 120      51.523  28.798  -0.296  1.00 94.43           C  
ANISOU  693  CD1 PHE A 120     5250  14666  15963   1678  -1004    791       C  
ATOM    694  CD2 PHE A 120      53.716  29.661  -0.647  1.00 90.62           C  
ANISOU  694  CD2 PHE A 120     4846  13933  15653   1659   -912    935       C  
ATOM    695  CE1 PHE A 120      51.188  29.105  -1.602  1.00 89.60           C  
ANISOU  695  CE1 PHE A 120     4624  14053  15367   1789  -1050    919       C  
ATOM    696  CE2 PHE A 120      53.388  29.970  -1.954  1.00 94.59           C  
ANISOU  696  CE2 PHE A 120     5336  14436  16169   1773   -947   1077       C  
ATOM    697  CZ  PHE A 120      52.123  29.692  -2.432  1.00 91.02           C  
ANISOU  697  CZ  PHE A 120     4839  14112  15631   1841  -1020   1068       C  
ATOM    698  N   GLY A 121      53.544  29.383   4.837  1.00 84.41           N  
ANISOU  698  N   GLY A 121     4008  13237  14827   1403   -770    429       N  
ATOM    699  CA  GLY A 121      53.563  28.918   6.210  1.00 83.80           C  
ANISOU  699  CA  GLY A 121     3932  13232  14676   1328   -744    315       C  
ATOM    700  C   GLY A 121      52.479  29.577   7.038  1.00 84.91           C  
ANISOU  700  C   GLY A 121     3988  13404  14870   1400   -714    265       C  
ATOM    701  O   GLY A 121      51.640  28.902   7.650  1.00 92.57           O  
ANISOU  701  O   GLY A 121     4930  14525  15716   1377   -719    214       O  
ATOM    702  N   SER A 122      52.485  30.913   7.047  1.00 86.14           N  
ANISOU  702  N   SER A 122     4099  13410  15221   1492   -678    284       N  
ATOM    703  CA  SER A 122      51.471  31.655   7.787  1.00 93.90           C  
ANISOU  703  CA  SER A 122     4998  14403  16275   1576   -646    235       C  
ATOM    704  C   SER A 122      50.080  31.429   7.210  1.00 90.35           C  
ANISOU  704  C   SER A 122     4495  14088  15745   1645   -683    275       C  
ATOM    705  O   SER A 122      49.084  31.526   7.934  1.00 88.64           O  
ANISOU  705  O   SER A 122     4214  13957  15509   1683   -664    225       O  
ATOM    706  CB  SER A 122      51.814  33.143   7.786  1.00 95.74           C  
ANISOU  706  CB  SER A 122     5198  14426  16754   1664   -600    246       C  
ATOM    707  OG  SER A 122      53.191  33.338   8.051  1.00 90.84           O  
ANISOU  707  OG  SER A 122     4627  13665  16223   1597   -577    215       O  
ATOM    708  N   PHE A 123      49.993  31.131   5.912  1.00 87.90           N  
ANISOU  708  N   PHE A 123     4206  13799  15394   1665   -737    363       N  
ATOM    709  CA  PHE A 123      48.702  30.824   5.306  1.00 88.52           C  
ANISOU  709  CA  PHE A 123     4233  14010  15393   1724   -787    385       C  
ATOM    710  C   PHE A 123      48.215  29.445   5.733  1.00 87.57           C  
ANISOU  710  C   PHE A 123     4119  14075  15080   1627   -817    309       C  
ATOM    711  O   PHE A 123      47.017  29.247   5.971  1.00 88.21           O  
ANISOU  711  O   PHE A 123     4131  14276  15108   1659   -829    274       O  
ATOM    712  CB  PHE A 123      48.811  30.921   3.783  1.00 88.83           C  
ANISOU  712  CB  PHE A 123     4293  14007  15452   1782   -842    498       C  
ATOM    713  CG  PHE A 123      47.493  30.826   3.069  1.00 94.18           C  
ANISOU  713  CG  PHE A 123     4907  14794  16082   1867   -902    522       C  
ATOM    714  CD1 PHE A 123      46.535  31.815   3.218  1.00103.79           C  
ANISOU  714  CD1 PHE A 123     6041  15996  17398   1989   -881    535       C  
ATOM    715  CD2 PHE A 123      47.221  29.756   2.234  1.00 96.85           C  
ANISOU  715  CD2 PHE A 123     5268  15243  16288   1828   -982    523       C  
ATOM    716  CE1 PHE A 123      45.323  31.731   2.557  1.00105.72           C  
ANISOU  716  CE1 PHE A 123     6223  16343  17602   2070   -942    551       C  
ATOM    717  CE2 PHE A 123      46.012  29.667   1.568  1.00 99.05           C  
ANISOU  717  CE2 PHE A 123     5483  15616  16537   1906  -1048    531       C  
ATOM    718  CZ  PHE A 123      45.062  30.655   1.731  1.00101.97           C  
ANISOU  718  CZ  PHE A 123     5768  15979  16998   2027  -1028    546       C  
ATOM    719  N   LEU A 124      49.133  28.482   5.840  1.00 86.14           N  
ANISOU  719  N   LEU A 124     4016  13913  14798   1508   -826    285       N  
ATOM    720  CA  LEU A 124      48.780  27.166   6.362  1.00 87.58           C  
ANISOU  720  CA  LEU A 124     4209  14253  14814   1410   -841    213       C  
ATOM    721  C   LEU A 124      48.266  27.270   7.793  1.00 89.03           C  
ANISOU  721  C   LEU A 124     4339  14503  14985   1403   -778    157       C  
ATOM    722  O   LEU A 124      47.190  26.753   8.124  1.00 89.04           O  
ANISOU  722  O   LEU A 124     4283  14641  14909   1402   -781    125       O  
ATOM    723  CB  LEU A 124      49.994  26.239   6.289  1.00 85.49           C  
ANISOU  723  CB  LEU A 124     4043  13973  14466   1293   -851    202       C  
ATOM    724  CG  LEU A 124      49.772  24.738   6.484  1.00 82.76           C  
ANISOU  724  CG  LEU A 124     3724  13763  13957   1188   -877    137       C  
ATOM    725  CD1 LEU A 124      49.417  24.075   5.164  1.00 89.88           C  
ANISOU  725  CD1 LEU A 124     4640  14688  14822   1190   -960    144       C  
ATOM    726  CD2 LEU A 124      51.002  24.094   7.095  1.00 81.43           C  
ANISOU  726  CD2 LEU A 124     3638  13576  13724   1082   -849    115       C  
ATOM    727  N   THR A 125      49.027  27.949   8.659  1.00 85.55           N  
ANISOU  727  N   THR A 125     3913  13959  14632   1403   -720    145       N  
ATOM    728  CA  THR A 125      48.587  28.138  10.039  1.00 86.00           C  
ANISOU  728  CA  THR A 125     3918  14059  14698   1412   -660     98       C  
ATOM    729  C   THR A 125      47.260  28.887  10.096  1.00 87.51           C  
ANISOU  729  C   THR A 125     4009  14284  14956   1526   -646    101       C  
ATOM    730  O   THR A 125      46.387  28.564  10.913  1.00 87.90           O  
ANISOU  730  O   THR A 125     3999  14448  14949   1529   -614     82       O  
ATOM    731  CB  THR A 125      49.662  28.883  10.832  1.00 85.95           C  
ANISOU  731  CB  THR A 125     3941  13904  14813   1408   -613     59       C  
ATOM    732  OG1 THR A 125      50.862  28.099  10.864  1.00 97.13           O  
ANISOU  732  OG1 THR A 125     5445  15307  16152   1299   -626     53       O  
ATOM    733  CG2 THR A 125      49.198  29.147  12.258  1.00 86.60           C  
ANISOU  733  CG2 THR A 125     3967  14014  14923   1434   -554     -3       C  
ATOM    734  N   LEU A 126      47.085  29.881   9.221  1.00 89.68           N  
ANISOU  734  N   LEU A 126     4260  14458  15357   1626   -665    140       N  
ATOM    735  CA  LEU A 126      45.846  30.651   9.202  1.00 94.87           C  
ANISOU  735  CA  LEU A 126     4822  15139  16084   1746   -654    147       C  
ATOM    736  C   LEU A 126      44.653  29.773   8.846  1.00 96.55           C  
ANISOU  736  C   LEU A 126     4986  15536  16164   1738   -698    147       C  
ATOM    737  O   LEU A 126      43.589  29.876   9.469  1.00 99.08           O  
ANISOU  737  O   LEU A 126     5223  15947  16475   1784   -668    126       O  
ATOM    738  CB  LEU A 126      45.971  31.815   8.218  1.00 96.75           C  
ANISOU  738  CB  LEU A 126     5053  15227  16483   1855   -670    208       C  
ATOM    739  CG  LEU A 126      44.746  32.715   8.057  1.00 95.74           C  
ANISOU  739  CG  LEU A 126     4829  15105  16442   1995   -662    226       C  
ATOM    740  CD1 LEU A 126      44.331  33.289   9.399  1.00 95.16           C  
ANISOU  740  CD1 LEU A 126     4697  15023  16435   2035   -588    155       C  
ATOM    741  CD2 LEU A 126      45.027  33.827   7.060  1.00 93.59           C  
ANISOU  741  CD2 LEU A 126     4560  14668  16332   2100   -671    309       C  
ATOM    742  N   ASN A 127      44.809  28.902   7.846  1.00 96.09           N  
ANISOU  742  N   ASN A 127     4973  15527  16012   1681   -769    162       N  
ATOM    743  CA  ASN A 127      43.725  27.989   7.498  1.00 89.55           C  
ANISOU  743  CA  ASN A 127     4095  14855  15074   1661   -819    129       C  
ATOM    744  C   ASN A 127      43.457  26.987   8.613  1.00 88.96           C  
ANISOU  744  C   ASN A 127     4046  14874  14880   1552   -773     84       C  
ATOM    745  O   ASN A 127      42.301  26.604   8.833  1.00109.60           O  
ANISOU  745  O   ASN A 127     6615  17580  17449   1553   -771     59       O  
ATOM    746  CB  ASN A 127      44.044  27.261   6.193  1.00 89.22           C  
ANISOU  746  CB  ASN A 127     4110  14807  14982   1620   -908    138       C  
ATOM    747  CG  ASN A 127      44.070  28.194   5.000  1.00103.53           C  
ANISOU  747  CG  ASN A 127     5919  16516  16904   1733   -952    218       C  
ATOM    748  OD1 ASN A 127      43.280  29.134   4.913  1.00 91.16           O  
ANISOU  748  OD1 ASN A 127     4277  14934  15424   1852   -944    246       O  
ATOM    749  ND2 ASN A 127      44.985  27.940   4.073  1.00115.44           N  
ANISOU  749  ND2 ASN A 127     7506  17949  18406   1704   -995    268       N  
ATOM    750  N   MET A 128      44.500  26.555   9.325  1.00 87.79           N  
ANISOU  750  N   MET A 128     3969  14698  14687   1462   -733     81       N  
ATOM    751  CA  MET A 128      44.294  25.665  10.465  1.00 87.35           C  
ANISOU  751  CA  MET A 128     3938  14720  14531   1372   -680     68       C  
ATOM    752  C   MET A 128      43.452  26.338  11.543  1.00 97.64           C  
ANISOU  752  C   MET A 128     5148  16055  15897   1448   -606     85       C  
ATOM    753  O   MET A 128      42.416  25.806  11.966  1.00 89.09           O  
ANISOU  753  O   MET A 128     4027  15067  14756   1432   -583     89       O  
ATOM    754  CB  MET A 128      45.640  25.225  11.039  1.00 86.02           C  
ANISOU  754  CB  MET A 128     3856  14502  14324   1282   -653     74       C  
ATOM    755  CG  MET A 128      45.522  24.511  12.373  1.00 85.75           C  
ANISOU  755  CG  MET A 128     3835  14524  14223   1214   -585     96       C  
ATOM    756  SD  MET A 128      47.065  24.519  13.301  1.00 90.84           S  
ANISOU  756  SD  MET A 128     4540  15079  14895   1160   -545    105       S  
ATOM    757  CE  MET A 128      46.549  23.735  14.827  1.00 84.88           C  
ANISOU  757  CE  MET A 128     3767  14369  14113   1114   -465    160       C  
ATOM    758  N   PHE A 129      43.886  27.517  12.002  1.00 98.40           N  
ANISOU  758  N   PHE A 129     5198  16064  16126   1533   -567     86       N  
ATOM    759  CA  PHE A 129      43.168  28.210  13.068  1.00100.79           C  
ANISOU  759  CA  PHE A 129     5408  16377  16512   1616   -495     81       C  
ATOM    760  C   PHE A 129      41.754  28.580  12.639  1.00 91.65           C  
ANISOU  760  C   PHE A 129     4164  15286  15371   1706   -507     90       C  
ATOM    761  O   PHE A 129      40.813  28.493  13.438  1.00 92.48           O  
ANISOU  761  O   PHE A 129     4208  15457  15471   1728   -453    100       O  
ATOM    762  CB  PHE A 129      43.943  29.454  13.500  1.00 90.68           C  
ANISOU  762  CB  PHE A 129     4129  14934  15390   1688   -461     36       C  
ATOM    763  CG  PHE A 129      45.055  29.167  14.466  1.00 89.78           C  
ANISOU  763  CG  PHE A 129     4080  14757  15276   1613   -426     -5       C  
ATOM    764  CD1 PHE A 129      44.950  28.123  15.370  1.00 89.24           C  
ANISOU  764  CD1 PHE A 129     4011  14785  15109   1537   -390     17       C  
ATOM    765  CD2 PHE A 129      46.205  29.937  14.469  1.00 98.61           C  
ANISOU  765  CD2 PHE A 129     5255  15709  16505   1622   -429    -63       C  
ATOM    766  CE1 PHE A 129      45.970  27.855  16.262  1.00 88.51           C  
ANISOU  766  CE1 PHE A 129     3977  14631  15021   1478   -363    -29       C  
ATOM    767  CE2 PHE A 129      47.229  29.674  15.359  1.00 97.86           C  
ANISOU  767  CE2 PHE A 129     5213  15561  16407   1557   -406   -122       C  
ATOM    768  CZ  PHE A 129      47.111  28.631  16.257  1.00 94.77           C  
ANISOU  768  CZ  PHE A 129     4825  15276  15907   1489   -376   -110       C  
ATOM    769  N   ALA A 130      41.583  28.999  11.383  1.00 92.00           N  
ANISOU  769  N   ALA A 130     4198  15309  15449   1764   -576     91       N  
ATOM    770  CA  ALA A 130      40.243  29.289  10.884  1.00 93.35           C  
ANISOU  770  CA  ALA A 130     4288  15545  15635   1849   -602     92       C  
ATOM    771  C   ALA A 130      39.374  28.038  10.894  1.00 93.22           C  
ANISOU  771  C   ALA A 130     4280  15656  15484   1759   -620     76       C  
ATOM    772  O   ALA A 130      38.183  28.100  11.225  1.00115.20           O  
ANISOU  772  O   ALA A 130     6983  18519  18269   1804   -596     73       O  
ATOM    773  CB  ALA A 130      40.321  29.881   9.477  1.00 93.73           C  
ANISOU  773  CB  ALA A 130     4327  15534  15751   1929   -681    108       C  
ATOM    774  N   SER A 131      39.958  26.889  10.544  1.00 91.90           N  
ANISOU  774  N   SER A 131     4204  15504  15210   1632   -660     56       N  
ATOM    775  CA  SER A 131      39.202  25.641  10.542  1.00 91.81           C  
ANISOU  775  CA  SER A 131     4197  15594  15092   1541   -679     12       C  
ATOM    776  C   SER A 131      38.749  25.269  11.949  1.00 92.07           C  
ANISOU  776  C   SER A 131     4198  15701  15085   1506   -581     52       C  
ATOM    777  O   SER A 131      37.563  25.000  12.182  1.00 93.09           O  
ANISOU  777  O   SER A 131     4251  15919  15199   1518   -564     38       O  
ATOM    778  CB  SER A 131      40.047  24.523   9.933  1.00 90.34           C  
ANISOU  778  CB  SER A 131     4119  15380  14827   1419   -736    -32       C  
ATOM    779  OG  SER A 131      39.336  23.298   9.912  1.00 90.34           O  
ANISOU  779  OG  SER A 131     4116  15444  14764   1330   -757   -110       O  
ATOM    780  N   ILE A 132      39.682  25.253  12.905  1.00 91.27           N  
ANISOU  780  N   ILE A 132     4145  15548  14986   1467   -514    111       N  
ATOM    781  CA  ILE A 132      39.334  24.857  14.268  1.00 91.55           C  
ANISOU  781  CA  ILE A 132     4148  15611  15024   1437   -417    190       C  
ATOM    782  C   ILE A 132      38.332  25.834  14.872  1.00 93.18           C  
ANISOU  782  C   ILE A 132     4236  15825  15342   1561   -357    210       C  
ATOM    783  O   ILE A 132      37.342  25.427  15.497  1.00100.84           O  
ANISOU  783  O   ILE A 132     5142  16856  16318   1555   -301    264       O  
ATOM    784  CB  ILE A 132      40.603  24.742  15.133  1.00 90.47           C  
ANISOU  784  CB  ILE A 132     4080  15373  14923   1386   -370    229       C  
ATOM    785  CG1 ILE A 132      41.595  23.770  14.495  1.00 92.83           C  
ANISOU  785  CG1 ILE A 132     4497  15670  15105   1269   -429    213       C  
ATOM    786  CG2 ILE A 132      40.247  24.290  16.540  1.00 90.86           C  
ANISOU  786  CG2 ILE A 132     4088  15388  15046   1362   -271    307       C  
ATOM    787  CD1 ILE A 132      42.871  23.596  15.287  1.00 96.27           C  
ANISOU  787  CD1 ILE A 132     5000  16005  15573   1215   -393    243       C  
ATOM    788  N   PHE A 133      38.566  27.136  14.688  1.00 93.74           N  
ANISOU  788  N   PHE A 133     4273  15825  15520   1677   -363    169       N  
ATOM    789  CA  PHE A 133      37.653  28.135  15.236  1.00109.99           C  
ANISOU  789  CA  PHE A 133     6219  17885  17687   1807   -306    166       C  
ATOM    790  C   PHE A 133      36.264  28.013  14.621  1.00106.29           C  
ANISOU  790  C   PHE A 133     5677  17528  17179   1844   -338    168       C  
ATOM    791  O   PHE A 133      35.253  28.196  15.311  1.00 99.31           O  
ANISOU  791  O   PHE A 133     4704  16691  16337   1900   -273    196       O  
ATOM    792  CB  PHE A 133      38.218  29.539  15.017  1.00105.78           C  
ANISOU  792  CB  PHE A 133     5664  17246  17283   1927   -314    113       C  
ATOM    793  CG  PHE A 133      39.437  29.840  15.844  1.00 95.09           C  
ANISOU  793  CG  PHE A 133     4346  15790  15996   1914   -272     75       C  
ATOM    794  CD1 PHE A 133      39.741  29.079  16.961  1.00 94.54           C  
ANISOU  794  CD1 PHE A 133     4300  15725  15895   1837   -212     82       C  
ATOM    795  CD2 PHE A 133      40.277  30.887  15.505  1.00 95.12           C  
ANISOU  795  CD2 PHE A 133     4374  15661  16106   1977   -293     18       C  
ATOM    796  CE1 PHE A 133      40.860  29.355  17.722  1.00 94.01           C  
ANISOU  796  CE1 PHE A 133     4266  15569  15886   1831   -184     13       C  
ATOM    797  CE2 PHE A 133      41.397  31.169  16.262  1.00 94.60           C  
ANISOU  797  CE2 PHE A 133     4372  15470  16102   1952   -262    -54       C  
ATOM    798  CZ  PHE A 133      41.689  30.402  17.372  1.00 95.51           C  
ANISOU  798  CZ  PHE A 133     4504  15620  16166   1881   -213    -69       C  
ATOM    799  N   PHE A 134      36.191  27.700  13.325  1.00106.00           N  
ANISOU  799  N   PHE A 134     5672  17525  17079   1819   -440    121       N  
ATOM    800  CA  PHE A 134      34.889  27.514  12.692  1.00 99.45           C  
ANISOU  800  CA  PHE A 134     4767  16793  16226   1850   -487     80       C  
ATOM    801  C   PHE A 134      34.190  26.268  13.217  1.00 97.37           C  
ANISOU  801  C   PHE A 134     4486  16642  15869   1747   -458     76       C  
ATOM    802  O   PHE A 134      32.964  26.262  13.377  1.00 98.71           O  
ANISOU  802  O   PHE A 134     4558  16897  16050   1787   -441     57       O  
ATOM    803  CB  PHE A 134      35.043  27.450  11.174  1.00 97.06           C  
ANISOU  803  CB  PHE A 134     4498  16458  15922   1851   -611     14       C  
ATOM    804  CG  PHE A 134      34.915  28.782  10.500  1.00 98.05           C  
ANISOU  804  CG  PHE A 134     4574  16516  16165   2001   -644     28       C  
ATOM    805  CD1 PHE A 134      34.011  29.722  10.968  1.00 99.63           C  
ANISOU  805  CD1 PHE A 134     4670  16738  16445   2128   -593     46       C  
ATOM    806  CD2 PHE A 134      35.701  29.101   9.408  1.00103.46           C  
ANISOU  806  CD2 PHE A 134     5312  17109  16889   2024   -720     32       C  
ATOM    807  CE1 PHE A 134      33.889  30.953  10.355  1.00100.63           C  
ANISOU  807  CE1 PHE A 134     4750  16796  16690   2274   -620     59       C  
ATOM    808  CE2 PHE A 134      35.586  30.330   8.792  1.00113.94           C  
ANISOU  808  CE2 PHE A 134     6589  18369  18335   2170   -744     62       C  
ATOM    809  CZ  PHE A 134      34.677  31.258   9.265  1.00117.71           C  
ANISOU  809  CZ  PHE A 134     6965  18866  18892   2296   -695     72       C  
ATOM    810  N   ILE A 135      34.947  25.202  13.490  1.00102.24           N  
ANISOU  810  N   ILE A 135     5191  17256  16399   1616   -449     86       N  
ATOM    811  CA  ILE A 135      34.345  24.003  14.069  1.00100.58           C  
ANISOU  811  CA  ILE A 135     4961  17143  16114   1520   -411     76       C  
ATOM    812  C   ILE A 135      33.777  24.306  15.450  1.00106.11           C  
ANISOU  812  C   ILE A 135     5582  17839  16897   1565   -276    262       C  
ATOM    813  O   ILE A 135      32.652  23.903  15.779  1.00112.97           O  
ANISOU  813  O   ILE A 135     6363  18805  17754   1564   -241    264       O  
ATOM    814  CB  ILE A 135      35.372  22.856  14.114  1.00 94.44           C  
ANISOU  814  CB  ILE A 135     4297  16342  15245   1381   -424     51       C  
ATOM    815  CG1 ILE A 135      35.718  22.398  12.696  1.00 93.70           C  
ANISOU  815  CG1 ILE A 135     4264  16183  15154   1331   -556   -144       C  
ATOM    816  CG2 ILE A 135      34.842  21.692  14.939  1.00 94.63           C  
ANISOU  816  CG2 ILE A 135     4295  16450  15210   1294   -364     16       C  
ATOM    817  CD1 ILE A 135      36.724  21.274  12.647  1.00 94.49           C  
ANISOU  817  CD1 ILE A 135     4476  16220  15205   1201   -577   -223       C  
ATOM    818  N   THR A 136      34.539  25.027  16.276  1.00 96.81           N  
ANISOU  818  N   THR A 136     4424  16510  15851   1609   -205    359       N  
ATOM    819  CA  THR A 136      34.042  25.414  17.593  1.00 97.88           C  
ANISOU  819  CA  THR A 136     4476  16550  16163   1668    -83    437       C  
ATOM    820  C   THR A 136      32.786  26.270  17.476  1.00115.96           C  
ANISOU  820  C   THR A 136     6648  18930  18482   1796    -70    410       C  
ATOM    821  O   THR A 136      31.799  26.052  18.191  1.00126.62           O  
ANISOU  821  O   THR A 136     7909  20273  19929   1808     11    483       O  
ATOM    822  CB  THR A 136      35.131  26.158  18.366  1.00 97.39           C  
ANISOU  822  CB  THR A 136     4448  16364  16191   1717    -40    374       C  
ATOM    823  OG1 THR A 136      36.234  25.277  18.606  1.00113.75           O  
ANISOU  823  OG1 THR A 136     6620  18356  18243   1598    -46    389       O  
ATOM    824  CG2 THR A 136      34.593  26.663  19.695  1.00 98.67           C  
ANISOU  824  CG2 THR A 136     4516  16475  16501   1807     77    346       C  
ATOM    825  N   CYS A 137      32.802  27.249  16.566  1.00104.75           N  
ANISOU  825  N   CYS A 137     5221  17550  17028   1893   -146    311       N  
ATOM    826  CA  CYS A 137      31.632  28.099  16.377  1.00115.67           C  
ANISOU  826  CA  CYS A 137     6494  18998  18458   2023   -142    279       C  
ATOM    827  C   CYS A 137      30.422  27.294  15.919  1.00116.43           C  
ANISOU  827  C   CYS A 137     6527  19252  18461   1981   -180    250       C  
ATOM    828  O   CYS A 137      29.287  27.609  16.297  1.00114.90           O  
ANISOU  828  O   CYS A 137     6224  19122  18312   2056   -131    266       O  
ATOM    829  CB  CYS A 137      31.947  29.210  15.376  1.00128.81           C  
ANISOU  829  CB  CYS A 137     8167  20619  20156   2127   -224    195       C  
ATOM    830  SG  CYS A 137      30.692  30.506  15.285  1.00151.25           S  
ANISOU  830  SG  CYS A 137    10876  23490  23103   2315   -207    169       S  
ATOM    831  N   MET A 138      30.641  26.251  15.113  1.00115.56           N  
ANISOU  831  N   MET A 138     6475  19201  18230   1864   -273    152       N  
ATOM    832  CA  MET A 138      29.535  25.385  14.718  1.00112.27           C  
ANISOU  832  CA  MET A 138     5990  18902  17767   1812   -326    -16       C  
ATOM    833  C   MET A 138      29.020  24.576  15.901  1.00106.27           C  
ANISOU  833  C   MET A 138     5182  18226  16970   1753   -220     19       C  
ATOM    834  O   MET A 138      27.816  24.309  15.999  1.00114.44           O  
ANISOU  834  O   MET A 138     6107  19319  18055   1762   -229   -199       O  
ATOM    835  CB  MET A 138      29.962  24.458  13.583  1.00118.02           C  
ANISOU  835  CB  MET A 138     6791  19573  18480   1699   -454   -194       C  
ATOM    836  CG  MET A 138      30.223  25.166  12.269  1.00127.80           C  
ANISOU  836  CG  MET A 138     8053  20736  19769   1766   -564   -203       C  
ATOM    837  SD  MET A 138      29.993  24.072  10.858  1.00132.76           S  
ANISOU  837  SD  MET A 138     8697  21296  20451   1666   -712   -351       S  
ATOM    838  CE  MET A 138      28.262  23.654  11.058  1.00137.62           C  
ANISOU  838  CE  MET A 138     9153  21978  21159   1666   -709   -445       C  
ATOM    839  N   SER A 139      29.915  24.167  16.804  1.00106.17           N  
ANISOU  839  N   SER A 139     5242  18117  16983   1684   -117    314       N  
ATOM    840  CA  SER A 139      29.467  23.495  18.020  1.00102.26           C  
ANISOU  840  CA  SER A 139     4689  17280  16884   1600     38    711       C  
ATOM    841  C   SER A 139      28.614  24.423  18.875  1.00103.94           C  
ANISOU  841  C   SER A 139     4784  17314  17394   1711    142    732       C  
ATOM    842  O   SER A 139      27.616  23.994  19.469  1.00112.44           O  
ANISOU  842  O   SER A 139     5753  17947  19020   1644    204    632       O  
ATOM    843  CB  SER A 139      30.669  22.983  18.814  1.00100.85           C  
ANISOU  843  CB  SER A 139     4598  16563  17156   1479     84    685       C  
ATOM    844  OG  SER A 139      31.368  21.984  18.093  1.00 99.41           O  
ANISOU  844  OG  SER A 139     4514  16194  17063   1332     -4    663       O  
ATOM    845  N   VAL A 140      28.983  25.705  18.940  1.00104.11           N  
ANISOU  845  N   VAL A 140     4814  17470  17273   1858    138    627       N  
ATOM    846  CA  VAL A 140      28.181  26.669  19.688  1.00112.63           C  
ANISOU  846  CA  VAL A 140     5784  18517  18492   1994    229    606       C  
ATOM    847  C   VAL A 140      26.824  26.870  19.023  1.00120.58           C  
ANISOU  847  C   VAL A 140     6688  19763  19364   2064    188    603       C  
ATOM    848  O   VAL A 140      25.785  26.904  19.697  1.00114.37           O  
ANISOU  848  O   VAL A 140     5790  18884  18781   2094    285    684       O  
ATOM    849  CB  VAL A 140      28.945  27.998  19.833  1.00105.66           C  
ANISOU  849  CB  VAL A 140     4933  17639  17574   2127    226    488       C  
ATOM    850  CG1 VAL A 140      28.094  29.024  20.567  1.00107.51           C  
ANISOU  850  CG1 VAL A 140     5054  17870  17923   2282    318    453       C  
ATOM    851  CG2 VAL A 140      30.261  27.775  20.559  1.00104.29           C  
ANISOU  851  CG2 VAL A 140     4848  17333  17445   2072    259    436       C  
ATOM    852  N   ASP A 141      26.807  26.998  17.693  1.00125.25           N  
ANISOU  852  N   ASP A 141     7306  20602  19680   2088     32    380       N  
ATOM    853  CA  ASP A 141      25.549  27.228  16.987  1.00119.46           C  
ANISOU  853  CA  ASP A 141     6467  20046  18877   2159    -53    134       C  
ATOM    854  C   ASP A 141      24.617  26.028  17.104  1.00112.59           C  
ANISOU  854  C   ASP A 141     5521  19268  17990   2056    -93   -227       C  
ATOM    855  O   ASP A 141      23.395  26.193  17.207  1.00112.47           O  
ANISOU  855  O   ASP A 141     5376  19250  18107   2102    -99   -425       O  
ATOM    856  CB  ASP A 141      25.821  27.558  15.520  1.00114.95           C  
ANISOU  856  CB  ASP A 141     5936  19430  18310   2173   -212    -28       C  
ATOM    857  CG  ASP A 141      24.565  27.957  14.769  1.00109.84           C  
ANISOU  857  CG  ASP A 141     5171  18819  17744   2254   -291   -174       C  
ATOM    858  OD1 ASP A 141      24.010  29.035  15.069  1.00111.18           O  
ANISOU  858  OD1 ASP A 141     5268  19006  17969   2400   -240   -107       O  
ATOM    859  OD2 ASP A 141      24.133  27.195  13.879  1.00109.93           O  
ANISOU  859  OD2 ASP A 141     5159  18808  17801   2173   -402   -329       O  
ATOM    860  N   ARG A 142      25.170  24.812  17.087  1.00108.90           N  
ANISOU  860  N   ARG A 142     5121  18680  17577   1891   -138   -470       N  
ATOM    861  CA  ARG A 142      24.339  23.628  17.284  1.00110.49           C  
ANISOU  861  CA  ARG A 142     5232  18566  18184   1739   -151   -785       C  
ATOM    862  C   ARG A 142      23.847  23.533  18.722  1.00113.90           C  
ANISOU  862  C   ARG A 142     5578  18623  19076   1704     -6   -857       C  
ATOM    863  O   ARG A 142      22.704  23.128  18.967  1.00119.64           O  
ANISOU  863  O   ARG A 142     6174  19401  19885   1692     40   -861       O  
ATOM    864  CB  ARG A 142      25.110  22.366  16.898  1.00111.99           C  
ANISOU  864  CB  ARG A 142     5514  18620  18416   1572   -195   -800       C  
ATOM    865  CG  ARG A 142      25.241  22.142  15.401  1.00125.88           C  
ANISOU  865  CG  ARG A 142     7315  20514  20000   1554   -331   -725       C  
ATOM    866  CD  ARG A 142      25.940  20.824  15.109  1.00143.49           C  
ANISOU  866  CD  ARG A 142     9629  22638  22252   1394   -363   -748       C  
ATOM    867  NE  ARG A 142      26.031  20.550  13.678  1.00154.12           N  
ANISOU  867  NE  ARG A 142    11009  24045  23505   1369   -494   -705       N  
ATOM    868  CZ  ARG A 142      26.624  19.479  13.159  1.00153.01           C  
ANISOU  868  CZ  ARG A 142    10944  23850  23342   1247   -544   -712       C  
ATOM    869  NH1 ARG A 142      26.660  19.310  11.845  1.00158.13           N  
ANISOU  869  NH1 ARG A 142    11615  24528  23938   1239   -666   -689       N  
ATOM    870  NH2 ARG A 142      27.182  18.577  13.955  1.00143.98           N  
ANISOU  870  NH2 ARG A 142     9850  22605  22250   1139   -471   -741       N  
ATOM    871  N   TYR A 143      24.697  23.894  19.688  1.00111.00           N  
ANISOU  871  N   TYR A 143     5271  17686  19218   1669    126   -552       N  
ATOM    872  CA  TYR A 143      24.268  23.926  21.083  1.00110.01           C  
ANISOU  872  CA  TYR A 143     5063  17476  19260   1705    331   -247       C  
ATOM    873  C   TYR A 143      23.075  24.856  21.265  1.00112.03           C  
ANISOU  873  C   TYR A 143     5185  17765  19615   1828    371   -274       C  
ATOM    874  O   TYR A 143      22.055  24.476  21.855  1.00114.61           O  
ANISOU  874  O   TYR A 143     5388  18245  19912   1838    431   -474       O  
ATOM    875  CB  TYR A 143      25.433  24.359  21.974  1.00117.45           C  
ANISOU  875  CB  TYR A 143     6096  18448  20079   1769    460    178       C  
ATOM    876  CG  TYR A 143      25.060  24.608  23.420  1.00110.23           C  
ANISOU  876  CG  TYR A 143     5100  17628  19154   1863    624    132       C  
ATOM    877  CD1 TYR A 143      25.039  23.569  24.340  1.00110.31           C  
ANISOU  877  CD1 TYR A 143     5083  17675  19154   1793    709    -32       C  
ATOM    878  CD2 TYR A 143      24.745  25.886  23.868  1.00111.39           C  
ANISOU  878  CD2 TYR A 143     5196  17876  19253   2038    698    249       C  
ATOM    879  CE1 TYR A 143      24.708  23.792  25.662  1.00111.53           C  
ANISOU  879  CE1 TYR A 143     5161  17930  19286   1888    867    -55       C  
ATOM    880  CE2 TYR A 143      24.409  26.118  25.188  1.00112.60           C  
ANISOU  880  CE2 TYR A 143     5274  18097  19414   2130    845    157       C  
ATOM    881  CZ  TYR A 143      24.392  25.068  26.080  1.00112.67           C  
ANISOU  881  CZ  TYR A 143     5257  18122  19432   2055    930     20       C  
ATOM    882  OH  TYR A 143      24.059  25.294  27.396  1.00113.99           O  
ANISOU  882  OH  TYR A 143     5346  18388  19576   2159   1087    -40       O  
ATOM    883  N   GLN A 144      23.188  26.085  20.755  1.00120.70           N  
ANISOU  883  N   GLN A 144     6306  18846  20708   1950    392    263       N  
ATOM    884  CA  GLN A 144      22.085  27.034  20.864  1.00122.34           C  
ANISOU  884  CA  GLN A 144     6395  19132  20957   2090    448    376       C  
ATOM    885  C   GLN A 144      20.866  26.556  20.086  1.00115.34           C  
ANISOU  885  C   GLN A 144     5399  18839  19586   2107    168   -913       C  
ATOM    886  O   GLN A 144      19.727  26.753  20.523  1.00117.17           O  
ANISOU  886  O   GLN A 144     5492  19052  19975   2155    240   -904       O  
ATOM    887  CB  GLN A 144      22.530  28.411  20.374  1.00114.04           C  
ANISOU  887  CB  GLN A 144     5410  19018  18901   2385    432    721       C  
ATOM    888  CG  GLN A 144      23.658  29.022  21.188  1.00113.18           C  
ANISOU  888  CG  GLN A 144     5375  18683  18944   2418    497    646       C  
ATOM    889  CD  GLN A 144      24.090  30.374  20.659  1.00113.20           C  
ANISOU  889  CD  GLN A 144     5412  18838  18762   2578    428    532       C  
ATOM    890  OE1 GLN A 144      23.708  30.774  19.559  1.00117.80           O  
ANISOU  890  OE1 GLN A 144     5979  19604  19175   2639    312    453       O  
ATOM    891  NE2 GLN A 144      24.889  31.089  21.442  1.00112.94           N  
ANISOU  891  NE2 GLN A 144     5414  18680  18816   2647    492    452       N  
ATOM    892  N   SER A 145      21.084  25.917  18.934  1.00114.77           N  
ANISOU  892  N   SER A 145     5381  19149  19077   2074     40   -891       N  
ATOM    893  CA  SER A 145      19.969  25.437  18.126  1.00115.61           C  
ANISOU  893  CA  SER A 145     5375  19367  19184   2049    -26   -872       C  
ATOM    894  C   SER A 145      19.258  24.249  18.761  1.00116.38           C  
ANISOU  894  C   SER A 145     5373  19361  19486   1919     56   -910       C  
ATOM    895  O   SER A 145      18.101  23.982  18.417  1.00117.93           O  
ANISOU  895  O   SER A 145     5437  19687  19683   1923     36   -911       O  
ATOM    896  CB  SER A 145      20.456  25.061  16.726  1.00114.47           C  
ANISOU  896  CB  SER A 145     5311  19327  18855   2001   -167   -791       C  
ATOM    897  OG  SER A 145      19.388  24.585  15.925  1.00115.71           O  
ANISOU  897  OG  SER A 145     5356  19546  19064   1972   -240   -797       O  
ATOM    898  N   VAL A 146      19.913  23.535  19.670  1.00119.69           N  
ANISOU  898  N   VAL A 146     5846  19589  20041   1815    156   -898       N  
ATOM    899  CA  VAL A 146      19.300  22.376  20.314  1.00119.05           C  
ANISOU  899  CA  VAL A 146     5673  19541  20019   1715    253   -885       C  
ATOM    900  C   VAL A 146      18.658  22.752  21.642  1.00117.75           C  
ANISOU  900  C   VAL A 146     5402  19300  20037   1782    425   -859       C  
ATOM    901  O   VAL A 146      17.483  22.459  21.878  1.00119.53           O  
ANISOU  901  O   VAL A 146     5478  19670  20269   1791    476   -883       O  
ATOM    902  CB  VAL A 146      20.343  21.252  20.493  1.00118.92           C  
ANISOU  902  CB  VAL A 146     5770  19443  19971   1573    271   -850       C  
ATOM    903  CG1 VAL A 146      19.814  20.185  21.439  1.00115.36           C  
ANISOU  903  CG1 VAL A 146     5225  19045  19560   1494    409   -829       C  
ATOM    904  CG2 VAL A 146      20.695  20.639  19.147  1.00114.57           C  
ANISOU  904  CG2 VAL A 146     5289  19012  19230   1495    115   -865       C  
ATOM    905  N   ILE A 147      19.409  23.405  22.531  1.00117.18           N  
ANISOU  905  N   ILE A 147     5398  19004  20120   1836    528   -762       N  
ATOM    906  CA  ILE A 147      18.862  23.720  23.848  1.00118.65           C  
ANISOU  906  CA  ILE A 147     5489  19163  20431   1914    712   -692       C  
ATOM    907  C   ILE A 147      17.842  24.850  23.755  1.00135.11           C  
ANISOU  907  C   ILE A 147     7463  21276  22598   2052    710   -730       C  
ATOM    908  O   ILE A 147      16.809  24.828  24.437  1.00128.07           O  
ANISOU  908  O   ILE A 147     6431  20488  21740   2100    816   -757       O  
ATOM    909  CB  ILE A 147      19.997  24.047  24.838  1.00117.60           C  
ANISOU  909  CB  ILE A 147     5459  18867  20355   1951    836   -499       C  
ATOM    910  CG1 ILE A 147      20.691  22.758  25.285  1.00116.45           C  
ANISOU  910  CG1 ILE A 147     5373  18767  20104   1828    881   -501       C  
ATOM    911  CG2 ILE A 147      19.467  24.813  26.042  1.00119.25           C  
ANISOU  911  CG2 ILE A 147     5579  19104  20627   2095   1008   -427       C  
ATOM    912  CD1 ILE A 147      21.486  22.896  26.567  1.00116.08           C  
ANISOU  912  CD1 ILE A 147     5376  18707  20023   1890   1035   -373       C  
ATOM    913  N   TYR A 148      18.096  25.844  22.899  1.00139.62           N  
ANISOU  913  N   TYR A 148     8088  21770  23190   2121    592   -739       N  
ATOM    914  CA  TYR A 148      17.228  27.011  22.752  1.00131.90           C  
ANISOU  914  CA  TYR A 148     7017  20823  22277   2266    580   -783       C  
ATOM    915  C   TYR A 148      16.676  27.053  21.331  1.00130.05           C  
ANISOU  915  C   TYR A 148     6753  20898  21763   2294    381   -949       C  
ATOM    916  O   TYR A 148      17.217  27.759  20.466  1.00128.08           O  
ANISOU  916  O   TYR A 148     6591  20774  21301   2370    256   -980       O  
ATOM    917  CB  TYR A 148      17.973  28.305  23.075  1.00124.10           C  
ANISOU  917  CB  TYR A 148     6109  19525  21518   2370    665   -463       C  
ATOM    918  CG  TYR A 148      18.745  28.269  24.372  1.00122.76           C  
ANISOU  918  CG  TYR A 148     5997  19330  21317   2405    863   -146       C  
ATOM    919  CD1 TYR A 148      18.096  28.392  25.593  1.00122.39           C  
ANISOU  919  CD1 TYR A 148     5849  19374  21280   2490   1022   -205       C  
ATOM    920  CD2 TYR A 148      20.125  28.122  24.374  1.00118.80           C  
ANISOU  920  CD2 TYR A 148     5646  18829  20665   2376    863     74       C  
ATOM    921  CE1 TYR A 148      18.800  28.363  26.781  1.00123.56           C  
ANISOU  921  CE1 TYR A 148     6044  19589  21315   2542   1164   -126       C  
ATOM    922  CE2 TYR A 148      20.838  28.092  25.556  1.00118.42           C  
ANISOU  922  CE2 TYR A 148     5640  18868  20487   2425    987     95       C  
ATOM    923  CZ  TYR A 148      20.171  28.212  26.755  1.00128.60           C  
ANISOU  923  CZ  TYR A 148     6827  20224  21811   2509   1136    -14       C  
ATOM    924  OH  TYR A 148      20.879  28.183  27.933  1.00134.61           O  
ANISOU  924  OH  TYR A 148     7626  21071  22449   2566   1254    -37       O  
ATOM    925  N   PRO A 149      15.585  26.331  21.055  1.00123.30           N  
ANISOU  925  N   PRO A 149     5769  20238  20842   2254    366   -972       N  
ATOM    926  CA  PRO A 149      14.967  26.420  19.724  1.00123.88           C  
ANISOU  926  CA  PRO A 149     5793  20525  20749   2289    211   -978       C  
ATOM    927  C   PRO A 149      14.334  27.781  19.466  1.00145.36           C  
ANISOU  927  C   PRO A 149     8450  23311  23471   2472    182   -986       C  
ATOM    928  O   PRO A 149      13.733  28.007  18.410  1.00151.24           O  
ANISOU  928  O   PRO A 149     9139  24184  24140   2523     69   -958       O  
ATOM    929  CB  PRO A 149      13.917  25.302  19.745  1.00125.17           C  
ANISOU  929  CB  PRO A 149     5815  20804  20940   2191    238   -977       C  
ATOM    930  CG  PRO A 149      13.647  25.057  21.191  1.00125.97           C  
ANISOU  930  CG  PRO A 149     5851  20821  21192   2177    424   -983       C  
ATOM    931  CD  PRO A 149      14.943  25.307  21.896  1.00124.25           C  
ANISOU  931  CD  PRO A 149     5784  20387  21039   2167    492   -957       C  
ATOM    932  N   PHE A 150      14.461  28.693  20.435  1.00136.66           N  
ANISOU  932  N   PHE A 150     7351  22085  22489   2573    289  -1014       N  
ATOM    933  CA  PHE A 150      14.003  30.063  20.236  1.00127.01           C  
ANISOU  933  CA  PHE A 150     6086  20958  21215   2766    266  -1019       C  
ATOM    934  C   PHE A 150      14.804  30.757  19.143  1.00125.82           C  
ANISOU  934  C   PHE A 150     6061  21010  20737   2866    141   -907       C  
ATOM    935  O   PHE A 150      14.249  31.514  18.338  1.00126.86           O  
ANISOU  935  O   PHE A 150     6140  21235  20826   2989     70   -843       O  
ATOM    936  CB  PHE A 150      14.101  30.837  21.552  1.00127.66           C  
ANISOU  936  CB  PHE A 150     6158  20802  21545   2836    421  -1055       C  
ATOM    937  CG  PHE A 150      14.118  32.329  21.381  1.00148.57           C  
ANISOU  937  CG  PHE A 150     8828  23690  23931   3071    388  -1061       C  
ATOM    938  CD1 PHE A 150      12.946  33.026  21.140  1.00157.17           C  
ANISOU  938  CD1 PHE A 150     9785  24884  25048   3205    380  -1056       C  
ATOM    939  CD2 PHE A 150      15.306  33.036  21.474  1.00127.02           C  
ANISOU  939  CD2 PHE A 150     6277  21572  20414   3290    478   -448       C  
ATOM    940  CE1 PHE A 150      12.960  34.401  20.985  1.00152.90           C  
ANISOU  940  CE1 PHE A 150     9273  24649  24174   3462    389   -882       C  
ATOM    941  CE2 PHE A 150      15.326  34.410  21.320  1.00127.78           C  
ANISOU  941  CE2 PHE A 150     6382  21604  20564   3488    599    131       C  
ATOM    942  CZ  PHE A 150      14.152  35.093  21.076  1.00140.42           C  
ANISOU  942  CZ  PHE A 150     7854  23297  22202   3610    515   -244       C  
ATOM    943  N   LEU A 151      16.110  30.504  19.093  1.00123.73           N  
ANISOU  943  N   LEU A 151     5954  20790  20267   2816    131   -822       N  
ATOM    944  CA  LEU A 151      16.992  31.118  18.099  1.00136.29           C  
ANISOU  944  CA  LEU A 151     7665  22512  21608   2896     59   -566       C  
ATOM    945  C   LEU A 151      16.694  30.507  16.733  1.00122.36           C  
ANISOU  945  C   LEU A 151     5879  20674  19939   2799   -100   -647       C  
ATOM    946  O   LEU A 151      17.328  29.546  16.290  1.00120.87           O  
ANISOU  946  O   LEU A 151     5768  20440  19718   2652   -159   -660       O  
ATOM    947  CB  LEU A 151      18.453  30.923  18.482  1.00141.19           C  
ANISOU  947  CB  LEU A 151     8448  23171  22028   2853    128   -307       C  
ATOM    948  CG  LEU A 151      18.985  31.741  19.663  1.00141.70           C  
ANISOU  948  CG  LEU A 151     8552  23175  22111   2967    345    183       C  
ATOM    949  CD1 LEU A 151      20.428  31.383  19.967  1.00118.35           C  
ANISOU  949  CD1 LEU A 151     5733  19983  19251   2856    401    424       C  
ATOM    950  CD2 LEU A 151      18.855  33.233  19.398  1.00142.71           C  
ANISOU  950  CD2 LEU A 151     8656  23217  22350   3149    344    202       C  
ATOM    951  N   SER A 152      15.704  31.081  16.053  1.00124.03           N  
ANISOU  951  N   SER A 152     5981  20890  20255   2895   -167   -673       N  
ATOM    952  CA  SER A 152      15.322  30.656  14.710  1.00129.69           C  
ANISOU  952  CA  SER A 152     6665  21577  21035   2844   -317   -698       C  
ATOM    953  C   SER A 152      14.931  31.865  13.873  1.00134.74           C  
ANISOU  953  C   SER A 152     7266  22210  21720   3017   -392   -658       C  
ATOM    954  O   SER A 152      13.926  31.850  13.156  1.00135.24           O  
ANISOU  954  O   SER A 152     7215  22269  21902   3043   -479   -709       O  
ATOM    955  CB  SER A 152      14.189  29.630  14.754  1.00125.49           C  
ANISOU  955  CB  SER A 152     5993  21055  20631   2736   -326   -791       C  
ATOM    956  OG  SER A 152      13.030  30.172  15.361  1.00127.61           O  
ANISOU  956  OG  SER A 152     6113  21352  21023   2834   -257   -838       O  
ATOM    957  N   GLN A 153      15.719  32.931  13.963  1.00148.02           N  
ANISOU  957  N   GLN A 153     9037  23882  23320   3141   -356   -555       N  
ATOM    958  CA  GLN A 153      15.450  34.180  13.270  1.00161.17           C  
ANISOU  958  CA  GLN A 153    10674  25512  25053   3318   -411   -517       C  
ATOM    959  C   GLN A 153      16.452  34.396  12.142  1.00163.61           C  
ANISOU  959  C   GLN A 153    11101  25732  25333   3320   -518   -456       C  
ATOM    960  O   GLN A 153      17.522  33.781  12.101  1.00150.83           O  
ANISOU  960  O   GLN A 153     9601  24086  23619   3203   -521   -420       O  
ATOM    961  CB  GLN A 153      15.503  35.365  14.241  1.00166.65           C  
ANISOU  961  CB  GLN A 153    11363  26231  25725   3482   -275   -438       C  
ATOM    962  CG  GLN A 153      16.844  35.516  14.943  1.00167.80           C  
ANISOU  962  CG  GLN A 153    11648  26353  25754   3464   -174   -300       C  
ATOM    963  CD  GLN A 153      16.869  36.670  15.924  1.00167.13           C  
ANISOU  963  CD  GLN A 153    11551  26257  25695   3627    -30   -196       C  
ATOM    964  OE1 GLN A 153      15.846  37.303  16.185  1.00171.41           O  
ANISOU  964  OE1 GLN A 153    11981  26840  26305   3754      4   -238       O  
ATOM    965  NE2 GLN A 153      18.045  36.950  16.476  1.00159.04           N  
ANISOU  965  NE2 GLN A 153    10635  25142  24650   3623     54    -71       N  
ATOM    966  N   ARG A 154      16.090  35.288  11.219  1.00176.57           N  
ANISOU  966  N   ARG A 154    12702  27316  27070   3457   -605   -449       N  
ATOM    967  CA  ARG A 154      16.986  35.669  10.133  1.00174.27           C  
ANISOU  967  CA  ARG A 154    12511  26923  26781   3489   -702   -391       C  
ATOM    968  C   ARG A 154      17.990  36.739  10.542  1.00162.22           C  
ANISOU  968  C   ARG A 154    11076  25336  25224   3597   -615   -287       C  
ATOM    969  O   ARG A 154      18.804  37.151   9.709  1.00144.85           O  
ANISOU  969  O   ARG A 154     8957  23037  23041   3633   -681   -236       O  
ATOM    970  CB  ARG A 154      16.182  36.147   8.921  1.00175.35           C  
ANISOU  970  CB  ARG A 154    12563  27009  27052   3596   -838   -414       C  
ATOM    971  CG  ARG A 154      15.515  35.021   8.148  1.00170.54           C  
ANISOU  971  CG  ARG A 154    11893  26403  26504   3472   -963   -493       C  
ATOM    972  CD  ARG A 154      14.944  35.510   6.828  1.00166.71           C  
ANISOU  972  CD  ARG A 154    11345  25842  26155   3579  -1112   -479       C  
ATOM    973  NE  ARG A 154      14.448  34.408   6.010  1.00162.78           N  
ANISOU  973  NE  ARG A 154    10799  25317  25734   3455  -1242   -533       N  
ATOM    974  CZ  ARG A 154      13.935  34.552   4.793  1.00158.96           C  
ANISOU  974  CZ  ARG A 154    10256  24757  25383   3514  -1391   -509       C  
ATOM    975  NH1 ARG A 154      13.508  33.492   4.121  1.00161.84           N  
ANISOU  975  NH1 ARG A 154    10575  25079  25837   3390  -1504   -542       N  
ATOM    976  NH2 ARG A 154      13.850  35.757   4.246  1.00153.74           N  
ANISOU  976  NH2 ARG A 154     9582  24057  24777   3700  -1426   -436       N  
ATOM    977  N   ARG A 155      17.950  37.200  11.793  1.00152.70           N  
ANISOU  977  N   ARG A 155     9854  24170  23995   3651   -468   -252       N  
ATOM    978  CA  ARG A 155      18.995  38.075  12.305  1.00134.21           C  
ANISOU  978  CA  ARG A 155     7600  21738  21656   3727   -376   -158       C  
ATOM    979  C   ARG A 155      20.263  37.307  12.646  1.00128.69           C  
ANISOU  979  C   ARG A 155     7027  21009  20860   3571   -345   -114       C  
ATOM    980  O   ARG A 155      21.319  37.924  12.826  1.00124.54           O  
ANISOU  980  O   ARG A 155     6584  20370  20365   3607   -302    -54       O  
ATOM    981  CB  ARG A 155      18.495  38.825  13.542  1.00127.10           C  
ANISOU  981  CB  ARG A 155     6634  20867  20791   3845   -228   -131       C  
ATOM    982  CG  ARG A 155      17.174  39.550  13.337  1.00131.42           C  
ANISOU  982  CG  ARG A 155     7048  21454  21430   3999   -246   -182       C  
ATOM    983  CD  ARG A 155      16.645  40.120  14.645  1.00128.75           C  
ANISOU  983  CD  ARG A 155     6645  21159  21113   4101    -91   -161       C  
ATOM    984  NE  ARG A 155      15.311  40.693  14.491  1.00131.08           N  
ANISOU  984  NE  ARG A 155     6806  21506  21491   4237   -109   -224       N  
ATOM    985  CZ  ARG A 155      14.593  41.195  15.491  1.00139.58           C  
ANISOU  985  CZ  ARG A 155     7804  22636  22595   4342     12   -226       C  
ATOM    986  NH1 ARG A 155      15.081  41.196  16.725  1.00142.28           N  
ANISOU  986  NH1 ARG A 155     8186  22975  22896   4332    164   -151       N  
ATOM    987  NH2 ARG A 155      13.387  41.697  15.259  1.00134.73           N  
ANISOU  987  NH2 ARG A 155     7065  22061  22066   4461    -19   -297       N  
ATOM    988  N   ASN A 156      20.179  35.981  12.739  1.00136.00           N  
ANISOU  988  N   ASN A 156     7964  22020  21689   3399   -369   -155       N  
ATOM    989  CA  ASN A 156      21.322  35.124  13.027  1.00149.40           C  
ANISOU  989  CA  ASN A 156     9778  23696  23290   3242   -348   -117       C  
ATOM    990  C   ASN A 156      22.275  35.067  11.832  1.00157.52           C  
ANISOU  990  C   ASN A 156    10906  24624  24321   3203   -465   -115       C  
ATOM    991  O   ASN A 156      23.496  35.079  12.034  1.00153.44           O  
ANISOU  991  O   ASN A 156    10496  24028  23777   3154   -434    -62       O  
ATOM    992  CB  ASN A 156      20.849  33.723  13.428  1.00144.92           C  
ANISOU  992  CB  ASN A 156     9184  23241  22637   3080   -340   -174       C  
ATOM    993  CG  ASN A 156      21.896  32.949  14.210  1.00132.78           C  
ANISOU  993  CG  ASN A 156     7751  21698  21002   2944   -264   -105       C  
ATOM    994  OD1 ASN A 156      23.096  33.086  13.972  1.00130.52           O  
ANISOU  994  OD1 ASN A 156     7576  21314  20701   2915   -280    -52       O  
ATOM    995  ND2 ASN A 156      21.443  32.130  15.152  1.00118.26           N  
ANISOU  995  ND2 ASN A 156     5871  19955  19109   2863   -182   -108       N  
ATOM    996  N   PRO A 157      21.787  34.988  10.584  1.00164.85           N  
ANISOU  996  N   PRO A 157    11800  25540  25294   3224   -601   -170       N  
ATOM    997  CA  PRO A 157      22.713  35.172   9.452  1.00161.17           C  
ANISOU  997  CA  PRO A 157    11424  24965  24848   3227   -700   -140       C  
ATOM    998  C   PRO A 157      23.420  36.516   9.466  1.00161.87           C  
ANISOU  998  C   PRO A 157    11549  24938  25017   3374   -655    -62       C  
ATOM    999  O   PRO A 157      24.630  36.578   9.207  1.00160.92           O  
ANISOU  999  O   PRO A 157    11531  24724  24888   3337   -662    -18       O  
ATOM   1000  CB  PRO A 157      21.800  35.019   8.229  1.00153.36           C  
ANISOU 1000  CB  PRO A 157    10362  23982  23927   3263   -842   -195       C  
ATOM   1001  CG  PRO A 157      20.736  34.105   8.687  1.00148.71           C  
ANISOU 1001  CG  PRO A 157     9681  23500  23321   3173   -835   -283       C  
ATOM   1002  CD  PRO A 157      20.483  34.467  10.125  1.00155.28           C  
ANISOU 1002  CD  PRO A 157    10476  24403  24123   3209   -679   -262       C  
ATOM   1003  N   TRP A 158      22.698  37.601   9.761  1.00155.99           N  
ANISOU 1003  N   TRP A 158    10718  24187  24365   3540   -606    -51       N  
ATOM   1004  CA  TRP A 158      23.341  38.908   9.854  1.00146.81           C  
ANISOU 1004  CA  TRP A 158     9581  22893  23307   3685   -551     10       C  
ATOM   1005  C   TRP A 158      24.343  38.955  10.999  1.00137.15           C  
ANISOU 1005  C   TRP A 158     8426  21615  22069   3630   -431     34       C  
ATOM   1006  O   TRP A 158      25.333  39.693  10.927  1.00133.61           O  
ANISOU 1006  O   TRP A 158     8035  21028  21703   3683   -409     67       O  
ATOM   1007  CB  TRP A 158      22.291  40.008  10.016  1.00153.38           C  
ANISOU 1007  CB  TRP A 158    10304  23729  24246   3876   -517      7       C  
ATOM   1008  CG  TRP A 158      21.495  40.267   8.771  1.00157.67           C  
ANISOU 1008  CG  TRP A 158    10784  24276  24847   3968   -642      0       C  
ATOM   1009  CD1 TRP A 158      20.162  40.039   8.586  1.00153.21           C  
ANISOU 1009  CD1 TRP A 158    10109  23811  24293   3996   -691    -57       C  
ATOM   1010  CD2 TRP A 158      21.987  40.796   7.532  1.00159.37           C  
ANISOU 1010  CD2 TRP A 158    11039  24382  25131   4049   -737     58       C  
ATOM   1011  NE1 TRP A 158      19.792  40.398   7.312  1.00154.22           N  
ANISOU 1011  NE1 TRP A 158    10204  23893  24497   4089   -815    -39       N  
ATOM   1012  CE2 TRP A 158      20.894  40.865   6.645  1.00158.17           C  
ANISOU 1012  CE2 TRP A 158    10799  24272  25027   4128   -843     41       C  
ATOM   1013  CE3 TRP A 158      23.244  41.219   7.089  1.00149.15           C  
ANISOU 1013  CE3 TRP A 158     9841  22955  23874   4066   -741    129       C  
ATOM   1014  CZ2 TRP A 158      21.021  41.340   5.341  1.00155.87           C  
ANISOU 1014  CZ2 TRP A 158    10517  23900  24806   4229   -951    106       C  
ATOM   1015  CZ3 TRP A 158      23.367  41.691   5.794  1.00144.34           C  
ANISOU 1015  CZ3 TRP A 158     9240  22270  23333   4167   -841    193       C  
ATOM   1016  CH2 TRP A 158      22.262  41.747   4.935  1.00147.79           C  
ANISOU 1016  CH2 TRP A 158     9593  22758  23804   4250   -945    188       C  
ATOM   1017  N   GLN A 159      24.106  38.183  12.062  1.00130.33           N  
ANISOU 1017  N   GLN A 159     7551  20848  21119   3526   -353     17       N  
ATOM   1018  CA  GLN A 159      25.115  38.047  13.107  1.00126.19           C  
ANISOU 1018  CA  GLN A 159     7097  20266  20583   3455   -253     40       C  
ATOM   1019  C   GLN A 159      26.334  37.294  12.591  1.00119.96           C  
ANISOU 1019  C   GLN A 159     6425  19427  19725   3309   -316     50       C  
ATOM   1020  O   GLN A 159      27.473  37.636  12.932  1.00112.99           O  
ANISOU 1020  O   GLN A 159     5612  18429  18891   3298   -276     62       O  
ATOM   1021  CB  GLN A 159      24.523  37.339  14.326  1.00117.44           C  
ANISOU 1021  CB  GLN A 159     5947  19272  19405   3385   -154     45       C  
ATOM   1022  CG  GLN A 159      25.521  37.112  15.450  1.00115.02           C  
ANISOU 1022  CG  GLN A 159     5706  18896  19098   3311    -54     68       C  
ATOM   1023  CD  GLN A 159      24.977  36.221  16.548  1.00119.13           C  
ANISOU 1023  CD  GLN A 159     6192  19520  19554   3226     39    103       C  
ATOM   1024  OE1 GLN A 159      25.718  35.771  17.423  1.00114.61           O  
ANISOU 1024  OE1 GLN A 159     5673  18899  18976   3143    110    126       O  
ATOM   1025  NE2 GLN A 159      23.675  35.960  16.509  1.00119.93           N  
ANISOU 1025  NE2 GLN A 159     6196  19755  19618   3251     40    104       N  
ATOM   1026  N   ALA A 160      26.115  36.268  11.764  1.00123.14           N  
ANISOU 1026  N   ALA A 160     6848  19910  20028   3197   -417     30       N  
ATOM   1027  CA  ALA A 160      27.228  35.539  11.168  1.00124.49           C  
ANISOU 1027  CA  ALA A 160     7131  20034  20134   3067   -483     36       C  
ATOM   1028  C   ALA A 160      28.029  36.421  10.220  1.00136.41           C  
ANISOU 1028  C   ALA A 160     8685  21405  21739   3156   -540     66       C  
ATOM   1029  O   ALA A 160      29.231  36.194  10.031  1.00138.81           O  
ANISOU 1029  O   ALA A 160     9083  21630  22028   3080   -554     85       O  
ATOM   1030  CB  ALA A 160      26.715  34.299  10.436  1.00122.38           C  
ANISOU 1030  CB  ALA A 160     6864  19867  19767   2945   -582    -13       C  
ATOM   1031  N   SER A 161      27.387  37.430   9.623  1.00112.94           N  
ANISOU 1031  N   SER A 161     5642  18399  18872   3322   -571     79       N  
ATOM   1032  CA  SER A 161      28.111  38.396   8.805  1.00114.70           C  
ANISOU 1032  CA  SER A 161     5895  18478  19207   3432   -606    129       C  
ATOM   1033  C   SER A 161      29.132  39.182   9.618  1.00119.31           C  
ANISOU 1033  C   SER A 161     6530  18916  19886   3460   -505    145       C  
ATOM   1034  O   SER A 161      30.009  39.829   9.034  1.00112.40           O  
ANISOU 1034  O   SER A 161     5738  17867  19104   3492   -519    192       O  
ATOM   1035  CB  SER A 161      27.130  39.355   8.130  1.00122.63           C  
ANISOU 1035  CB  SER A 161     6809  19472  20314   3616   -647    149       C  
ATOM   1036  OG  SER A 161      26.237  38.655   7.281  1.00128.62           O  
ANISOU 1036  OG  SER A 161     7528  20330  21009   3586   -756    123       O  
ATOM   1037  N   TYR A 162      29.029  39.153  10.946  1.00123.43           N  
ANISOU 1037  N   TYR A 162     7026  19471  20402   3439   -399    108       N  
ATOM   1038  CA  TYR A 162      30.043  39.713  11.829  1.00118.19           C  
ANISOU 1038  CA  TYR A 162     6437  18642  19829   3427   -309     91       C  
ATOM   1039  C   TYR A 162      30.900  38.649  12.497  1.00119.14           C  
ANISOU 1039  C   TYR A 162     6626  18799  19842   3252   -286     70       C  
ATOM   1040  O   TYR A 162      32.063  38.917  12.814  1.00115.69           O  
ANISOU 1040  O   TYR A 162     6281  18208  19468   3208   -257     50       O  
ATOM   1041  CB  TYR A 162      29.391  40.578  12.913  1.00117.65           C  
ANISOU 1041  CB  TYR A 162     6294  18548  19859   3550   -202     51       C  
ATOM   1042  CG  TYR A 162      28.742  41.840  12.392  1.00129.50           C  
ANISOU 1042  CG  TYR A 162     7743  19962  21498   3736   -205     68       C  
ATOM   1043  CD1 TYR A 162      29.472  43.013  12.252  1.00135.41           C  
ANISOU 1043  CD1 TYR A 162     8554  20476  22422   3820   -177     68       C  
ATOM   1044  CD2 TYR A 162      27.398  41.859  12.043  1.00126.20           C  
ANISOU 1044  CD2 TYR A 162     7213  19691  21048   3829   -236     81       C  
ATOM   1045  CE1 TYR A 162      28.883  44.169  11.777  1.00131.33           C  
ANISOU 1045  CE1 TYR A 162     7993  19869  22039   3995   -174     97       C  
ATOM   1046  CE2 TYR A 162      26.800  43.011  11.567  1.00124.03           C  
ANISOU 1046  CE2 TYR A 162     6891  19335  20900   4006   -240    102       C  
ATOM   1047  CZ  TYR A 162      27.547  44.163  11.436  1.00125.88           C  
ANISOU 1047  CZ  TYR A 162     7194  19332  21303   4091   -206    118       C  
ATOM   1048  OH  TYR A 162      26.957  45.312  10.963  1.00123.97           O  
ANISOU 1048  OH  TYR A 162     6909  19000  21193   4271   -204    150       O  
ATOM   1049  N   ILE A 163      30.354  37.451  12.714  1.00120.21           N  
ANISOU 1049  N   ILE A 163     6727  19120  19826   3148   -299     72       N  
ATOM   1050  CA  ILE A 163      31.117  36.391  13.365  1.00115.58           C  
ANISOU 1050  CA  ILE A 163     6218  18559  19138   2980   -273     67       C  
ATOM   1051  C   ILE A 163      32.199  35.858  12.435  1.00108.22           C  
ANISOU 1051  C   ILE A 163     5387  17578  18154   2876   -359     81       C  
ATOM   1052  O   ILE A 163      33.344  35.650  12.851  1.00105.06           O  
ANISOU 1052  O   ILE A 163     5067  17099  17753   2794   -335     72       O  
ATOM   1053  CB  ILE A 163      30.176  35.271  13.844  1.00108.07           C  
ANISOU 1053  CB  ILE A 163     5237  17767  18057   2884   -254     78       C  
ATOM   1054  CG1 ILE A 163      29.242  35.788  14.940  1.00109.64           C  
ANISOU 1054  CG1 ILE A 163     5339  18003  18317   2984   -147     75       C  
ATOM   1055  CG2 ILE A 163      30.973  34.078  14.347  1.00106.30           C  
ANISOU 1055  CG2 ILE A 163     5100  17563  17725   2708   -238     91       C  
ATOM   1056  CD1 ILE A 163      28.327  34.728  15.514  1.00110.74           C  
ANISOU 1056  CD1 ILE A 163     5437  18287  18352   2896   -108    104       C  
ATOM   1057  N   VAL A 164      31.858  35.631  11.162  1.00106.47           N  
ANISOU 1057  N   VAL A 164     5170  17389  17896   2880   -463     97       N  
ATOM   1058  CA  VAL A 164      32.848  35.115  10.214  1.00107.90           C  
ANISOU 1058  CA  VAL A 164     5444  17521  18031   2792   -545    112       C  
ATOM   1059  C   VAL A 164      34.040  36.055  10.066  1.00104.69           C  
ANISOU 1059  C   VAL A 164     5112  16914  17752   2835   -525    137       C  
ATOM   1060  O   VAL A 164      35.185  35.582  10.169  1.00114.54           O  
ANISOU 1060  O   VAL A 164     6455  18100  18964   2722   -525    136       O  
ATOM   1061  CB  VAL A 164      32.171  34.787   8.868  1.00105.52           C  
ANISOU 1061  CB  VAL A 164     5126  17273  17694   2809   -662    117       C  
ATOM   1062  CG1 VAL A 164      33.207  34.345   7.846  1.00104.19           C  
ANISOU 1062  CG1 VAL A 164     5050  17041  17496   2739   -744    140       C  
ATOM   1063  CG2 VAL A 164      31.111  33.714   9.058  1.00105.74           C  
ANISOU 1063  CG2 VAL A 164     5119  17450  17609   2721   -682     69       C  
ATOM   1064  N   PRO A 165      33.866  37.364   9.841  1.00106.09           N  
ANISOU 1064  N   PRO A 165     5265  16960  18084   2984   -505    160       N  
ATOM   1065  CA  PRO A 165      35.040  38.252   9.866  1.00105.86           C  
ANISOU 1065  CA  PRO A 165     5317  16706  18197   3006   -469    172       C  
ATOM   1066  C   PRO A 165      35.706  38.314  11.227  1.00111.11           C  
ANISOU 1066  C   PRO A 165     6013  17306  18896   2948   -379    100       C  
ATOM   1067  O   PRO A 165      36.910  38.586  11.307  1.00115.02           O  
ANISOU 1067  O   PRO A 165     6592  17644  19467   2901   -365     85       O  
ATOM   1068  CB  PRO A 165      34.462  39.614   9.454  1.00107.80           C  
ANISOU 1068  CB  PRO A 165     5510  16842  18605   3188   -455    207       C  
ATOM   1069  CG  PRO A 165      33.206  39.292   8.732  1.00108.70           C  
ANISOU 1069  CG  PRO A 165     5540  17121  18639   3248   -524    234       C  
ATOM   1070  CD  PRO A 165      32.652  38.099   9.440  1.00108.00           C  
ANISOU 1070  CD  PRO A 165     5407  17238  18389   3139   -520    176       C  
ATOM   1071  N   LEU A 166      34.956  38.073  12.306  1.00106.98           N  
ANISOU 1071  N   LEU A 166     5421  16898  18328   2954   -318     53       N  
ATOM   1072  CA  LEU A 166      35.570  38.007  13.627  1.00113.21           C  
ANISOU 1072  CA  LEU A 166     6239  17638  19137   2898   -238    -22       C  
ATOM   1073  C   LEU A 166      36.395  36.737  13.784  1.00115.40           C  
ANISOU 1073  C   LEU A 166     6592  17983  19273   2725   -263    -18       C  
ATOM   1074  O   LEU A 166      37.475  36.761  14.386  1.00111.83           O  
ANISOU 1074  O   LEU A 166     6210  17422  18857   2662   -234    -73       O  
ATOM   1075  CB  LEU A 166      34.496  38.090  14.712  1.00112.33           C  
ANISOU 1075  CB  LEU A 166     6031  17631  19020   2964   -160    -58       C  
ATOM   1076  CG  LEU A 166      34.984  38.066  16.162  1.00111.36           C  
ANISOU 1076  CG  LEU A 166     5926  17463  18925   2932    -73   -150       C  
ATOM   1077  CD1 LEU A 166      35.930  39.227  16.432  1.00106.68           C  
ANISOU 1077  CD1 LEU A 166     5386  16637  18509   2990    -47   -245       C  
ATOM   1078  CD2 LEU A 166      33.805  38.094  17.123  1.00112.10           C  
ANISOU 1078  CD2 LEU A 166     5915  17669  19008   3007      7   -166       C  
ATOM   1079  N   VAL A 167      35.905  35.617  13.246  1.00116.44           N  
ANISOU 1079  N   VAL A 167     6708  18288  19245   2647   -318     35       N  
ATOM   1080  CA  VAL A 167      36.669  34.373  13.290  1.00109.04           C  
ANISOU 1080  CA  VAL A 167     5846  17412  18173   2484   -344     46       C  
ATOM   1081  C   VAL A 167      37.952  34.513  12.480  1.00 99.75           C  
ANISOU 1081  C   VAL A 167     4776  16094  17031   2436   -398     53       C  
ATOM   1082  O   VAL A 167      39.037  34.123  12.929  1.00 98.51           O  
ANISOU 1082  O   VAL A 167     4698  15878  16853   2338   -384     28       O  
ATOM   1083  CB  VAL A 167      35.810  33.195  12.793  1.00100.58           C  
ANISOU 1083  CB  VAL A 167     4740  16532  16942   2414   -397     81       C  
ATOM   1084  CG1 VAL A 167      36.672  31.961  12.579  1.00 98.74           C  
ANISOU 1084  CG1 VAL A 167     4616  16320  16581   2246   -437     89       C  
ATOM   1085  CG2 VAL A 167      34.698  32.895  13.786  1.00101.50           C  
ANISOU 1085  CG2 VAL A 167     4787  16752  17025   2421   -325     84       C  
ATOM   1086  N   TRP A 168      37.849  35.080  11.274  1.00100.57           N  
ANISOU 1086  N   TRP A 168     4881  16136  17194   2510   -459     94       N  
ATOM   1087  CA  TRP A 168      39.046  35.295  10.466  1.00 99.45           C  
ANISOU 1087  CA  TRP A 168     4834  15846  17107   2477   -500    124       C  
ATOM   1088  C   TRP A 168      39.990  36.297  11.116  1.00 99.66           C  
ANISOU 1088  C   TRP A 168     4898  15667  17299   2506   -436     80       C  
ATOM   1089  O   TRP A 168      41.213  36.173  10.978  1.00 98.57           O  
ANISOU 1089  O   TRP A 168     4846  15424  17181   2428   -446     77       O  
ATOM   1090  CB  TRP A 168      38.665  35.765   9.062  1.00100.25           C  
ANISOU 1090  CB  TRP A 168     4921  15916  17256   2570   -569    195       C  
ATOM   1091  CG  TRP A 168      38.071  34.692   8.200  1.00105.79           C  
ANISOU 1091  CG  TRP A 168     5608  16782  17805   2520   -657    213       C  
ATOM   1092  CD1 TRP A 168      37.235  33.689   8.596  1.00 99.65           C  
ANISOU 1092  CD1 TRP A 168     4777  16195  16892   2458   -668    169       C  
ATOM   1093  CD2 TRP A 168      38.281  34.508   6.794  1.00115.19           C  
ANISOU 1093  CD2 TRP A 168     6837  17951  18980   2529   -747    272       C  
ATOM   1094  NE1 TRP A 168      36.904  32.898   7.523  1.00109.80           N  
ANISOU 1094  NE1 TRP A 168     6063  17568  18090   2424   -766    171       N  
ATOM   1095  CE2 TRP A 168      37.534  33.378   6.405  1.00115.52           C  
ANISOU 1095  CE2 TRP A 168     6845  18167  18882   2470   -818    235       C  
ATOM   1096  CE3 TRP A 168      39.024  35.190   5.826  1.00117.08           C  
ANISOU 1096  CE3 TRP A 168     7132  18034  19320   2585   -771    356       C  
ATOM   1097  CZ2 TRP A 168      37.510  32.914   5.091  1.00111.74           C  
ANISOU 1097  CZ2 TRP A 168     6388  17704  18364   2468   -921    265       C  
ATOM   1098  CZ3 TRP A 168      38.998  34.729   4.522  1.00112.23           C  
ANISOU 1098  CZ3 TRP A 168     6542  17452  18650   2588   -865    412       C  
ATOM   1099  CH2 TRP A 168      38.246  33.602   4.167  1.00107.49           C  
ANISOU 1099  CH2 TRP A 168     5909  17022  17912   2531   -943    360       C  
ATOM   1100  N   CYS A 169      39.449  37.290  11.826  1.00103.62           N  
ANISOU 1100  N   CYS A 169     5336  16107  17927   2619   -373     34       N  
ATOM   1101  CA  CYS A 169      40.297  38.265  12.503  1.00117.62           C  
ANISOU 1101  CA  CYS A 169     7138  17678  19875   2650   -315    -42       C  
ATOM   1102  C   CYS A 169      41.068  37.618  13.647  1.00122.42           C  
ANISOU 1102  C   CYS A 169     7790  18303  20421   2536   -282   -133       C  
ATOM   1103  O   CYS A 169      42.286  37.797  13.768  1.00117.67           O  
ANISOU 1103  O   CYS A 169     7258  17561  19890   2478   -281   -178       O  
ATOM   1104  CB  CYS A 169      39.449  39.433  13.011  1.00122.04           C  
ANISOU 1104  CB  CYS A 169     7616  18176  20580   2804   -256    -87       C  
ATOM   1105  SG  CYS A 169      40.386  40.728  13.857  1.00128.81           S  
ANISOU 1105  SG  CYS A 169     8496  18770  21678   2856   -187   -215       S  
ATOM   1106  N   MET A 170      40.372  36.858  14.498  1.00130.26           N  
ANISOU 1106  N   MET A 170     8740  19464  21287   2504   -253   -157       N  
ATOM   1107  CA  MET A 170      41.050  36.152  15.580  1.00122.83           C  
ANISOU 1107  CA  MET A 170     7841  18552  20276   2402   -222   -229       C  
ATOM   1108  C   MET A 170      42.034  35.121  15.042  1.00114.88           C  
ANISOU 1108  C   MET A 170     6926  17572  19152   2257   -278   -181       C  
ATOM   1109  O   MET A 170      43.055  34.844  15.682  1.00117.52           O  
ANISOU 1109  O   MET A 170     7321  17851  19480   2179   -267   -246       O  
ATOM   1110  CB  MET A 170      40.028  35.476  16.497  1.00125.87           C  
ANISOU 1110  CB  MET A 170     8157  19113  20554   2402   -173   -229       C  
ATOM   1111  CG  MET A 170      38.993  36.413  17.116  1.00135.16           C  
ANISOU 1111  CG  MET A 170     9238  20283  21833   2548   -109   -278       C  
ATOM   1112  SD  MET A 170      39.680  37.659  18.224  1.00146.34           S  
ANISOU 1112  SD  MET A 170    10664  21502  23435   2632    -46   -460       S  
ATOM   1113  CE  MET A 170      39.660  39.111  17.174  1.00148.83           C  
ANISOU 1113  CE  MET A 170    10968  21631  23949   2754    -70   -441       C  
ATOM   1114  N   ALA A 171      41.749  34.549  13.870  1.00105.62           N  
ANISOU 1114  N   ALA A 171     5764  16482  17883   2226   -343    -80       N  
ATOM   1115  CA  ALA A 171      42.662  33.575  13.283  1.00 95.16           C  
ANISOU 1115  CA  ALA A 171     4528  15181  16447   2096   -397    -40       C  
ATOM   1116  C   ALA A 171      43.917  34.249  12.741  1.00101.29           C  
ANISOU 1116  C   ALA A 171     5376  15762  17346   2090   -416    -49       C  
ATOM   1117  O   ALA A 171      45.019  33.699  12.852  1.00104.21           O  
ANISOU 1117  O   ALA A 171     5825  16098  17672   1985   -428    -65       O  
ATOM   1118  CB  ALA A 171      41.954  32.787  12.182  1.00 94.87           C  
ANISOU 1118  CB  ALA A 171     4477  15288  16280   2074   -464     40       C  
ATOM   1119  N   CYS A 172      43.772  35.435  12.145  1.00 97.17           N  
ANISOU 1119  N   CYS A 172     4827  15104  16988   2203   -414    -30       N  
ATOM   1120  CA  CYS A 172      44.943  36.171  11.676  1.00 95.92           C  
ANISOU 1120  CA  CYS A 172     4726  14740  16980   2204   -418    -26       C  
ATOM   1121  C   CYS A 172      45.787  36.654  12.848  1.00 99.46           C  
ANISOU 1121  C   CYS A 172     5190  15060  17538   2182   -366   -153       C  
ATOM   1122  O   CYS A 172      47.013  36.479  12.861  1.00103.88           O  
ANISOU 1122  O   CYS A 172     5819  15530  18120   2096   -377   -179       O  
ATOM   1123  CB  CYS A 172      44.513  37.346  10.798  1.00103.31           C  
ANISOU 1123  CB  CYS A 172     5621  15552  18079   2340   -418     41       C  
ATOM   1124  SG  CYS A 172      43.827  36.871   9.194  1.00114.76           S  
ANISOU 1124  SG  CYS A 172     7067  17114  19422   2372   -497    185       S  
ATOM   1125  N   LEU A 173      45.145  37.263  13.850  1.00102.83           N  
ANISOU 1125  N   LEU A 173     5552  15481  18037   2262   -313   -246       N  
ATOM   1126  CA  LEU A 173      45.861  37.664  15.056  1.00107.55           C  
ANISOU 1126  CA  LEU A 173     6158  15978  18726   2249   -271   -399       C  
ATOM   1127  C   LEU A 173      46.445  36.468  15.795  1.00101.82           C  
ANISOU 1127  C   LEU A 173     5484  15369  17833   2121   -280   -442       C  
ATOM   1128  O   LEU A 173      47.370  36.637  16.597  1.00 95.78           O  
ANISOU 1128  O   LEU A 173     4749  14518  17126   2085   -267   -565       O  
ATOM   1129  CB  LEU A 173      44.933  38.455  15.980  1.00107.18           C  
ANISOU 1129  CB  LEU A 173     6029  15928  18766   2370   -213   -495       C  
ATOM   1130  CG  LEU A 173      44.341  39.740  15.395  1.00109.96           C  
ANISOU 1130  CG  LEU A 173     6327  16150  19303   2511   -194   -464       C  
ATOM   1131  CD1 LEU A 173      43.454  40.440  16.413  1.00115.88           C  
ANISOU 1131  CD1 LEU A 173     6999  16906  20125   2628   -133   -574       C  
ATOM   1132  CD2 LEU A 173      45.441  40.672  14.906  1.00101.10           C  
ANISOU 1132  CD2 LEU A 173     5243  14779  18390   2517   -197   -482       C  
ATOM   1133  N   SER A 174      45.924  35.265  15.544  1.00 97.92           N  
ANISOU 1133  N   SER A 174     4998  15066  17140   2056   -303   -348       N  
ATOM   1134  CA  SER A 174      46.532  34.056  16.083  1.00 93.49           C  
ANISOU 1134  CA  SER A 174     4494  14604  16422   1930   -313   -359       C  
ATOM   1135  C   SER A 174      47.707  33.591  15.234  1.00 92.10           C  
ANISOU 1135  C   SER A 174     4408  14373  16212   1829   -365   -306       C  
ATOM   1136  O   SER A 174      48.628  32.950  15.754  1.00 91.05           O  
ANISOU 1136  O   SER A 174     4334  14246  16014   1735   -370   -349       O  
ATOM   1137  CB  SER A 174      45.488  32.943  16.180  1.00100.37           C  
ANISOU 1137  CB  SER A 174     5333  15688  17115   1898   -309   -276       C  
ATOM   1138  OG  SER A 174      44.350  33.375  16.905  1.00113.58           O  
ANISOU 1138  OG  SER A 174     6915  17414  18825   1996   -255   -310       O  
ATOM   1139  N   SER A 175      47.694  33.902  13.941  1.00 92.15           N  
ANISOU 1139  N   SER A 175     4426  14326  16261   1853   -403   -213       N  
ATOM   1140  CA  SER A 175      48.748  33.502  13.020  1.00 92.09           C  
ANISOU 1140  CA  SER A 175     4500  14263  16227   1771   -448   -152       C  
ATOM   1141  C   SER A 175      49.844  34.549  12.883  1.00 95.47           C  
ANISOU 1141  C   SER A 175     4951  14464  16857   1790   -437   -196       C  
ATOM   1142  O   SER A 175      50.795  34.330  12.125  1.00 90.55           O  
ANISOU 1142  O   SER A 175     4393  13775  16239   1728   -465   -141       O  
ATOM   1143  CB  SER A 175      48.154  33.198  11.642  1.00 91.34           C  
ANISOU 1143  CB  SER A 175     4403  14237  16064   1792   -497    -28       C  
ATOM   1144  OG  SER A 175      47.123  32.232  11.737  1.00 90.61           O  
ANISOU 1144  OG  SER A 175     4280  14349  15799   1770   -511     -2       O  
ATOM   1145  N   LEU A 176      49.730  35.678  13.583  1.00104.43           N  
ANISOU 1145  N   LEU A 176     6034  15474  18170   1874   -393   -294       N  
ATOM   1146  CA  LEU A 176      50.793  36.679  13.546  1.00 99.94           C  
ANISOU 1146  CA  LEU A 176     5479  14676  17816   1884   -378   -353       C  
ATOM   1147  C   LEU A 176      52.155  36.139  13.975  1.00 92.13           C  
ANISOU 1147  C   LEU A 176     4559  13652  16793   1765   -394   -421       C  
ATOM   1148  O   LEU A 176      53.149  36.467  13.302  1.00106.06           O  
ANISOU 1148  O   LEU A 176     6361  15270  18668   1731   -404   -384       O  
ATOM   1149  CB  LEU A 176      50.397  37.891  14.400  1.00 95.04           C  
ANISOU 1149  CB  LEU A 176     4789  13940  17384   1991   -330   -482       C  
ATOM   1150  CG  LEU A 176      49.264  38.761  13.854  1.00 96.52           C  
ANISOU 1150  CG  LEU A 176     4908  14094  17673   2127   -308   -413       C  
ATOM   1151  CD1 LEU A 176      49.063  39.986  14.731  1.00 98.26           C  
ANISOU 1151  CD1 LEU A 176     5067  14172  18096   2228   -257   -558       C  
ATOM   1152  CD2 LEU A 176      49.543  39.166  12.415  1.00 96.65           C  
ANISOU 1152  CD2 LEU A 176     4945  13996  17782   2151   -325   -260       C  
ATOM   1153  N   PRO A 177      52.291  35.345  15.046  1.00 96.02           N  
ANISOU 1153  N   PRO A 177     5069  14266  17148   1703   -394   -512       N  
ATOM   1154  CA  PRO A 177      53.617  34.779  15.349  1.00 99.42           C  
ANISOU 1154  CA  PRO A 177     5568  14670  17536   1592   -416   -563       C  
ATOM   1155  C   PRO A 177      54.158  33.897  14.239  1.00 97.00           C  
ANISOU 1155  C   PRO A 177     5335  14409  17112   1504   -455   -421       C  
ATOM   1156  O   PRO A 177      55.375  33.875  14.015  1.00 88.25           O  
ANISOU 1156  O   PRO A 177     4278  13201  16053   1436   -469   -431       O  
ATOM   1157  CB  PRO A 177      53.376  33.983  16.641  1.00 98.65           C  
ANISOU 1157  CB  PRO A 177     5468  14728  17285   1562   -406   -656       C  
ATOM   1158  CG  PRO A 177      51.906  33.742  16.677  1.00 90.34           C  
ANISOU 1158  CG  PRO A 177     4362  13821  16142   1625   -385   -592       C  
ATOM   1159  CD  PRO A 177      51.302  34.965  16.071  1.00 91.74           C  
ANISOU 1159  CD  PRO A 177     4482  13879  16497   1737   -369   -571       C  
ATOM   1160  N   THR A 178      53.289  33.173  13.531  1.00100.78           N  
ANISOU 1160  N   THR A 178     5816  15035  17440   1505   -473   -298       N  
ATOM   1161  CA  THR A 178      53.716  32.412  12.363  1.00 95.90           C  
ANISOU 1161  CA  THR A 178     5263  14456  16720   1439   -513   -176       C  
ATOM   1162  C   THR A 178      53.979  33.305  11.157  1.00 88.06           C  
ANISOU 1162  C   THR A 178     4266  13305  15889   1495   -516    -90       C  
ATOM   1163  O   THR A 178      54.491  32.819  10.144  1.00 89.77           O  
ANISOU 1163  O   THR A 178     4535  13522  16050   1451   -545      7       O  
ATOM   1164  CB  THR A 178      52.664  31.356  12.010  1.00105.42           C  
ANISOU 1164  CB  THR A 178     6464  15869  17721   1426   -537    -98       C  
ATOM   1165  OG1 THR A 178      52.063  30.861  13.213  1.00123.60           O  
ANISOU 1165  OG1 THR A 178     8737  18298  19930   1415   -512   -162       O  
ATOM   1166  CG2 THR A 178      53.303  30.188  11.267  1.00 87.53           C  
ANISOU 1166  CG2 THR A 178     4279  13677  15300   1324   -580    -28       C  
ATOM   1167  N   PHE A 179      53.641  34.591  11.238  1.00 94.05           N  
ANISOU 1167  N   PHE A 179     4961  13923  16852   1597   -483   -117       N  
ATOM   1168  CA  PHE A 179      53.943  35.537  10.173  1.00103.86           C  
ANISOU 1168  CA  PHE A 179     6194  14989  18279   1659   -472    -24       C  
ATOM   1169  C   PHE A 179      55.206  36.341  10.436  1.00107.55           C  
ANISOU 1169  C   PHE A 179     6671  15236  18958   1633   -442    -88       C  
ATOM   1170  O   PHE A 179      55.854  36.786   9.483  1.00108.09           O  
ANISOU 1170  O   PHE A 179     6755  15163  19151   1640   -432     12       O  
ATOM   1171  CB  PHE A 179      52.766  36.499   9.968  1.00120.03           C  
ANISOU 1171  CB  PHE A 179     8164  17003  20440   1797   -449      7       C  
ATOM   1172  CG  PHE A 179      52.931  37.421   8.791  1.00126.44           C  
ANISOU 1172  CG  PHE A 179     8964  17646  21429   1877   -433    135       C  
ATOM   1173  CD1 PHE A 179      52.596  37.002   7.513  1.00123.19           C  
ANISOU 1173  CD1 PHE A 179     8574  17309  20923   1902   -469    290       C  
ATOM   1174  CD2 PHE A 179      53.413  38.709   8.963  1.00121.29           C  
ANISOU 1174  CD2 PHE A 179     8278  16760  21047   1932   -382    100       C  
ATOM   1175  CE1 PHE A 179      52.744  37.848   6.429  1.00117.10           C  
ANISOU 1175  CE1 PHE A 179     7792  16389  20312   1987   -449    426       C  
ATOM   1176  CE2 PHE A 179      53.565  39.559   7.883  1.00110.78           C  
ANISOU 1176  CE2 PHE A 179     6935  15267  19889   2010   -355    239       C  
ATOM   1177  CZ  PHE A 179      53.230  39.128   6.615  1.00109.93           C  
ANISOU 1177  CZ  PHE A 179     6852  15244  19674   2041   -387    411       C  
ATOM   1178  N   TYR A 180      55.578  36.525  11.702  1.00 90.78           N  
ANISOU 1178  N   TYR A 180     4533  13079  16880   1604   -428   -255       N  
ATOM   1179  CA  TYR A 180      56.731  37.347  12.041  1.00 91.40           C  
ANISOU 1179  CA  TYR A 180     4606  12943  17177   1581   -405   -348       C  
ATOM   1180  C   TYR A 180      58.024  36.549  12.138  1.00100.76           C  
ANISOU 1180  C   TYR A 180     5862  14142  18281   1454   -431   -370       C  
ATOM   1181  O   TYR A 180      59.105  37.114  11.934  1.00 98.19           O  
ANISOU 1181  O   TYR A 180     5541  13633  18132   1422   -417   -387       O  
ATOM   1182  CB  TYR A 180      56.477  38.081  13.362  1.00 92.59           C  
ANISOU 1182  CB  TYR A 180     4697  13040  17443   1630   -382   -543       C  
ATOM   1183  CG  TYR A 180      57.461  39.193  13.648  1.00 96.46           C  
ANISOU 1183  CG  TYR A 180     5157  13279  18213   1632   -357   -655       C  
ATOM   1184  CD1 TYR A 180      57.272  40.465  13.121  1.00 95.37           C  
ANISOU 1184  CD1 TYR A 180     4965  12935  18335   1723   -313   -616       C  
ATOM   1185  CD2 TYR A 180      58.575  38.974  14.447  1.00103.57           C  
ANISOU 1185  CD2 TYR A 180     6081  14145  19126   1544   -377   -801       C  
ATOM   1186  CE1 TYR A 180      58.168  41.486  13.380  1.00 96.56           C  
ANISOU 1186  CE1 TYR A 180     5082  12842  18765   1719   -286   -721       C  
ATOM   1187  CE2 TYR A 180      59.477  39.988  14.711  1.00109.82           C  
ANISOU 1187  CE2 TYR A 180     6837  14704  20186   1540   -359   -919       C  
ATOM   1188  CZ  TYR A 180      59.269  41.242  14.175  1.00112.12           C  
ANISOU 1188  CZ  TYR A 180     7071  14783  20747   1624   -312   -879       C  
ATOM   1189  OH  TYR A 180      60.165  42.254  14.437  1.00108.36           O  
ANISOU 1189  OH  TYR A 180     6552  14061  20559   1615   -291   -999       O  
ATOM   1190  N   PHE A 181      57.946  35.249  12.436  1.00 81.34           N  
ANISOU 1190  N   PHE A 181     5388  12693  12824   2096    128  -1652       N  
ATOM   1191  CA  PHE A 181      59.138  34.437  12.634  1.00 76.38           C  
ANISOU 1191  CA  PHE A 181     4828  12090  12103   2078     32  -1744       C  
ATOM   1192  C   PHE A 181      59.397  33.423  11.530  1.00 67.91           C  
ANISOU 1192  C   PHE A 181     3803  10980  11020   2062    -90  -1682       C  
ATOM   1193  O   PHE A 181      60.549  33.013  11.356  1.00 79.47           O  
ANISOU 1193  O   PHE A 181     5340  12439  12415   2049   -166  -1774       O  
ATOM   1194  CB  PHE A 181      59.061  33.691  13.975  1.00 69.46           C  
ANISOU 1194  CB  PHE A 181     3899  11320  11173   2086     17  -1793       C  
ATOM   1195  CG  PHE A 181      59.127  34.592  15.175  1.00 70.42           C  
ANISOU 1195  CG  PHE A 181     3979  11504  11272   2100    118  -1917       C  
ATOM   1196  CD1 PHE A 181      60.330  35.156  15.567  1.00 70.38           C  
ANISOU 1196  CD1 PHE A 181     4026  11520  11195   2095    126  -2094       C  
ATOM   1197  CD2 PHE A 181      57.990  34.868  15.915  1.00 81.94           C  
ANISOU 1197  CD2 PHE A 181     5348  13005  12781   2115    206  -1862       C  
ATOM   1198  CE1 PHE A 181      60.396  35.982  16.672  1.00 71.35           C  
ANISOU 1198  CE1 PHE A 181     4109  11707  11293   2103    219  -2218       C  
ATOM   1199  CE2 PHE A 181      58.050  35.694  17.021  1.00 77.50           C  
ANISOU 1199  CE2 PHE A 181     4749  12504  12195   2124    302  -1982       C  
ATOM   1200  CZ  PHE A 181      59.255  36.251  17.400  1.00 72.34           C  
ANISOU 1200  CZ  PHE A 181     4145  11874  11466   2117    308  -2163       C  
ATOM   1201  N   ARG A 182      58.373  33.006  10.790  1.00 67.93           N  
ANISOU 1201  N   ARG A 182     3766  10959  11087   2060   -110  -1534       N  
ATOM   1202  CA  ARG A 182      58.548  32.010   9.737  1.00 67.25           C  
ANISOU 1202  CA  ARG A 182     3718  10841  10991   2040   -224  -1477       C  
ATOM   1203  C   ARG A 182      59.405  32.594   8.620  1.00 82.44           C  
ANISOU 1203  C   ARG A 182     5716  12702  12906   2038   -251  -1556       C  
ATOM   1204  O   ARG A 182      58.970  33.500   7.903  1.00 66.91           O  
ANISOU 1204  O   ARG A 182     3731  10694  10997   2054   -197  -1524       O  
ATOM   1205  CB  ARG A 182      57.190  31.561   9.208  1.00 67.56           C  
ANISOU 1205  CB  ARG A 182     3688  10878  11103   2038   -230  -1311       C  
ATOM   1206  CG  ARG A 182      57.251  30.513   8.108  1.00 67.00           C  
ANISOU 1206  CG  ARG A 182     3648  10781  11027   2013   -344  -1252       C  
ATOM   1207  CD  ARG A 182      57.799  29.190   8.620  1.00 73.82           C  
ANISOU 1207  CD  ARG A 182     4538  11674  11836   1991   -428  -1262       C  
ATOM   1208  NE  ARG A 182      56.975  28.623   9.685  1.00 67.25           N  
ANISOU 1208  NE  ARG A 182     3630  10896  11028   1994   -398  -1176       N  
ATOM   1209  CZ  ARG A 182      57.195  27.440  10.250  1.00 67.36           C  
ANISOU 1209  CZ  ARG A 182     3634  10948  11013   1986   -462  -1173       C  
ATOM   1210  NH1 ARG A 182      56.394  27.004  11.213  1.00 75.89           N  
ANISOU 1210  NH1 ARG A 182     4624  12087  12123   2000   -433  -1127       N  
ATOM   1211  NH2 ARG A 182      58.215  26.691   9.853  1.00 66.66           N  
ANISOU 1211  NH2 ARG A 182     3620  10841  10868   1968   -551  -1219       N  
ATOM   1212  N   ASP A 183      60.623  32.079   8.469  1.00 85.68           N  
ANISOU 1212  N   ASP A 183     6207  13103  13244   2022   -332  -1653       N  
ATOM   1213  CA  ASP A 183      61.543  32.555   7.446  1.00 93.58           C  
ANISOU 1213  CA  ASP A 183     7283  14044  14231   2019   -363  -1734       C  
ATOM   1214  C   ASP A 183      62.485  31.419   7.070  1.00 94.19           C  
ANISOU 1214  C   ASP A 183     7435  14115  14240   1995   -483  -1774       C  
ATOM   1215  O   ASP A 183      62.543  30.384   7.738  1.00 91.61           O  
ANISOU 1215  O   ASP A 183     7103  13834  13872   1985   -531  -1753       O  
ATOM   1216  CB  ASP A 183      62.325  33.783   7.929  1.00106.02           C  
ANISOU 1216  CB  ASP A 183     8882  15608  15791   2031   -286  -1878       C  
ATOM   1217  CG  ASP A 183      62.892  34.603   6.786  1.00119.43           C  
ANISOU 1217  CG  ASP A 183    10630  17234  17516   2035   -280  -1926       C  
ATOM   1218  OD1 ASP A 183      62.998  34.069   5.661  1.00120.17           O  
ANISOU 1218  OD1 ASP A 183    10757  17290  17610   2026   -357  -1877       O  
ATOM   1219  OD2 ASP A 183      63.233  35.783   7.014  1.00123.13           O  
ANISOU 1219  OD2 ASP A 183    11098  17681  18006   2047   -196  -2012       O  
ATOM   1220  N   VAL A 184      63.225  31.624   5.984  1.00 91.27           N  
ANISOU 1220  N   VAL A 184     7132  13688  13860   1988   -526  -1827       N  
ATOM   1221  CA  VAL A 184      64.187  30.642   5.497  1.00 80.45           C  
ANISOU 1221  CA  VAL A 184     5839  12300  12426   1966   -635  -1873       C  
ATOM   1222  C   VAL A 184      65.544  30.922   6.128  1.00 62.98           C  
ANISOU 1222  C   VAL A 184     3692  10098  10139   1966   -640  -2034       C  
ATOM   1223  O   VAL A 184      66.048  32.050   6.070  1.00 66.38           O  
ANISOU 1223  O   VAL A 184     4142  10502  10578   1975   -583  -2130       O  
ATOM   1224  CB  VAL A 184      64.279  30.672   3.962  1.00 62.86           C  
ANISOU 1224  CB  VAL A 184     3650  10010  10224   1959   -681  -1847       C  
ATOM   1225  CG1 VAL A 184      65.434  29.807   3.482  1.00 62.07           C  
ANISOU 1225  CG1 VAL A 184     3640   9886  10056   1936   -783  -1921       C  
ATOM   1226  CG2 VAL A 184      62.973  30.204   3.345  1.00100.89           C  
ANISOU 1226  CG2 VAL A 184     8400  14832  15100   1956   -693  -1692       C  
ATOM   1227  N   ARG A 185      66.133  29.894   6.735  1.00 62.72           N  
ANISOU 1227  N   ARG A 185     3687  10106  10037   1956   -705  -2063       N  
ATOM   1228  CA  ARG A 185      67.466  29.978   7.311  1.00 62.42           C  
ANISOU 1228  CA  ARG A 185     3712  10089   9916   1956   -724  -2212       C  
ATOM   1229  C   ARG A 185      68.304  28.811   6.809  1.00 66.99           C  
ANISOU 1229  C   ARG A 185     4363  10651  10439   1939   -833  -2227       C  
ATOM   1230  O   ARG A 185      67.785  27.727   6.527  1.00 73.06           O  
ANISOU 1230  O   ARG A 185     5115  11419  11224   1927   -887  -2116       O  
ATOM   1231  CB  ARG A 185      67.424  29.970   8.846  1.00 63.01           C  
ANISOU 1231  CB  ARG A 185     3740  10254   9947   1971   -679  -2243       C  
ATOM   1232  CG  ARG A 185      66.665  31.137   9.457  1.00 63.78           C  
ANISOU 1232  CG  ARG A 185     3767  10371  10095   1987   -564  -2246       C  
ATOM   1233  CD  ARG A 185      67.283  32.469   9.065  1.00 63.75           C  
ANISOU 1233  CD  ARG A 185     3797  10318  10108   1987   -511  -2369       C  
ATOM   1234  NE  ARG A 185      66.531  33.596   9.608  1.00 68.15           N  
ANISOU 1234  NE  ARG A 185     4284  10885  10723   2001   -393  -2367       N  
ATOM   1235  CZ  ARG A 185      66.836  34.872   9.395  1.00 82.03           C  
ANISOU 1235  CZ  ARG A 185     6050  12600  12520   2003   -321  -2456       C  
ATOM   1236  NH1 ARG A 185      67.884  35.189   8.647  1.00103.65           N  
ANISOU 1236  NH1 ARG A 185     8859  15281  15242   1991   -358  -2553       N  
ATOM   1237  NH2 ARG A 185      66.094  35.831   9.931  1.00 70.30           N  
ANISOU 1237  NH2 ARG A 185     4497  11122  11091   2016   -210  -2446       N  
ATOM   1238  N   THR A 186      69.608  29.046   6.697  1.00 76.86           N  
ANISOU 1238  N   THR A 186     5690  11884  11628   1935   -862  -2366       N  
ATOM   1239  CA  THR A 186      70.537  28.028   6.229  1.00 60.56           C  
ANISOU 1239  CA  THR A 186     3701   9799   9508   1921   -959  -2396       C  
ATOM   1240  C   THR A 186      70.994  27.170   7.401  1.00 60.72           C  
ANISOU 1240  C   THR A 186     3717   9900   9454   1931   -987  -2411       C  
ATOM   1241  O   THR A 186      71.373  27.693   8.453  1.00 61.09           O  
ANISOU 1241  O   THR A 186     3747  10012   9452   1947   -943  -2496       O  
ATOM   1242  CB  THR A 186      71.744  28.669   5.541  1.00 59.98           C  
ANISOU 1242  CB  THR A 186     3712   9670   9406   1915   -977  -2537       C  
ATOM   1243  OG1 THR A 186      71.315  29.353   4.357  1.00 59.85           O  
ANISOU 1243  OG1 THR A 186     3698   9581   9463   1910   -956  -2503       O  
ATOM   1244  CG2 THR A 186      72.764  27.611   5.158  1.00 59.31           C  
ANISOU 1244  CG2 THR A 186     3708   9567   9260   1902  -1072  -2577       C  
ATOM   1245  N   ILE A 187      70.945  25.854   7.217  1.00 60.53           N  
ANISOU 1245  N   ILE A 187     3701   9874   9421   1921  -1058  -2325       N  
ATOM   1246  CA  ILE A 187      71.431  24.891   8.197  1.00 60.68           C  
ANISOU 1246  CA  ILE A 187     3718   9964   9375   1932  -1093  -2318       C  
ATOM   1247  C   ILE A 187      72.611  24.168   7.564  1.00 69.40           C  
ANISOU 1247  C   ILE A 187     4913  11027  10430   1921  -1176  -2379       C  
ATOM   1248  O   ILE A 187      72.433  23.366   6.636  1.00 66.93           O  
ANISOU 1248  O   ILE A 187     4622  10653  10154   1899  -1231  -2308       O  
ATOM   1249  CB  ILE A 187      70.339  23.904   8.630  1.00 61.20           C  
ANISOU 1249  CB  ILE A 187     3703  10062   9486   1932  -1098  -2151       C  
ATOM   1250  CG1 ILE A 187      69.128  24.663   9.174  1.00 61.87           C  
ANISOU 1250  CG1 ILE A 187     3700  10181   9628   1943  -1011  -2090       C  
ATOM   1251  CG2 ILE A 187      70.877  22.942   9.675  1.00 61.45           C  
ANISOU 1251  CG2 ILE A 187     3725  10170   9453   1950  -1128  -2134       C  
ATOM   1252  CD1 ILE A 187      67.984  23.770   9.595  1.00 62.42           C  
ANISOU 1252  CD1 ILE A 187     3684  10280   9752   1942  -1009  -1925       C  
ATOM   1253  N   GLU A 188      73.818  24.455   8.058  1.00 59.81           N  
ANISOU 1253  N   GLU A 188     3749   9845   9131   1934  -1183  -2516       N  
ATOM   1254  CA  GLU A 188      75.023  23.906   7.447  1.00 59.13           C  
ANISOU 1254  CA  GLU A 188     3755   9716   8997   1926  -1255  -2590       C  
ATOM   1255  C   GLU A 188      75.220  22.436   7.793  1.00 59.20           C  
ANISOU 1255  C   GLU A 188     3761   9753   8981   1929  -1315  -2503       C  
ATOM   1256  O   GLU A 188      75.672  21.656   6.946  1.00 58.70           O  
ANISOU 1256  O   GLU A 188     3753   9625   8925   1911  -1378  -2491       O  
ATOM   1257  CB  GLU A 188      76.248  24.715   7.873  1.00 71.75           C  
ANISOU 1257  CB  GLU A 188     5405  11344  10515   1939  -1242  -2769       C  
ATOM   1258  CG  GLU A 188      76.340  26.091   7.242  1.00 70.68           C  
ANISOU 1258  CG  GLU A 188     5291  11151  10413   1927  -1197  -2869       C  
ATOM   1259  CD  GLU A 188      77.709  26.715   7.420  1.00 76.74           C  
ANISOU 1259  CD  GLU A 188     6121  11927  11108   1931  -1204  -3052       C  
ATOM   1260  OE1 GLU A 188      78.574  26.076   8.056  1.00 73.72           O  
ANISOU 1260  OE1 GLU A 188     5766  11604  10641   1945  -1242  -3103       O  
ATOM   1261  OE2 GLU A 188      77.922  27.840   6.922  1.00 86.37           O  
ANISOU 1261  OE2 GLU A 188     7360  13098  12361   1918  -1169  -3142       O  
ATOM   1262  N   TYR A 189      74.902  22.038   9.029  1.00 59.88           N  
ANISOU 1262  N   TYR A 189     3778   9934   9039   1953  -1294  -2440       N  
ATOM   1263  CA  TYR A 189      75.075  20.639   9.406  1.00 60.06           C  
ANISOU 1263  CA  TYR A 189     3787   9985   9047   1960  -1346  -2342       C  
ATOM   1264  C   TYR A 189      74.205  19.723   8.559  1.00 59.98           C  
ANISOU 1264  C   TYR A 189     3754   9904   9132   1929  -1380  -2198       C  
ATOM   1265  O   TYR A 189      74.594  18.585   8.274  1.00 59.83           O  
ANISOU 1265  O   TYR A 189     3757   9858   9116   1919  -1440  -2146       O  
ATOM   1266  CB  TYR A 189      74.766  20.435  10.888  1.00 61.12           C  
ANISOU 1266  CB  TYR A 189     3831  10250   9140   2003  -1318  -2315       C  
ATOM   1267  CG  TYR A 189      74.912  18.995  11.321  1.00 61.58           C  
ANISOU 1267  CG  TYR A 189     3859  10350   9191   2022  -1373  -2220       C  
ATOM   1268  CD1 TYR A 189      76.167  18.437  11.527  1.00 61.43           C  
ANISOU 1268  CD1 TYR A 189     3893  10356   9090   2040  -1422  -2280       C  
ATOM   1269  CD2 TYR A 189      73.797  18.189  11.511  1.00 62.23           C  
ANISOU 1269  CD2 TYR A 189     3854  10440   9351   2023  -1373  -2066       C  
ATOM   1270  CE1 TYR A 189      76.308  17.119  11.914  1.00 61.93           C  
ANISOU 1270  CE1 TYR A 189     3922  10454   9154   2061  -1469  -2182       C  
ATOM   1271  CE2 TYR A 189      73.929  16.869  11.899  1.00 62.74           C  
ANISOU 1271  CE2 TYR A 189     3882  10537   9421   2042  -1420  -1972       C  
ATOM   1272  CZ  TYR A 189      75.186  16.340  12.100  1.00 62.60           C  
ANISOU 1272  CZ  TYR A 189     3917  10544   9324   2062  -1467  -2027       C  
ATOM   1273  OH  TYR A 189      75.324  15.028  12.488  1.00 63.18           O  
ANISOU 1273  OH  TYR A 189     3948  10648   9411   2084  -1510  -1925       O  
ATOM   1274  N   LEU A 190      73.030  20.193   8.150  1.00 60.14           N  
ANISOU 1274  N   LEU A 190     3726   9896   9230   1913  -1343  -2134       N  
ATOM   1275  CA  LEU A 190      72.200  19.459   7.210  1.00 60.08           C  
ANISOU 1275  CA  LEU A 190     3698   9822   9307   1881  -1375  -2019       C  
ATOM   1276  C   LEU A 190      72.481  19.834   5.762  1.00 59.39           C  
ANISOU 1276  C   LEU A 190     3684   9641   9239   1854  -1403  -2089       C  
ATOM   1277  O   LEU A 190      71.999  19.145   4.856  1.00 59.29           O  
ANISOU 1277  O   LEU A 190     3669   9575   9285   1826  -1442  -2017       O  
ATOM   1278  CB  LEU A 190      70.717  19.691   7.520  1.00 60.71           C  
ANISOU 1278  CB  LEU A 190     3679   9928   9461   1880  -1320  -1903       C  
ATOM   1279  CG  LEU A 190      70.261  19.311   8.929  1.00 61.48           C  
ANISOU 1279  CG  LEU A 190     3691  10116   9553   1907  -1285  -1816       C  
ATOM   1280  CD1 LEU A 190      68.794  19.653   9.129  1.00 62.14           C  
ANISOU 1280  CD1 LEU A 190     3679  10218   9714   1909  -1230  -1724       C  
ATOM   1281  CD2 LEU A 190      70.511  17.836   9.193  1.00 61.81           C  
ANISOU 1281  CD2 LEU A 190     3711  10174   9598   1911  -1346  -1741       C  
ATOM   1282  N   GLY A 191      73.257  20.892   5.528  1.00 73.62           N  
ANISOU 1282  N   GLY A 191     5549  11425  10997   1864  -1385  -2229       N  
ATOM   1283  CA  GLY A 191      73.520  21.373   4.185  1.00 76.33           C  
ANISOU 1283  CA  GLY A 191     5958  11683  11362   1844  -1404  -2293       C  
ATOM   1284  C   GLY A 191      72.238  21.685   3.445  1.00 58.59           C  
ANISOU 1284  C   GLY A 191     3658   9408   9198   1829  -1379  -2202       C  
ATOM   1285  O   GLY A 191      72.064  21.286   2.289  1.00 58.33           O  
ANISOU 1285  O   GLY A 191     3647   9314   9201   1805  -1420  -2174       O  
ATOM   1286  N   VAL A 192      71.332  22.402   4.104  1.00 63.06           N  
ANISOU 1286  N   VAL A 192     4149  10020   9793   1843  -1311  -2156       N  
ATOM   1287  CA  VAL A 192      69.964  22.548   3.619  1.00 59.53           C  
ANISOU 1287  CA  VAL A 192     3631   9563   9426   1833  -1284  -2044       C  
ATOM   1288  C   VAL A 192      69.433  23.917   4.022  1.00 73.20           C  
ANISOU 1288  C   VAL A 192     5318  11317  11178   1854  -1198  -2063       C  
ATOM   1289  O   VAL A 192      69.565  24.328   5.179  1.00 60.21           O  
ANISOU 1289  O   VAL A 192     3646   9730   9501   1876  -1150  -2097       O  
ATOM   1290  CB  VAL A 192      69.064  21.422   4.169  1.00 60.08           C  
ANISOU 1290  CB  VAL A 192     3623   9671   9533   1824  -1298  -1903       C  
ATOM   1291  CG1 VAL A 192      67.631  21.883   4.266  1.00 60.93           C  
ANISOU 1291  CG1 VAL A 192     3639   9801   9711   1827  -1241  -1802       C  
ATOM   1292  CG2 VAL A 192      69.165  20.181   3.294  1.00 59.84           C  
ANISOU 1292  CG2 VAL A 192     3619   9596   9523   1793  -1376  -1859       C  
ATOM   1293  N   ASN A 193      68.836  24.625   3.062  1.00 77.56           N  
ANISOU 1293  N   ASN A 193     5859  11828  11784   1850  -1174  -2039       N  
ATOM   1294  CA  ASN A 193      68.095  25.852   3.345  1.00 60.35           C  
ANISOU 1294  CA  ASN A 193     3621   9665   9646   1870  -1086  -2025       C  
ATOM   1295  C   ASN A 193      66.684  25.471   3.774  1.00 61.03           C  
ANISOU 1295  C   ASN A 193     3609   9792   9790   1870  -1057  -1882       C  
ATOM   1296  O   ASN A 193      65.876  25.028   2.952  1.00 61.15           O  
ANISOU 1296  O   ASN A 193     3593   9787   9855   1854  -1083  -1787       O  
ATOM   1297  CB  ASN A 193      68.064  26.764   2.123  1.00 60.15           C  
ANISOU 1297  CB  ASN A 193     3618   9580   9656   1872  -1069  -2046       C  
ATOM   1298  CG  ASN A 193      69.367  27.505   1.915  1.00 66.19           C  
ANISOU 1298  CG  ASN A 193     4463  10309  10376   1878  -1067  -2193       C  
ATOM   1299  OD1 ASN A 193      70.091  27.791   2.868  1.00 71.83           O  
ANISOU 1299  OD1 ASN A 193     5198  11054  11042   1887  -1046  -2288       O  
ATOM   1300  ND2 ASN A 193      69.670  27.826   0.663  1.00 75.64           N  
ANISOU 1300  ND2 ASN A 193     5705  11447  11589   1873  -1089  -2215       N  
ATOM   1301  N   ALA A 194      66.382  25.643   5.056  1.00 61.53           N  
ANISOU 1301  N   ALA A 194     3618   9914   9845   1887  -1003  -1868       N  
ATOM   1302  CA  ALA A 194      65.126  25.186   5.630  1.00 62.19           C  
ANISOU 1302  CA  ALA A 194     3607  10040   9980   1888   -976  -1735       C  
ATOM   1303  C   ALA A 194      64.200  26.362   5.905  1.00 62.74           C  
ANISOU 1303  C   ALA A 194     3611  10125  10104   1908   -879  -1705       C  
ATOM   1304  O   ALA A 194      64.652  27.450   6.279  1.00 62.78           O  
ANISOU 1304  O   ALA A 194     3631  10133  10090   1927   -819  -1800       O  
ATOM   1305  CB  ALA A 194      65.370  24.401   6.922  1.00 62.44           C  
ANISOU 1305  CB  ALA A 194     3618  10137   9971   1896   -984  -1721       C  
ATOM   1306  N   CYS A 195      62.902  26.135   5.714  1.00 63.23           N  
ANISOU 1306  N   CYS A 195     3596  10194  10235   1903   -861  -1575       N  
ATOM   1307  CA  CYS A 195      61.868  27.119   6.029  1.00 68.67           C  
ANISOU 1307  CA  CYS A 195     4209  10900  10982   1924   -766  -1523       C  
ATOM   1308  C   CYS A 195      61.412  26.854   7.460  1.00 68.37           C  
ANISOU 1308  C   CYS A 195     4107  10927  10943   1935   -721  -1483       C  
ATOM   1309  O   CYS A 195      60.591  25.968   7.710  1.00 64.79           O  
ANISOU 1309  O   CYS A 195     3594  10498  10524   1925   -738  -1369       O  
ATOM   1310  CB  CYS A 195      60.722  27.025   5.026  1.00 64.12           C  
ANISOU 1310  CB  CYS A 195     3582  10304  10477   1915   -773  -1406       C  
ATOM   1311  SG  CYS A 195      59.178  27.866   5.468  1.00 68.60           S  
ANISOU 1311  SG  CYS A 195     4037  10900  11126   1938   -664  -1298       S  
ATOM   1312  N   ILE A 196      61.959  27.618   8.405  1.00 74.80           N  
ANISOU 1312  N   ILE A 196     4930  11772  11717   1956   -661  -1580       N  
ATOM   1313  CA  ILE A 196      61.751  27.363   9.827  1.00 65.12           C  
ANISOU 1313  CA  ILE A 196     3652  10619  10473   1970   -621  -1564       C  
ATOM   1314  C   ILE A 196      61.124  28.576  10.500  1.00 79.15           C  
ANISOU 1314  C   ILE A 196     5370  12420  12283   1994   -507  -1584       C  
ATOM   1315  O   ILE A 196      60.736  29.542   9.835  1.00 80.67           O  
ANISOU 1315  O   ILE A 196     5557  12568  12525   1998   -456  -1580       O  
ATOM   1316  CB  ILE A 196      63.076  26.996  10.517  1.00 64.93           C  
ANISOU 1316  CB  ILE A 196     3683  10638  10351   1979   -665  -1693       C  
ATOM   1317  CG1 ILE A 196      64.053  28.172  10.444  1.00 64.57           C  
ANISOU 1317  CG1 ILE A 196     3701  10571  10261   1984   -627  -1838       C  
ATOM   1318  CG2 ILE A 196      63.679  25.754   9.887  1.00 81.67           C  
ANISOU 1318  CG2 ILE A 196     5859  12729  12444   1956   -770  -1660       C  
ATOM   1319  CD1 ILE A 196      65.313  27.969  11.249  1.00 73.16           C  
ANISOU 1319  CD1 ILE A 196     4831  11721  11246   1997   -659  -1983       C  
ATOM   1320  N   MET A 197      61.021  28.529  11.827  1.00 78.78           N  
ANISOU 1320  N   MET A 197     5265  12460  12208   2018   -470  -1637       N  
ATOM   1321  CA  MET A 197      60.601  29.669  12.635  1.00 67.43           C  
ANISOU 1321  CA  MET A 197     3774  11059  10787   2041   -360  -1691       C  
ATOM   1322  C   MET A 197      61.860  30.370  13.134  1.00 67.33           C  
ANISOU 1322  C   MET A 197     3818  11074  10692   2049   -343  -1873       C  
ATOM   1323  O   MET A 197      62.552  29.860  14.021  1.00 67.63           O  
ANISOU 1323  O   MET A 197     3856  11194  10644   2062   -377  -1963       O  
ATOM   1324  CB  MET A 197      59.718  29.222  13.798  1.00 79.77           C  
ANISOU 1324  CB  MET A 197     5236  12710  12364   2061   -325  -1647       C  
ATOM   1325  CG  MET A 197      58.390  28.604  13.384  1.00 76.02           C  
ANISOU 1325  CG  MET A 197     4694  12210  11980   2052   -331  -1472       C  
ATOM   1326  SD  MET A 197      57.164  29.821  12.866  1.00 69.01           S  
ANISOU 1326  SD  MET A 197     3758  11268  11193   2055   -225  -1385       S  
ATOM   1327  CE  MET A 197      56.879  30.692  14.403  1.00 70.17           C  
ANISOU 1327  CE  MET A 197     3835  11499  11328   2085   -106  -1478       C  
ATOM   1328  N   ALA A 198      62.157  31.537  12.561  1.00 66.99           N  
ANISOU 1328  N   ALA A 198     3816  10966  10673   2042   -289  -1924       N  
ATOM   1329  CA  ALA A 198      63.403  32.248  12.846  1.00 76.03           C  
ANISOU 1329  CA  ALA A 198     5019  12119  11748   2042   -277  -2098       C  
ATOM   1330  C   ALA A 198      63.240  33.067  14.124  1.00 76.89           C  
ANISOU 1330  C   ALA A 198     5067  12308  11840   2061   -180  -2202       C  
ATOM   1331  O   ALA A 198      63.071  34.289  14.108  1.00 72.38           O  
ANISOU 1331  O   ALA A 198     4486  11700  11315   2061    -85  -2240       O  
ATOM   1332  CB  ALA A 198      63.801  33.124  11.665  1.00 83.21           C  
ANISOU 1332  CB  ALA A 198     5989  12929  12699   2031   -264  -2127       C  
ATOM   1333  N   PHE A 199      63.297  32.370  15.255  1.00 75.45           N  
ANISOU 1333  N   PHE A 199     4840  12240  11587   2078   -202  -2244       N  
ATOM   1334  CA  PHE A 199      63.317  33.037  16.544  1.00 75.14           C  
ANISOU 1334  CA  PHE A 199     4745  12301  11503   2095   -122  -2367       C  
ATOM   1335  C   PHE A 199      64.706  33.605  16.816  1.00 71.64           C  
ANISOU 1335  C   PHE A 199     4363  11886  10972   2088   -131  -2562       C  
ATOM   1336  O   PHE A 199      65.697  33.149  16.240  1.00 68.69           O  
ANISOU 1336  O   PHE A 199     4067  11484  10550   2078   -217  -2600       O  
ATOM   1337  CB  PHE A 199      62.928  32.067  17.656  1.00 76.72           C  
ANISOU 1337  CB  PHE A 199     4873  12630  11646   2121   -143  -2342       C  
ATOM   1338  CG  PHE A 199      61.545  31.500  17.520  1.00 82.68           C  
ANISOU 1338  CG  PHE A 199     5558  13364  12491   2126   -130  -2159       C  
ATOM   1339  CD1 PHE A 199      60.435  32.327  17.553  1.00 88.01           C  
ANISOU 1339  CD1 PHE A 199     6176  14005  13260   2126    -28  -2096       C  
ATOM   1340  CD2 PHE A 199      61.355  30.135  17.384  1.00 70.56           C  
ANISOU 1340  CD2 PHE A 199     4013  11844  10951   2130   -218  -2049       C  
ATOM   1341  CE1 PHE A 199      59.161  31.805  17.435  1.00 89.47           C  
ANISOU 1341  CE1 PHE A 199     6294  14176  13527   2129    -17  -1932       C  
ATOM   1342  CE2 PHE A 199      60.084  29.607  17.268  1.00 80.73           C  
ANISOU 1342  CE2 PHE A 199     5233  13114  12329   2131   -207  -1887       C  
ATOM   1343  CZ  PHE A 199      58.985  30.443  17.293  1.00 86.32           C  
ANISOU 1343  CZ  PHE A 199     5882  13791  13123   2130   -108  -1831       C  
ATOM   1344  N   PRO A 200      64.805  34.614  17.679  1.00 79.13           N  
ANISOU 1344  N   PRO A 200     5275  12889  11899   2090    -41  -2691       N  
ATOM   1345  CA  PRO A 200      66.122  35.110  18.091  1.00 89.53           C  
ANISOU 1345  CA  PRO A 200     6637  14255  13125   2081    -51  -2892       C  
ATOM   1346  C   PRO A 200      66.937  34.001  18.731  1.00 92.07           C  
ANISOU 1346  C   PRO A 200     6969  14703  13310   2101   -149  -2957       C  
ATOM   1347  O   PRO A 200      66.476  33.350  19.680  1.00 93.35           O  
ANISOU 1347  O   PRO A 200     7062  14988  13418   2130   -151  -2929       O  
ATOM   1348  CB  PRO A 200      65.782  36.212  19.105  1.00 87.28           C  
ANISOU 1348  CB  PRO A 200     6287  14032  12846   2080     69  -2997       C  
ATOM   1349  CG  PRO A 200      64.424  36.670  18.708  1.00 71.92           C  
ANISOU 1349  CG  PRO A 200     4295  12000  11032   2081    155  -2844       C  
ATOM   1350  CD  PRO A 200      63.712  35.443  18.216  1.00 71.88           C  
ANISOU 1350  CD  PRO A 200     4279  11979  11053   2096     81  -2660       C  
ATOM   1351  N   PRO A 201      68.149  33.748  18.230  1.00 85.27           N  
ANISOU 1351  N   PRO A 201     6191  13819  12390   2090   -231  -3035       N  
ATOM   1352  CA  PRO A 201      68.944  32.629  18.763  1.00 77.65           C  
ANISOU 1352  CA  PRO A 201     5238  12970  11294   2115   -327  -3079       C  
ATOM   1353  C   PRO A 201      69.305  32.774  20.231  1.00 82.51           C  
ANISOU 1353  C   PRO A 201     5793  13772  11783   2141   -300  -3227       C  
ATOM   1354  O   PRO A 201      69.625  31.766  20.874  1.00 71.44           O  
ANISOU 1354  O   PRO A 201     4373  12497  10274   2177   -363  -3223       O  
ATOM   1355  CB  PRO A 201      70.198  32.636  17.875  1.00 68.71           C  
ANISOU 1355  CB  PRO A 201     4211  11758  10137   2092   -399  -3153       C  
ATOM   1356  CG  PRO A 201      69.781  33.356  16.629  1.00 67.89           C  
ANISOU 1356  CG  PRO A 201     4147  11480  10167   2060   -360  -3072       C  
ATOM   1357  CD  PRO A 201      68.800  34.395  17.079  1.00 68.76           C  
ANISOU 1357  CD  PRO A 201     4184  11588  10353   2058   -239  -3065       C  
ATOM   1358  N   GLU A 202      69.263  33.989  20.784  1.00 80.02           N  
ANISOU 1358  N   GLU A 202     5444  13484  11476   2126   -207  -3353       N  
ATOM   1359  CA  GLU A 202      69.576  34.172  22.198  1.00 86.22           C  
ANISOU 1359  CA  GLU A 202     6166  14461  12133   2147   -178  -3503       C  
ATOM   1360  C   GLU A 202      68.556  33.465  23.083  1.00 93.66           C  
ANISOU 1360  C   GLU A 202     7016  15523  13046   2188   -155  -3397       C  
ATOM   1361  O   GLU A 202      68.921  32.723  24.003  1.00 95.01           O  
ANISOU 1361  O   GLU A 202     7151  15868  13079   2228   -198  -3435       O  
ATOM   1362  CB  GLU A 202      69.643  35.664  22.528  1.00 91.33           C  
ANISOU 1362  CB  GLU A 202     6793  15091  12817   2111    -75  -3652       C  
ATOM   1363  CG  GLU A 202      68.506  36.486  21.937  1.00 98.09           C  
ANISOU 1363  CG  GLU A 202     7632  15796  13843   2088     26  -3539       C  
ATOM   1364  CD  GLU A 202      68.489  37.911  22.449  1.00102.51           C  
ANISOU 1364  CD  GLU A 202     8160  16352  14439   2057    141  -3678       C  
ATOM   1365  OE1 GLU A 202      69.395  38.276  23.228  1.00103.21           O  
ANISOU 1365  OE1 GLU A 202     8239  16553  14423   2046    137  -3872       O  
ATOM   1366  OE2 GLU A 202      67.567  38.667  22.074  1.00105.84           O  
ANISOU 1366  OE2 GLU A 202     8561  16660  14994   2044    236  -3591       O  
ATOM   1367  N   LYS A 203      67.268  33.681  22.818  1.00 94.40           N  
ANISOU 1367  N   LYS A 203     7069  15530  13269   2181    -87  -3256       N  
ATOM   1368  CA  LYS A 203      66.206  33.032  23.576  1.00 82.10           C  
ANISOU 1368  CA  LYS A 203     5422  14067  11705   2215    -60  -3141       C  
ATOM   1369  C   LYS A 203      65.362  32.166  22.649  1.00 78.15           C  
ANISOU 1369  C   LYS A 203     4930  13445  11318   2216   -102  -2920       C  
ATOM   1370  O   LYS A 203      64.136  32.310  22.601  1.00 74.47           O  
ANISOU 1370  O   LYS A 203     4409  12932  10956   2213    -38  -2800       O  
ATOM   1371  CB  LYS A 203      65.332  34.071  24.281  1.00 76.13           C  
ANISOU 1371  CB  LYS A 203     4591  13338  10996   2206     70  -3180       C  
ATOM   1372  CG  LYS A 203      66.113  35.142  25.030  1.00 78.12           C  
ANISOU 1372  CG  LYS A 203     4839  13677  11167   2189    124  -3405       C  
ATOM   1373  CD  LYS A 203      67.016  34.536  26.092  1.00 88.38           C  
ANISOU 1373  CD  LYS A 203     6116  15194  12271   2224     64  -3531       C  
ATOM   1374  CE  LYS A 203      67.824  35.609  26.806  1.00 89.90           C  
ANISOU 1374  CE  LYS A 203     6300  15475  12381   2199    110  -3767       C  
ATOM   1375  NZ  LYS A 203      68.736  35.031  27.832  1.00 79.48           N  
ANISOU 1375  NZ  LYS A 203     4955  14388  10855   2237     47  -3893       N  
ATOM   1376  N   TYR A 204      66.014  31.266  21.909  1.00 76.64           N  
ANISOU 1376  N   TYR A 204     4806  13205  11109   2216   -209  -2869       N  
ATOM   1377  CA  TYR A 204      65.301  30.471  20.913  1.00 72.37           C  
ANISOU 1377  CA  TYR A 204     4279  12539  10679   2206   -255  -2672       C  
ATOM   1378  C   TYR A 204      64.415  29.419  21.570  1.00 89.03           C  
ANISOU 1378  C   TYR A 204     6306  14734  12789   2240   -263  -2537       C  
ATOM   1379  O   TYR A 204      63.270  29.215  21.148  1.00 92.09           O  
ANISOU 1379  O   TYR A 204     6655  15041  13293   2230   -240  -2384       O  
ATOM   1380  CB  TYR A 204      66.296  29.813  19.957  1.00 71.17           C  
ANISOU 1380  CB  TYR A 204     4224  12310  10506   2193   -364  -2665       C  
ATOM   1381  CG  TYR A 204      65.670  29.283  18.686  1.00 70.18           C  
ANISOU 1381  CG  TYR A 204     4130  12032  10503   2167   -404  -2490       C  
ATOM   1382  CD1 TYR A 204      65.050  28.040  18.657  1.00 70.26           C  
ANISOU 1382  CD1 TYR A 204     4102  12049  10543   2179   -455  -2334       C  
ATOM   1383  CD2 TYR A 204      65.705  30.023  17.512  1.00 69.25           C  
ANISOU 1383  CD2 TYR A 204     4075  11768  10469   2130   -391  -2480       C  
ATOM   1384  CE1 TYR A 204      64.477  27.553  17.497  1.00 69.45           C  
ANISOU 1384  CE1 TYR A 204     4024  11815  10547   2150   -494  -2185       C  
ATOM   1385  CE2 TYR A 204      65.134  29.545  16.347  1.00 68.44           C  
ANISOU 1385  CE2 TYR A 204     3997  11544  10462   2108   -430  -2325       C  
ATOM   1386  CZ  TYR A 204      64.522  28.309  16.345  1.00 74.90           C  
ANISOU 1386  CZ  TYR A 204     4777  12376  11306   2115   -483  -2183       C  
ATOM   1387  OH  TYR A 204      63.953  27.827  15.188  1.00 67.82           O  
ANISOU 1387  OH  TYR A 204     3901  11368  10500   2088   -522  -2039       O  
ATOM   1388  N   ALA A 205      64.927  28.737  22.596  1.00 78.29           N  
ANISOU 1388  N   ALA A 205     4913  13539  11296   2282   -296  -2586       N  
ATOM   1389  CA  ALA A 205      64.141  27.699  23.258  1.00 80.16           C  
ANISOU 1389  CA  ALA A 205     5065  13861  11529   2320   -301  -2453       C  
ATOM   1390  C   ALA A 205      62.938  28.291  23.981  1.00 85.49           C  
ANISOU 1390  C   ALA A 205     5647  14584  12253   2326   -191  -2425       C  
ATOM   1391  O   ALA A 205      61.858  27.687  23.999  1.00 99.06           O  
ANISOU 1391  O   ALA A 205     7304  16279  14056   2334   -178  -2269       O  
ATOM   1392  CB  ALA A 205      65.021  26.914  24.229  1.00 75.42           C  
ANISOU 1392  CB  ALA A 205     4450  13445  10762   2372   -353  -2512       C  
ATOM   1393  N   GLN A 206      63.103  29.473  24.579  1.00 76.34           N  
ANISOU 1393  N   GLN A 206     4474  13484  11046   2320   -110  -2578       N  
ATOM   1394  CA  GLN A 206      61.994  30.105  25.286  1.00 86.37           C  
ANISOU 1394  CA  GLN A 206     5659  14796  12362   2324      3  -2561       C  
ATOM   1395  C   GLN A 206      60.896  30.535  24.320  1.00 94.53           C  
ANISOU 1395  C   GLN A 206     6692  15647  13578   2287     49  -2432       C  
ATOM   1396  O   GLN A 206      59.706  30.353  24.605  1.00 93.47           O  
ANISOU 1396  O   GLN A 206     6482  15514  13518   2295    102  -2315       O  
ATOM   1397  CB  GLN A 206      62.499  31.299  26.095  1.00 93.63           C  
ANISOU 1397  CB  GLN A 206     6569  15813  13193   2318     80  -2765       C  
ATOM   1398  CG  GLN A 206      63.630  30.965  27.059  1.00 98.86           C  
ANISOU 1398  CG  GLN A 206     7229  16676  13658   2355     34  -2908       C  
ATOM   1399  CD  GLN A 206      63.213  29.989  28.144  1.00 98.52           C  
ANISOU 1399  CD  GLN A 206     7098  16816  13517   2414     31  -2833       C  
ATOM   1400  OE1 GLN A 206      62.035  29.887  28.487  1.00 83.79           O  
ANISOU 1400  OE1 GLN A 206     5159  14955  11720   2423     96  -2723       O  
ATOM   1401  NE2 GLN A 206      64.183  29.263  28.689  1.00105.12           N  
ANISOU 1401  NE2 GLN A 206     7941  17808  14190   2458    -41  -2887       N  
ATOM   1402  N   TRP A 207      61.274  31.108  23.175  1.00 96.04           N  
ANISOU 1402  N   TRP A 207     6965  15686  13840   2249     31  -2448       N  
ATOM   1403  CA  TRP A 207      60.280  31.469  22.169  1.00 85.22           C  
ANISOU 1403  CA  TRP A 207     5596  14155  12629   2220     66  -2313       C  
ATOM   1404  C   TRP A 207      59.616  30.231  21.580  1.00 82.04           C  
ANISOU 1404  C   TRP A 207     5177  13699  12296   2222     -6  -2124       C  
ATOM   1405  O   TRP A 207      58.414  30.243  21.287  1.00 74.71           O  
ANISOU 1405  O   TRP A 207     4199  12707  11481   2214     36  -1990       O  
ATOM   1406  CB  TRP A 207      60.926  32.303  21.063  1.00 78.71           C  
ANISOU 1406  CB  TRP A 207     4864  13196  11848   2187     58  -2368       C  
ATOM   1407  CG  TRP A 207      60.963  33.768  21.356  1.00 74.45           C  
ANISOU 1407  CG  TRP A 207     4319  12643  11325   2173    168  -2488       C  
ATOM   1408  CD1 TRP A 207      62.009  34.476  21.871  1.00 95.28           C  
ANISOU 1408  CD1 TRP A 207     6987  15341  13873   2167    187  -2682       C  
ATOM   1409  CD2 TRP A 207      59.904  34.709  21.150  1.00 81.68           C  
ANISOU 1409  CD2 TRP A 207     5196  13479  12359   2163    277  -2422       C  
ATOM   1410  NE1 TRP A 207      61.667  35.800  21.998  1.00 94.69           N  
ANISOU 1410  NE1 TRP A 207     6895  15221  13863   2150    303  -2741       N  
ATOM   1411  CE2 TRP A 207      60.379  35.969  21.562  1.00 85.33           C  
ANISOU 1411  CE2 TRP A 207     5667  13949  12803   2150    362  -2579       C  
ATOM   1412  CE3 TRP A 207      58.600  34.608  20.656  1.00 79.68           C  
ANISOU 1412  CE3 TRP A 207     4898  13151  12227   2163    311  -2243       C  
ATOM   1413  CZ2 TRP A 207      59.596  37.120  21.497  1.00 76.44           C  
ANISOU 1413  CZ2 TRP A 207     4511  12753  11779   2141    484  -2556       C  
ATOM   1414  CZ3 TRP A 207      57.824  35.751  20.592  1.00 77.65           C  
ANISOU 1414  CZ3 TRP A 207     4609  12833  12060   2157    429  -2220       C  
ATOM   1415  CH2 TRP A 207      58.325  36.990  21.010  1.00 75.65           C  
ANISOU 1415  CH2 TRP A 207     4369  12584  11790   2148    517  -2372       C  
ATOM   1416  N   SER A 208      60.382  29.154  21.399  1.00 81.80           N  
ANISOU 1416  N   SER A 208     5186  13691  12201   2232   -113  -2111       N  
ATOM   1417  CA  SER A 208      59.821  27.929  20.839  1.00 90.18           C  
ANISOU 1417  CA  SER A 208     6233  14699  13334   2228   -184  -1938       C  
ATOM   1418  C   SER A 208      58.790  27.318  21.781  1.00 87.51           C  
ANISOU 1418  C   SER A 208     5784  14449  13015   2258   -144  -1843       C  
ATOM   1419  O   SER A 208      57.673  26.985  21.365  1.00 80.68           O  
ANISOU 1419  O   SER A 208     4873  13513  12269   2244   -132  -1696       O  
ATOM   1420  CB  SER A 208      60.940  26.933  20.537  1.00 73.13           C  
ANISOU 1420  CB  SER A 208     4139  12548  11098   2233   -299  -1954       C  
ATOM   1421  OG  SER A 208      60.432  25.782  19.889  1.00 74.01           O  
ANISOU 1421  OG  SER A 208     4240  12590  11290   2222   -366  -1791       O  
ATOM   1422  N   ALA A 209      59.147  27.168  23.060  1.00 84.63           N  
ANISOU 1422  N   ALA A 209     5374  14249  12531   2300   -122  -1926       N  
ATOM   1423  CA  ALA A 209      58.197  26.632  24.029  1.00 82.84           C  
ANISOU 1423  CA  ALA A 209     5040  14122  12313   2333    -74  -1841       C  
ATOM   1424  C   ALA A 209      57.017  27.572  24.239  1.00 87.66           C  
ANISOU 1424  C   ALA A 209     5590  14703  13014   2319     41  -1817       C  
ATOM   1425  O   ALA A 209      55.893  27.112  24.471  1.00 88.32           O  
ANISOU 1425  O   ALA A 209     5594  14785  13179   2327     74  -1690       O  
ATOM   1426  CB  ALA A 209      58.900  26.354  25.357  1.00 78.18           C  
ANISOU 1426  CB  ALA A 209     4417  13737  11553   2386    -71  -1941       C  
ATOM   1427  N   GLY A 210      57.248  28.884  24.158  1.00 88.24           N  
ANISOU 1427  N   GLY A 210     5698  14748  13081   2299    106  -1936       N  
ATOM   1428  CA  GLY A 210      56.157  29.828  24.336  1.00 78.08           C  
ANISOU 1428  CA  GLY A 210     4356  13426  11884   2287    222  -1912       C  
ATOM   1429  C   GLY A 210      55.142  29.763  23.210  1.00 77.40           C  
ANISOU 1429  C   GLY A 210     4267  13182  11961   2258    220  -1748       C  
ATOM   1430  O   GLY A 210      53.935  29.667  23.450  1.00 85.10           O  
ANISOU 1430  O   GLY A 210     5163  14150  13020   2261    277  -1640       O  
ATOM   1431  N   ILE A 211      55.619  29.817  21.963  1.00 83.83           N  
ANISOU 1431  N   ILE A 211     5165  13874  12814   2230    154  -1729       N  
ATOM   1432  CA  ILE A 211      54.715  29.713  20.821  1.00 75.56           C  
ANISOU 1432  CA  ILE A 211     4117  12694  11900   2204    141  -1573       C  
ATOM   1433  C   ILE A 211      54.057  28.341  20.781  1.00 76.01           C  
ANISOU 1433  C   ILE A 211     4120  12756  12005   2208     79  -1426       C  
ATOM   1434  O   ILE A 211      52.892  28.212  20.384  1.00 88.30           O  
ANISOU 1434  O   ILE A 211     5622  14254  13672   2196    104  -1291       O  
ATOM   1435  CB  ILE A 211      55.469  30.027  19.513  1.00 83.59           C  
ANISOU 1435  CB  ILE A 211     5237  13598  12926   2176     81  -1592       C  
ATOM   1436  CG1 ILE A 211      55.996  31.463  19.537  1.00 86.24           C  
ANISOU 1436  CG1 ILE A 211     5616  13915  13238   2172    158  -1726       C  
ATOM   1437  CG2 ILE A 211      54.569  29.822  18.303  1.00 73.70           C  
ANISOU 1437  CG2 ILE A 211     3982  12232  11790   2153     59  -1428       C  
ATOM   1438  CD1 ILE A 211      54.913  32.507  19.703  1.00 77.14           C  
ANISOU 1438  CD1 ILE A 211     4404  12734  12172   2174    282  -1685       C  
ATOM   1439  N   ALA A 212      54.779  27.298  21.202  1.00 80.49           N  
ANISOU 1439  N   ALA A 212     4695  13396  12493   2226      2  -1446       N  
ATOM   1440  CA  ALA A 212      54.172  25.973  21.287  1.00 86.30           C  
ANISOU 1440  CA  ALA A 212     5369  14140  13280   2233    -47  -1309       C  
ATOM   1441  C   ALA A 212      53.028  25.958  22.294  1.00 89.51           C  
ANISOU 1441  C   ALA A 212     5663  14619  13729   2257     43  -1253       C  
ATOM   1442  O   ALA A 212      51.968  25.373  22.035  1.00 77.63           O  
ANISOU 1442  O   ALA A 212     4094  13065  12335   2246     44  -1112       O  
ATOM   1443  CB  ALA A 212      55.230  24.933  21.655  1.00 76.12           C  
ANISOU 1443  CB  ALA A 212     4107  12924  11890   2257   -135  -1346       C  
ATOM   1444  N   LEU A 213      53.222  26.602  23.448  1.00 91.10           N  
ANISOU 1444  N   LEU A 213     5834  14939  13840   2286    121  -1366       N  
ATOM   1445  CA  LEU A 213      52.146  26.701  24.430  1.00 79.49           C  
ANISOU 1445  CA  LEU A 213     4259  13542  12403   2308    218  -1323       C  
ATOM   1446  C   LEU A 213      50.982  27.520  23.889  1.00 79.42           C  
ANISOU 1446  C   LEU A 213     4222  13427  12527   2279    295  -1249       C  
ATOM   1447  O   LEU A 213      49.817  27.230  24.189  1.00 80.12           O  
ANISOU 1447  O   LEU A 213     4223  13515  12703   2282    344  -1142       O  
ATOM   1448  CB  LEU A 213      52.675  27.308  25.729  1.00 90.67           C  
ANISOU 1448  CB  LEU A 213     5656  15118  13676   2342    287  -1474       C  
ATOM   1449  CG  LEU A 213      53.034  26.337  26.857  1.00 81.42           C  
ANISOU 1449  CG  LEU A 213     4435  14117  12386   2394    265  -1482       C  
ATOM   1450  CD1 LEU A 213      53.945  25.229  26.359  1.00 80.74           C  
ANISOU 1450  CD1 LEU A 213     4401  14016  12259   2403    139  -1451       C  
ATOM   1451  CD2 LEU A 213      53.681  27.082  28.013  1.00 82.30           C  
ANISOU 1451  CD2 LEU A 213     4541  14397  12333   2424    328  -1651       C  
ATOM   1452  N   MET A 214      51.277  28.551  23.093  1.00 79.46           N  
ANISOU 1452  N   MET A 214     4296  13345  12549   2253    309  -1301       N  
ATOM   1453  CA  MET A 214      50.212  29.311  22.447  1.00 78.52           C  
ANISOU 1453  CA  MET A 214     4156  13127  12553   2232    376  -1214       C  
ATOM   1454  C   MET A 214      49.413  28.430  21.496  1.00 83.43           C  
ANISOU 1454  C   MET A 214     4755  13662  13284   2212    312  -1042       C  
ATOM   1455  O   MET A 214      48.184  28.544  21.415  1.00 91.45           O  
ANISOU 1455  O   MET A 214     5701  14646  14399   2207    367   -932       O  
ATOM   1456  CB  MET A 214      50.799  30.511  21.702  1.00 77.76           C  
ANISOU 1456  CB  MET A 214     4143  12957  12447   2215    397  -1295       C  
ATOM   1457  CG  MET A 214      49.766  31.352  20.971  1.00 89.04           C  
ANISOU 1457  CG  MET A 214     5551  14290  13989   2202    467  -1197       C  
ATOM   1458  SD  MET A 214      50.504  32.650  19.962  1.00100.21           S  
ANISOU 1458  SD  MET A 214     7065  15612  15398   2188    486  -1271       S  
ATOM   1459  CE  MET A 214      49.039  33.440  19.300  1.00 95.52           C  
ANISOU 1459  CE  MET A 214     6418  14942  14932   2189    576  -1118       C  
ATOM   1460  N   LYS A 215      50.094  27.539  20.770  1.00 85.73           N  
ANISOU 1460  N   LYS A 215     5102  13918  13554   2198    195  -1019       N  
ATOM   1461  CA  LYS A 215      49.390  26.612  19.891  1.00 84.19           C  
ANISOU 1461  CA  LYS A 215     4883  13652  13452   2176    129   -866       C  
ATOM   1462  C   LYS A 215      48.573  25.599  20.681  1.00 90.69           C  
ANISOU 1462  C   LYS A 215     5602  14529  14328   2191    140   -777       C  
ATOM   1463  O   LYS A 215      47.494  25.194  20.235  1.00 78.14           O  
ANISOU 1463  O   LYS A 215     3954  12893  12843   2174    142   -645       O  
ATOM   1464  CB  LYS A 215      50.381  25.889  18.978  1.00 82.22           C  
ANISOU 1464  CB  LYS A 215     4720  13357  13163   2156      6   -874       C  
ATOM   1465  CG  LYS A 215      51.123  26.796  18.012  1.00 74.88           C  
ANISOU 1465  CG  LYS A 215     3893  12360  12198   2138    -10   -944       C  
ATOM   1466  CD  LYS A 215      51.979  25.984  17.054  1.00 73.88           C  
ANISOU 1466  CD  LYS A 215     3847  12185  12041   2114   -131   -936       C  
ATOM   1467  CE  LYS A 215      52.960  25.100  17.806  1.00 90.37           C  
ANISOU 1467  CE  LYS A 215     5949  14341  14044   2133   -189  -1005       C  
ATOM   1468  NZ  LYS A 215      53.773  24.260  16.885  1.00 85.30           N  
ANISOU 1468  NZ  LYS A 215     5384  13648  13379   2109   -302   -992       N  
ATOM   1469  N   ASN A 216      49.064  25.179  21.849  1.00 83.02           N  
ANISOU 1469  N   ASN A 216     4603  13662  13278   2225    150   -845       N  
ATOM   1470  CA  ASN A 216      48.324  24.213  22.656  1.00 86.21           C  
ANISOU 1470  CA  ASN A 216     4904  14121  13730   2246    168   -761       C  
ATOM   1471  C   ASN A 216      47.067  24.837  23.251  1.00 99.19           C  
ANISOU 1471  C   ASN A 216     6459  15781  15447   2251    287   -720       C  
ATOM   1472  O   ASN A 216      45.984  24.243  23.201  1.00109.33           O  
ANISOU 1472  O   ASN A 216     7662  17034  16844   2244    301   -596       O  
ATOM   1473  CB  ASN A 216      49.222  23.652  23.759  1.00 91.03           C  
ANISOU 1473  CB  ASN A 216     5509  14862  14217   2290    152   -844       C  
ATOM   1474  CG  ASN A 216      50.250  22.672  23.231  1.00107.15           C  
ANISOU 1474  CG  ASN A 216     7613  16885  16215   2289     32   -841       C  
ATOM   1475  OD1 ASN A 216      49.984  21.921  22.292  1.00110.53           O  
ANISOU 1475  OD1 ASN A 216     8046  17215  16734   2258    -37   -737       O  
ATOM   1476  ND2 ASN A 216      51.434  22.672  23.835  1.00116.45           N  
ANISOU 1476  ND2 ASN A 216     8837  18162  17247   2321      8   -956       N  
ATOM   1477  N   ILE A 217      47.191  26.038  23.817  1.00 90.31           N  
ANISOU 1477  N   ILE A 217     5347  14704  14264   2263    376   -825       N  
ATOM   1478  CA  ILE A 217      46.042  26.681  24.449  1.00 92.00           C  
ANISOU 1478  CA  ILE A 217     5479  14936  14541   2269    497   -794       C  
ATOM   1479  C   ILE A 217      45.048  27.153  23.396  1.00 99.89           C  
ANISOU 1479  C   ILE A 217     6470  15818  15667   2237    516   -682       C  
ATOM   1480  O   ILE A 217      43.846  26.873  23.480  1.00111.49           O  
ANISOU 1480  O   ILE A 217     7854  17267  17240   2233    558   -568       O  
ATOM   1481  CB  ILE A 217      46.504  27.844  25.345  1.00 82.34           C  
ANISOU 1481  CB  ILE A 217     4272  13799  13213   2287    590   -945       C  
ATOM   1482  CG1 ILE A 217      47.412  27.330  26.463  1.00 82.97           C  
ANISOU 1482  CG1 ILE A 217     4348  14032  13145   2326    573  -1048       C  
ATOM   1483  CG2 ILE A 217      45.304  28.580  25.922  1.00 92.07           C  
ANISOU 1483  CG2 ILE A 217     5425  15039  14517   2289    721   -911       C  
ATOM   1484  CD1 ILE A 217      47.930  28.421  27.374  1.00 83.55           C  
ANISOU 1484  CD1 ILE A 217     4436  14211  13099   2342    658  -1210       C  
ATOM   1485  N   LEU A 218      45.534  27.874  22.386  1.00 80.40           N  
ANISOU 1485  N   LEU A 218     4087  13278  13183   2218    487   -710       N  
ATOM   1486  CA  LEU A 218      44.654  28.495  21.406  1.00 80.06           C  
ANISOU 1486  CA  LEU A 218     4039  13150  13229   2199    514   -610       C  
ATOM   1487  C   LEU A 218      44.195  27.529  20.321  1.00 88.48           C  
ANISOU 1487  C   LEU A 218     5098  14158  14362   2175    419   -473       C  
ATOM   1488  O   LEU A 218      43.222  27.824  19.620  1.00 96.47           O  
ANISOU 1488  O   LEU A 218     6080  15131  15443   2164    442   -365       O  
ATOM   1489  CB  LEU A 218      45.363  29.695  20.773  1.00 87.69           C  
ANISOU 1489  CB  LEU A 218     5096  14073  14147   2195    530   -694       C  
ATOM   1490  CG  LEU A 218      44.536  30.699  19.970  1.00 90.24           C  
ANISOU 1490  CG  LEU A 218     5415  14336  14538   2191    593   -614       C  
ATOM   1491  CD1 LEU A 218      43.311  31.137  20.756  1.00 95.73           C  
ANISOU 1491  CD1 LEU A 218     6013  15064  15296   2206    711   -558       C  
ATOM   1492  CD2 LEU A 218      45.397  31.896  19.609  1.00 78.60           C  
ANISOU 1492  CD2 LEU A 218     4025  12829  13011   2195    624   -721       C  
ATOM   1493  N   GLY A 219      44.855  26.384  20.176  1.00 79.21           N  
ANISOU 1493  N   GLY A 219     3948  12988  13159   2167    317   -474       N  
ATOM   1494  CA  GLY A 219      44.539  25.481  19.088  1.00 85.17           C  
ANISOU 1494  CA  GLY A 219     4705  13693  13964   2140    224   -360       C  
ATOM   1495  C   GLY A 219      43.924  24.161  19.502  1.00 79.43           C  
ANISOU 1495  C   GLY A 219     3889  12988  13302   2139    198   -267       C  
ATOM   1496  O   GLY A 219      43.677  23.302  18.650  1.00 79.12           O  
ANISOU 1496  O   GLY A 219     3846  12921  13296   2115    121   -177       O  
ATOM   1497  N   PHE A 220      43.666  23.978  20.797  1.00 80.45           N  
ANISOU 1497  N   PHE A 220     3945  13176  13446   2167    266   -289       N  
ATOM   1498  CA  PHE A 220      43.086  22.721  21.255  1.00 81.25           C  
ANISOU 1498  CA  PHE A 220     3954  13294  13623   2171    252   -201       C  
ATOM   1499  C   PHE A 220      42.358  22.868  22.586  1.00101.00           C  
ANISOU 1499  C   PHE A 220     6357  15851  16167   2200    363   -208       C  
ATOM   1500  O   PHE A 220      41.216  22.418  22.718  1.00104.35           O  
ANISOU 1500  O   PHE A 220     6685  16259  16702   2194    401   -103       O  
ATOM   1501  CB  PHE A 220      44.168  21.646  21.370  1.00 81.02           C  
ANISOU 1501  CB  PHE A 220     3960  13281  13542   2180    160   -238       C  
ATOM   1502  CG  PHE A 220      43.625  20.249  21.481  1.00 81.67           C  
ANISOU 1502  CG  PHE A 220     3956  13356  13720   2179    129   -128       C  
ATOM   1503  CD1 PHE A 220      43.286  19.533  20.345  1.00 81.22           C  
ANISOU 1503  CD1 PHE A 220     3900  13251  13710   2144     56    -22       C  
ATOM   1504  CD2 PHE A 220      43.456  19.651  22.719  1.00 82.81           C  
ANISOU 1504  CD2 PHE A 220     4016  13555  13893   2215    177   -137       C  
ATOM   1505  CE1 PHE A 220      42.786  18.248  20.440  1.00 83.49           C  
ANISOU 1505  CE1 PHE A 220     4137  13531  14055   2133     32     64       C  
ATOM   1506  CE2 PHE A 220      42.958  18.365  22.821  1.00 86.37           C  
ANISOU 1506  CE2 PHE A 220     4381  13982  14454   2216    156    -42       C  
ATOM   1507  CZ  PHE A 220      42.622  17.663  21.680  1.00 83.03           C  
ANISOU 1507  CZ  PHE A 220     3996  13495  14058   2167     83     57       C  
ATOM   1508  N   ILE A 221      43.005  23.495  23.572  1.00 96.00           N  
ANISOU 1508  N   ILE A 221     5746  15294  15435   2231    417   -336       N  
ATOM   1509  CA  ILE A 221      42.453  23.541  24.927  1.00 84.96           C  
ANISOU 1509  CA  ILE A 221     4260  13980  14043   2262    520   -361       C  
ATOM   1510  C   ILE A 221      41.096  24.237  24.932  1.00 84.64           C  
ANISOU 1510  C   ILE A 221     4151  13898  14110   2247    619   -290       C  
ATOM   1511  O   ILE A 221      40.081  23.660  25.340  1.00 85.51           O  
ANISOU 1511  O   ILE A 221     4163  14000  14329   2247    661   -210       O  
ATOM   1512  CB  ILE A 221      43.439  24.227  25.889  1.00 84.37           C  
ANISOU 1512  CB  ILE A 221     4231  14023  13804   2296    561   -516       C  
ATOM   1513  CG1 ILE A 221      44.688  23.365  26.068  1.00 84.13           C  
ANISOU 1513  CG1 ILE A 221     4248  14058  13661   2321    467   -570       C  
ATOM   1514  CG2 ILE A 221      42.776  24.493  27.232  1.00 85.74           C  
ANISOU 1514  CG2 ILE A 221     4317  14300  13960   2326    681   -542       C  
ATOM   1515  CD1 ILE A 221      44.401  21.993  26.637  1.00 84.99           C  
ANISOU 1515  CD1 ILE A 221     4276  14211  13807   2348    446   -493       C  
ATOM   1516  N   ILE A 222      41.060  25.493  24.480  1.00 87.66           N  
ANISOU 1516  N   ILE A 222     4585  14253  14469   2236    662   -319       N  
ATOM   1517  CA  ILE A 222      39.796  26.231  24.441  1.00 84.61           C  
ANISOU 1517  CA  ILE A 222     4138  13836  14173   2229    760   -242       C  
ATOM   1518  C   ILE A 222      38.775  25.564  23.523  1.00 84.50           C  
ANISOU 1518  C   ILE A 222     4107  13754  14248   2195    710    -90       C  
ATOM   1519  O   ILE A 222      37.618  25.391  23.945  1.00 95.90           O  
ANISOU 1519  O   ILE A 222     5493  15189  15755   2183    770    -25       O  
ATOM   1520  CB  ILE A 222      40.054  27.703  24.080  1.00 84.10           C  
ANISOU 1520  CB  ILE A 222     4143  13758  14054   2229    812   -304       C  
ATOM   1521  CG1 ILE A 222      40.995  28.345  25.101  1.00 84.41           C  
ANISOU 1521  CG1 ILE A 222     4219  13879  13975   2251    865   -472       C  
ATOM   1522  CG2 ILE A 222      38.746  28.473  23.996  1.00 90.72           C  
ANISOU 1522  CG2 ILE A 222     4920  14576  14974   2228    913   -210       C  
ATOM   1523  CD1 ILE A 222      41.354  29.778  24.782  1.00 83.98           C  
ANISOU 1523  CD1 ILE A 222     4232  13802  13874   2250    920   -548       C  
ATOM   1524  N   PRO A 223      39.111  25.170  22.286  1.00 83.53           N  
ANISOU 1524  N   PRO A 223     4052  13588  14098   2171    600    -43       N  
ATOM   1525  CA  PRO A 223      38.121  24.446  21.472  1.00 83.60           C  
ANISOU 1525  CA  PRO A 223     4059  13573  14131   2136    549     86       C  
ATOM   1526  C   PRO A 223      37.649  23.147  22.104  1.00101.62           C  
ANISOU 1526  C   PRO A 223     6272  15860  16480   2130    540    139       C  
ATOM   1527  O   PRO A 223      36.488  22.766  21.911  1.00 90.42           O  
ANISOU 1527  O   PRO A 223     4818  14460  15076   2112    554    245       O  
ATOM   1528  CB  PRO A 223      38.867  24.194  20.155  1.00 82.41           C  
ANISOU 1528  CB  PRO A 223     3990  13399  13922   2117    431     90       C  
ATOM   1529  CG  PRO A 223      39.879  25.275  20.090  1.00 81.70           C  
ANISOU 1529  CG  PRO A 223     3953  13298  13789   2138    449    -14       C  
ATOM   1530  CD  PRO A 223      40.326  25.472  21.505  1.00 82.36           C  
ANISOU 1530  CD  PRO A 223     3984  13427  13884   2175    527   -105       C  
ATOM   1531  N   LEU A 224      38.509  22.452  22.854  1.00108.76           N  
ANISOU 1531  N   LEU A 224     7151  16772  17402   2151    518     68       N  
ATOM   1532  CA  LEU A 224      38.066  21.239  23.534  1.00107.37           C  
ANISOU 1532  CA  LEU A 224     6900  16583  17311   2149    520     99       C  
ATOM   1533  C   LEU A 224      37.129  21.559  24.691  1.00 96.50           C  
ANISOU 1533  C   LEU A 224     5437  15214  16017   2158    640     65       C  
ATOM   1534  O   LEU A 224      36.216  20.778  24.981  1.00 90.30           O  
ANISOU 1534  O   LEU A 224     4587  14374  15348   2135    656     90       O  
ATOM   1535  CB  LEU A 224      39.268  20.438  24.034  1.00 85.61           C  
ANISOU 1535  CB  LEU A 224     4136  13863  14530   2182    464     22       C  
ATOM   1536  CG  LEU A 224      38.962  19.085  24.677  1.00 86.62           C  
ANISOU 1536  CG  LEU A 224     4186  13977  14750   2188    454     28       C  
ATOM   1537  CD1 LEU A 224      38.237  18.186  23.691  1.00 86.54           C  
ANISOU 1537  CD1 LEU A 224     4190  13878  14813   2134    395    156       C  
ATOM   1538  CD2 LEU A 224      40.237  18.424  25.177  1.00 86.59           C  
ANISOU 1538  CD2 LEU A 224     4175  14049  14676   2239    403    -37       C  
ATOM   1539  N   ILE A 225      37.336  22.695  25.360  1.00 90.28           N  
ANISOU 1539  N   ILE A 225     4640  14485  15177   2188    727    -16       N  
ATOM   1540  CA  ILE A 225      36.428  23.101  26.428  1.00 95.55           C  
ANISOU 1540  CA  ILE A 225     5228  15179  15899   2196    850    -51       C  
ATOM   1541  C   ILE A 225      35.059  23.450  25.856  1.00100.34           C  
ANISOU 1541  C   ILE A 225     5837  15699  16587   2151    885     55       C  
ATOM   1542  O   ILE A 225      34.025  22.978  26.343  1.00 95.41           O  
ANISOU 1542  O   ILE A 225     5142  15020  16090   2125    926     37       O  
ATOM   1543  CB  ILE A 225      37.025  24.275  27.225  1.00 92.50           C  
ANISOU 1543  CB  ILE A 225     4835  14896  15415   2240    941   -148       C  
ATOM   1544  CG1 ILE A 225      38.269  23.823  27.994  1.00 88.43           C  
ANISOU 1544  CG1 ILE A 225     4324  14505  14772   2288    912   -247       C  
ATOM   1545  CG2 ILE A 225      35.991  24.856  28.177  1.00 97.61           C  
ANISOU 1545  CG2 ILE A 225     5410  15571  16105   2242   1076   -166       C  
ATOM   1546  CD1 ILE A 225      38.918  24.922  28.806  1.00 88.65           C  
ANISOU 1546  CD1 ILE A 225     4398  14647  14637   2316    986   -369       C  
ATOM   1547  N   PHE A 226      35.033  24.274  24.804  1.00 87.46           N  
ANISOU 1547  N   PHE A 226     4284  14075  14872   2144    864    136       N  
ATOM   1548  CA  PHE A 226      33.759  24.671  24.211  1.00 87.64           C  
ANISOU 1548  CA  PHE A 226     4311  14127  14863   2131    895    274       C  
ATOM   1549  C   PHE A 226      33.033  23.475  23.603  1.00 87.85           C  
ANISOU 1549  C   PHE A 226     4320  14261  14796   2128    822    416       C  
ATOM   1550  O   PHE A 226      31.857  23.231  23.900  1.00 88.73           O  
ANISOU 1550  O   PHE A 226     4381  14660  14673   2170    849    467       O  
ATOM   1551  CB  PHE A 226      33.983  25.760  23.162  1.00 86.67           C  
ANISOU 1551  CB  PHE A 226     4267  14052  14612   2141    870    280       C  
ATOM   1552  CG  PHE A 226      33.914  27.157  23.713  1.00 86.91           C  
ANISOU 1552  CG  PHE A 226     4297  14079  14644   2160    983    218       C  
ATOM   1553  CD1 PHE A 226      34.467  28.219  23.017  1.00 90.41           C  
ANISOU 1553  CD1 PHE A 226     4808  14521  15023   2171    978    174       C  
ATOM   1554  CD2 PHE A 226      33.289  27.409  24.924  1.00 95.33           C  
ANISOU 1554  CD2 PHE A 226     5293  15145  15783   2166   1102    197       C  
ATOM   1555  CE1 PHE A 226      34.402  29.506  23.520  1.00 88.12           C  
ANISOU 1555  CE1 PHE A 226     4517  14242  14724   2192   1089    119       C  
ATOM   1556  CE2 PHE A 226      33.221  28.693  25.432  1.00 94.00           C  
ANISOU 1556  CE2 PHE A 226     5124  14999  15593   2186   1211    141       C  
ATOM   1557  CZ  PHE A 226      33.778  29.743  24.729  1.00 92.52           C  
ANISOU 1557  CZ  PHE A 226     5004  14820  15328   2201   1205    105       C  
ATOM   1558  N   ILE A 227      33.721  22.716  22.746  1.00 87.08           N  
ANISOU 1558  N   ILE A 227     4267  14190  14627   2122    704    420       N  
ATOM   1559  CA  ILE A 227      33.097  21.564  22.098  1.00 96.24           C  
ANISOU 1559  CA  ILE A 227     5408  15655  15504   2147    603    414       C  
ATOM   1560  C   ILE A 227      32.649  20.542  23.135  1.00 97.54           C  
ANISOU 1560  C   ILE A 227     5490  16120  15450   2200    589    220       C  
ATOM   1561  O   ILE A 227      31.549  19.980  23.042  1.00 89.18           O  
ANISOU 1561  O   ILE A 227     4337  15126  14422   2167    502   -235       O  
ATOM   1562  CB  ILE A 227      34.063  20.944  21.070  1.00 98.92           C  
ANISOU 1562  CB  ILE A 227     5808  15900  15878   2118    488    413       C  
ATOM   1563  CG1 ILE A 227      34.225  21.871  19.863  1.00 98.30           C  
ANISOU 1563  CG1 ILE A 227     5800  15763  15786   2095    445    389       C  
ATOM   1564  CG2 ILE A 227      33.579  19.569  20.631  1.00 95.62           C  
ANISOU 1564  CG2 ILE A 227     5343  15703  15287   2127    383    280       C  
ATOM   1565  CD1 ILE A 227      35.178  21.344  18.812  1.00 84.22           C  
ANISOU 1565  CD1 ILE A 227     4081  13910  14010   2068    331    371       C  
ATOM   1566  N   ALA A 228      33.485  20.296  24.146  1.00 96.46           N  
ANISOU 1566  N   ALA A 228     5320  15132  16200   2075    710    400       N  
ATOM   1567  CA  ALA A 228      33.141  19.322  25.178  1.00 97.55           C  
ANISOU 1567  CA  ALA A 228     5330  15369  16366   2053    558   -589       C  
ATOM   1568  C   ALA A 228      31.896  19.751  25.945  1.00 91.00           C  
ANISOU 1568  C   ALA A 228     4411  14817  15349   2095    650   -634       C  
ATOM   1569  O   ALA A 228      30.942  18.976  26.083  1.00 91.87           O  
ANISOU 1569  O   ALA A 228     4427  15137  15343   2131    673   -530       O  
ATOM   1570  CB  ALA A 228      34.322  19.127  26.129  1.00 97.75           C  
ANISOU 1570  CB  ALA A 228     5341  15285  16516   2096    659   -257       C  
ATOM   1571  N   THR A 229      31.886  20.990  26.447  1.00 91.01           N  
ANISOU 1571  N   THR A 229     4426  14551  15601   2053    775   -559       N  
ATOM   1572  CA  THR A 229      30.726  21.472  27.191  1.00102.34           C  
ANISOU 1572  CA  THR A 229     5781  16206  16898   2080    864   -633       C  
ATOM   1573  C   THR A 229      29.469  21.461  26.328  1.00 98.89           C  
ANISOU 1573  C   THR A 229     5327  16114  16132   2111    808   -619       C  
ATOM   1574  O   THR A 229      28.371  21.172  26.821  1.00 95.13           O  
ANISOU 1574  O   THR A 229     4746  15681  15718   2114    889   -526       O  
ATOM   1575  CB  THR A 229      30.994  22.876  27.736  1.00106.59           C  
ANISOU 1575  CB  THR A 229     6353  16473  17672   2052   1022   -463       C  
ATOM   1576  OG1 THR A 229      31.505  23.711  26.689  1.00115.90           O  
ANISOU 1576  OG1 THR A 229     7652  17462  18923   2045   1053    -63       O  
ATOM   1577  CG2 THR A 229      31.999  22.823  28.880  1.00101.20           C  
ANISOU 1577  CG2 THR A 229     5642  15883  16926   2127   1118   -294       C  
ATOM   1578  N   CYS A 230      29.610  21.765  25.034  1.00 97.06           N  
ANISOU 1578  N   CYS A 230     5187  16042  15648   2132    716   -541       N  
ATOM   1579  CA  CYS A 230      28.463  21.691  24.134  1.00 91.17           C  
ANISOU 1579  CA  CYS A 230     4402  15329  14908   2115    707   -407       C  
ATOM   1580  C   CYS A 230      27.945  20.263  24.017  1.00 91.80           C  
ANISOU 1580  C   CYS A 230     4387  15349  15146   2091    681   -352       C  
ATOM   1581  O   CYS A 230      26.729  20.032  24.033  1.00105.15           O  
ANISOU 1581  O   CYS A 230     5981  17021  16951   2067    726   -300       O  
ATOM   1582  CB  CYS A 230      28.836  22.242  22.757  1.00 89.97           C  
ANISOU 1582  CB  CYS A 230     4357  15229  14601   2125    640   -272       C  
ATOM   1583  SG  CYS A 230      29.040  24.039  22.691  1.00 89.42           S  
ANISOU 1583  SG  CYS A 230     4373  15210  14392   2162    722   -141       S  
ATOM   1584  N   TYR A 231      28.852  19.289  23.904  1.00102.67           N  
ANISOU 1584  N   TYR A 231     5785  16704  16522   2100    614   -345       N  
ATOM   1585  CA  TYR A 231      28.422  17.897  23.810  1.00100.52           C  
ANISOU 1585  CA  TYR A 231     5417  16387  16389   2083    599   -267       C  
ATOM   1586  C   TYR A 231      27.735  17.440  25.089  1.00 96.04           C  
ANISOU 1586  C   TYR A 231     4720  15796  15974   2093    716   -230       C  
ATOM   1587  O   TYR A 231      26.722  16.733  25.035  1.00103.04           O  
ANISOU 1587  O   TYR A 231     5500  16670  16979   2073    749   -143       O  
ATOM   1588  CB  TYR A 231      29.608  16.989  23.493  1.00 99.62           C  
ANISOU 1588  CB  TYR A 231     5352  16257  16241   2096    512   -261       C  
ATOM   1589  CG  TYR A 231      29.260  15.520  23.565  1.00104.96           C  
ANISOU 1589  CG  TYR A 231     5921  16890  17071   2086    513   -177       C  
ATOM   1590  CD1 TYR A 231      28.506  14.917  22.567  1.00110.81           C  
ANISOU 1590  CD1 TYR A 231     6615  17611  17878   2042    470   -114       C  
ATOM   1591  CD2 TYR A 231      29.675  14.738  24.635  1.00110.68           C  
ANISOU 1591  CD2 TYR A 231     6580  17590  17885   2120    565   -150       C  
ATOM   1592  CE1 TYR A 231      28.178  13.576  22.630  1.00117.58           C  
ANISOU 1592  CE1 TYR A 231     7399  18395  18881   2017    479    -30       C  
ATOM   1593  CE2 TYR A 231      29.352  13.396  24.707  1.00119.26           C  
ANISOU 1593  CE2 TYR A 231     7594  18619  19099   2107    581    -33       C  
ATOM   1594  CZ  TYR A 231      28.604  12.821  23.701  1.00124.14           C  
ANISOU 1594  CZ  TYR A 231     8198  19189  19782   2048    537     21       C  
ATOM   1595  OH  TYR A 231      28.280  11.485  23.767  1.00133.50           O  
ANISOU 1595  OH  TYR A 231     9332  20280  21111   2020    560    134       O  
ATOM   1596  N   PHE A 232      28.273  17.822  26.251  1.00 93.89           N  
ANISOU 1596  N   PHE A 232     4449  15517  15709   2124    787   -280       N  
ATOM   1597  CA  PHE A 232      27.625  17.461  27.507  1.00 99.96           C  
ANISOU 1597  CA  PHE A 232     5094  16295  16593   2145    919   -201       C  
ATOM   1598  C   PHE A 232      26.252  18.112  27.621  1.00 98.20           C  
ANISOU 1598  C   PHE A 232     4812  16098  16401   2122   1000   -179       C  
ATOM   1599  O   PHE A 232      25.311  17.508  28.152  1.00 97.05           O  
ANISOU 1599  O   PHE A 232     4606  15922  16346   2107   1082    -50       O  
ATOM   1600  CB  PHE A 232      28.507  17.852  28.694  1.00106.11           C  
ANISOU 1600  CB  PHE A 232     5885  17062  17372   2184    990   -239       C  
ATOM   1601  CG  PHE A 232      29.761  17.032  28.816  1.00104.50           C  
ANISOU 1601  CG  PHE A 232     5704  16827  17174   2216    936   -217       C  
ATOM   1602  CD1 PHE A 232      29.692  15.655  28.955  1.00102.04           C  
ANISOU 1602  CD1 PHE A 232     5347  16524  16899   2234    936    -73       C  
ATOM   1603  CD2 PHE A 232      31.007  17.637  28.809  1.00104.45           C  
ANISOU 1603  CD2 PHE A 232     5798  16739  17151   2217    896   -301       C  
ATOM   1604  CE1 PHE A 232      30.843  14.897  29.071  1.00 98.94           C  
ANISOU 1604  CE1 PHE A 232     4983  16115  16494   2268    888    -39       C  
ATOM   1605  CE2 PHE A 232      32.161  16.885  28.924  1.00 94.12           C  
ANISOU 1605  CE2 PHE A 232     4506  15406  15850   2250    849   -257       C  
ATOM   1606  CZ  PHE A 232      32.079  15.513  29.056  1.00 94.83           C  
ANISOU 1606  CZ  PHE A 232     4523  15562  15947   2285    840   -146       C  
ATOM   1607  N   GLY A 233      26.115  19.340  27.118  1.00104.46           N  
ANISOU 1607  N   GLY A 233     5683  16904  17104   2104    979   -265       N  
ATOM   1608  CA  GLY A 233      24.819  19.999  27.153  1.00100.42           C  
ANISOU 1608  CA  GLY A 233     5117  16416  16624   2083   1051   -241       C  
ATOM   1609  C   GLY A 233      23.793  19.310  26.271  1.00 96.02           C  
ANISOU 1609  C   GLY A 233     4505  15832  16145   2045   1012   -151       C  
ATOM   1610  O   GLY A 233      22.673  19.026  26.707  1.00 97.08           O  
ANISOU 1610  O   GLY A 233     4579  15927  16379   2019   1093    -61       O  
ATOM   1611  N   ILE A 234      24.165  19.025  25.020  1.00 95.11           N  
ANISOU 1611  N   ILE A 234     4441  15713  15985   2030    891   -163       N  
ATOM   1612  CA  ILE A 234      23.228  18.393  24.095  1.00 95.39           C  
ANISOU 1612  CA  ILE A 234     4444  15698  16102   1980    848    -89       C  
ATOM   1613  C   ILE A 234      22.885  16.980  24.556  1.00 96.43           C  
ANISOU 1613  C   ILE A 234     4517  15748  16374   1956    882     19       C  
ATOM   1614  O   ILE A 234      21.737  16.534  24.432  1.00103.25           O  
ANISOU 1614  O   ILE A 234     5323  16555  17351   1912    917     94       O  
ATOM   1615  CB  ILE A 234      23.798  18.408  22.664  1.00 94.22           C  
ANISOU 1615  CB  ILE A 234     4359  15575  15866   1973    716   -123       C  
ATOM   1616  CG1 ILE A 234      23.815  19.838  22.119  1.00 93.43           C  
ANISOU 1616  CG1 ILE A 234     4351  15507  15640   1980    702   -172       C  
ATOM   1617  CG2 ILE A 234      22.995  17.495  21.747  1.00 94.62           C  
ANISOU 1617  CG2 ILE A 234     4373  15560  16017   1915    666    -56       C  
ATOM   1618  CD1 ILE A 234      24.176  19.932  20.654  1.00 92.42           C  
ANISOU 1618  CD1 ILE A 234     4304  15384  15428   1965    589   -165       C  
ATOM   1619  N   ARG A 235      23.863  16.258  25.106  1.00 96.44           N  
ANISOU 1619  N   ARG A 235     4529  15740  16373   1986    878     35       N  
ATOM   1620  CA  ARG A 235      23.590  14.914  25.605  1.00 99.58           C  
ANISOU 1620  CA  ARG A 235     4871  16061  16902   1972    924    158       C  
ATOM   1621  C   ARG A 235      22.671  14.952  26.820  1.00 98.90           C  
ANISOU 1621  C   ARG A 235     4719  15963  16896   1978   1071    248       C  
ATOM   1622  O   ARG A 235      21.727  14.157  26.917  1.00103.43           O  
ANISOU 1622  O   ARG A 235     5232  16468  17600   1942   1122    355       O  
ATOM   1623  CB  ARG A 235      24.900  14.203  25.943  1.00104.94           C  
ANISOU 1623  CB  ARG A 235     5580  16741  17552   2013    892    164       C  
ATOM   1624  CG  ARG A 235      24.718  12.806  26.514  1.00103.47           C  
ANISOU 1624  CG  ARG A 235     5338  16479  17498   2010    951    311       C  
ATOM   1625  CD  ARG A 235      26.054  12.125  26.761  1.00103.20           C  
ANISOU 1625  CD  ARG A 235     5336  16448  17426   2055    912    322       C  
ATOM   1626  NE  ARG A 235      25.888  10.797  27.345  1.00103.00           N  
ANISOU 1626  NE  ARG A 235     5256  16353  17526   2059    983    482       N  
ATOM   1627  CZ  ARG A 235      25.736   9.683  26.637  1.00107.86           C  
ANISOU 1627  CZ  ARG A 235     5852  16877  18254   2016    940    536       C  
ATOM   1628  NH1 ARG A 235      25.730   9.731  25.312  1.00109.13           N  
ANISOU 1628  NH1 ARG A 235     6044  17016  18405   1964    823    445       N  
ATOM   1629  NH2 ARG A 235      25.590   8.518  27.254  1.00110.44           N  
ANISOU 1629  NH2 ARG A 235     6125  17135  18702   2025   1021    686       N  
ATOM   1630  N   LYS A 236      22.928  15.870  27.753  1.00 98.89           N  
ANISOU 1630  N   LYS A 236     4726  16028  16819   2020   1144    204       N  
ATOM   1631  CA  LYS A 236      22.095  15.988  28.947  1.00100.16           C  
ANISOU 1631  CA  LYS A 236     4828  16194  17033   2029   1290    291       C  
ATOM   1632  C   LYS A 236      20.661  16.356  28.581  1.00119.62           C  
ANISOU 1632  C   LYS A 236     7254  18628  19568   1979   1323    312       C  
ATOM   1633  O   LYS A 236      19.711  15.630  28.905  1.00111.38           O  
ANISOU 1633  O   LYS A 236     6149  17526  18644   1953   1395    430       O  
ATOM   1634  CB  LYS A 236      22.706  17.028  29.889  1.00100.01           C  
ANISOU 1634  CB  LYS A 236     4831  16258  16909   2078   1354    212       C  
ATOM   1635  CG  LYS A 236      21.924  17.294  31.162  1.00101.29           C  
ANISOU 1635  CG  LYS A 236     4939  16449  17097   2093   1510    291       C  
ATOM   1636  CD  LYS A 236      22.623  18.361  31.994  1.00101.09           C  
ANISOU 1636  CD  LYS A 236     4936  16506  16968   2135   1566    191       C  
ATOM   1637  CE  LYS A 236      21.870  18.663  33.278  1.00105.36           C  
ANISOU 1637  CE  LYS A 236     5424  17091  17517   2151   1726    265       C  
ATOM   1638  NZ  LYS A 236      22.558  19.715  34.079  1.00102.29           N  
ANISOU 1638  NZ  LYS A 236     5055  16778  17034   2185   1786    158       N  
ATOM   1639  N   HIS A 237      20.493  17.486  27.887  1.00118.79           N  
ANISOU 1639  N   HIS A 237     7182  18560  19391   1967   1275    202       N  
ATOM   1640  CA  HIS A 237      19.161  17.955  27.515  1.00110.43           C  
ANISOU 1640  CA  HIS A 237     6089  17481  18389   1925   1304    219       C  
ATOM   1641  C   HIS A 237      18.433  16.939  26.643  1.00113.64           C  
ANISOU 1641  C   HIS A 237     6459  17806  18911   1871   1250    288       C  
ATOM   1642  O   HIS A 237      17.227  16.719  26.808  1.00121.26           O  
ANISOU 1642  O   HIS A 237     7364  18727  19984   1836   1316    361       O  
ATOM   1643  CB  HIS A 237      19.276  19.302  26.800  1.00103.68           C  
ANISOU 1643  CB  HIS A 237     5283  16683  17426   1930   1250     98       C  
ATOM   1644  CG  HIS A 237      18.026  19.728  26.096  1.00115.38           C  
ANISOU 1644  CG  HIS A 237     6738  18145  18958   1889   1247    113       C  
ATOM   1645  ND1 HIS A 237      16.870  20.064  26.766  1.00120.03           N  
ANISOU 1645  ND1 HIS A 237     7273  18718  19616   1874   1358    165       N  
ATOM   1646  CD2 HIS A 237      17.753  19.879  24.778  1.00117.86           C  
ANISOU 1646  CD2 HIS A 237     7070  18455  19258   1863   1149     84       C  
ATOM   1647  CE1 HIS A 237      15.938  20.400  25.892  1.00122.17           C  
ANISOU 1647  CE1 HIS A 237     7528  18973  19920   1840   1324    164       C  
ATOM   1648  NE2 HIS A 237      16.448  20.296  24.678  1.00119.07           N  
ANISOU 1648  NE2 HIS A 237     7176  18590  19476   1834   1199    116       N  
ATOM   1649  N   LEU A 238      19.152  16.301  25.718  1.00 99.83           N  
ANISOU 1649  N   LEU A 238     4744  16040  17148   1861   1135    262       N  
ATOM   1650  CA  LEU A 238      18.519  15.358  24.801  1.00100.18           C  
ANISOU 1650  CA  LEU A 238     4751  16013  17300   1804   1079    307       C  
ATOM   1651  C   LEU A 238      18.064  14.097  25.529  1.00101.51           C  
ANISOU 1651  C   LEU A 238     4852  16098  17620   1786   1162    433       C  
ATOM   1652  O   LEU A 238      16.901  13.688  25.418  1.00110.31           O  
ANISOU 1652  O   LEU A 238     5902  17154  18858   1739   1204    493       O  
ATOM   1653  CB  LEU A 238      19.485  15.012  23.667  1.00 99.07           C  
ANISOU 1653  CB  LEU A 238     4666  15881  17095   1799    940    244       C  
ATOM   1654  CG  LEU A 238      18.935  14.184  22.505  1.00101.18           C  
ANISOU 1654  CG  LEU A 238     4902  16093  17449   1737    865    260       C  
ATOM   1655  CD1 LEU A 238      17.833  14.943  21.786  1.00102.18           C  
ANISOU 1655  CD1 LEU A 238     5005  16245  17574   1707    852    231       C  
ATOM   1656  CD2 LEU A 238      20.051  13.808  21.541  1.00 99.69           C  
ANISOU 1656  CD2 LEU A 238     4773  15919  17185   1739    739    207       C  
ATOM   1657  N   LEU A 239      18.971  13.468  26.283  1.00101.66           N  
ANISOU 1657  N   LEU A 239     4882  16111  17633   1826   1192    480       N  
ATOM   1658  CA  LEU A 239      18.628  12.232  26.981  1.00115.70           C  
ANISOU 1658  CA  LEU A 239     6598  17810  19554   1818   1279    619       C  
ATOM   1659  C   LEU A 239      17.520  12.464  28.001  1.00125.18           C  
ANISOU 1659  C   LEU A 239     7740  19004  20820   1819   1423    706       C  
ATOM   1660  O   LEU A 239      16.538  11.712  28.050  1.00125.15           O  
ANISOU 1660  O   LEU A 239     7670  18918  20964   1777   1481    796       O  
ATOM   1661  CB  LEU A 239      19.869  11.644  27.654  1.00104.58           C  
ANISOU 1661  CB  LEU A 239     5216  16415  18104   1875   1290    662       C  
ATOM   1662  CG  LEU A 239      20.918  11.015  26.734  1.00102.01           C  
ANISOU 1662  CG  LEU A 239     4935  16067  17756   1869   1163    611       C  
ATOM   1663  CD1 LEU A 239      22.068  10.443  27.547  1.00102.13           C  
ANISOU 1663  CD1 LEU A 239     4969  16099  17736   1932   1191    671       C  
ATOM   1664  CD2 LEU A 239      20.292   9.943  25.857  1.00102.52           C  
ANISOU 1664  CD2 LEU A 239     4954  16027  17973   1799   1125    648       C  
ATOM   1665  N   LYS A 240      17.657  13.508  28.825  1.00133.98           N  
ANISOU 1665  N   LYS A 240     8875  20201  21829   1864   1487    676       N  
ATOM   1666  CA  LYS A 240      16.617  13.798  29.808  1.00132.66           C  
ANISOU 1666  CA  LYS A 240     8656  20036  21711   1866   1626    755       C  
ATOM   1667  C   LYS A 240      15.297  14.132  29.124  1.00114.69           C  
ANISOU 1667  C   LYS A 240     6345  17720  19514   1804   1618    736       C  
ATOM   1668  O   LYS A 240      14.220  13.773  29.620  1.00116.01           O  
ANISOU 1668  O   LYS A 240     6448  17836  19793   1781   1717    831       O  
ATOM   1669  CB  LYS A 240      17.063  14.939  30.721  1.00136.35           C  
ANISOU 1669  CB  LYS A 240     9156  20609  22043   1921   1688    702       C  
ATOM   1670  CG  LYS A 240      16.193  15.123  31.953  1.00137.10           C  
ANISOU 1670  CG  LYS A 240     9200  20720  22173   1935   1848    798       C  
ATOM   1671  CD  LYS A 240      16.813  16.118  32.919  1.00141.29           C  
ANISOU 1671  CD  LYS A 240     9758  21361  22564   1991   1912    742       C  
ATOM   1672  CE  LYS A 240      15.992  16.236  34.193  1.00147.59           C  
ANISOU 1672  CE  LYS A 240    10505  22186  23385   2008   2076    844       C  
ATOM   1673  NZ  LYS A 240      16.619  17.168  35.170  1.00148.95           N  
ANISOU 1673  NZ  LYS A 240    10699  22475  23419   2061   2144    783       N  
ATOM   1674  N   THR A 241      15.362  14.806  27.972  1.00111.13           N  
ANISOU 1674  N   THR A 241     5931  17293  19000   1781   1503    618       N  
ATOM   1675  CA  THR A 241      14.154  15.116  27.214  1.00104.65           C  
ANISOU 1675  CA  THR A 241     5074  16445  18242   1728   1483    600       C  
ATOM   1676  C   THR A 241      13.438  13.844  26.774  1.00110.27           C  
ANISOU 1676  C   THR A 241     5722  17058  19118   1671   1478    675       C  
ATOM   1677  O   THR A 241      12.227  13.698  26.978  1.00114.55           O  
ANISOU 1677  O   THR A 241     6200  17554  19769   1636   1550    734       O  
ATOM   1678  CB  THR A 241      14.505  15.981  26.002  1.00103.31           C  
ANISOU 1678  CB  THR A 241     4961  16331  17963   1724   1357    474       C  
ATOM   1679  OG1 THR A 241      14.867  17.297  26.439  1.00102.70           O  
ANISOU 1679  OG1 THR A 241     4929  16334  17759   1768   1385    405       O  
ATOM   1680  CG2 THR A 241      13.325  16.073  25.047  1.00103.62           C  
ANISOU 1680  CG2 THR A 241     4957  16345  18069   1670   1319    464       C  
ATOM   1681  N   ASN A 242      14.175  12.907  26.170  1.00105.22           N  
ANISOU 1681  N   ASN A 242     5095  16380  18503   1660   1396    670       N  
ATOM   1682  CA  ASN A 242      13.548  11.675  25.701  1.00115.58           C  
ANISOU 1682  CA  ASN A 242     6342  17592  19980   1601   1391    727       C  
ATOM   1683  C   ASN A 242      13.006  10.853  26.865  1.00117.64           C  
ANISOU 1683  C   ASN A 242     6540  17779  20378   1603   1537    869       C  
ATOM   1684  O   ASN A 242      11.910  10.280  26.777  1.00108.76           O  
ANISOU 1684  O   ASN A 242     5343  16578  19402   1552   1586    922       O  
ATOM   1685  CB  ASN A 242      14.547  10.859  24.879  1.00105.46           C  
ANISOU 1685  CB  ASN A 242     5090  16285  18694   1590   1280    689       C  
ATOM   1686  CG  ASN A 242      13.869   9.864  23.956  1.00106.42           C  
ANISOU 1686  CG  ASN A 242     5149  16322  18961   1516   1238    692       C  
ATOM   1687  OD1 ASN A 242      13.739   8.684  24.282  1.00107.14           O  
ANISOU 1687  OD1 ASN A 242     5191  16317  19202   1493   1294    776       O  
ATOM   1688  ND2 ASN A 242      13.431  10.338  22.795  1.00111.56           N  
ANISOU 1688  ND2 ASN A 242     5801  17014  19572   1479   1142    602       N  
ATOM   1689  N   ALA A1001      13.754  10.792  27.971  1.00114.87           N  
ANISOU 1689  N   ALA A1001     6214  17455  19976   1666   1612    934       N  
ATOM   1690  CA  ALA A1001      13.286  10.065  29.147  1.00111.96           C  
ANISOU 1690  CA  ALA A1001     5789  17032  19718   1681   1763   1086       C  
ATOM   1691  C   ALA A1001      11.975  10.645  29.665  1.00110.15           C  
ANISOU 1691  C   ALA A1001     5515  16804  19534   1664   1864   1121       C  
ATOM   1692  O   ALA A1001      11.026   9.907  29.957  1.00118.29           O  
ANISOU 1692  O   ALA A1001     6477  17749  20721   1630   1952   1218       O  
ATOM   1693  CB  ALA A1001      14.357  10.087  30.238  1.00109.22           C  
ANISOU 1693  CB  ALA A1001     5481  16749  19270   1763   1823   1144       C  
ATOM   1694  N   ASP A1002      11.903  11.975  29.781  1.00109.45           N  
ANISOU 1694  N   ASP A1002     5463  16808  19316   1685   1857   1042       N  
ATOM   1695  CA  ASP A1002      10.657  12.605  30.205  1.00110.21           C  
ANISOU 1695  CA  ASP A1002     5519  16907  19451   1667   1947   1066       C  
ATOM   1696  C   ASP A1002       9.535  12.358  29.204  1.00114.93           C  
ANISOU 1696  C   ASP A1002     6064  17435  20167   1592   1899   1040       C  
ATOM   1697  O   ASP A1002       8.368  12.241  29.596  1.00111.71           O  
ANISOU 1697  O   ASP A1002     5596  16982  19866   1565   1991   1107       O  
ATOM   1698  CB  ASP A1002      10.866  14.105  30.409  1.00109.35           C  
ANISOU 1698  CB  ASP A1002     5460  16904  19183   1701   1941    971       C  
ATOM   1699  CG  ASP A1002      11.775  14.412  31.581  1.00120.37           C  
ANISOU 1699  CG  ASP A1002     6891  18377  20467   1772   2015    997       C  
ATOM   1700  OD1 ASP A1002      12.240  13.457  32.239  1.00123.06           O  
ANISOU 1700  OD1 ASP A1002     7218  18695  20844   1801   2071   1100       O  
ATOM   1701  OD2 ASP A1002      12.024  15.607  31.846  1.00119.38           O  
ANISOU 1701  OD2 ASP A1002     6803  18337  20218   1800   2022    914       O  
ATOM   1702  N   LEU A1003       9.867  12.268  27.914  1.00115.34           N  
ANISOU 1702  N   LEU A1003     6137  17488  20200   1561   1757    944       N  
ATOM   1703  CA  LEU A1003       8.849  11.998  26.904  1.00112.89           C  
ANISOU 1703  CA  LEU A1003     5772  17131  19992   1493   1705    913       C  
ATOM   1704  C   LEU A1003       8.239  10.614  27.098  1.00115.16           C  
ANISOU 1704  C   LEU A1003     5981  17299  20476   1448   1772   1011       C  
ATOM   1705  O   LEU A1003       7.011  10.456  27.084  1.00113.70           O  
ANISOU 1705  O   LEU A1003     5728  17065  20409   1404   1826   1042       O  
ATOM   1706  CB  LEU A1003       9.451  12.137  25.505  1.00108.82           C  
ANISOU 1706  CB  LEU A1003     5295  16654  19397   1475   1541    795       C  
ATOM   1707  CG  LEU A1003       8.474  12.067  24.331  1.00109.09           C  
ANISOU 1707  CG  LEU A1003     5276  16678  19494   1413   1470    741       C  
ATOM   1708  CD1 LEU A1003       7.396  13.131  24.467  1.00109.37           C  
ANISOU 1708  CD1 LEU A1003     5291  16758  19509   1412   1517    732       C  
ATOM   1709  CD2 LEU A1003       9.213  12.216  23.010  1.00107.86           C  
ANISOU 1709  CD2 LEU A1003     5167  16580  19236   1407   1315    634       C  
ATOM   1710  N   GLU A1004       9.085   9.596  27.287  1.00117.01           N  
ANISOU 1710  N   GLU A1004     6223  17481  20756   1460   1774   1060       N  
ATOM   1711  CA  GLU A1004       8.567   8.256  27.552  1.00114.53           C  
ANISOU 1711  CA  GLU A1004     5834  17041  20641   1422   1855   1162       C  
ATOM   1712  C   GLU A1004       7.775   8.217  28.854  1.00124.03           C  
ANISOU 1712  C   GLU A1004     6997  18212  21918   1442   2026   1292       C  
ATOM   1713  O   GLU A1004       6.725   7.566  28.931  1.00138.11           O  
ANISOU 1713  O   GLU A1004     8704  19902  23868   1395   2099   1352       O  
ATOM   1714  CB  GLU A1004       9.711   7.243  27.596  1.00119.74           C  
ANISOU 1714  CB  GLU A1004     6516  17654  21327   1442   1836   1201       C  
ATOM   1715  CG  GLU A1004      10.368   6.982  26.254  1.00129.29           C  
ANISOU 1715  CG  GLU A1004     7751  18868  22507   1407   1676   1084       C  
ATOM   1716  CD  GLU A1004      11.352   5.830  26.305  1.00137.79           C  
ANISOU 1716  CD  GLU A1004     8835  19873  23646   1417   1671   1132       C  
ATOM   1717  OE1 GLU A1004      11.667   5.366  27.421  1.00140.27           O  
ANISOU 1717  OE1 GLU A1004     9145  20155  23997   1466   1787   1259       O  
ATOM   1718  OE2 GLU A1004      11.806   5.386  25.230  1.00139.20           O  
ANISOU 1718  OE2 GLU A1004     9022  20031  23835   1379   1556   1048       O  
ATOM   1719  N   ASP A1005       8.268   8.905  29.887  1.00121.80           N  
ANISOU 1719  N   ASP A1005     6760  18008  21510   1513   2093   1335       N  
ATOM   1720  CA  ASP A1005       7.553   8.993  31.157  1.00134.60           C  
ANISOU 1720  CA  ASP A1005     8348  19620  23173   1539   2257   1456       C  
ATOM   1721  C   ASP A1005       6.131   9.509  30.950  1.00136.31           C  
ANISOU 1721  C   ASP A1005     8516  19820  23456   1489   2286   1432       C  
ATOM   1722  O   ASP A1005       5.146   8.846  31.308  1.00128.40           O  
ANISOU 1722  O   ASP A1005     7445  18727  22613   1456   2386   1522       O  
ATOM   1723  CB  ASP A1005       8.333   9.902  32.112  1.00139.97           C  
ANISOU 1723  CB  ASP A1005     9091  20421  23672   1619   2300   1463       C  
ATOM   1724  CG  ASP A1005       7.721   9.967  33.500  1.00151.43           C  
ANISOU 1724  CG  ASP A1005    10511  21880  25144   1655   2475   1594       C  
ATOM   1725  OD1 ASP A1005       6.860   9.121  33.822  1.00158.99           O  
ANISOU 1725  OD1 ASP A1005    11405  22740  26266   1627   2573   1703       O  
ATOM   1726  OD2 ASP A1005       8.106  10.871  34.271  1.00153.80           O  
ANISOU 1726  OD2 ASP A1005    10851  22289  25298   1710   2518   1582       O  
ATOM   1727  N   ASN A1006       6.013  10.697  30.352  1.00133.12           N  
ANISOU 1727  N   ASN A1006     8145  19500  22934   1484   2200   1312       N  
ATOM   1728  CA  ASN A1006       4.699  11.290  30.134  1.00121.23           C  
ANISOU 1728  CA  ASN A1006     6596  17990  21475   1443   2222   1288       C  
ATOM   1729  C   ASN A1006       3.818  10.386  29.282  1.00116.15           C  
ANISOU 1729  C   ASN A1006     5877  17250  21004   1367   2190   1283       C  
ATOM   1730  O   ASN A1006       2.660  10.138  29.628  1.00117.40           O  
ANISOU 1730  O   ASN A1006     5970  17348  21290   1335   2282   1344       O  
ATOM   1731  CB  ASN A1006       4.845  12.670  29.494  1.00114.02           C  
ANISOU 1731  CB  ASN A1006     5735  17182  20406   1455   2126   1160       C  
ATOM   1732  CG  ASN A1006       5.261  13.732  30.493  1.00113.63           C  
ANISOU 1732  CG  ASN A1006     5738  17219  20216   1517   2196   1164       C  
ATOM   1733  OD1 ASN A1006       4.891  13.675  31.666  1.00114.61           O  
ANISOU 1733  OD1 ASN A1006     5841  17333  20371   1539   2334   1261       O  
ATOM   1734  ND2 ASN A1006       6.032  14.709  30.032  1.00115.40           N  
ANISOU 1734  ND2 ASN A1006     6028  17531  20286   1545   2106   1055       N  
ATOM   1735  N   TRP A1007       4.354   9.869  28.173  1.00115.51           N  
ANISOU 1735  N   TRP A1007     5802  17156  20932   1337   2063   1206       N  
ATOM   1736  CA  TRP A1007       3.559   9.023  27.283  1.00116.30           C  
ANISOU 1736  CA  TRP A1007     5826  17177  21188   1261   2024   1181       C  
ATOM   1737  C   TRP A1007       2.989   7.817  28.026  1.00117.98           C  
ANISOU 1737  C   TRP A1007     5968  17258  21602   1237   2159   1306       C  
ATOM   1738  O   TRP A1007       1.795   7.498  27.907  1.00119.14           O  
ANISOU 1738  O   TRP A1007     6038  17342  21888   1184   2207   1321       O  
ATOM   1739  CB  TRP A1007       4.418   8.577  26.099  1.00115.38           C  
ANISOU 1739  CB  TRP A1007     5732  17071  21037   1240   1876   1086       C  
ATOM   1740  CG  TRP A1007       3.667   7.836  25.039  1.00116.08           C  
ANISOU 1740  CG  TRP A1007     5743  17104  21258   1161   1818   1031       C  
ATOM   1741  CD1 TRP A1007       3.388   6.501  25.013  1.00124.67           C  
ANISOU 1741  CD1 TRP A1007     6762  18068  22538   1111   1864   1075       C  
ATOM   1742  CD2 TRP A1007       3.109   8.387  23.840  1.00115.69           C  
ANISOU 1742  CD2 TRP A1007     5671  17128  21157   1125   1705    919       C  
ATOM   1743  NE1 TRP A1007       2.685   6.187  23.875  1.00129.82           N  
ANISOU 1743  NE1 TRP A1007     7349  18714  23263   1040   1785    986       N  
ATOM   1744  CE2 TRP A1007       2.502   7.327  23.138  1.00132.38           C  
ANISOU 1744  CE2 TRP A1007     7700  19167  23433   1051   1685    894       C  
ATOM   1745  CE3 TRP A1007       3.062   9.673  23.293  1.00114.64           C  
ANISOU 1745  CE3 TRP A1007     5579  17120  20858   1151   1625    841       C  
ATOM   1746  CZ2 TRP A1007       1.854   7.514  21.918  1.00133.08           C  
ANISOU 1746  CZ2 TRP A1007     7740  19317  23508   1004   1584    793       C  
ATOM   1747  CZ3 TRP A1007       2.419   9.856  22.082  1.00114.67           C  
ANISOU 1747  CZ3 TRP A1007     5538  17179  20852   1109   1528    752       C  
ATOM   1748  CH2 TRP A1007       1.824   8.783  21.408  1.00115.72           C  
ANISOU 1748  CH2 TRP A1007     5584  17251  21135   1037   1506    729       C  
ATOM   1749  N   GLU A1008       3.830   7.137  28.811  1.00126.20           N  
ANISOU 1749  N   GLU A1008     7033  18257  22661   1278   2227   1400       N  
ATOM   1750  CA  GLU A1008       3.354   5.982  29.564  1.00128.96           C  
ANISOU 1750  CA  GLU A1008     7319  18477  23201   1264   2368   1534       C  
ATOM   1751  C   GLU A1008       2.293   6.383  30.580  1.00136.59           C  
ANISOU 1751  C   GLU A1008     8254  19437  24208   1276   2512   1626       C  
ATOM   1752  O   GLU A1008       1.322   5.645  30.796  1.00140.22           O  
ANISOU 1752  O   GLU A1008     8638  19788  24850   1233   2607   1694       O  
ATOM   1753  CB  GLU A1008       4.526   5.276  30.245  1.00125.04           C  
ANISOU 1753  CB  GLU A1008     6860  17956  22694   1321   2417   1630       C  
ATOM   1754  CG  GLU A1008       5.451   4.562  29.273  1.00140.30           C  
ANISOU 1754  CG  GLU A1008     8807  19857  24644   1297   2297   1559       C  
ATOM   1755  CD  GLU A1008       6.570   3.813  29.968  1.00154.04           C  
ANISOU 1755  CD  GLU A1008    10578  21566  26384   1356   2353   1665       C  
ATOM   1756  OE1 GLU A1008       6.672   3.913  31.208  1.00162.61           O  
ANISOU 1756  OE1 GLU A1008    11676  22674  27434   1422   2481   1795       O  
ATOM   1757  OE2 GLU A1008       7.346   3.125  29.272  1.00155.74           O  
ANISOU 1757  OE2 GLU A1008    10803  21741  26629   1339   2270   1622       O  
ATOM   1758  N   THR A1009       2.447   7.554  31.208  1.00136.10           N  
ANISOU 1758  N   THR A1009     8245  19486  23982   1331   2534   1625       N  
ATOM   1759  CA  THR A1009       1.384   8.032  32.090  1.00131.83           C  
ANISOU 1759  CA  THR A1009     7674  18944  23470   1337   2663   1696       C  
ATOM   1760  C   THR A1009       0.096   8.304  31.319  1.00125.18           C  
ANISOU 1760  C   THR A1009     6773  18078  22713   1267   2625   1623       C  
ATOM   1761  O   THR A1009      -1.002   8.101  31.853  1.00122.96           O  
ANISOU 1761  O   THR A1009     6434  17733  22552   1244   2738   1697       O  
ATOM   1762  CB  THR A1009       1.830   9.288  32.840  1.00132.20           C  
ANISOU 1762  CB  THR A1009     7789  19120  23320   1405   2687   1688       C  
ATOM   1763  OG1 THR A1009       2.203  10.302  31.900  1.00135.44           O  
ANISOU 1763  OG1 THR A1009     8247  19624  23591   1401   2541   1539       O  
ATOM   1764  CG2 THR A1009       3.012   8.976  33.747  1.00128.78           C  
ANISOU 1764  CG2 THR A1009     7403  18722  22805   1479   2744   1774       C  
ATOM   1765  N   LEU A1010       0.209   8.758  30.066  1.00121.67           N  
ANISOU 1765  N   LEU A1010     6339  17686  22202   1236   2469   1483       N  
ATOM   1766  CA  LEU A1010      -0.967   8.952  29.223  1.00120.96           C  
ANISOU 1766  CA  LEU A1010     6187  17588  22185   1172   2422   1412       C  
ATOM   1767  C   LEU A1010      -1.709   7.639  29.018  1.00130.59           C  
ANISOU 1767  C   LEU A1010     7315  18673  23629   1107   2471   1452       C  
ATOM   1768  O   LEU A1010      -2.917   7.547  29.273  1.00129.65           O  
ANISOU 1768  O   LEU A1010     7131  18503  23629   1072   2552   1489       O  
ATOM   1769  CB  LEU A1010      -0.561   9.544  27.870  1.00119.59           C  
ANISOU 1769  CB  LEU A1010     6042  17505  21891   1159   2245   1265       C  
ATOM   1770  CG  LEU A1010      -0.649  11.047  27.597  1.00118.52           C  
ANISOU 1770  CG  LEU A1010     5954  17493  21585   1190   2186   1189       C  
ATOM   1771  CD1 LEU A1010       0.346  11.819  28.429  1.00122.06           C  
ANISOU 1771  CD1 LEU A1010     6491  18009  21877   1263   2217   1210       C  
ATOM   1772  CD2 LEU A1010      -0.420  11.319  26.119  1.00117.55           C  
ANISOU 1772  CD2 LEU A1010     5837  17440  21386   1166   2019   1060       C  
ATOM   1773  N   ASN A1011      -0.998   6.605  28.557  1.00129.83           N  
ANISOU 1773  N   ASN A1011     7213  18516  23601   1087   2424   1441       N  
ATOM   1774  CA  ASN A1011      -1.662   5.328  28.305  1.00125.87           C  
ANISOU 1774  CA  ASN A1011     6622  17877  23324   1020   2471   1465       C  
ATOM   1775  C   ASN A1011      -2.232   4.732  29.588  1.00125.49           C  
ANISOU 1775  C   ASN A1011     6538  17722  23422   1033   2663   1623       C  
ATOM   1776  O   ASN A1011      -3.339   4.177  29.585  1.00126.91           O  
ANISOU 1776  O   ASN A1011     6636  17808  23777    978   2733   1645       O  
ATOM   1777  CB  ASN A1011      -0.700   4.350  27.633  1.00133.20           C  
ANISOU 1777  CB  ASN A1011     7556  18757  24299   1000   2395   1426       C  
ATOM   1778  CG  ASN A1011      -0.695   4.487  26.123  1.00137.44           C  
ANISOU 1778  CG  ASN A1011     8077  19354  24790    948   2223   1265       C  
ATOM   1779  OD1 ASN A1011      -0.891   5.579  25.587  1.00127.74           O  
ANISOU 1779  OD1 ASN A1011     6873  18248  23414    958   2133   1183       O  
ATOM   1780  ND2 ASN A1011      -0.484   3.375  25.428  1.00147.96           N  
ANISOU 1780  ND2 ASN A1011     9365  20604  26249    894   2183   1222       N  
ATOM   1781  N   ASP A1012      -1.497   4.848  30.697  1.00125.33           N  
ANISOU 1781  N   ASP A1012     6576  17719  23324   1108   2751   1735       N  
ATOM   1782  CA  ASP A1012      -1.998   4.339  31.970  1.00126.85           C  
ANISOU 1782  CA  ASP A1012     6740  17826  23630   1132   2941   1899       C  
ATOM   1783  C   ASP A1012      -3.291   5.040  32.371  1.00132.23           C  
ANISOU 1783  C   ASP A1012     7387  18524  24332   1117   3013   1913       C  
ATOM   1784  O   ASP A1012      -4.269   4.390  32.760  1.00138.31           O  
ANISOU 1784  O   ASP A1012     8088  19183  25280   1083   3129   1988       O  
ATOM   1785  CB  ASP A1012      -0.936   4.502  33.057  1.00130.10           C  
ANISOU 1785  CB  ASP A1012     7224  18295  23914   1225   3012   2009       C  
ATOM   1786  CG  ASP A1012       0.264   3.603  32.838  1.00137.19           C  
ANISOU 1786  CG  ASP A1012     8145  19152  24828   1243   2974   2030       C  
ATOM   1787  OD1 ASP A1012       0.090   2.509  32.261  1.00141.21           O  
ANISOU 1787  OD1 ASP A1012     8599  19538  25517   1187   2968   2021       O  
ATOM   1788  OD2 ASP A1012       1.380   3.990  33.243  1.00139.51           O  
ANISOU 1788  OD2 ASP A1012     8512  19538  24958   1314   2952   2050       O  
ATOM   1789  N   ASN A1013      -3.318   6.372  32.270  1.00130.76           N  
ANISOU 1789  N   ASN A1013     7247  18468  23969   1141   2948   1840       N  
ATOM   1790  CA  ASN A1013      -4.503   7.116  32.686  1.00130.95           C  
ANISOU 1790  CA  ASN A1013     7242  18511  24000   1131   3017   1855       C  
ATOM   1791  C   ASN A1013      -5.690   6.839  31.770  1.00127.75           C  
ANISOU 1791  C   ASN A1013     6752  18049  23739   1048   2974   1780       C  
ATOM   1792  O   ASN A1013      -6.836   6.785  32.233  1.00129.00           O  
ANISOU 1792  O   ASN A1013     6854  18150  24008   1024   3077   1834       O  
ATOM   1793  CB  ASN A1013      -4.193   8.611  32.730  1.00130.54           C  
ANISOU 1793  CB  ASN A1013     7260  18607  23731   1176   2957   1787       C  
ATOM   1794  CG  ASN A1013      -3.212   8.967  33.828  1.00135.93           C  
ANISOU 1794  CG  ASN A1013     8016  19355  24275   1258   3027   1864       C  
ATOM   1795  OD1 ASN A1013      -3.357   8.535  34.971  1.00137.83           O  
ANISOU 1795  OD1 ASN A1013     8247  19553  24569   1290   3178   2001       O  
ATOM   1796  ND2 ASN A1013      -2.198   9.752  33.482  1.00138.91           N  
ANISOU 1796  ND2 ASN A1013     8466  19842  24470   1295   2920   1777       N  
ATOM   1797  N   LEU A1014      -5.442   6.661  30.469  1.00129.92           N  
ANISOU 1797  N   LEU A1014     7011  18343  24008   1005   2822   1653       N  
ATOM   1798  CA  LEU A1014      -6.535   6.319  29.563  1.00127.89           C  
ANISOU 1798  CA  LEU A1014     6664  18045  23883    926   2778   1575       C  
ATOM   1799  C   LEU A1014      -7.101   4.940  29.883  1.00130.54           C  
ANISOU 1799  C   LEU A1014     6920  18216  24463    879   2893   1651       C  
ATOM   1800  O   LEU A1014      -8.326   4.759  29.926  1.00130.94           O  
ANISOU 1800  O   LEU A1014     6895  18209  24649    833   2957   1660       O  
ATOM   1801  CB  LEU A1014      -6.060   6.389  28.110  1.00126.82           C  
ANISOU 1801  CB  LEU A1014     6530  17981  23674    896   2593   1426       C  
ATOM   1802  CG  LEU A1014      -7.109   6.212  27.008  1.00127.50           C  
ANISOU 1802  CG  LEU A1014     6523  18072  23850    821   2520   1322       C  
ATOM   1803  CD1 LEU A1014      -6.823   7.150  25.846  1.00126.10           C  
ANISOU 1803  CD1 LEU A1014     6375  18047  23491    828   2349   1192       C  
ATOM   1804  CD2 LEU A1014      -7.161   4.770  26.520  1.00128.58           C  
ANISOU 1804  CD2 LEU A1014     6587  18088  24180    754   2522   1301       C  
ATOM   1805  N   LYS A1015      -6.226   3.956  30.118  1.00135.14           N  
ANISOU 1805  N   LYS A1015     7518  18717  25111    890   2927   1709       N  
ATOM   1806  CA  LYS A1015      -6.704   2.638  30.521  1.00136.39           C  
ANISOU 1806  CA  LYS A1015     7606  18706  25510    853   3056   1796       C  
ATOM   1807  C   LYS A1015      -7.451   2.696  31.848  1.00141.00           C  
ANISOU 1807  C   LYS A1015     8179  19234  26161    884   3242   1946       C  
ATOM   1808  O   LYS A1015      -8.365   1.896  32.080  1.00141.98           O  
ANISOU 1808  O   LYS A1015     8226  19227  26491    839   3350   1997       O  
ATOM   1809  CB  LYS A1015      -5.538   1.653  30.610  1.00131.58           C  
ANISOU 1809  CB  LYS A1015     7024  18024  24945    873   3067   1845       C  
ATOM   1810  CG  LYS A1015      -4.909   1.310  29.269  1.00131.76           C  
ANISOU 1810  CG  LYS A1015     7042  18068  24954    827   2901   1699       C  
ATOM   1811  CD  LYS A1015      -3.891   0.190  29.409  1.00133.26           C  
ANISOU 1811  CD  LYS A1015     7246  18158  25230    839   2934   1758       C  
ATOM   1812  CE  LYS A1015      -2.793   0.561  30.393  1.00130.12           C  
ANISOU 1812  CE  LYS A1015     6942  17820  24679    938   2981   1875       C  
ATOM   1813  NZ  LYS A1015      -1.811  -0.543  30.569  1.00130.45           N  
ANISOU 1813  NZ  LYS A1015     6994  17765  24805    957   3021   1947       N  
ATOM   1814  N   VAL A1016      -7.083   3.632  32.726  1.00142.07           N  
ANISOU 1814  N   VAL A1016     8388  19467  26126    959   3283   2014       N  
ATOM   1815  CA  VAL A1016      -7.832   3.816  33.965  1.00138.99           C  
ANISOU 1815  CA  VAL A1016     7989  19045  25774    990   3453   2148       C  
ATOM   1816  C   VAL A1016      -9.220   4.371  33.672  1.00133.81           C  
ANISOU 1816  C   VAL A1016     7275  18396  25170    939   3451   2088       C  
ATOM   1817  O   VAL A1016     -10.217   3.923  34.251  1.00135.37           O  
ANISOU 1817  O   VAL A1016     7416  18494  25526    917   3584   2169       O  
ATOM   1818  CB  VAL A1016      -7.050   4.721  34.936  1.00132.34           C  
ANISOU 1818  CB  VAL A1016     7238  18323  24722   1082   3491   2219       C  
ATOM   1819  CG1 VAL A1016      -7.948   5.193  36.069  1.00133.33           C  
ANISOU 1819  CG1 VAL A1016     7355  18450  24854   1108   3643   2323       C  
ATOM   1820  CG2 VAL A1016      -5.846   3.980  35.494  1.00132.33           C  
ANISOU 1820  CG2 VAL A1016     7278  18297  24702   1140   3541   2322       C  
ATOM   1821  N   ILE A1017      -9.311   5.347  32.764  1.00133.67           N  
ANISOU 1821  N   ILE A1017     7270  18497  25023    922   3303   1948       N  
ATOM   1822  CA  ILE A1017     -10.609   5.922  32.412  1.00140.43           C  
ANISOU 1822  CA  ILE A1017     8069  19372  25916    878   3291   1889       C  
ATOM   1823  C   ILE A1017     -11.518   4.861  31.806  1.00150.61           C  
ANISOU 1823  C   ILE A1017     9252  20540  27432    795   3304   1854       C  
ATOM   1824  O   ILE A1017     -12.724   4.823  32.085  1.00151.72           O  
ANISOU 1824  O   ILE A1017     9330  20627  27691    763   3388   1881       O  
ATOM   1825  CB  ILE A1017     -10.426   7.118  31.458  1.00131.50           C  
ANISOU 1825  CB  ILE A1017     6971  18394  24598    883   3125   1751       C  
ATOM   1826  CG1 ILE A1017      -9.845   8.316  32.206  1.00134.31           C  
ANISOU 1826  CG1 ILE A1017     7420  18859  24751    960   3143   1785       C  
ATOM   1827  CG2 ILE A1017     -11.745   7.497  30.799  1.00132.10           C  
ANISOU 1827  CG2 ILE A1017     6971  18489  24733    829   3088   1675       C  
ATOM   1828  CD1 ILE A1017      -9.705   9.556  31.354  1.00130.60           C  
ANISOU 1828  CD1 ILE A1017     6987  18530  24107    970   3000   1661       C  
ATOM   1829  N   GLU A1018     -10.956   3.974  30.981  1.00158.74           N  
ANISOU 1829  N   GLU A1018    10259  21525  28531    758   3224   1789       N  
ATOM   1830  CA  GLU A1018     -11.789   3.014  30.263  1.00159.65           C  
ANISOU 1830  CA  GLU A1018    10268  21538  28854    673   3220   1725       C  
ATOM   1831  C   GLU A1018     -12.471   2.024  31.202  1.00158.10           C  
ANISOU 1831  C   GLU A1018    10019  21169  28885    656   3411   1853       C  
ATOM   1832  O   GLU A1018     -13.556   1.523  30.884  1.00157.69           O  
ANISOU 1832  O   GLU A1018     9872  21037  29005    589   3444   1814       O  
ATOM   1833  CB  GLU A1018     -10.952   2.270  29.221  1.00156.81           C  
ANISOU 1833  CB  GLU A1018     9899  21166  28514    638   3100   1626       C  
ATOM   1834  CG  GLU A1018     -11.759   1.398  28.263  1.00155.48           C  
ANISOU 1834  CG  GLU A1018     9618  20925  28532    544   3065   1520       C  
ATOM   1835  CD  GLU A1018     -12.791   2.183  27.469  1.00146.79           C  
ANISOU 1835  CD  GLU A1018     8460  19935  27377    508   2973   1408       C  
ATOM   1836  OE1 GLU A1018     -13.892   2.443  28.001  1.00139.91           O  
ANISOU 1836  OE1 GLU A1018     7547  19036  26577    499   3067   1455       O  
ATOM   1837  OE2 GLU A1018     -12.501   2.543  26.309  1.00142.71           O  
ANISOU 1837  OE2 GLU A1018     7941  19539  26744    491   2809   1276       O  
ATOM   1838  N   LYS A1019     -11.873   1.736  32.360  1.00157.52           N  
ANISOU 1838  N   LYS A1019    10000  21039  28812    718   3541   2007       N  
ATOM   1839  CA  LYS A1019     -12.405   0.732  33.281  1.00161.58           C  
ANISOU 1839  CA  LYS A1019    10470  21385  29539    712   3733   2147       C  
ATOM   1840  C   LYS A1019     -12.544   1.328  34.686  1.00164.33           C  
ANISOU 1840  C   LYS A1019    10871  21761  29806    788   3877   2304       C  
ATOM   1841  O   LYS A1019     -12.012   0.807  35.665  1.00170.61           O  
ANISOU 1841  O   LYS A1019    11701  22497  30627    844   4006   2456       O  
ATOM   1842  CB  LYS A1019     -11.521  -0.514  33.297  1.00160.81           C  
ANISOU 1842  CB  LYS A1019    10373  21169  29559    714   3773   2199       C  
ATOM   1843  CG  LYS A1019     -12.243  -1.783  33.724  1.00158.97           C  
ANISOU 1843  CG  LYS A1019    10061  20733  29606    674   3939   2287       C  
ATOM   1844  CD  LYS A1019     -13.373  -2.121  32.762  1.00150.61           C  
ANISOU 1844  CD  LYS A1019     8897  19617  28710    573   3889   2145       C  
ATOM   1845  CE  LYS A1019     -14.080  -3.406  33.161  1.00145.72           C  
ANISOU 1845  CE  LYS A1019     8198  18784  28384    530   4058   2220       C  
ATOM   1846  NZ  LYS A1019     -15.169  -3.755  32.206  1.00146.72           N  
ANISOU 1846  NZ  LYS A1019     8216  18862  28670    429   4008   2068       N  
ATOM   1847  N   ALA A1020     -13.281   2.434  34.780  1.00154.95           N  
ANISOU 1847  N   ALA A1020     9687  20668  28517    791   3857   2269       N  
ATOM   1848  CA  ALA A1020     -13.570   3.063  36.067  1.00150.09           C  
ANISOU 1848  CA  ALA A1020     9114  20084  27831    853   3992   2400       C  
ATOM   1849  C   ALA A1020     -14.736   4.018  35.881  1.00147.29           C  
ANISOU 1849  C   ALA A1020     8726  19788  27447    824   3968   2332       C  
ATOM   1850  O   ALA A1020     -14.613   5.006  35.149  1.00138.91           O  
ANISOU 1850  O   ALA A1020     7689  18857  26233    821   3825   2212       O  
ATOM   1851  CB  ALA A1020     -12.349   3.803  36.613  1.00148.69           C  
ANISOU 1851  CB  ALA A1020     9040  20036  27419    940   3968   2442       C  
ATOM   1852  N   ASP A1021     -15.859   3.732  36.537  1.00163.28           N  
ANISOU 1852  N   ASP A1021    10700  21718  29622    805   4111   2413       N  
ATOM   1853  CA  ASP A1021     -17.080   4.530  36.424  1.00173.01           C  
ANISOU 1853  CA  ASP A1021    11892  22988  30856    774   4106   2361       C  
ATOM   1854  C   ASP A1021     -17.405   5.117  37.795  1.00172.18           C  
ANISOU 1854  C   ASP A1021    11829  22901  30691    833   4259   2497       C  
ATOM   1855  O   ASP A1021     -18.271   4.615  38.515  1.00158.00           O  
ANISOU 1855  O   ASP A1021     9990  20996  29048    822   4410   2595       O  
ATOM   1856  CB  ASP A1021     -18.243   3.682  35.880  1.00175.58           C  
ANISOU 1856  CB  ASP A1021    12105  23186  31421    689   4132   2315       C  
ATOM   1857  CG  ASP A1021     -17.953   3.107  34.508  1.00177.93           C  
ANISOU 1857  CG  ASP A1021    12353  23478  31772    628   3982   2170       C  
ATOM   1858  OD1 ASP A1021     -17.118   3.687  33.783  1.00180.19           O  
ANISOU 1858  OD1 ASP A1021    12688  23890  31887    644   3828   2076       O  
ATOM   1859  OD2 ASP A1021     -18.562   2.076  34.154  1.00177.48           O  
ANISOU 1859  OD2 ASP A1021    12210  23294  31931    563   4020   2144       O  
ATOM   1860  N   ASN A1022     -16.704   6.191  38.151  1.00180.57           N  
ANISOU 1860  N   ASN A1022    12975  24104  31529    896   4220   2496       N  
ATOM   1861  CA  ASN A1022     -16.946   6.917  39.388  1.00178.35           C  
ANISOU 1861  CA  ASN A1022    12738  23870  31156    952   4347   2600       C  
ATOM   1862  C   ASN A1022     -17.059   8.405  39.082  1.00172.38           C  
ANISOU 1862  C   ASN A1022    12019  23260  30218    963   4249   2497       C  
ATOM   1863  O   ASN A1022     -16.846   8.850  37.951  1.00171.85           O  
ANISOU 1863  O   ASN A1022    11950  23260  30084    936   4086   2360       O  
ATOM   1864  CB  ASN A1022     -15.838   6.663  40.420  1.00179.76           C  
ANISOU 1864  CB  ASN A1022    12988  24074  31239   1032   4439   2728       C  
ATOM   1865  CG  ASN A1022     -15.869   5.252  40.975  1.00177.15           C  
ANISOU 1865  CG  ASN A1022    12621  23592  31094   1035   4580   2868       C  
ATOM   1866  OD1 ASN A1022     -15.238   4.345  40.433  1.00179.68           O  
ANISOU 1866  OD1 ASN A1022    12930  23848  31492   1020   4534   2857       O  
ATOM   1867  ND2 ASN A1022     -16.604   5.061  42.065  1.00169.22           N  
ANISOU 1867  ND2 ASN A1022    11602  22529  30166   1057   4757   3004       N  
ATOM   1868  N   ALA A1023     -17.396   9.178  40.114  1.00163.03           N  
ANISOU 1868  N   ALA A1023    10868  22124  28952   1005   4356   2567       N  
ATOM   1869  CA  ALA A1023     -17.602  10.612  39.938  1.00151.33           C  
ANISOU 1869  CA  ALA A1023     9418  20765  27315   1015   4288   2479       C  
ATOM   1870  C   ALA A1023     -16.277  11.367  39.899  1.00150.74           C  
ANISOU 1870  C   ALA A1023     9432  20824  27020   1071   4202   2429       C  
ATOM   1871  O   ALA A1023     -15.974  12.062  38.924  1.00153.69           O  
ANISOU 1871  O   ALA A1023     9822  21276  27297   1060   4051   2302       O  
ATOM   1872  CB  ALA A1023     -18.500  11.154  41.054  1.00140.27           C  
ANISOU 1872  CB  ALA A1023     8015  19361  25919   1034   4439   2563       C  
ATOM   1873  N   ALA A1024     -15.472  11.238  40.954  1.00146.66           N  
ANISOU 1873  N   ALA A1024     8969  20337  26417   1134   4299   2528       N  
ATOM   1874  CA  ALA A1024     -14.238  11.997  41.094  1.00136.17           C  
ANISOU 1874  CA  ALA A1024     7722  19140  24874   1192   4238   2485       C  
ATOM   1875  C   ALA A1024     -13.010  11.221  40.628  1.00135.73           C  
ANISOU 1875  C   ALA A1024     7692  19081  24798   1207   4157   2477       C  
ATOM   1876  O   ALA A1024     -11.891  11.542  41.043  1.00134.60           O  
ANISOU 1876  O   ALA A1024     7614  19030  24496   1266   4148   2484       O  
ATOM   1877  CB  ALA A1024     -14.058  12.446  42.545  1.00136.66           C  
ANISOU 1877  CB  ALA A1024     7828  19268  24828   1257   4388   2585       C  
ATOM   1878  N   GLN A1025     -13.190  10.214  39.774  1.00140.67           N  
ANISOU 1878  N   GLN A1025     8264  19603  25580   1155   4099   2457       N  
ATOM   1879  CA  GLN A1025     -12.074   9.438  39.244  1.00143.54           C  
ANISOU 1879  CA  GLN A1025     8646  19952  25939   1162   4018   2442       C  
ATOM   1880  C   GLN A1025     -11.738   9.804  37.803  1.00141.87           C  
ANISOU 1880  C   GLN A1025     8438  19790  25676   1124   3820   2278       C  
ATOM   1881  O   GLN A1025     -10.569  10.045  37.481  1.00144.03           O  
ANISOU 1881  O   GLN A1025     8771  20142  25813   1157   3724   2226       O  
ATOM   1882  CB  GLN A1025     -12.375   7.937  39.344  1.00143.73           C  
ANISOU 1882  CB  GLN A1025     8609  19820  26180   1133   4103   2539       C  
ATOM   1883  CG  GLN A1025     -12.314   7.385  40.759  1.00142.60           C  
ANISOU 1883  CG  GLN A1025     8477  19635  26069   1189   4296   2722       C  
ATOM   1884  CD  GLN A1025     -12.474   5.878  40.801  1.00140.12           C  
ANISOU 1884  CD  GLN A1025     8108  19159  25971   1166   4380   2820       C  
ATOM   1885  OE1 GLN A1025     -12.572   5.223  39.764  1.00139.39           O  
ANISOU 1885  OE1 GLN A1025     7969  18986  26006   1104   4290   2740       O  
ATOM   1886  NE2 GLN A1025     -12.502   5.319  42.006  1.00140.74           N  
ANISOU 1886  NE2 GLN A1025     8191  19192  26092   1218   4558   2994       N  
ATOM   1887  N   VAL A1026     -12.745   9.848  36.927  1.00135.05           N  
ANISOU 1887  N   VAL A1026     7510  18889  24913   1059   3757   2198       N  
ATOM   1888  CA  VAL A1026     -12.510  10.233  35.538  1.00134.29           C  
ANISOU 1888  CA  VAL A1026     7411  18855  24757   1027   3572   2047       C  
ATOM   1889  C   VAL A1026     -11.973  11.655  35.460  1.00143.82           C  
ANISOU 1889  C   VAL A1026     8693  20206  25747   1072   3498   1974       C  
ATOM   1890  O   VAL A1026     -11.154  11.974  34.588  1.00146.60           O  
ANISOU 1890  O   VAL A1026     9082  20630  25990   1079   3356   1875       O  
ATOM   1891  CB  VAL A1026     -13.805  10.070  34.717  1.00133.66           C  
ANISOU 1891  CB  VAL A1026     7239  18726  24818    954   3535   1983       C  
ATOM   1892  CG1 VAL A1026     -13.534  10.296  33.237  1.00132.57           C  
ANISOU 1892  CG1 VAL A1026     7091  18658  24622    924   3346   1835       C  
ATOM   1893  CG2 VAL A1026     -14.411   8.694  34.951  1.00135.36           C  
ANISOU 1893  CG2 VAL A1026     7379  18788  25263    909   3635   2059       C  
ATOM   1894  N   LYS A1027     -12.411  12.526  36.372  1.00148.51           N  
ANISOU 1894  N   LYS A1027     9309  20840  26276   1103   3596   2019       N  
ATOM   1895  CA  LYS A1027     -11.922  13.901  36.390  1.00149.96           C  
ANISOU 1895  CA  LYS A1027     9562  21151  26266   1146   3544   1950       C  
ATOM   1896  C   LYS A1027     -10.438  13.954  36.740  1.00152.67           C  
ANISOU 1896  C   LYS A1027     9984  21559  26463   1203   3522   1954       C  
ATOM   1897  O   LYS A1027      -9.662  14.666  36.092  1.00147.33           O  
ANISOU 1897  O   LYS A1027     9358  20970  25649   1222   3403   1853       O  
ATOM   1898  CB  LYS A1027     -12.744  14.729  37.380  1.00142.63           C  
ANISOU 1898  CB  LYS A1027     8635  20241  25317   1163   3671   2002       C  
ATOM   1899  CG  LYS A1027     -12.336  16.189  37.473  1.00136.28           C  
ANISOU 1899  CG  LYS A1027     7896  19557  24328   1203   3637   1928       C  
ATOM   1900  CD  LYS A1027     -13.204  16.933  38.477  1.00133.47           C  
ANISOU 1900  CD  LYS A1027     7534  19210  23967   1214   3772   1979       C  
ATOM   1901  CE  LYS A1027     -12.806  18.397  38.579  1.00129.51           C  
ANISOU 1901  CE  LYS A1027     7095  18822  23293   1250   3746   1899       C  
ATOM   1902  NZ  LYS A1027     -13.650  19.132  39.561  1.00130.37           N  
ANISOU 1902  NZ  LYS A1027     7196  18939  23399   1258   3880   1942       N  
ATOM   1903  N   ASP A1028     -10.025  13.201  37.763  1.00157.51           N  
ANISOU 1903  N   ASP A1028    10607  22134  27104   1236   3640   2072       N  
ATOM   1904  CA  ASP A1028      -8.620  13.198  38.159  1.00149.52           C  
ANISOU 1904  CA  ASP A1028     9664  21192  25954   1295   3627   2083       C  
ATOM   1905  C   ASP A1028      -7.744  12.551  37.093  1.00140.65           C  
ANISOU 1905  C   ASP A1028     8550  20053  24837   1279   3485   2018       C  
ATOM   1906  O   ASP A1028      -6.635  13.027  36.821  1.00140.09           O  
ANISOU 1906  O   ASP A1028     8542  20069  24617   1315   3396   1949       O  
ATOM   1907  CB  ASP A1028      -8.449  12.482  39.499  1.00154.94           C  
ANISOU 1907  CB  ASP A1028    10351  21847  26671   1339   3793   2239       C  
ATOM   1908  CG  ASP A1028      -9.074  13.245  40.650  1.00166.72           C  
ANISOU 1908  CG  ASP A1028    11849  23386  28111   1367   3931   2296       C  
ATOM   1909  OD1 ASP A1028      -9.699  14.296  40.400  1.00172.28           O  
ANISOU 1909  OD1 ASP A1028    12554  24132  28774   1347   3902   2214       O  
ATOM   1910  OD2 ASP A1028      -8.935  12.794  41.807  1.00171.87           O  
ANISOU 1910  OD2 ASP A1028    12505  24037  28760   1412   4073   2424       O  
ATOM   1911  N   ALA A1029      -8.221  11.465  36.480  1.00128.90           N  
ANISOU 1911  N   ALA A1029     6998  18454  23523   1225   3465   2032       N  
ATOM   1912  CA  ALA A1029      -7.448  10.828  35.420  1.00128.12           C  
ANISOU 1912  CA  ALA A1029     6902  18339  23438   1204   3330   1961       C  
ATOM   1913  C   ALA A1029      -7.312  11.745  34.210  1.00138.16           C  
ANISOU 1913  C   ALA A1029     8195  19699  24602   1186   3162   1807       C  
ATOM   1914  O   ALA A1029      -6.245  11.804  33.585  1.00138.81           O  
ANISOU 1914  O   ALA A1029     8325  19833  24584   1203   3046   1736       O  
ATOM   1915  CB  ALA A1029      -8.092   9.500  35.026  1.00129.39           C  
ANISOU 1915  CB  ALA A1029     6981  18361  23819   1143   3354   1998       C  
ATOM   1916  N   LEU A1030      -8.379  12.474  33.868  1.00126.92           N  
ANISOU 1916  N   LEU A1030     6737  18293  23193   1157   3149   1758       N  
ATOM   1917  CA  LEU A1030      -8.278  13.468  32.805  1.00129.80           C  
ANISOU 1917  CA  LEU A1030     7125  18753  23441   1152   3006   1628       C  
ATOM   1918  C   LEU A1030      -7.318  14.589  33.179  1.00129.51           C  
ANISOU 1918  C   LEU A1030     7178  18824  23204   1215   2988   1593       C  
ATOM   1919  O   LEU A1030      -6.621  15.125  32.309  1.00123.05           O  
ANISOU 1919  O   LEU A1030     6402  18079  22271   1227   2857   1492       O  
ATOM   1920  CB  LEU A1030      -9.658  14.039  32.478  1.00126.32           C  
ANISOU 1920  CB  LEU A1030     6624  18312  23058   1116   3014   1600       C  
ATOM   1921  CG  LEU A1030     -10.517  13.227  31.509  1.00127.15           C  
ANISOU 1921  CG  LEU A1030     6638  18357  23316   1047   2957   1563       C  
ATOM   1922  CD1 LEU A1030     -11.863  13.900  31.298  1.00140.14           C  
ANISOU 1922  CD1 LEU A1030     8227  20018  25002   1021   2973   1542       C  
ATOM   1923  CD2 LEU A1030      -9.793  13.045  30.184  1.00126.10           C  
ANISOU 1923  CD2 LEU A1030     6513  18275  23124   1033   2787   1454       C  
ATOM   1924  N   THR A1031      -7.270  14.959  34.462  1.00127.81           N  
ANISOU 1924  N   THR A1031     6993  18625  22945   1257   3120   1671       N  
ATOM   1925  CA  THR A1031      -6.299  15.955  34.905  1.00127.55           C  
ANISOU 1925  CA  THR A1031     7041  18696  22727   1316   3114   1632       C  
ATOM   1926  C   THR A1031      -4.874  15.451  34.715  1.00122.71           C  
ANISOU 1926  C   THR A1031     6479  18107  22039   1346   3042   1614       C  
ATOM   1927  O   THR A1031      -3.997  16.197  34.263  1.00121.36           O  
ANISOU 1927  O   THR A1031     6367  18019  21725   1373   2948   1521       O  
ATOM   1928  CB  THR A1031      -6.548  16.320  36.369  1.00129.25           C  
ANISOU 1928  CB  THR A1031     7266  18927  22914   1352   3279   1721       C  
ATOM   1929  OG1 THR A1031      -7.876  16.838  36.516  1.00125.29           O  
ANISOU 1929  OG1 THR A1031     6721  18403  22482   1323   3342   1732       O  
ATOM   1930  CG2 THR A1031      -5.545  17.365  36.839  1.00123.41           C  
ANISOU 1930  CG2 THR A1031     6604  18303  21983   1409   3276   1665       C  
ATOM   1931  N   LYS A1032      -4.627  14.181  35.051  1.00131.85           N  
ANISOU 1931  N   LYS A1032     7612  19190  23297   1342   3090   1704       N  
ATOM   1932  CA  LYS A1032      -3.306  13.602  34.829  1.00130.46           C  
ANISOU 1932  CA  LYS A1032     7477  19027  23063   1369   3022   1693       C  
ATOM   1933  C   LYS A1032      -2.966  13.563  33.344  1.00131.47           C  
ANISOU 1933  C   LYS A1032     7611  19164  23179   1335   2846   1573       C  
ATOM   1934  O   LYS A1032      -1.818  13.814  32.955  1.00133.58           O  
ANISOU 1934  O   LYS A1032     7938  19494  23323   1365   2752   1506       O  
ATOM   1935  CB  LYS A1032      -3.238  12.200  35.434  1.00128.09           C  
ANISOU 1935  CB  LYS A1032     7141  18631  22896   1370   3117   1824       C  
ATOM   1936  CG  LYS A1032      -3.411  12.160  36.945  1.00127.66           C  
ANISOU 1936  CG  LYS A1032     7087  18582  22834   1417   3294   1958       C  
ATOM   1937  CD  LYS A1032      -3.260  10.743  37.480  1.00126.82           C  
ANISOU 1937  CD  LYS A1032     6948  18381  22858   1425   3388   2097       C  
ATOM   1938  CE  LYS A1032      -3.376  10.706  38.996  1.00127.32           C  
ANISOU 1938  CE  LYS A1032     7014  18467  22893   1483   3568   2241       C  
ATOM   1939  NZ  LYS A1032      -3.182   9.331  39.535  1.00128.56           N  
ANISOU 1939  NZ  LYS A1032     7142  18533  23171   1502   3669   2393       N  
ATOM   1940  N   MET A1033      -3.953  13.256  32.497  1.00122.11           N  
ANISOU 1940  N   MET A1033     6359  17922  22113   1273   2800   1541       N  
ATOM   1941  CA  MET A1033      -3.711  13.251  31.058  1.00125.26           C  
ANISOU 1941  CA  MET A1033     6757  18347  22490   1242   2635   1425       C  
ATOM   1942  C   MET A1033      -3.384  14.648  30.545  1.00126.36           C  
ANISOU 1942  C   MET A1033     6954  18600  22456   1271   2546   1321       C  
ATOM   1943  O   MET A1033      -2.534  14.806  29.661  1.00118.66           O  
ANISOU 1943  O   MET A1033     6020  17677  21388   1279   2418   1235       O  
ATOM   1944  CB  MET A1033      -4.921  12.681  30.318  1.00122.21           C  
ANISOU 1944  CB  MET A1033     6279  17894  22261   1172   2615   1410       C  
ATOM   1945  CG  MET A1033      -5.105  11.187  30.492  1.00123.43           C  
ANISOU 1945  CG  MET A1033     6374  17925  22598   1134   2674   1484       C  
ATOM   1946  SD  MET A1033      -6.370  10.507  29.404  1.00134.64           S  
ANISOU 1946  SD  MET A1033     7683  19282  24192   1046   2623   1428       S  
ATOM   1947  CE  MET A1033      -5.688  10.914  27.799  1.00123.00           C  
ANISOU 1947  CE  MET A1033     6234  17914  22586   1037   2413   1273       C  
ATOM   1948  N   ARG A1034      -4.047  15.675  31.084  1.00127.50           N  
ANISOU 1948  N   ARG A1034     7102  18782  22560   1287   2617   1330       N  
ATOM   1949  CA  ARG A1034      -3.776  17.036  30.635  1.00123.64           C  
ANISOU 1949  CA  ARG A1034     6666  18390  21920   1315   2548   1236       C  
ATOM   1950  C   ARG A1034      -2.406  17.511  31.101  1.00120.20           C  
ANISOU 1950  C   ARG A1034     6318  18020  21333   1373   2539   1210       C  
ATOM   1951  O   ARG A1034      -1.667  18.137  30.333  1.00118.01           O  
ANISOU 1951  O   ARG A1034     6091  17808  20938   1392   2429   1116       O  
ATOM   1952  CB  ARG A1034      -4.865  17.988  31.130  1.00119.52           C  
ANISOU 1952  CB  ARG A1034     6123  17882  21407   1315   2636   1255       C  
ATOM   1953  CG  ARG A1034      -4.685  19.417  30.638  1.00120.60           C  
ANISOU 1953  CG  ARG A1034     6307  18108  21407   1344   2575   1164       C  
ATOM   1954  CD  ARG A1034      -5.715  20.360  31.235  1.00127.34           C  
ANISOU 1954  CD  ARG A1034     7142  18969  22274   1346   2676   1188       C  
ATOM   1955  NE  ARG A1034      -5.583  21.712  30.698  1.00131.10           N  
ANISOU 1955  NE  ARG A1034     7658  19519  22634   1372   2621   1104       N  
ATOM   1956  CZ  ARG A1034      -4.782  22.644  31.204  1.00126.19           C  
ANISOU 1956  CZ  ARG A1034     7107  18954  21886   1417   2648   1066       C  
ATOM   1957  NH1 ARG A1034      -4.036  22.374  32.267  1.00121.20           N  
ANISOU 1957  NH1 ARG A1034     6509  18327  21216   1442   2725   1100       N  
ATOM   1958  NH2 ARG A1034      -4.726  23.847  30.648  1.00124.45           N  
ANISOU 1958  NH2 ARG A1034     6918  18789  21579   1438   2603    993       N  
ATOM   1959  N   ALA A1035      -2.052  17.229  32.357  1.00118.28           N  
ANISOU 1959  N   ALA A1035     6090  17765  21086   1404   2657   1292       N  
ATOM   1960  CA  ALA A1035      -0.748  17.641  32.868  1.00117.35           C  
ANISOU 1960  CA  ALA A1035     6046  17719  20823   1460   2655   1265       C  
ATOM   1961  C   ALA A1035       0.377  16.932  32.125  1.00116.45           C  
ANISOU 1961  C   ALA A1035     5963  17604  20679   1465   2537   1226       C  
ATOM   1962  O   ALA A1035       1.349  17.564  31.690  1.00115.17           O  
ANISOU 1962  O   ALA A1035     5863  17511  20384   1494   2449   1136       O  
ATOM   1963  CB  ALA A1035      -0.662  17.367  34.369  1.00118.28           C  
ANISOU 1963  CB  ALA A1035     6162  17836  20944   1495   2811   1371       C  
ATOM   1964  N   ALA A1036       0.258  15.613  31.963  1.00117.15           N  
ANISOU 1964  N   ALA A1036     6006  17609  20896   1434   2536   1290       N  
ATOM   1965  CA  ALA A1036       1.293  14.864  31.261  1.00116.39           C  
ANISOU 1965  CA  ALA A1036     5936  17503  20786   1434   2428   1256       C  
ATOM   1966  C   ALA A1036       1.323  15.202  29.776  1.00115.83           C  
ANISOU 1966  C   ALA A1036     5872  17461  20677   1405   2270   1137       C  
ATOM   1967  O   ALA A1036       2.367  15.053  29.130  1.00121.74           O  
ANISOU 1967  O   ALA A1036     6666  18239  21352   1418   2163   1075       O  
ATOM   1968  CB  ALA A1036       1.088  13.366  31.473  1.00120.15           C  
ANISOU 1968  CB  ALA A1036     6356  17872  21425   1406   2480   1356       C  
ATOM   1969  N   ALA A1037       0.200  15.660  29.218  1.00115.78           N  
ANISOU 1969  N   ALA A1037     5822  17455  20716   1369   2255   1107       N  
ATOM   1970  CA  ALA A1037       0.195  16.119  27.834  1.00114.93           C  
ANISOU 1970  CA  ALA A1037     5719  17397  20551   1352   2112   1000       C  
ATOM   1971  C   ALA A1037       0.820  17.500  27.694  1.00113.67           C  
ANISOU 1971  C   ALA A1037     5636  17334  20219   1400   2069    922       C  
ATOM   1972  O   ALA A1037       1.371  17.822  26.635  1.00112.64           O  
ANISOU 1972  O   ALA A1037     5538  17256  20002   1406   1945    835       O  
ATOM   1973  CB  ALA A1037      -1.233  16.128  27.285  1.00115.86           C  
ANISOU 1973  CB  ALA A1037     5757  17492  20772   1302   2113    999       C  
ATOM   1974  N   LEU A1038       0.746  18.324  28.741  1.00114.70           N  
ANISOU 1974  N   LEU A1038     5792  17489  20299   1435   2175    949       N  
ATOM   1975  CA  LEU A1038       1.379  19.638  28.705  1.00115.03           C  
ANISOU 1975  CA  LEU A1038     5904  17615  20188   1480   2150    872       C  
ATOM   1976  C   LEU A1038       2.881  19.542  28.941  1.00123.59           C  
ANISOU 1976  C   LEU A1038     7058  18735  21164   1521   2114    839       C  
ATOM   1977  O   LEU A1038       3.652  20.314  28.362  1.00126.30           O  
ANISOU 1977  O   LEU A1038     7461  19140  21387   1548   2033    749       O  
ATOM   1978  CB  LEU A1038       0.738  20.563  29.740  1.00113.30           C  
ANISOU 1978  CB  LEU A1038     5681  17411  19958   1497   2281    903       C  
ATOM   1979  CG  LEU A1038      -0.611  21.171  29.359  1.00113.92           C  
ANISOU 1979  CG  LEU A1038     5710  17481  20096   1470   2299    903       C  
ATOM   1980  CD1 LEU A1038      -1.150  22.026  30.494  1.00114.54           C  
ANISOU 1980  CD1 LEU A1038     5787  17569  20162   1487   2437    937       C  
ATOM   1981  CD2 LEU A1038      -0.479  21.988  28.084  1.00112.96           C  
ANISOU 1981  CD2 LEU A1038     5612  17414  19893   1477   2177    809       C  
ATOM   1982  N   ASP A1039       3.314  18.609  29.793  1.00126.58           N  
ANISOU 1982  N   ASP A1039     7431  19077  21586   1530   2178    913       N  
ATOM   1983  CA  ASP A1039       4.747  18.424  29.997  1.00111.33           C  
ANISOU 1983  CA  ASP A1039     5561  17184  19557   1571   2141    886       C  
ATOM   1984  C   ASP A1039       5.400  17.754  28.795  1.00110.53           C  
ANISOU 1984  C   ASP A1039     5475  17068  19454   1553   1996    835       C  
ATOM   1985  O   ASP A1039       6.569  18.024  28.497  1.00109.39           O  
ANISOU 1985  O   ASP A1039     5395  16974  19195   1585   1920    767       O  
ATOM   1986  CB  ASP A1039       4.999  17.614  31.268  1.00112.24           C  
ANISOU 1986  CB  ASP A1039     5660  17271  19715   1592   2257    992       C  
ATOM   1987  CG  ASP A1039       4.616  18.370  32.524  1.00119.31           C  
ANISOU 1987  CG  ASP A1039     6552  18207  20573   1621   2399   1029       C  
ATOM   1988  OD1 ASP A1039       4.696  19.617  32.517  1.00112.27           O  
ANISOU 1988  OD1 ASP A1039     5695  17382  19581   1639   2396    946       O  
ATOM   1989  OD2 ASP A1039       4.237  17.718  33.520  1.00126.57           O  
ANISOU 1989  OD2 ASP A1039     7433  19093  21565   1626   2518   1140       O  
ATOM   1990  N   ALA A1040       4.669  16.889  28.094  1.00111.15           N  
ANISOU 1990  N   ALA A1040     5494  17082  19655   1501   1958    862       N  
ATOM   1991  CA  ALA A1040       5.164  16.279  26.867  1.00119.34           C  
ANISOU 1991  CA  ALA A1040     6538  18112  20692   1477   1820    805       C  
ATOM   1992  C   ALA A1040       5.000  17.182  25.652  1.00130.19           C  
ANISOU 1992  C   ALA A1040     7931  19552  21983   1472   1710    704       C  
ATOM   1993  O   ALA A1040       5.439  16.808  24.559  1.00126.74           O  
ANISOU 1993  O   ALA A1040     7504  19130  21522   1457   1589    648       O  
ATOM   1994  CB  ALA A1040       4.456  14.946  26.616  1.00111.62           C  
ANISOU 1994  CB  ALA A1040     5482  17043  19887   1420   1829    866       C  
ATOM   1995  N   GLN A1041       4.379  18.353  25.817  1.00138.49           N  
ANISOU 1995  N   GLN A1041     8986  20646  22990   1487   1752    686       N  
ATOM   1996  CA  GLN A1041       4.232  19.287  24.704  1.00132.52           C  
ANISOU 1996  CA  GLN A1041     8247  19955  22150   1493   1660    602       C  
ATOM   1997  C   GLN A1041       5.583  19.772  24.196  1.00128.24           C  
ANISOU 1997  C   GLN A1041     7791  19474  21461   1534   1567    521       C  
ATOM   1998  O   GLN A1041       5.737  20.052  23.001  1.00128.78           O  
ANISOU 1998  O   GLN A1041     7873  19588  21468   1534   1457    456       O  
ATOM   1999  CB  GLN A1041       3.366  20.474  25.139  1.00125.93           C  
ANISOU 1999  CB  GLN A1041     7402  19143  21303   1506   1742    608       C  
ATOM   2000  CG  GLN A1041       3.212  21.574  24.100  1.00124.27           C  
ANISOU 2000  CG  GLN A1041     7211  19000  21006   1523   1666    533       C  
ATOM   2001  CD  GLN A1041       2.298  21.179  22.960  1.00129.02           C  
ANISOU 2001  CD  GLN A1041     7743  19607  21670   1483   1590    525       C  
ATOM   2002  OE1 GLN A1041       1.137  20.828  23.173  1.00131.79           O  
ANISOU 2002  OE1 GLN A1041     8018  19920  22135   1447   1647    577       O  
ATOM   2003  NE2 GLN A1041       2.818  21.233  21.740  1.00129.75           N  
ANISOU 2003  NE2 GLN A1041     7858  19757  21685   1491   1464    457       N  
ATOM   2004  N   LYS A1042       6.575  19.862  25.082  1.00116.84           N  
ANISOU 2004  N   LYS A1042     6401  18037  19956   1571   1611    523       N  
ATOM   2005  CA  LYS A1042       7.897  20.386  24.740  1.00116.62           C  
ANISOU 2005  CA  LYS A1042     6456  18067  19787   1613   1536    444       C  
ATOM   2006  C   LYS A1042       8.599  19.394  23.815  1.00118.82           C  
ANISOU 2006  C   LYS A1042     6747  18336  20064   1596   1416    421       C  
ATOM   2007  O   LYS A1042       9.370  18.525  24.236  1.00105.09           O  
ANISOU 2007  O   LYS A1042     5021  16566  18341   1601   1416    448       O  
ATOM   2008  CB  LYS A1042       8.708  20.634  26.005  1.00114.89           C  
ANISOU 2008  CB  LYS A1042     6277  17863  19512   1655   1622    452       C  
ATOM   2009  CG  LYS A1042       7.978  21.470  27.052  1.00111.60           C  
ANISOU 2009  CG  LYS A1042     5841  17455  19107   1666   1755    481       C  
ATOM   2010  CD  LYS A1042       8.786  21.598  28.340  1.00115.64           C  
ANISOU 2010  CD  LYS A1042     6382  17996  19561   1706   1844    488       C  
ATOM   2011  CE  LYS A1042       8.014  22.366  29.405  1.00117.76           C  
ANISOU 2011  CE  LYS A1042     6623  18277  19842   1713   1984    517       C  
ATOM   2012  NZ  LYS A1042       8.798  22.512  30.663  1.00115.99           N  
ANISOU 2012  NZ  LYS A1042     6421  18100  19551   1753   2073    516       N  
ATOM   2013  N   ALA A1043       8.335  19.544  22.510  1.00126.70           N  
ANISOU 2013  N   ALA A1043     7738  19365  21038   1579   1313    372       N  
ATOM   2014  CA  ALA A1043       8.937  18.685  21.485  1.00128.51           C  
ANISOU 2014  CA  ALA A1043     7975  19597  21256   1560   1193    342       C  
ATOM   2015  C   ALA A1043       8.886  19.458  20.163  1.00135.30           C  
ANISOU 2015  C   ALA A1043     8853  20533  22019   1570   1091    270       C  
ATOM   2016  O   ALA A1043       8.044  19.210  19.295  1.00145.64           O  
ANISOU 2016  O   ALA A1043    10104  21858  23375   1536   1045    267       O  
ATOM   2017  CB  ALA A1043       8.224  17.339  21.373  1.00124.78           C  
ANISOU 2017  CB  ALA A1043     7421  19053  20936   1501   1198    399       C  
ATOM   2018  N   THR A1044       9.807  20.401  20.016  1.00125.26           N  
ANISOU 2018  N   THR A1044     7662  19318  20613   1620   1060    212       N  
ATOM   2019  CA  THR A1044       9.818  21.279  18.852  1.00121.38           C  
ANISOU 2019  CA  THR A1044     7195  18901  20023   1641    980    152       C  
ATOM   2020  C   THR A1044      10.549  20.605  17.696  1.00122.80           C  
ANISOU 2020  C   THR A1044     7397  19115  20146   1632    851    116       C  
ATOM   2021  O   THR A1044      11.659  20.098  17.885  1.00110.55           O  
ANISOU 2021  O   THR A1044     5899  17550  18557   1642    820    106       O  
ATOM   2022  CB  THR A1044      10.495  22.604  19.189  1.00113.53           C  
ANISOU 2022  CB  THR A1044     6276  17945  18916   1698   1011    107       C  
ATOM   2023  OG1 THR A1044       9.819  23.222  20.290  1.00111.79           O  
ANISOU 2023  OG1 THR A1044     6032  17696  18746   1703   1136    139       O  
ATOM   2024  CG2 THR A1044      10.467  23.538  17.995  1.00112.74           C  
ANISOU 2024  CG2 THR A1044     6198  17915  18724   1725    940     54       C  
ATOM   2025  N   PRO A1045       9.963  20.578  16.489  1.00133.15           N  
ANISOU 2025  N   PRO A1045     8667  20479  21447   1615    776     97       N  
ATOM   2026  CA  PRO A1045      10.613  20.024  15.298  1.00133.02           C  
ANISOU 2026  CA  PRO A1045     8668  20512  21363   1608    654     64       C  
ATOM   2027  C   PRO A1045      11.435  21.062  14.534  1.00124.55           C  
ANISOU 2027  C   PRO A1045     7672  19520  20130   1664    591      9       C  
ATOM   2028  O   PRO A1045      10.871  22.026  14.014  1.00118.78           O  
ANISOU 2028  O   PRO A1045     6928  18845  19357   1690    591    -12       O  
ATOM   2029  CB  PRO A1045       9.432  19.535  14.457  1.00131.57           C  
ANISOU 2029  CB  PRO A1045     8385  20358  21248   1563    619     73       C  
ATOM   2030  CG  PRO A1045       8.238  20.344  14.928  1.00127.23           C  
ANISOU 2030  CG  PRO A1045     7785  19804  20753   1569    705     94       C  
ATOM   2031  CD  PRO A1045       8.614  21.081  16.187  1.00127.17           C  
ANISOU 2031  CD  PRO A1045     7835  19745  20737   1604    804    108       C  
ATOM   2032  N   ASP A1060       3.175  20.272  12.762  1.00148.01           N  
ANISOU 2032  N   ASP A1060    10023  22614  23600   1471    688    111       N  
ATOM   2033  CA  ASP A1060       2.829  18.856  12.732  1.00146.15           C  
ANISOU 2033  CA  ASP A1060     9715  22338  23479   1400    676    131       C  
ATOM   2034  C   ASP A1060       2.786  18.273  14.142  1.00147.87           C  
ANISOU 2034  C   ASP A1060     9942  22411  23830   1370    783    191       C  
ATOM   2035  O   ASP A1060       1.739  17.814  14.600  1.00159.87           O  
ANISOU 2035  O   ASP A1060    11382  23879  25483   1327    849    230       O  
ATOM   2036  CB  ASP A1060       3.823  18.079  11.866  1.00138.85           C  
ANISOU 2036  CB  ASP A1060     8818  21452  22487   1387    569     97       C  
ATOM   2037  CG  ASP A1060       3.828  18.546  10.423  1.00131.71           C  
ANISOU 2037  CG  ASP A1060     7892  20704  21447   1416    465     48       C  
ATOM   2038  OD1 ASP A1060       2.766  18.984   9.933  1.00127.55           O  
ANISOU 2038  OD1 ASP A1060     7284  20259  20921   1421    463     39       O  
ATOM   2039  OD2 ASP A1060       4.896  18.475   9.778  1.00129.28           O  
ANISOU 2039  OD2 ASP A1060     7649  20444  21030   1436    386     23       O  
ATOM   2040  N   PHE A1061       3.933  18.292  14.824  1.00137.89           N  
ANISOU 2040  N   PHE A1061     8774  21088  22529   1394    803    199       N  
ATOM   2041  CA  PHE A1061       3.991  17.795  16.196  1.00135.22           C  
ANISOU 2041  CA  PHE A1061     8447  20628  22301   1377    909    259       C  
ATOM   2042  C   PHE A1061       3.143  18.657  17.124  1.00137.59           C  
ANISOU 2042  C   PHE A1061     8734  20901  22642   1395   1023    302       C  
ATOM   2043  O   PHE A1061       2.288  18.145  17.859  1.00133.92           O  
ANISOU 2043  O   PHE A1061     8208  20365  22313   1358   1109    359       O  
ATOM   2044  CB  PHE A1061       5.441  17.755  16.680  1.00133.24           C  
ANISOU 2044  CB  PHE A1061     8300  20346  21978   1410    901    253       C  
ATOM   2045  CG  PHE A1061       6.314  16.798  15.918  1.00143.94           C  
ANISOU 2045  CG  PHE A1061     9672  21709  23310   1388    801    222       C  
ATOM   2046  CD1 PHE A1061       6.826  17.139  14.677  1.00148.22           C  
ANISOU 2046  CD1 PHE A1061    10243  22352  23721   1409    687    162       C  
ATOM   2047  CD2 PHE A1061       6.636  15.562  16.453  1.00151.90           C  
ANISOU 2047  CD2 PHE A1061    10667  22621  24429   1350    827    257       C  
ATOM   2048  CE1 PHE A1061       7.633  16.262  13.979  1.00147.95           C  
ANISOU 2048  CE1 PHE A1061    10226  22324  23664   1387    599    138       C  
ATOM   2049  CE2 PHE A1061       7.445  14.682  15.760  1.00153.76           C  
ANISOU 2049  CE2 PHE A1061    10918  22853  24651   1328    739    228       C  
ATOM   2050  CZ  PHE A1061       7.943  15.033  14.522  1.00148.55           C  
ANISOU 2050  CZ  PHE A1061    10289  22296  23857   1344    624    168       C  
ATOM   2051  N   ARG A1062       3.370  19.974  17.101  1.00139.48           N  
ANISOU 2051  N   ARG A1062     9030  21193  22772   1450   1029    276       N  
ATOM   2052  CA  ARG A1062       2.578  20.889  17.916  1.00140.53           C  
ANISOU 2052  CA  ARG A1062     9153  21304  22939   1468   1137    313       C  
ATOM   2053  C   ARG A1062       1.095  20.789  17.586  1.00142.45           C  
ANISOU 2053  C   ARG A1062     9289  21560  23274   1433   1156    334       C  
ATOM   2054  O   ARG A1062       0.247  21.047  18.448  1.00140.32           O  
ANISOU 2054  O   ARG A1062     8987  21241  23087   1424   1261    387       O  
ATOM   2055  CB  ARG A1062       3.070  22.321  17.711  1.00137.10           C  
ANISOU 2055  CB  ARG A1062     8790  20926  22374   1530   1128    270       C  
ATOM   2056  CG  ARG A1062       4.582  22.448  17.643  1.00135.22           C  
ANISOU 2056  CG  ARG A1062     8652  20702  22022   1566   1077    227       C  
ATOM   2057  CD  ARG A1062       4.994  23.555  16.686  1.00138.14           C  
ANISOU 2057  CD  ARG A1062     9069  21156  22262   1616   1010    165       C  
ATOM   2058  NE  ARG A1062       6.437  23.583  16.465  1.00143.38           N  
ANISOU 2058  NE  ARG A1062     9823  21838  22816   1647    948    120       N  
ATOM   2059  CZ  ARG A1062       7.038  24.336  15.549  1.00140.76           C  
ANISOU 2059  CZ  ARG A1062     9540  21575  22367   1690    877     64       C  
ATOM   2060  NH1 ARG A1062       6.318  25.124  14.762  1.00148.17           N  
ANISOU 2060  NH1 ARG A1062    10443  22571  23284   1710    859     45       N  
ATOM   2061  NH2 ARG A1062       8.357  24.299  15.417  1.00125.40           N  
ANISOU 2061  NH2 ARG A1062     7677  19641  20327   1715    826     29       N  
ATOM   2062  N   HIS A1063       0.764  20.421  16.347  1.00140.49           N  
ANISOU 2062  N   HIS A1063     8983  21388  23010   1414   1056    293       N  
ATOM   2063  CA  HIS A1063      -0.632  20.211  15.983  1.00132.26           C  
ANISOU 2063  CA  HIS A1063     7827  20369  22054   1378   1066    306       C  
ATOM   2064  C   HIS A1063      -1.207  18.995  16.699  1.00133.60           C  
ANISOU 2064  C   HIS A1063     7933  20441  22388   1314   1132    360       C  
ATOM   2065  O   HIS A1063      -2.335  19.040  17.203  1.00149.92           O  
ANISOU 2065  O   HIS A1063     9935  22472  24557   1292   1213    403       O  
ATOM   2066  CB  HIS A1063      -0.755  20.058  14.466  1.00132.27           C  
ANISOU 2066  CB  HIS A1063     7777  20495  21986   1376    941    243       C  
ATOM   2067  CG  HIS A1063      -2.165  20.093  13.965  1.00143.69           C  
ANISOU 2067  CG  HIS A1063     9105  22000  23490   1353    942    243       C  
ATOM   2068  ND1 HIS A1063      -3.023  21.140  14.226  1.00147.15           N  
ANISOU 2068  ND1 HIS A1063     9522  22451  23935   1382   1005    262       N  
ATOM   2069  CD2 HIS A1063      -2.865  19.213  13.211  1.00148.19           C  
ANISOU 2069  CD2 HIS A1063     9568  22622  24114   1303    890    224       C  
ATOM   2070  CE1 HIS A1063      -4.191  20.901  13.658  1.00147.44           C  
ANISOU 2070  CE1 HIS A1063     9444  22550  24026   1354    989    255       C  
ATOM   2071  NE2 HIS A1063      -4.122  19.739  13.035  1.00148.09           N  
ANISOU 2071  NE2 HIS A1063     9471  22662  24135   1306    919    230       N  
ATOM   2072  N   GLY A1064      -0.441  17.904  16.765  1.00122.44           N  
ANISOU 2072  N   GLY A1064     6538  18975  21009   1285   1103    360       N  
ATOM   2073  CA  GLY A1064      -0.928  16.712  17.442  1.00112.67           C  
ANISOU 2073  CA  GLY A1064     5240  17630  19940   1226   1172    413       C  
ATOM   2074  C   GLY A1064      -1.036  16.898  18.944  1.00112.91           C  
ANISOU 2074  C   GLY A1064     5302  17561  20039   1238   1311    491       C  
ATOM   2075  O   GLY A1064      -2.068  16.590  19.549  1.00114.11           O  
ANISOU 2075  O   GLY A1064     5386  17652  20320   1205   1401    545       O  
ATOM   2076  N   PHE A1065       0.031  17.407  19.569  1.00113.76           N  
ANISOU 2076  N   PHE A1065     5509  17658  20057   1286   1332    497       N  
ATOM   2077  CA  PHE A1065      -0.003  17.634  21.011  1.00113.04           C  
ANISOU 2077  CA  PHE A1065     5447  17493  20011   1303   1465    569       C  
ATOM   2078  C   PHE A1065      -1.070  18.657  21.383  1.00113.77           C  
ANISOU 2078  C   PHE A1065     5512  17602  20113   1316   1542    593       C  
ATOM   2079  O   PHE A1065      -1.799  18.476  22.366  1.00114.51           O  
ANISOU 2079  O   PHE A1065     5570  17628  20311   1299   1658    664       O  
ATOM   2080  CB  PHE A1065       1.370  18.089  21.510  1.00117.14           C  
ANISOU 2080  CB  PHE A1065     6073  18022  20412   1355   1464    556       C  
ATOM   2081  CG  PHE A1065       2.445  17.047  21.375  1.00121.39           C  
ANISOU 2081  CG  PHE A1065     6642  18529  20953   1346   1409    547       C  
ATOM   2082  CD1 PHE A1065       2.390  15.875  22.111  1.00111.15           C  
ANISOU 2082  CD1 PHE A1065     5310  17135  19788   1314   1477    616       C  
ATOM   2083  CD2 PHE A1065       3.522  17.250  20.527  1.00127.36           C  
ANISOU 2083  CD2 PHE A1065     7461  19348  21582   1371   1294    476       C  
ATOM   2084  CE1 PHE A1065       3.381  14.919  21.992  1.00110.89           C  
ANISOU 2084  CE1 PHE A1065     5302  17066  19765   1307   1431    612       C  
ATOM   2085  CE2 PHE A1065       4.516  16.298  20.404  1.00121.99           C  
ANISOU 2085  CE2 PHE A1065     6810  18637  20906   1362   1244    469       C  
ATOM   2086  CZ  PHE A1065       4.446  15.131  21.138  1.00117.12           C  
ANISOU 2086  CZ  PHE A1065     6155  17920  20425   1330   1312    537       C  
ATOM   2087  N   ASP A1066      -1.182  19.736  20.603  1.00112.09           N  
ANISOU 2087  N   ASP A1066     5315  17479  19795   1348   1483    538       N  
ATOM   2088  CA  ASP A1066      -2.170  20.767  20.903  1.00112.61           C  
ANISOU 2088  CA  ASP A1066     5356  17560  19871   1363   1555    559       C  
ATOM   2089  C   ASP A1066      -3.590  20.245  20.718  1.00118.02           C  
ANISOU 2089  C   ASP A1066     5929  18227  20686   1313   1580    589       C  
ATOM   2090  O   ASP A1066      -4.480  20.552  21.521  1.00118.56           O  
ANISOU 2090  O   ASP A1066     5966  18252  20828   1306   1687    645       O  
ATOM   2091  CB  ASP A1066      -1.925  21.994  20.025  1.00111.77           C  
ANISOU 2091  CB  ASP A1066     5288  17548  19630   1411   1484    494       C  
ATOM   2092  CG  ASP A1066      -2.761  23.187  20.444  1.00117.83           C  
ANISOU 2092  CG  ASP A1066     6047  18322  20402   1435   1569    518       C  
ATOM   2093  OD1 ASP A1066      -2.541  23.705  21.559  1.00120.49           O  
ANISOU 2093  OD1 ASP A1066     6432  18613  20734   1455   1670    552       O  
ATOM   2094  OD2 ASP A1066      -3.635  23.610  19.658  1.00117.42           O  
ANISOU 2094  OD2 ASP A1066     5935  18325  20354   1436   1535    501       O  
ATOM   2095  N   ILE A1067      -3.821  19.455  19.665  1.00126.11           N  
ANISOU 2095  N   ILE A1067     6889  19288  21737   1277   1485    550       N  
ATOM   2096  CA  ILE A1067      -5.129  18.832  19.475  1.00115.87           C  
ANISOU 2096  CA  ILE A1067     5477  17976  20571   1224   1507    571       C  
ATOM   2097  C   ILE A1067      -5.460  17.925  20.652  1.00116.78           C  
ANISOU 2097  C   ILE A1067     5567  17964  20838   1184   1623    649       C  
ATOM   2098  O   ILE A1067      -6.589  17.925  21.158  1.00117.91           O  
ANISOU 2098  O   ILE A1067     5648  18066  21087   1160   1710    698       O  
ATOM   2099  CB  ILE A1067      -5.170  18.068  18.137  1.00116.09           C  
ANISOU 2099  CB  ILE A1067     5440  18075  20593   1190   1382    505       C  
ATOM   2100  CG1 ILE A1067      -5.498  19.020  16.984  1.00115.87           C  
ANISOU 2100  CG1 ILE A1067     5389  18188  20450   1225   1295    445       C  
ATOM   2101  CG2 ILE A1067      -6.173  16.923  18.192  1.00117.61           C  
ANISOU 2101  CG2 ILE A1067     5522  18211  20954   1119   1416    528       C  
ATOM   2102  CD1 ILE A1067      -5.615  18.330  15.643  1.00116.23           C  
ANISOU 2102  CD1 ILE A1067     5359  18329  20473   1195   1175    380       C  
ATOM   2103  N   LEU A1068      -4.477  17.147  21.115  1.00119.73           N  
ANISOU 2103  N   LEU A1068     5991  18274  21228   1179   1631    668       N  
ATOM   2104  CA  LEU A1068      -4.702  16.281  22.268  1.00117.22           C  
ANISOU 2104  CA  LEU A1068     5652  17834  21052   1151   1749    751       C  
ATOM   2105  C   LEU A1068      -5.067  17.092  23.506  1.00117.43           C  
ANISOU 2105  C   LEU A1068     5709  17829  21079   1182   1881    820       C  
ATOM   2106  O   LEU A1068      -5.992  16.729  24.244  1.00118.63           O  
ANISOU 2106  O   LEU A1068     5806  17910  21360   1154   1987    888       O  
ATOM   2107  CB  LEU A1068      -3.461  15.428  22.529  1.00119.40           C  
ANISOU 2107  CB  LEU A1068     5983  18060  21325   1153   1732    760       C  
ATOM   2108  CG  LEU A1068      -3.571  14.372  23.631  1.00118.89           C  
ANISOU 2108  CG  LEU A1068     5893  17868  21410   1127   1851    852       C  
ATOM   2109  CD1 LEU A1068      -4.608  13.324  23.263  1.00119.04           C  
ANISOU 2109  CD1 LEU A1068     5802  17825  21603   1057   1863    860       C  
ATOM   2110  CD2 LEU A1068      -2.220  13.727  23.893  1.00119.84           C  
ANISOU 2110  CD2 LEU A1068     6079  17955  21501   1146   1831    861       C  
ATOM   2111  N   VAL A1069      -4.358  18.200  23.744  1.00126.22           N  
ANISOU 2111  N   VAL A1069     6909  18996  22053   1239   1879    800       N  
ATOM   2112  CA  VAL A1069      -4.657  19.043  24.900  1.00124.41           C  
ANISOU 2112  CA  VAL A1069     6709  18748  21814   1268   2003    854       C  
ATOM   2113  C   VAL A1069      -6.064  19.618  24.795  1.00117.46           C  
ANISOU 2113  C   VAL A1069     5760  17877  20990   1252   2046    868       C  
ATOM   2114  O   VAL A1069      -6.799  19.684  25.788  1.00118.35           O  
ANISOU 2114  O   VAL A1069     5850  17936  21183   1244   2169    938       O  
ATOM   2115  CB  VAL A1069      -3.598  20.153  25.040  1.00122.15           C  
ANISOU 2115  CB  VAL A1069     6523  18523  21365   1328   1984    811       C  
ATOM   2116  CG1 VAL A1069      -4.008  21.153  26.113  1.00115.43           C  
ANISOU 2116  CG1 VAL A1069     5694  17666  20498   1355   2109    851       C  
ATOM   2117  CG2 VAL A1069      -2.240  19.552  25.365  1.00114.36           C  
ANISOU 2117  CG2 VAL A1069     5600  17521  20331   1346   1962    808       C  
ATOM   2118  N   GLY A1070      -6.465  20.034  23.592  1.00117.33           N  
ANISOU 2118  N   GLY A1070     5710  17937  20933   1250   1946    805       N  
ATOM   2119  CA  GLY A1070      -7.804  20.575  23.420  1.00127.47           C  
ANISOU 2119  CA  GLY A1070     6923  19240  22269   1238   1980    817       C  
ATOM   2120  C   GLY A1070      -8.892  19.542  23.649  1.00123.42           C  
ANISOU 2120  C   GLY A1070     6311  18658  21924   1179   2034    865       C  
ATOM   2121  O   GLY A1070      -9.902  19.825  24.303  1.00120.70           O  
ANISOU 2121  O   GLY A1070     5927  18276  21657   1168   2133    918       O  
ATOM   2122  N   GLN A1071      -8.702  18.331  23.119  1.00134.06           N  
ANISOU 2122  N   GLN A1071     7616  19984  23336   1137   1972    845       N  
ATOM   2123  CA  GLN A1071      -9.692  17.276  23.313  1.00121.53           C  
ANISOU 2123  CA  GLN A1071     5932  18321  21922   1075   2026    884       C  
ATOM   2124  C   GLN A1071      -9.789  16.869  24.778  1.00122.15           C  
ANISOU 2124  C   GLN A1071     6028  18283  22101   1070   2177    983       C  
ATOM   2125  O   GLN A1071     -10.892  16.648  25.293  1.00123.41           O  
ANISOU 2125  O   GLN A1071     6122  18384  22384   1040   2270   1037       O  
ATOM   2126  CB  GLN A1071      -9.352  16.067  22.443  1.00121.69           C  
ANISOU 2126  CB  GLN A1071     5907  18338  21990   1031   1932    834       C  
ATOM   2127  CG  GLN A1071      -9.434  16.327  20.951  1.00121.39           C  
ANISOU 2127  CG  GLN A1071     5829  18427  21864   1030   1788    738       C  
ATOM   2128  CD  GLN A1071      -9.099  15.097  20.133  1.00124.26           C  
ANISOU 2128  CD  GLN A1071     6145  18788  22278    981   1702    687       C  
ATOM   2129  OE1 GLN A1071      -8.726  14.058  20.680  1.00130.10           O  
ANISOU 2129  OE1 GLN A1071     6889  19420  23123    950   1749    722       O  
ATOM   2130  NE2 GLN A1071      -9.230  15.206  18.817  1.00124.73           N  
ANISOU 2130  NE2 GLN A1071     6157  18970  22264    976   1579    605       N  
ATOM   2131  N   ILE A1072      -8.648  16.755  25.463  1.00129.66           N  
ANISOU 2131  N   ILE A1072     7063  19204  22997   1101   2205   1011       N  
ATOM   2132  CA  ILE A1072      -8.676  16.463  26.894  1.00127.89           C  
ANISOU 2132  CA  ILE A1072     6859  18890  22844   1108   2353   1111       C  
ATOM   2133  C   ILE A1072      -9.356  17.593  27.655  1.00122.18           C  
ANISOU 2133  C   ILE A1072     6148  18183  22090   1135   2450   1148       C  
ATOM   2134  O   ILE A1072     -10.041  17.357  28.658  1.00123.23           O  
ANISOU 2134  O   ILE A1072     6254  18247  22322   1123   2580   1231       O  
ATOM   2135  CB  ILE A1072      -7.247  16.200  27.413  1.00123.62           C  
ANISOU 2135  CB  ILE A1072     6404  18339  22227   1144   2355   1127       C  
ATOM   2136  CG1 ILE A1072      -6.663  14.947  26.757  1.00120.95           C  
ANISOU 2136  CG1 ILE A1072     6044  17963  21948   1111   2276   1102       C  
ATOM   2137  CG2 ILE A1072      -7.232  16.049  28.927  1.00122.92           C  
ANISOU 2137  CG2 ILE A1072     6336  18185  22182   1164   2512   1233       C  
ATOM   2138  CD1 ILE A1072      -5.246  14.641  27.184  1.00120.03           C  
ANISOU 2138  CD1 ILE A1072     6008  17840  21760   1148   2269   1117       C  
ATOM   2139  N   ASP A1073      -9.201  18.831  27.181  1.00131.35           N  
ANISOU 2139  N   ASP A1073     7351  19435  23120   1172   2393   1089       N  
ATOM   2140  CA  ASP A1073      -9.818  19.968  27.856  1.00134.74           C  
ANISOU 2140  CA  ASP A1073     7794  19879  23521   1197   2484   1117       C  
ATOM   2141  C   ASP A1073     -11.336  19.939  27.710  1.00135.18           C  
ANISOU 2141  C   ASP A1073     7757  19912  23695   1159   2524   1142       C  
ATOM   2142  O   ASP A1073     -12.067  20.142  28.687  1.00129.41           O  
ANISOU 2142  O   ASP A1073     7010  19131  23028   1155   2650   1210       O  
ATOM   2143  CB  ASP A1073      -9.242  21.273  27.305  1.00134.72           C  
ANISOU 2143  CB  ASP A1073     7857  19970  23360   1245   2413   1045       C  
ATOM   2144  CG  ASP A1073      -9.444  22.444  28.246  1.00143.21           C  
ANISOU 2144  CG  ASP A1073     8974  21053  24387   1279   2522   1072       C  
ATOM   2145  OD1 ASP A1073     -10.035  22.246  29.328  1.00147.76           O  
ANISOU 2145  OD1 ASP A1073     9530  21570  25044   1267   2649   1146       O  
ATOM   2146  OD2 ASP A1073      -9.008  23.563  27.903  1.00147.50           O  
ANISOU 2146  OD2 ASP A1073     9569  21659  24814   1319   2484   1017       O  
ATOM   2147  N   ASP A1074     -11.831  19.687  26.493  1.00136.15           N  
ANISOU 2147  N   ASP A1074     7812  20075  23843   1131   2418   1085       N  
ATOM   2148  CA  ASP A1074     -13.276  19.603  26.293  1.00124.36           C  
ANISOU 2148  CA  ASP A1074     6220  18569  22463   1094   2449   1101       C  
ATOM   2149  C   ASP A1074     -13.867  18.397  27.013  1.00125.68           C  
ANISOU 2149  C   ASP A1074     6327  18623  22801   1044   2545   1171       C  
ATOM   2150  O   ASP A1074     -14.965  18.481  27.577  1.00126.80           O  
ANISOU 2150  O   ASP A1074     6418  18719  23039   1025   2642   1224       O  
ATOM   2151  CB  ASP A1074     -13.602  19.548  24.801  1.00124.38           C  
ANISOU 2151  CB  ASP A1074     6156  18660  22443   1077   2310   1017       C  
ATOM   2152  CG  ASP A1074     -13.463  20.895  24.124  1.00142.69           C  
ANISOU 2152  CG  ASP A1074     8510  21086  24619   1129   2243    965       C  
ATOM   2153  OD1 ASP A1074     -13.756  21.921  24.773  1.00145.04           O  
ANISOU 2153  OD1 ASP A1074     8843  21378  24888   1160   2324    999       O  
ATOM   2154  OD2 ASP A1074     -13.063  20.926  22.942  1.00147.62           O  
ANISOU 2154  OD2 ASP A1074     9127  21800  25164   1138   2115    890       O  
ATOM   2155  N   ALA A1075     -13.160  17.264  26.997  1.00136.25           N  
ANISOU 2155  N   ALA A1075     7671  19912  24186   1022   2523   1175       N  
ATOM   2156  CA  ALA A1075     -13.616  16.102  27.751  1.00136.29           C  
ANISOU 2156  CA  ALA A1075     7627  19797  24360    980   2627   1251       C  
ATOM   2157  C   ALA A1075     -13.674  16.409  29.241  1.00131.64           C  
ANISOU 2157  C   ALA A1075     7084  19149  23785   1008   2784   1351       C  
ATOM   2158  O   ALA A1075     -14.563  15.922  29.951  1.00128.51           O  
ANISOU 2158  O   ALA A1075     6636  18668  23525    980   2899   1424       O  
ATOM   2159  CB  ALA A1075     -12.703  14.906  27.481  1.00136.09           C  
ANISOU 2159  CB  ALA A1075     7608  19726  24372    960   2579   1239       C  
ATOM   2160  N   LEU A1076     -12.734  17.220  29.732  1.00135.31           N  
ANISOU 2160  N   LEU A1076     7645  19662  24106   1064   2794   1353       N  
ATOM   2161  CA  LEU A1076     -12.803  17.673  31.116  1.00135.38           C  
ANISOU 2161  CA  LEU A1076     7694  19642  24101   1095   2940   1436       C  
ATOM   2162  C   LEU A1076     -13.981  18.613  31.333  1.00134.41           C  
ANISOU 2162  C   LEU A1076     7540  19534  23995   1093   3000   1447       C  
ATOM   2163  O   LEU A1076     -14.553  18.644  32.429  1.00127.89           O  
ANISOU 2163  O   LEU A1076     6707  18657  23230   1094   3138   1527       O  
ATOM   2164  CB  LEU A1076     -11.491  18.352  31.511  1.00133.06           C  
ANISOU 2164  CB  LEU A1076     7503  19411  23642   1153   2927   1416       C  
ATOM   2165  CG  LEU A1076     -11.313  18.708  32.988  1.00130.22           C  
ANISOU 2165  CG  LEU A1076     7189  19039  23248   1189   3075   1494       C  
ATOM   2166  CD1 LEU A1076     -11.432  17.465  33.857  1.00127.95           C  
ANISOU 2166  CD1 LEU A1076     6872  18658  23087   1173   3184   1600       C  
ATOM   2167  CD2 LEU A1076      -9.977  19.399  33.215  1.00123.96           C  
ANISOU 2167  CD2 LEU A1076     6490  18324  22284   1243   3045   1451       C  
ATOM   2168  N   LYS A1077     -14.360  19.381  30.307  1.00137.46           N  
ANISOU 2168  N   LYS A1077     7907  19993  24329   1093   2902   1370       N  
ATOM   2169  CA  LYS A1077     -15.558  20.208  30.409  1.00135.19           C  
ANISOU 2169  CA  LYS A1077     7578  19717  24072   1089   2954   1382       C  
ATOM   2170  C   LYS A1077     -16.812  19.348  30.512  1.00135.46           C  
ANISOU 2170  C   LYS A1077     7511  19672  24284   1034   3013   1429       C  
ATOM   2171  O   LYS A1077     -17.754  19.698  31.232  1.00129.80           O  
ANISOU 2171  O   LYS A1077     6769  18919  23630   1029   3122   1484       O  
ATOM   2172  CB  LYS A1077     -15.654  21.156  29.213  1.00131.72           C  
ANISOU 2172  CB  LYS A1077     7133  19376  23538   1106   2833   1296       C  
ATOM   2173  CG  LYS A1077     -14.550  22.197  29.148  1.00130.98           C  
ANISOU 2173  CG  LYS A1077     7137  19353  23276   1162   2791   1250       C  
ATOM   2174  CD  LYS A1077     -14.734  23.122  27.955  1.00133.47           C  
ANISOU 2174  CD  LYS A1077     7442  19760  23511   1183   2683   1176       C  
ATOM   2175  CE  LYS A1077     -13.625  24.160  27.885  1.00140.80           C  
ANISOU 2175  CE  LYS A1077     8467  20747  24282   1238   2648   1129       C  
ATOM   2176  NZ  LYS A1077     -13.796  25.083  26.729  1.00142.97           N  
ANISOU 2176  NZ  LYS A1077     8732  21107  24482   1264   2553   1066       N  
ATOM   2177  N   LEU A1078     -16.845  18.221  29.795  1.00135.53           N  
ANISOU 2177  N   LEU A1078     7461  19654  24380    992   2944   1403       N  
ATOM   2178  CA  LEU A1078     -17.957  17.289  29.951  1.00134.52           C  
ANISOU 2178  CA  LEU A1078     7236  19439  24434    936   3009   1444       C  
ATOM   2179  C   LEU A1078     -17.919  16.595  31.306  1.00133.77           C  
ANISOU 2179  C   LEU A1078     7160  19232  24434    933   3162   1552       C  
ATOM   2180  O   LEU A1078     -18.974  16.273  31.864  1.00132.99           O  
ANISOU 2180  O   LEU A1078     7003  19059  24469    904   3267   1612       O  
ATOM   2181  CB  LEU A1078     -17.945  16.251  28.828  1.00132.05           C  
ANISOU 2181  CB  LEU A1078     6854  19128  24192    888   2898   1378       C  
ATOM   2182  CG  LEU A1078     -18.603  16.657  27.509  1.00132.55           C  
ANISOU 2182  CG  LEU A1078     6845  19293  24227    872   2777   1286       C  
ATOM   2183  CD1 LEU A1078     -18.517  15.525  26.499  1.00131.60           C  
ANISOU 2183  CD1 LEU A1078     6653  19176  24176    822   2678   1218       C  
ATOM   2184  CD2 LEU A1078     -20.051  17.059  27.742  1.00133.68           C  
ANISOU 2184  CD2 LEU A1078     6913  19423  24455    854   2850   1314       C  
ATOM   2185  N   ALA A1079     -16.722  16.356  31.847  1.00133.72           N  
ANISOU 2185  N   ALA A1079     7232  19217  24360    966   3180   1582       N  
ATOM   2186  CA  ALA A1079     -16.619  15.727  33.159  1.00137.86           C  
ANISOU 2186  CA  ALA A1079     7774  19651  24957    974   3330   1694       C  
ATOM   2187  C   ALA A1079     -17.065  16.668  34.270  1.00138.39           C  
ANISOU 2187  C   ALA A1079     7875  19729  24979   1007   3455   1755       C  
ATOM   2188  O   ALA A1079     -17.641  16.218  35.267  1.00133.13           O  
ANISOU 2188  O   ALA A1079     7185  18983  24414    999   3596   1851       O  
ATOM   2189  CB  ALA A1079     -15.187  15.253  33.405  1.00134.82           C  
ANISOU 2189  CB  ALA A1079     7460  19269  24497   1006   3310   1708       C  
ATOM   2190  N   ASN A1080     -16.814  17.970  34.119  1.00136.87           N  
ANISOU 2190  N   ASN A1080     7734  19631  24638   1043   3412   1700       N  
ATOM   2191  CA  ASN A1080     -17.214  18.938  35.133  1.00137.99           C  
ANISOU 2191  CA  ASN A1080     7907  19790  24732   1072   3529   1744       C  
ATOM   2192  C   ASN A1080     -18.714  19.204  35.138  1.00138.39           C  
ANISOU 2192  C   ASN A1080     7885  19805  24891   1039   3583   1764       C  
ATOM   2193  O   ASN A1080     -19.193  19.922  36.022  1.00137.42           O  
ANISOU 2193  O   ASN A1080     7779  19683  24751   1057   3692   1806       O  
ATOM   2194  CB  ASN A1080     -16.455  20.251  34.933  1.00141.13           C  
ANISOU 2194  CB  ASN A1080     8381  20292  24948   1119   3469   1672       C  
ATOM   2195  CG  ASN A1080     -14.956  20.090  35.108  1.00139.08           C  
ANISOU 2195  CG  ASN A1080     8199  20072  24572   1156   3432   1655       C  
ATOM   2196  OD1 ASN A1080     -14.495  19.225  35.853  1.00140.18           O  
ANISOU 2196  OD1 ASN A1080     8350  20168  24746   1163   3502   1724       O  
ATOM   2197  ND2 ASN A1080     -14.186  20.925  34.419  1.00127.68           N  
ANISOU 2197  ND2 ASN A1080     6808  18713  22992   1185   3326   1566       N  
ATOM   2198  N   GLU A1081     -19.461  18.652  34.181  1.00144.01           N  
ANISOU 2198  N   GLU A1081     8515  20492  25712    992   3511   1729       N  
ATOM   2199  CA  GLU A1081     -20.911  18.784  34.153  1.00143.49           C  
ANISOU 2199  CA  GLU A1081     8368  20391  25759    959   3560   1746       C  
ATOM   2200  C   GLU A1081     -21.634  17.541  34.653  1.00135.69           C  
ANISOU 2200  C   GLU A1081     7312  19284  24959    914   3658   1821       C  
ATOM   2201  O   GLU A1081     -22.830  17.620  34.950  1.00141.57           O  
ANISOU 2201  O   GLU A1081     7999  19985  25806    889   3734   1855       O  
ATOM   2202  CB  GLU A1081     -21.391  19.113  32.732  1.00147.49           C  
ANISOU 2202  CB  GLU A1081     8816  20967  26257    939   3419   1651       C  
ATOM   2203  CG  GLU A1081     -20.922  20.461  32.211  1.00152.03           C  
ANISOU 2203  CG  GLU A1081     9448  21653  26664    985   3337   1586       C  
ATOM   2204  CD  GLU A1081     -21.615  20.859  30.923  1.00151.42           C  
ANISOU 2204  CD  GLU A1081     9301  21648  26585    972   3223   1511       C  
ATOM   2205  OE1 GLU A1081     -22.603  20.192  30.548  1.00145.80           O  
ANISOU 2205  OE1 GLU A1081     8491  20905  26001    925   3220   1511       O  
ATOM   2206  OE2 GLU A1081     -21.174  21.838  30.284  1.00151.91           O  
ANISOU 2206  OE2 GLU A1081     9403  21802  26515   1010   3139   1454       O  
ATOM   2207  N   GLY A1082     -20.946  16.405  34.751  1.00135.76           N  
ANISOU 2207  N   GLY A1082     7327  19236  25021    903   3661   1848       N  
ATOM   2208  CA  GLY A1082     -21.531  15.177  35.251  1.00137.26           C  
ANISOU 2208  CA  GLY A1082     7456  19301  25396    864   3763   1924       C  
ATOM   2209  C   GLY A1082     -21.736  14.100  34.209  1.00138.15           C  
ANISOU 2209  C   GLY A1082     7488  19371  25633    807   3675   1867       C  
ATOM   2210  O   GLY A1082     -22.121  12.981  34.570  1.00139.02           O  
ANISOU 2210  O   GLY A1082     7547  19364  25909    772   3759   1924       O  
ATOM   2211  N   LYS A1083     -21.493  14.393  32.933  1.00139.94           N  
ANISOU 2211  N   LYS A1083     7698  19688  25785    798   3514   1754       N  
ATOM   2212  CA  LYS A1083     -21.686  13.416  31.866  1.00137.38           C  
ANISOU 2212  CA  LYS A1083     7291  19342  25565    742   3422   1683       C  
ATOM   2213  C   LYS A1083     -20.463  12.510  31.795  1.00136.81           C  
ANISOU 2213  C   LYS A1083     7259  19234  25489    745   3389   1685       C  
ATOM   2214  O   LYS A1083     -19.388  12.937  31.361  1.00137.36           O  
ANISOU 2214  O   LYS A1083     7397  19388  25406    780   3289   1636       O  
ATOM   2215  CB  LYS A1083     -21.933  14.125  30.538  1.00136.76           C  
ANISOU 2215  CB  LYS A1083     7175  19393  25396    736   3266   1565       C  
ATOM   2216  CG  LYS A1083     -23.123  15.074  30.563  1.00137.77           C  
ANISOU 2216  CG  LYS A1083     7260  19563  25522    738   3295   1565       C  
ATOM   2217  CD  LYS A1083     -23.343  15.738  29.214  1.00136.81           C  
ANISOU 2217  CD  LYS A1083     7096  19578  25306    740   3143   1457       C  
ATOM   2218  CE  LYS A1083     -24.549  16.666  29.250  1.00140.27           C  
ANISOU 2218  CE  LYS A1083     7488  20056  25751    745   3177   1464       C  
ATOM   2219  NZ  LYS A1083     -24.815  17.291  27.925  1.00139.39           N  
ANISOU 2219  NZ  LYS A1083     7325  20087  25550    752   3035   1368       N  
ATOM   2220  N   VAL A1084     -20.625  11.258  32.215  1.00138.00           N  
ANISOU 2220  N   VAL A1084     7369  19254  25812    710   3477   1743       N  
ATOM   2221  CA  VAL A1084     -19.508  10.320  32.273  1.00137.66           C  
ANISOU 2221  CA  VAL A1084     7361  19158  25786    715   3469   1763       C  
ATOM   2222  C   VAL A1084     -19.396   9.501  30.992  1.00137.75           C  
ANISOU 2222  C   VAL A1084     7306  19170  25865    660   3343   1655       C  
ATOM   2223  O   VAL A1084     -18.293   9.290  30.481  1.00138.27           O  
ANISOU 2223  O   VAL A1084     7415  19273  25848    673   3249   1610       O  
ATOM   2224  CB  VAL A1084     -19.654   9.412  33.511  1.00138.95           C  
ANISOU 2224  CB  VAL A1084     7522  19175  26098    716   3650   1900       C  
ATOM   2225  CG1 VAL A1084     -18.465   8.470  33.627  1.00138.63           C  
ANISOU 2225  CG1 VAL A1084     7521  19080  26073    729   3651   1934       C  
ATOM   2226  CG2 VAL A1084     -19.802  10.253  34.770  1.00138.94           C  
ANISOU 2226  CG2 VAL A1084     7582  19191  26017    771   3775   2002       C  
ATOM   2227  N   LYS A1085     -20.527   9.031  30.458  1.00140.21           N  
ANISOU 2227  N   LYS A1085     7508  19443  26322    597   3341   1607       N  
ATOM   2228  CA  LYS A1085     -20.492   8.196  29.260  1.00139.37           C  
ANISOU 2228  CA  LYS A1085     7326  19339  26288    539   3229   1497       C  
ATOM   2229  C   LYS A1085     -19.926   8.957  28.067  1.00147.26           C  
ANISOU 2229  C   LYS A1085     8347  20507  27098    557   3046   1381       C  
ATOM   2230  O   LYS A1085     -19.101   8.423  27.315  1.00158.49           O  
ANISOU 2230  O   LYS A1085     9775  21951  28493    543   2946   1313       O  
ATOM   2231  CB  LYS A1085     -21.894   7.674  28.945  1.00141.13           C  
ANISOU 2231  CB  LYS A1085     7422  19508  26692    470   3265   1462       C  
ATOM   2232  CG  LYS A1085     -22.508   6.829  30.050  1.00142.74           C  
ANISOU 2232  CG  LYS A1085     7597  19534  27104    448   3450   1573       C  
ATOM   2233  CD  LYS A1085     -21.693   5.572  30.301  1.00151.04           C  
ANISOU 2233  CD  LYS A1085     8662  20456  28270    434   3501   1613       C  
ATOM   2234  CE  LYS A1085     -22.333   4.705  31.374  1.00161.18           C  
ANISOU 2234  CE  LYS A1085     9914  21560  29769    416   3694   1731       C  
ATOM   2235  NZ  LYS A1085     -21.552   3.462  31.621  1.00167.26           N  
ANISOU 2235  NZ  LYS A1085    10695  22197  30661    407   3755   1779       N  
ATOM   2236  N   GLU A1086     -20.358  10.206  27.878  1.00137.32           N  
ANISOU 2236  N   GLU A1086     7101  19367  25709    589   3003   1358       N  
ATOM   2237  CA  GLU A1086     -19.837  11.008  26.776  1.00135.98           C  
ANISOU 2237  CA  GLU A1086     6954  19358  25353    615   2839   1259       C  
ATOM   2238  C   GLU A1086     -18.346  11.274  26.947  1.00147.27           C  
ANISOU 2238  C   GLU A1086     8503  20817  26635    669   2796   1271       C  
ATOM   2239  O   GLU A1086     -17.599  11.323  25.962  1.00150.23           O  
ANISOU 2239  O   GLU A1086     8895  21282  26904    674   2660   1186       O  
ATOM   2240  CB  GLU A1086     -20.611  12.322  26.672  1.00135.80           C  
ANISOU 2240  CB  GLU A1086     6925  19440  25234    645   2826   1250       C  
ATOM   2241  CG  GLU A1086     -22.107  12.142  26.468  1.00144.31           C  
ANISOU 2241  CG  GLU A1086     7882  20504  26445    596   2861   1235       C  
ATOM   2242  CD  GLU A1086     -22.847  13.461  26.366  1.00140.25           C  
ANISOU 2242  CD  GLU A1086     7361  20092  25835    631   2850   1231       C  
ATOM   2243  OE1 GLU A1086     -22.186  14.520  26.409  1.00142.19           O  
ANISOU 2243  OE1 GLU A1086     7696  20416  25912    691   2813   1235       O  
ATOM   2244  OE2 GLU A1086     -24.089  13.440  26.242  1.00138.55           O  
ANISOU 2244  OE2 GLU A1086     7049  19875  25717    597   2881   1223       O  
ATOM   2245  N   ALA A1087     -17.895  11.444  28.192  1.00144.44           N  
ANISOU 2245  N   ALA A1087     8227  20391  26264    710   2913   1377       N  
ATOM   2246  CA  ALA A1087     -16.468  11.618  28.440  1.00140.03           C  
ANISOU 2246  CA  ALA A1087     7776  19857  25573    760   2883   1391       C  
ATOM   2247  C   ALA A1087     -15.689  10.344  28.145  1.00132.70           C  
ANISOU 2247  C   ALA A1087     6839  18858  24723    731   2853   1378       C  
ATOM   2248  O   ALA A1087     -14.532  10.413  27.715  1.00131.42           O  
ANISOU 2248  O   ALA A1087     6740  18751  24443    758   2759   1335       O  
ATOM   2249  CB  ALA A1087     -16.234  12.064  29.883  1.00135.71           C  
ANISOU 2249  CB  ALA A1087     7305  19267  24993    811   3024   1507       C  
ATOM   2250  N   GLN A1088     -16.299   9.177  28.367  1.00134.23           N  
ANISOU 2250  N   GLN A1088     6955  18924  25122    677   2935   1412       N  
ATOM   2251  CA  GLN A1088     -15.622   7.922  28.057  1.00134.47           C  
ANISOU 2251  CA  GLN A1088     6970  18873  25249    644   2914   1396       C  
ATOM   2252  C   GLN A1088     -15.551   7.692  26.552  1.00134.19           C  
ANISOU 2252  C   GLN A1088     6879  18919  25188    601   2749   1253       C  
ATOM   2253  O   GLN A1088     -14.534   7.206  26.040  1.00142.12           O  
ANISOU 2253  O   GLN A1088     7915  19930  26155    600   2669   1209       O  
ATOM   2254  CB  GLN A1088     -16.327   6.760  28.753  1.00140.85           C  
ANISOU 2254  CB  GLN A1088     7710  19511  26296    599   3063   1475       C  
ATOM   2255  CG  GLN A1088     -16.199   6.788  30.268  1.00146.22           C  
ANISOU 2255  CG  GLN A1088     8449  20108  26999    648   3232   1630       C  
ATOM   2256  CD  GLN A1088     -16.951   5.658  30.940  1.00156.66           C  
ANISOU 2256  CD  GLN A1088     9703  21260  28562    608   3387   1716       C  
ATOM   2257  OE1 GLN A1088     -17.803   5.013  30.329  1.00161.80           O  
ANISOU 2257  OE1 GLN A1088    10254  21854  29367    539   3377   1653       O  
ATOM   2258  NE2 GLN A1088     -16.637   5.410  32.206  1.00159.99           N  
ANISOU 2258  NE2 GLN A1088    10174  21602  29013    652   3535   1860       N  
ATOM   2259  N   ALA A1089     -16.620   8.028  25.825  1.00134.82           N  
ANISOU 2259  N   ALA A1089     6874  19068  25283    567   2698   1181       N  
ATOM   2260  CA  ALA A1089     -16.556   7.977  24.368  1.00134.51           C  
ANISOU 2260  CA  ALA A1089     6783  19144  25183    536   2535   1046       C  
ATOM   2261  C   ALA A1089     -15.508   8.947  23.838  1.00132.61           C  
ANISOU 2261  C   ALA A1089     6635  19045  24705    597   2410   1002       C  
ATOM   2262  O   ALA A1089     -14.764   8.624  22.902  1.00131.95           O  
ANISOU 2262  O   ALA A1089     6556  19019  24560    587   2291    920       O  
ATOM   2263  CB  ALA A1089     -17.928   8.282  23.769  1.00135.59           C  
ANISOU 2263  CB  ALA A1089     6809  19349  25359    500   2511    988       C  
ATOM   2264  N   ALA A1090     -15.428  10.139  24.435  1.00131.74           N  
ANISOU 2264  N   ALA A1090     6600  18989  24466    660   2442   1054       N  
ATOM   2265  CA  ALA A1090     -14.364  11.073  24.082  1.00134.72           C  
ANISOU 2265  CA  ALA A1090     7076  19481  24630    721   2344   1021       C  
ATOM   2266  C   ALA A1090     -12.993  10.503  24.416  1.00135.68           C  
ANISOU 2266  C   ALA A1090     7280  19545  24726    741   2341   1046       C  
ATOM   2267  O   ALA A1090     -12.005  10.838  23.753  1.00130.07           O  
ANISOU 2267  O   ALA A1090     6629  18922  23869    770   2227    986       O  
ATOM   2268  CB  ALA A1090     -14.576  12.408  24.796  1.00129.38           C  
ANISOU 2268  CB  ALA A1090     6462  18850  23847    780   2401   1075       C  
ATOM   2269  N   ALA A1091     -12.910   9.644  25.436  1.00140.43           N  
ANISOU 2269  N   ALA A1091     7886  20003  25468    729   2468   1138       N  
ATOM   2270  CA  ALA A1091     -11.650   8.969  25.728  1.00129.20           C  
ANISOU 2270  CA  ALA A1091     6529  18522  24039    745   2470   1167       C  
ATOM   2271  C   ALA A1091     -11.322   7.937  24.656  1.00129.41           C  
ANISOU 2271  C   ALA A1091     6504  18533  24131    691   2371   1079       C  
ATOM   2272  O   ALA A1091     -10.148   7.732  24.323  1.00137.98           O  
ANISOU 2272  O   ALA A1091     7649  19640  25137    710   2296   1049       O  
ATOM   2273  CB  ALA A1091     -11.708   8.315  27.109  1.00130.14           C  
ANISOU 2273  CB  ALA A1091     6658  18497  24291    752   2643   1301       C  
ATOM   2274  N   GLU A1092     -12.344   7.275  24.107  1.00138.12           N  
ANISOU 2274  N   GLU A1092     7494  19602  25382    622   2370   1031       N  
ATOM   2275  CA  GLU A1092     -12.113   6.393  22.967  1.00137.96           C  
ANISOU 2275  CA  GLU A1092     7416  19590  25414    566   2265    927       C  
ATOM   2276  C   GLU A1092     -11.610   7.183  21.765  1.00134.70           C  
ANISOU 2276  C   GLU A1092     7029  19355  24795    590   2093    821       C  
ATOM   2277  O   GLU A1092     -10.716   6.726  21.039  1.00130.22           O  
ANISOU 2277  O   GLU A1092     6482  18812  24183    580   1996    757       O  
ATOM   2278  CB  GLU A1092     -13.393   5.634  22.615  1.00136.31           C  
ANISOU 2278  CB  GLU A1092     7072  19324  25396    488   2301    887       C  
ATOM   2279  CG  GLU A1092     -13.233   4.656  21.460  1.00136.06           C  
ANISOU 2279  CG  GLU A1092     6969  19296  25434    422   2204    771       C  
ATOM   2280  CD  GLU A1092     -14.523   3.938  21.118  1.00137.05           C  
ANISOU 2280  CD  GLU A1092     6956  19371  25748    343   2241    721       C  
ATOM   2281  OE1 GLU A1092     -15.563   4.256  21.732  1.00136.22           O  
ANISOU 2281  OE1 GLU A1092     6812  19236  25711    342   2335    775       O  
ATOM   2282  OE2 GLU A1092     -14.497   3.056  20.234  1.00137.38           O  
ANISOU 2282  OE2 GLU A1092     6925  19403  25870    281   2178    622       O  
ATOM   2283  N   GLN A1093     -12.168   8.377  21.542  1.00135.24           N  
ANISOU 2283  N   GLN A1093     7100  19549  24738    623   2057    805       N  
ATOM   2284  CA  GLN A1093     -11.643   9.243  20.492  1.00131.92           C  
ANISOU 2284  CA  GLN A1093     6715  19299  24110    660   1908    722       C  
ATOM   2285  C   GLN A1093     -10.210   9.667  20.789  1.00126.78           C  
ANISOU 2285  C   GLN A1093     6195  18662  23314    722   1877    745       C  
ATOM   2286  O   GLN A1093      -9.406   9.835  19.864  1.00125.25           O  
ANISOU 2286  O   GLN A1093     6035  18565  22989    737   1751    671       O  
ATOM   2287  CB  GLN A1093     -12.540  10.469  20.321  1.00135.63           C  
ANISOU 2287  CB  GLN A1093     7162  19884  24487    691   1897    717       C  
ATOM   2288  CG  GLN A1093     -12.253  11.278  19.066  1.00136.99           C  
ANISOU 2288  CG  GLN A1093     7341  20241  24468    722   1746    627       C  
ATOM   2289  CD  GLN A1093     -12.607  10.528  17.796  1.00143.83           C  
ANISOU 2289  CD  GLN A1093     8099  21182  25367    665   1643    530       C  
ATOM   2290  OE1 GLN A1093     -13.478   9.659  17.796  1.00145.86           O  
ANISOU 2290  OE1 GLN A1093     8253  21373  25794    599   1688    520       O  
ATOM   2291  NE2 GLN A1093     -11.927  10.861  16.704  1.00149.94           N  
ANISOU 2291  NE2 GLN A1093     8895  22096  25979    689   1507    457       N  
ATOM   2292  N   LEU A1094      -9.872   9.845  22.070  1.00129.17           N  
ANISOU 2292  N   LEU A1094     6570  18876  23633    759   1993    846       N  
ATOM   2293  CA  LEU A1094      -8.485  10.108  22.441  1.00126.28           C  
ANISOU 2293  CA  LEU A1094     6320  18514  23145    815   1975    868       C  
ATOM   2294  C   LEU A1094      -7.589   8.937  22.062  1.00124.48           C  
ANISOU 2294  C   LEU A1094     6095  18225  22975    785   1928    840       C  
ATOM   2295  O   LEU A1094      -6.474   9.135  21.565  1.00123.16           O  
ANISOU 2295  O   LEU A1094     5999  18121  22676    815   1831    794       O  
ATOM   2296  CB  LEU A1094      -8.382  10.395  23.939  1.00124.61           C  
ANISOU 2296  CB  LEU A1094     6168  18224  22954    856   2120    986       C  
ATOM   2297  CG  LEU A1094      -8.962  11.716  24.444  1.00126.59           C  
ANISOU 2297  CG  LEU A1094     6445  18538  23116    899   2169   1016       C  
ATOM   2298  CD1 LEU A1094      -8.877  11.792  25.960  1.00124.66           C  
ANISOU 2298  CD1 LEU A1094     6247  18210  22907    932   2323   1134       C  
ATOM   2299  CD2 LEU A1094      -8.238  12.889  23.807  1.00124.55           C  
ANISOU 2299  CD2 LEU A1094     6262  18414  22646    952   2058    947       C  
ATOM   2300  N   LYS A1095      -8.059   7.708  22.295  1.00125.90           N  
ANISOU 2300  N   LYS A1095     6200  18276  23359    725   2001    867       N  
ATOM   2301  CA  LYS A1095      -7.320   6.535  21.840  1.00126.00           C  
ANISOU 2301  CA  LYS A1095     6202  18222  23451    687   1959    831       C  
ATOM   2302  C   LYS A1095      -7.154   6.548  20.326  1.00126.46           C  
ANISOU 2302  C   LYS A1095     6229  18398  23421    659   1794    699       C  
ATOM   2303  O   LYS A1095      -6.102   6.155  19.804  1.00124.74           O  
ANISOU 2303  O   LYS A1095     6053  18191  23150    661   1712    654       O  
ATOM   2304  CB  LYS A1095      -8.031   5.260  22.294  1.00127.83           C  
ANISOU 2304  CB  LYS A1095     6345  18288  23935    624   2076    876       C  
ATOM   2305  CG  LYS A1095      -7.400   3.976  21.780  1.00130.43           C  
ANISOU 2305  CG  LYS A1095     6648  18531  24377    575   2042    831       C  
ATOM   2306  CD  LYS A1095      -8.225   2.759  22.166  1.00136.61           C  
ANISOU 2306  CD  LYS A1095     7334  19147  25425    508   2164    865       C  
ATOM   2307  CE  LYS A1095      -7.620   1.482  21.603  1.00140.87           C  
ANISOU 2307  CE  LYS A1095     7843  19594  26089    456   2135    810       C  
ATOM   2308  NZ  LYS A1095      -8.435   0.284  21.946  1.00142.39           N  
ANISOU 2308  NZ  LYS A1095     7937  19611  26554    388   2261    836       N  
ATOM   2309  N   THR A1096      -8.180   7.006  19.603  1.00130.76           N  
ANISOU 2309  N   THR A1096     6697  19042  23944    637   1745    639       N  
ATOM   2310  CA  THR A1096      -8.073   7.106  18.151  1.00132.17           C  
ANISOU 2310  CA  THR A1096     6840  19361  24017    618   1591    522       C  
ATOM   2311  C   THR A1096      -7.008   8.119  17.744  1.00123.86           C  
ANISOU 2311  C   THR A1096     5895  18436  22729    689   1488    498       C  
ATOM   2312  O   THR A1096      -6.259   7.892  16.786  1.00123.18           O  
ANISOU 2312  O   THR A1096     5826  18419  22560    683   1372    425       O  
ATOM   2313  CB  THR A1096      -9.429   7.483  17.549  1.00132.00           C  
ANISOU 2313  CB  THR A1096     6712  19435  24008    590   1569    478       C  
ATOM   2314  OG1 THR A1096     -10.416   6.525  17.949  1.00131.93           O  
ANISOU 2314  OG1 THR A1096     6602  19299  24226    522   1670    495       O  
ATOM   2315  CG2 THR A1096      -9.351   7.516  16.029  1.00129.78           C  
ANISOU 2315  CG2 THR A1096     6382  19313  23616    572   1414    365       C  
ATOM   2316  N   THR A1097      -6.917   9.237  18.468  1.00123.12           N  
ANISOU 2316  N   THR A1097     5878  18373  22531    755   1533    557       N  
ATOM   2317  CA  THR A1097      -5.953  10.274  18.109  1.00130.31           C  
ANISOU 2317  CA  THR A1097     6890  19399  23225    824   1446    531       C  
ATOM   2318  C   THR A1097      -4.527   9.847  18.439  1.00137.17           C  
ANISOU 2318  C   THR A1097     7853  20206  24059    846   1434    546       C  
ATOM   2319  O   THR A1097      -3.634   9.918  17.585  1.00138.86           O  
ANISOU 2319  O   THR A1097     8111  20498  24152    861   1319    482       O  
ATOM   2320  CB  THR A1097      -6.300  11.584  18.818  1.00127.57           C  
ANISOU 2320  CB  THR A1097     6591  19089  22792    884   1508    582       C  
ATOM   2321  OG1 THR A1097      -6.372  11.361  20.232  1.00127.48           O  
ANISOU 2321  OG1 THR A1097     6606  18946  22886    890   1652    682       O  
ATOM   2322  CG2 THR A1097      -7.634  12.120  18.321  1.00127.39           C  
ANISOU 2322  CG2 THR A1097     6476  19149  22777    870   1500    558       C  
ATOM   2323  N   ARG A1098      -4.290   9.404  19.678  1.00145.14           N  
ANISOU 2323  N   ARG A1098     8895  21082  25171    853   1555    636       N  
ATOM   2324  CA  ARG A1098      -2.940   9.010  20.069  1.00132.55           C  
ANISOU 2324  CA  ARG A1098     7386  19434  23542    880   1551    660       C  
ATOM   2325  C   ARG A1098      -2.470   7.792  19.283  1.00130.49           C  
ANISOU 2325  C   ARG A1098     7090  19129  23361    826   1482    604       C  
ATOM   2326  O   ARG A1098      -1.319   7.742  18.838  1.00129.40           O  
ANISOU 2326  O   ARG A1098     7020  19026  23122    848   1396    565       O  
ATOM   2327  CB  ARG A1098      -2.877   8.740  21.574  1.00138.29           C  
ANISOU 2327  CB  ARG A1098     8140  20039  24366    901   1705    779       C  
ATOM   2328  CG  ARG A1098      -3.716   7.561  22.030  1.00166.12           C  
ANISOU 2328  CG  ARG A1098    11572  23423  28124    840   1812    834       C  
ATOM   2329  CD  ARG A1098      -3.348   7.094  23.420  1.00181.41           C  
ANISOU 2329  CD  ARG A1098    13542  25240  30145    868   1955    959       C  
ATOM   2330  NE  ARG A1098      -3.751   5.706  23.629  1.00190.05           N  
ANISOU 2330  NE  ARG A1098    14559  26186  31465    809   2036   1000       N  
ATOM   2331  CZ  ARG A1098      -3.899   5.145  24.823  1.00188.95           C  
ANISOU 2331  CZ  ARG A1098    14412  25926  31455    820   2189   1124       C  
ATOM   2332  NH1 ARG A1098      -3.688   5.859  25.917  1.00192.33           N  
ANISOU 2332  NH1 ARG A1098    14903  26377  31796    886   2274   1217       N  
ATOM   2333  NH2 ARG A1098      -4.267   3.874  24.923  1.00184.85           N  
ANISOU 2333  NH2 ARG A1098    13820  25266  31150    766   2264   1156       N  
ATOM   2334  N   ASN A1099      -3.350   6.802  19.092  1.00137.27           N  
ANISOU 2334  N   ASN A1099     7841  19908  24405    754   1520    594       N  
ATOM   2335  CA  ASN A1099      -2.983   5.632  18.302  1.00139.36           C  
ANISOU 2335  CA  ASN A1099     8063  20127  24761    695   1459    528       C  
ATOM   2336  C   ASN A1099      -2.803   5.989  16.835  1.00140.04           C  
ANISOU 2336  C   ASN A1099     8139  20368  24702    686   1297    413       C  
ATOM   2337  O   ASN A1099      -2.007   5.352  16.135  1.00139.13           O  
ANISOU 2337  O   ASN A1099     8037  20251  24576    663   1217    356       O  
ATOM   2338  CB  ASN A1099      -4.035   4.534  18.460  1.00145.10           C  
ANISOU 2338  CB  ASN A1099     8672  20728  25730    617   1547    537       C  
ATOM   2339  CG  ASN A1099      -3.868   3.745  19.745  1.00148.10           C  
ANISOU 2339  CG  ASN A1099     9064  20929  26278    619   1699    650       C  
ATOM   2340  OD1 ASN A1099      -4.319   4.165  20.810  1.00145.26           O  
ANISOU 2340  OD1 ASN A1099     8719  20531  25943    652   1813    748       O  
ATOM   2341  ND2 ASN A1099      -3.217   2.592  19.648  1.00151.37           N  
ANISOU 2341  ND2 ASN A1099     9471  21233  26810    585   1707    643       N  
ATOM   2342  N   ALA A1100      -3.527   6.997  16.354  1.00142.88           N  
ANISOU 2342  N   ALA A1100     8474  20865  24949    706   1253    385       N  
ATOM   2343  CA  ALA A1100      -3.317   7.519  15.012  1.00142.11           C  
ANISOU 2343  CA  ALA A1100     8375  20937  24682    716   1106    295       C  
ATOM   2344  C   ALA A1100      -2.171   8.518  14.944  1.00128.79           C  
ANISOU 2344  C   ALA A1100     6815  19338  22783    795   1042    297       C  
ATOM   2345  O   ALA A1100      -1.935   9.091  13.875  1.00119.24           O  
ANISOU 2345  O   ALA A1100     5615  18276  21415    817    927    236       O  
ATOM   2346  CB  ALA A1100      -4.603   8.170  14.493  1.00146.66           C  
ANISOU 2346  CB  ALA A1100     8863  21632  25230    709   1090    270       C  
ATOM   2347  N   TYR A1101      -1.453   8.741  16.051  1.00125.93           N  
ANISOU 2347  N   TYR A1101     6545  18892  22411    841   1116    367       N  
ATOM   2348  CA  TYR A1101      -0.356   9.701  16.060  1.00131.35           C  
ANISOU 2348  CA  TYR A1101     7350  19654  22903    915   1063    364       C  
ATOM   2349  C   TYR A1101       0.881   9.147  16.763  1.00132.49           C  
ANISOU 2349  C   TYR A1101     7576  19696  23066    933   1092    402       C  
ATOM   2350  O   TYR A1101       1.643   9.906  17.373  1.00122.26           O  
ANISOU 2350  O   TYR A1101     6377  18417  21659    997   1110    432       O  
ATOM   2351  CB  TYR A1101      -0.786  11.016  16.712  1.00134.44           C  
ANISOU 2351  CB  TYR A1101     7778  20092  23210    974   1122    406       C  
ATOM   2352  CG  TYR A1101      -0.226  12.241  16.028  1.00137.72           C  
ANISOU 2352  CG  TYR A1101     8265  20651  23412   1036   1030    357       C  
ATOM   2353  CD1 TYR A1101       0.967  12.815  16.448  1.00144.82           C  
ANISOU 2353  CD1 TYR A1101     9281  21553  24192   1096   1023    366       C  
ATOM   2354  CD2 TYR A1101      -0.890  12.822  14.956  1.00135.13           C  
ANISOU 2354  CD2 TYR A1101     7883  20457  23002   1039    954    304       C  
ATOM   2355  CE1 TYR A1101       1.481  13.934  15.822  1.00151.67           C  
ANISOU 2355  CE1 TYR A1101    10213  22539  24874   1153    946    320       C  
ATOM   2356  CE2 TYR A1101      -0.385  13.941  14.324  1.00138.07           C  
ANISOU 2356  CE2 TYR A1101     8319  20955  23186   1100    879    266       C  
ATOM   2357  CZ  TYR A1101       0.800  14.493  14.761  1.00152.41           C  
ANISOU 2357  CZ  TYR A1101    10255  22758  24898   1156    877    273       C  
ATOM   2358  OH  TYR A1101       1.305  15.607  14.133  1.00165.71           O  
ANISOU 2358  OH  TYR A1101    12001  24556  26405   1217    810    233       O  
ATOM   2359  N   ILE A1102       1.100   7.828  16.694  1.00136.50           N  
ANISOU 2359  N   ILE A1102     8045  20099  23719    878   1101    398       N  
ATOM   2360  CA  ILE A1102       2.343   7.244  17.194  1.00130.08           C  
ANISOU 2360  CA  ILE A1102     7305  19201  22918    896   1113    428       C  
ATOM   2361  C   ILE A1102       3.452   7.282  16.153  1.00128.58           C  
ANISOU 2361  C   ILE A1102     7175  19092  22587    907    975    351       C  
ATOM   2362  O   ILE A1102       4.609   6.974  16.481  1.00113.31           O  
ANISOU 2362  O   ILE A1102     5315  17111  20628    933    969    368       O  
ATOM   2363  CB  ILE A1102       2.152   5.781  17.650  1.00125.91           C  
ANISOU 2363  CB  ILE A1102     6711  18508  22623    836   1198    468       C  
ATOM   2364  CG1 ILE A1102       0.723   5.544  18.137  1.00129.35           C  
ANISOU 2364  CG1 ILE A1102     7047  18879  23220    795   1305    511       C  
ATOM   2365  CG2 ILE A1102       3.135   5.427  18.761  1.00116.33           C  
ANISOU 2365  CG2 ILE A1102     5568  17195  21437    878   1277    555       C  
ATOM   2366  CD1 ILE A1102       0.470   4.131  18.631  1.00128.67           C  
ANISOU 2366  CD1 ILE A1102     6894  18619  23378    738   1406    557       C  
ATOM   2367  N   GLN A1103       3.140   7.657  14.910  1.00131.80           N  
ANISOU 2367  N   GLN A1103     7553  19627  22899    893    867    272       N  
ATOM   2368  CA  GLN A1103       4.121   7.583  13.832  1.00125.05           C  
ANISOU 2368  CA  GLN A1103     6745  18849  21920    896    738    202       C  
ATOM   2369  C   GLN A1103       5.278   8.549  14.062  1.00116.29           C  
ANISOU 2369  C   GLN A1103     5763  17798  20622    978    703    212       C  
ATOM   2370  O   GLN A1103       6.448   8.178  13.913  1.00119.30           O  
ANISOU 2370  O   GLN A1103     6213  18157  20960    988    654    197       O  
ATOM   2371  CB  GLN A1103       3.440   7.864  12.492  1.00125.84           C  
ANISOU 2371  CB  GLN A1103     6778  19090  21947    871    641    132       C  
ATOM   2372  CG  GLN A1103       4.369   7.790  11.293  1.00121.93           C  
ANISOU 2372  CG  GLN A1103     6323  18685  21319    872    509     69       C  
ATOM   2373  CD  GLN A1103       4.931   6.399  11.075  1.00118.95           C  
ANISOU 2373  CD  GLN A1103     5927  18195  21073    809    492     38       C  
ATOM   2374  OE1 GLN A1103       6.087   6.238  10.685  1.00118.73           O  
ANISOU 2374  OE1 GLN A1103     5975  18174  20965    823    423     15       O  
ATOM   2375  NE2 GLN A1103       4.110   5.383  11.322  1.00116.39           N  
ANISOU 2375  NE2 GLN A1103     5502  17761  20959    738    558     36       N  
ATOM   2376  N   LYS A1104       4.972   9.796  14.423  1.00111.06           N  
ANISOU 2376  N   LYS A1104     5135  17210  19852   1034    730    233       N  
ATOM   2377  CA  LYS A1104       6.010  10.799  14.629  1.00117.57           C  
ANISOU 2377  CA  LYS A1104     6076  18093  20501   1110    703    232       C  
ATOM   2378  C   LYS A1104       6.740  10.622  15.955  1.00124.45           C  
ANISOU 2378  C   LYS A1104     7011  18860  21415   1141    792    294       C  
ATOM   2379  O   LYS A1104       7.883  11.086  16.094  1.00130.38           O  
ANISOU 2379  O   LYS A1104     7859  19639  22039   1193    760    284       O  
ATOM   2380  CB  LYS A1104       5.401  12.201  14.536  1.00119.05           C  
ANISOU 2380  CB  LYS A1104     6272  18388  20573   1158    709    226       C  
ATOM   2381  CG  LYS A1104       5.534  12.841  13.158  1.00126.39           C  
ANISOU 2381  CG  LYS A1104     7210  19468  21343   1177    590    162       C  
ATOM   2382  CD  LYS A1104       5.160  11.869  12.047  1.00129.11           C  
ANISOU 2382  CD  LYS A1104     7469  19843  21744   1111    514    123       C  
ATOM   2383  CE  LYS A1104       5.779  12.274  10.720  1.00125.55           C  
ANISOU 2383  CE  LYS A1104     7052  19531  21120   1136    389     73       C  
ATOM   2384  NZ  LYS A1104       5.658  11.192   9.704  1.00121.92           N  
ANISOU 2384  NZ  LYS A1104     6520  19090  20716   1067    315     38       N  
ATOM   2385  N   TYR A1105       6.107   9.955  16.924  1.00116.59           N  
ANISOU 2385  N   TYR A1105     5959  17750  20590   1112    906    362       N  
ATOM   2386  CA  TYR A1105       6.791   9.615  18.165  1.00119.59           C  
ANISOU 2386  CA  TYR A1105     6385  18035  21019   1141    996    434       C  
ATOM   2387  C   TYR A1105       8.053   8.804  17.899  1.00129.92           C  
ANISOU 2387  C   TYR A1105     7741  19305  22318   1140    936    416       C  
ATOM   2388  O   TYR A1105       9.026   8.904  18.655  1.00130.98           O  
ANISOU 2388  O   TYR A1105     7947  19418  22400   1189    965    451       O  
ATOM   2389  CB  TYR A1105       5.843   8.850  19.089  1.00117.18           C  
ANISOU 2389  CB  TYR A1105     5998  17611  20915   1104   1128    518       C  
ATOM   2390  CG  TYR A1105       6.430   8.536  20.443  1.00120.97           C  
ANISOU 2390  CG  TYR A1105     6515  18006  21441   1142   1237    613       C  
ATOM   2391  CD1 TYR A1105       6.576   9.529  21.402  1.00117.71           C  
ANISOU 2391  CD1 TYR A1105     6157  17634  20933   1205   1304    657       C  
ATOM   2392  CD2 TYR A1105       6.833   7.248  20.767  1.00125.64           C  
ANISOU 2392  CD2 TYR A1105     7083  18480  22174   1117   1279    662       C  
ATOM   2393  CE1 TYR A1105       7.111   9.249  22.643  1.00116.30           C  
ANISOU 2393  CE1 TYR A1105     6006  17398  20783   1244   1406    747       C  
ATOM   2394  CE2 TYR A1105       7.369   6.958  22.006  1.00118.85           C  
ANISOU 2394  CE2 TYR A1105     6253  17557  21349   1160   1383    762       C  
ATOM   2395  CZ  TYR A1105       7.506   7.963  22.940  1.00114.94           C  
ANISOU 2395  CZ  TYR A1105     5810  17120  20743   1225   1445    805       C  
ATOM   2396  OH  TYR A1105       8.039   7.682  24.176  1.00112.24           O  
ANISOU 2396  OH  TYR A1105     5491  16733  20421   1272   1551    909       O  
ATOM   2397  N   LEU A1106       8.058   8.003  16.831  1.00137.79           N  
ANISOU 2397  N   LEU A1106     8696  20294  23363   1084    853    358       N  
ATOM   2398  CA  LEU A1106       9.274   7.309  16.425  1.00134.55           C  
ANISOU 2398  CA  LEU A1106     8335  19855  22932   1080    783    329       C  
ATOM   2399  C   LEU A1106      10.227   8.230  15.676  1.00125.58           C  
ANISOU 2399  C   LEU A1106     7294  18844  21575   1129    668    266       C  
ATOM   2400  O   LEU A1106      11.444   8.023  15.724  1.00118.73           O  
ANISOU 2400  O   LEU A1106     6500  17964  20648   1156    630    260       O  
ATOM   2401  CB  LEU A1106       8.929   6.096  15.560  1.00134.99           C  
ANISOU 2401  CB  LEU A1106     8309  19851  23128    997    742    285       C  
ATOM   2402  CG  LEU A1106       8.006   5.052  16.191  1.00135.32           C  
ANISOU 2402  CG  LEU A1106     8250  19754  23410    941    857    340       C  
ATOM   2403  CD1 LEU A1106       7.926   3.810  15.316  1.00137.82           C  
ANISOU 2403  CD1 LEU A1106     8497  20003  23864    860    812    280       C  
ATOM   2404  CD2 LEU A1106       8.471   4.697  17.596  1.00133.71           C  
ANISOU 2404  CD2 LEU A1106     8076  19441  23287    979    977    446       C  
ATOM   2405  N   LYS A 246       9.696   9.237  14.976  1.00123.58           N  
ANISOU 2405  N   LYS A 246     7039  18713  21204   1143    616    225       N  
ATOM   2406  CA  LYS A 246      10.553  10.229  14.335  1.00126.09           C  
ANISOU 2406  CA  LYS A 246     7448  19148  21312   1198    525    178       C  
ATOM   2407  C   LYS A 246      11.423  10.941  15.364  1.00125.29           C  
ANISOU 2407  C   LYS A 246     7440  19041  21122   1269    574    208       C  
ATOM   2408  O   LYS A 246      12.624  11.153  15.138  1.00119.62           O  
ANISOU 2408  O   LYS A 246     6809  18356  20285   1306    512    180       O  
ATOM   2409  CB  LYS A 246       9.692  11.226  13.556  1.00130.12           C  
ANISOU 2409  CB  LYS A 246     7928  19783  21728   1208    487    147       C  
ATOM   2410  CG  LYS A 246      10.451  12.309  12.806  1.00131.57           C  
ANISOU 2410  CG  LYS A 246     8198  20092  21702   1266    401    106       C  
ATOM   2411  CD  LYS A 246       9.482  13.171  12.002  1.00131.63           C  
ANISOU 2411  CD  LYS A 246     8156  20219  21638   1275    373     85       C  
ATOM   2412  CE  LYS A 246      10.177  14.351  11.342  1.00124.12           C  
ANISOU 2412  CE  LYS A 246     7288  19387  20486   1342    307     55       C  
ATOM   2413  NZ  LYS A 246       9.206  15.231  10.631  1.00116.38           N  
ANISOU 2413  NZ  LYS A 246     6255  18523  19442   1360    291     42       N  
ATOM   2414  N   ASN A 247      10.837  11.295  16.514  1.00126.56           N  
ANISOU 2414  N   ASN A 247     7583  19162  21343   1288    687    264       N  
ATOM   2415  CA  ASN A 247      11.620  11.915  17.583  1.00124.85           C  
ANISOU 2415  CA  ASN A 247     7443  18942  21051   1353    744    292       C  
ATOM   2416  C   ASN A 247      12.741  10.993  18.058  1.00129.65           C  
ANISOU 2416  C   ASN A 247     8087  19478  21694   1360    747    317       C  
ATOM   2417  O   ASN A 247      13.865  11.446  18.309  1.00142.81           O  
ANISOU 2417  O   ASN A 247     9840  21182  23241   1413    723    299       O  
ATOM   2418  CB  ASN A 247      10.703  12.293  18.748  1.00118.33           C  
ANISOU 2418  CB  ASN A 247     6577  18081  20302   1363    875    357       C  
ATOM   2419  CG  ASN A 247      11.348  13.275  19.715  1.00114.44           C  
ANISOU 2419  CG  ASN A 247     6159  17623  19700   1432    930    367       C  
ATOM   2420  OD1 ASN A 247      12.569  13.316  19.864  1.00120.78           O  
ANISOU 2420  OD1 ASN A 247     7034  18441  20414   1470    896    347       O  
ATOM   2421  ND2 ASN A 247      10.521  14.073  20.380  1.00106.96           N  
ANISOU 2421  ND2 ASN A 247     5190  16688  18761   1447   1018    395       N  
ATOM   2422  N   ARG A 248      12.458   9.696  18.185  1.00125.54           N  
ANISOU 2422  N   ARG A 248     7502  18853  21345   1308    781    358       N  
ATOM   2423  CA  ARG A 248      13.474   8.763  18.661  1.00130.79           C  
ANISOU 2423  CA  ARG A 248     8193  19440  22060   1317    793    394       C  
ATOM   2424  C   ARG A 248      14.593   8.592  17.637  1.00128.92           C  
ANISOU 2424  C   ARG A 248     8020  19243  21722   1317    664    321       C  
ATOM   2425  O   ARG A 248      15.780   8.589  17.995  1.00128.83           O  
ANISOU 2425  O   ARG A 248     8080  19235  21635   1363    648    324       O  
ATOM   2426  CB  ARG A 248      12.823   7.419  18.992  1.00137.87           C  
ANISOU 2426  CB  ARG A 248     8998  20206  23182   1259    870    458       C  
ATOM   2427  CG  ARG A 248      13.755   6.400  19.619  1.00140.16           C  
ANISOU 2427  CG  ARG A 248     9303  20401  23550   1272    909    517       C  
ATOM   2428  CD  ARG A 248      12.978   5.266  20.277  1.00145.52           C  
ANISOU 2428  CD  ARG A 248     9889  20944  24458   1231   1028    609       C  
ATOM   2429  NE  ARG A 248      12.293   5.699  21.494  1.00151.90           N  
ANISOU 2429  NE  ARG A 248    10674  21745  25296   1264   1160    702       N  
ATOM   2430  CZ  ARG A 248      11.000   6.001  21.564  1.00156.08           C  
ANISOU 2430  CZ  ARG A 248    11141  22273  25891   1233   1214    714       C  
ATOM   2431  NH1 ARG A 248      10.470   6.386  22.717  1.00158.15           N  
ANISOU 2431  NH1 ARG A 248    11390  22528  26174   1266   1337    802       N  
ATOM   2432  NH2 ARG A 248      10.234   5.914  20.484  1.00155.49           N  
ANISOU 2432  NH2 ARG A 248    11015  22210  25855   1169   1145    637       N  
ATOM   2433  N   ILE A 249      14.233   8.463  16.358  1.00120.88           N  
ANISOU 2433  N   ILE A 249     6975  18262  20693   1269    573    258       N  
ATOM   2434  CA  ILE A 249      15.234   8.300  15.307  1.00117.35           C  
ANISOU 2434  CA  ILE A 249     6586  17856  20146   1266    452    195       C  
ATOM   2435  C   ILE A 249      16.144   9.520  15.246  1.00116.20           C  
ANISOU 2435  C   ILE A 249     6547  17817  19788   1338    403    165       C  
ATOM   2436  O   ILE A 249      17.376   9.397  15.204  1.00120.02           O  
ANISOU 2436  O   ILE A 249     7106  18303  20195   1367    355    150       O  
ATOM   2437  CB  ILE A 249      14.554   8.034  13.952  1.00112.77           C  
ANISOU 2437  CB  ILE A 249     5948  17317  19584   1203    371    140       C  
ATOM   2438  CG1 ILE A 249      13.773   6.719  13.995  1.00115.06           C  
ANISOU 2438  CG1 ILE A 249     6132  17490  20098   1125    419    156       C  
ATOM   2439  CG2 ILE A 249      15.585   8.002  12.834  1.00109.18           C  
ANISOU 2439  CG2 ILE A 249     5560  16919  19006   1203    248     83       C  
ATOM   2440  CD1 ILE A 249      13.008   6.423  12.723  1.00119.91           C  
ANISOU 2440  CD1 ILE A 249     6673  18147  20739   1059    348     96       C  
ATOM   2441  N   THR A 250      15.554  10.721  15.249  1.00104.96           N  
ANISOU 2441  N   THR A 250     5130  16480  18272   1370    418    154       N  
ATOM   2442  CA  THR A 250      16.393  11.916  15.217  1.00106.09           C  
ANISOU 2442  CA  THR A 250     5369  16714  18225   1438    384    123       C  
ATOM   2443  C   THR A 250      17.201  12.064  16.502  1.00111.74           C  
ANISOU 2443  C   THR A 250     6136  17397  18922   1491    452    151       C  
ATOM   2444  O   THR A 250      18.293  12.646  16.479  1.00120.08           O  
ANISOU 2444  O   THR A 250     7280  18507  19840   1542    412    119       O  
ATOM   2445  CB  THR A 250      15.548  13.168  14.953  1.00105.85           C  
ANISOU 2445  CB  THR A 250     5328  16773  18116   1460    395    105       C  
ATOM   2446  OG1 THR A 250      16.412  14.274  14.666  1.00102.69           O  
ANISOU 2446  OG1 THR A 250     5022  16460  17536   1521    351     68       O  
ATOM   2447  CG2 THR A 250      14.685  13.517  16.152  1.00109.78           C  
ANISOU 2447  CG2 THR A 250     5782  17232  18697   1470    517    149       C  
ATOM   2448  N   ARG A 251      16.701  11.528  17.619  1.00110.36           N  
ANISOU 2448  N   ARG A 251     5906  17141  18885   1482    559    215       N  
ATOM   2449  CA  ARG A 251      17.495  11.496  18.845  1.00119.64           C  
ANISOU 2449  CA  ARG A 251     7119  18290  20049   1533    627    253       C  
ATOM   2450  C   ARG A 251      18.766  10.679  18.648  1.00125.17           C  
ANISOU 2450  C   ARG A 251     7867  18960  20734   1540    565    244       C  
ATOM   2451  O   ARG A 251      19.876  11.155  18.923  1.00124.52           O  
ANISOU 2451  O   ARG A 251     7861  18927  20525   1596    541    217       O  
ATOM   2452  CB  ARG A 251      16.665  10.923  19.995  1.00116.15           C  
ANISOU 2452  CB  ARG A 251     6600  17764  19767   1519    757    344       C  
ATOM   2453  CG  ARG A 251      17.493  10.527  21.209  1.00124.11           C  
ANISOU 2453  CG  ARG A 251     7629  18737  20789   1567    830    405       C  
ATOM   2454  CD  ARG A 251      16.756   9.525  22.084  1.00137.48           C  
ANISOU 2454  CD  ARG A 251     9240  20327  22671   1542    948    518       C  
ATOM   2455  NE  ARG A 251      16.443   8.293  21.364  1.00148.47           N  
ANISOU 2455  NE  ARG A 251    10576  21626  24211   1475    916    530       N  
ATOM   2456  CZ  ARG A 251      17.259   7.246  21.281  1.00145.20           C  
ANISOU 2456  CZ  ARG A 251    10167  21145  23855   1470    893    552       C  
ATOM   2457  NH1 ARG A 251      16.891   6.167  20.604  1.00152.16           N  
ANISOU 2457  NH1 ARG A 251    10992  21938  24884   1402    870    552       N  
ATOM   2458  NH2 ARG A 251      18.445   7.278  21.873  1.00125.22           N  
ANISOU 2458  NH2 ARG A 251     7698  18639  21240   1532    893    569       N  
ATOM   2459  N   ASP A 252      18.619   9.441  18.165  1.00120.57           N  
ANISOU 2459  N   ASP A 252     7234  18294  20281   1483    541    263       N  
ATOM   2460  CA  ASP A 252      19.785   8.588  17.945  1.00114.95           C  
ANISOU 2460  CA  ASP A 252     6562  17541  19573   1484    485    257       C  
ATOM   2461  C   ASP A 252      20.751   9.222  16.949  1.00116.09           C  
ANISOU 2461  C   ASP A 252     6797  17775  19535   1506    364    179       C  
ATOM   2462  O   ASP A 252      21.965   9.282  17.192  1.00110.32           O  
ANISOU 2462  O   ASP A 252     6139  17064  18716   1551    335    167       O  
ATOM   2463  CB  ASP A 252      19.333   7.209  17.461  1.00115.10           C  
ANISOU 2463  CB  ASP A 252     6506  17452  19776   1409    481    277       C  
ATOM   2464  CG  ASP A 252      20.455   6.186  17.471  1.00130.73           C  
ANISOU 2464  CG  ASP A 252     8512  19361  21799   1410    453    290       C  
ATOM   2465  OD1 ASP A 252      21.552   6.503  17.976  1.00137.56           O  
ANISOU 2465  OD1 ASP A 252     9449  20262  22555   1474    444    293       O  
ATOM   2466  OD2 ASP A 252      20.237   5.061  16.974  1.00137.24           O  
ANISOU 2466  OD2 ASP A 252     9282  20092  22771   1347    442    291       O  
ATOM   2467  N   GLN A 253      20.224   9.719  15.826  1.00116.41           N  
ANISOU 2467  N   GLN A 253     6836  17878  19518   1476    296    132       N  
ATOM   2468  CA  GLN A 253      21.082  10.286  14.789  1.00111.32           C  
ANISOU 2468  CA  GLN A 253     6275  17315  18706   1495    188     78       C  
ATOM   2469  C   GLN A 253      21.854  11.496  15.305  1.00105.58           C  
ANISOU 2469  C   GLN A 253     5634  16670  17813   1573    198     62       C  
ATOM   2470  O   GLN A 253      23.069  11.603  15.102  1.00102.55           O  
ANISOU 2470  O   GLN A 253     5331  16313  17322   1605    142     43       O  
ATOM   2471  CB  GLN A 253      20.246  10.661  13.565  1.00113.84           C  
ANISOU 2471  CB  GLN A 253     6563  17696  18993   1457    130     51       C  
ATOM   2472  CG  GLN A 253      21.038  11.347  12.462  1.00110.15           C  
ANISOU 2472  CG  GLN A 253     6180  17321  18351   1479     31     19       C  
ATOM   2473  CD  GLN A 253      20.183  11.694  11.258  1.00104.23           C  
ANISOU 2473  CD  GLN A 253     5389  16643  17569   1448    -20      7       C  
ATOM   2474  OE1 GLN A 253      19.228  10.987  10.935  1.00 98.68           O  
ANISOU 2474  OE1 GLN A 253     4596  15908  16990   1388    -15      5       O  
ATOM   2475  NE2 GLN A 253      20.521  12.791  10.590  1.00100.56           N  
ANISOU 2475  NE2 GLN A 253     4988  16281  16941   1491    -64      3       N  
ATOM   2476  N   VAL A 254      21.165  12.420  15.980  1.00103.90           N  
ANISOU 2476  N   VAL A 254     5402  16494  17582   1602    272     68       N  
ATOM   2477  CA  VAL A 254      21.834  13.619  16.479  1.00 97.74           C  
ANISOU 2477  CA  VAL A 254     4695  15789  16654   1672    290     41       C  
ATOM   2478  C   VAL A 254      22.870  13.256  17.538  1.00 99.47           C  
ANISOU 2478  C   VAL A 254     4947  15981  16868   1714    325     51       C  
ATOM   2479  O   VAL A 254      23.975  13.817  17.564  1.00107.40           O  
ANISOU 2479  O   VAL A 254     6030  17042  17735   1763    291     18       O  
ATOM   2480  CB  VAL A 254      20.799  14.628  17.008  1.00 95.35           C  
ANISOU 2480  CB  VAL A 254     4355  15518  16354   1687    372     41       C  
ATOM   2481  CG1 VAL A 254      21.482  15.728  17.805  1.00102.58           C  
ANISOU 2481  CG1 VAL A 254     5332  16492  17153   1755    415      9       C  
ATOM   2482  CG2 VAL A 254      20.015  15.229  15.852  1.00 95.27           C  
ANISOU 2482  CG2 VAL A 254     4330  15564  16304   1666    323     22       C  
ATOM   2483  N   LEU A 255      22.538  12.308  18.421  1.00 95.77           N  
ANISOU 2483  N   LEU A 255     4414  15427  16546   1697    398    105       N  
ATOM   2484  CA  LEU A 255      23.504  11.860  19.422  1.00110.95           C  
ANISOU 2484  CA  LEU A 255     6358  17328  18472   1740    434    128       C  
ATOM   2485  C   LEU A 255      24.773  11.334  18.759  1.00112.61           C  
ANISOU 2485  C   LEU A 255     6633  17538  18617   1746    335    101       C  
ATOM   2486  O   LEU A 255      25.891  11.732  19.119  1.00112.49           O  
ANISOU 2486  O   LEU A 255     6682  17575  18483   1802    317     71       O  
ATOM   2487  CB  LEU A 255      22.870  10.792  20.317  1.00118.28           C  
ANISOU 2487  CB  LEU A 255     7201  18156  19584   1718    531    219       C  
ATOM   2488  CG  LEU A 255      23.652  10.291  21.536  1.00119.56           C  
ANISOU 2488  CG  LEU A 255     7364  18294  19768   1769    597    274       C  
ATOM   2489  CD1 LEU A 255      22.695   9.963  22.670  1.00124.95           C  
ANISOU 2489  CD1 LEU A 255     7967  18925  20584   1768    735    376       C  
ATOM   2490  CD2 LEU A 255      24.501   9.071  21.198  1.00111.13           C  
ANISOU 2490  CD2 LEU A 255     6307  17161  18758   1757    544    298       C  
ATOM   2491  N   LYS A 256      24.617  10.445  17.773  1.00116.57           N  
ANISOU 2491  N   LYS A 256     7115  17983  19194   1686    271    108       N  
ATOM   2492  CA  LYS A 256      25.784   9.910  17.078  1.00103.50           C  
ANISOU 2492  CA  LYS A 256     5521  16318  17485   1684    177     86       C  
ATOM   2493  C   LYS A 256      26.531  10.992  16.309  1.00101.03           C  
ANISOU 2493  C   LYS A 256     5304  16108  16976   1716     99     37       C  
ATOM   2494  O   LYS A 256      27.742  10.871  16.088  1.00103.21           O  
ANISOU 2494  O   LYS A 256     5651  16397  17167   1741     41     25       O  
ATOM   2495  CB  LYS A 256      25.365   8.778  16.140  1.00 94.85           C  
ANISOU 2495  CB  LYS A 256     4379  15140  16521   1605    131     94       C  
ATOM   2496  CG  LYS A 256      24.995   7.490  16.859  1.00 98.96           C  
ANISOU 2496  CG  LYS A 256     4817  15539  17245   1577    205    156       C  
ATOM   2497  CD  LYS A 256      24.553   6.414  15.882  1.00104.93           C  
ANISOU 2497  CD  LYS A 256     5520  16210  18138   1493    162    146       C  
ATOM   2498  CE  LYS A 256      24.385   5.074  16.581  1.00106.31           C  
ANISOU 2498  CE  LYS A 256     5621  16252  18521   1468    241    216       C  
ATOM   2499  NZ  LYS A 256      23.466   5.167  17.750  1.00 99.22           N  
ANISOU 2499  NZ  LYS A 256     4655  15328  17716   1486    369    293       N  
ATOM   2500  N   MET A 257      25.837  12.055  15.895  1.00 94.84           N  
ANISOU 2500  N   MET A 257     4523  15391  16122   1718    102     20       N  
ATOM   2501  CA  MET A 257      26.514  13.149  15.206  1.00 95.43           C  
ANISOU 2501  CA  MET A 257     4687  15555  16019   1753     46      0       C  
ATOM   2502  C   MET A 257      27.399  13.938  16.162  1.00101.93           C  
ANISOU 2502  C   MET A 257     5566  16435  16730   1827     87    -14       C  
ATOM   2503  O   MET A 257      28.564  14.221  15.855  1.00117.44           O  
ANISOU 2503  O   MET A 257     7643  18402  18576   1847     38     -8       O  
ATOM   2504  CB  MET A 257      25.491  14.065  14.534  1.00117.90           C  
ANISOU 2504  CB  MET A 257     7511  18454  18831   1741     49     -4       C  
ATOM   2505  CG  MET A 257      24.919  13.504  13.245  1.00127.74           C  
ANISOU 2505  CG  MET A 257     8725  19683  20129   1676    -20      3       C  
ATOM   2506  SD  MET A 257      26.211  13.085  12.058  1.00118.73           S  
ANISOU 2506  SD  MET A 257     7672  18534  18907   1661   -133     13       S  
ATOM   2507  CE  MET A 257      27.005  14.676  11.849  1.00110.36           C  
ANISOU 2507  CE  MET A 257     6750  17530  17652   1720   -138     34       C  
ATOM   2508  N   ALA A 258      26.865  14.303  17.331  1.00 91.24           N  
ANISOU 2508  N   ALA A 258     4163  15089  15414   1854    181    -28       N  
ATOM   2509  CA  ALA A 258      27.665  15.038  18.307  1.00 93.81           C  
ANISOU 2509  CA  ALA A 258     4559  15446  15639   1912    226    -54       C  
ATOM   2510  C   ALA A 258      28.849  14.203  18.784  1.00 90.62           C  
ANISOU 2510  C   ALA A 258     4180  15023  15228   1938    203    -51       C  
ATOM   2511  O   ALA A 258      29.995  14.677  18.806  1.00 89.67           O  
ANISOU 2511  O   ALA A 258     4172  14925  14972   1970    173    -59       O  
ATOM   2512  CB  ALA A 258      26.792  15.465  19.486  1.00 91.78           C  
ANISOU 2512  CB  ALA A 258     4223  15200  15449   1930    337    -70       C  
ATOM   2513  N   ALA A 259      28.589  12.947  19.163  1.00 91.57           N  
ANISOU 2513  N   ALA A 259     4210  15083  15501   1920    222    -23       N  
ATOM   2514  CA  ALA A 259      29.674  12.072  19.596  1.00 91.52           C  
ANISOU 2514  CA  ALA A 259     4221  15048  15505   1946    202    -13       C  
ATOM   2515  C   ALA A 259      30.701  11.877  18.487  1.00108.60           C  
ANISOU 2515  C   ALA A 259     6466  17224  17575   1937     93    -15       C  
ATOM   2516  O   ALA A 259      31.907  11.801  18.752  1.00114.57           O  
ANISOU 2516  O   ALA A 259     7297  17990  18247   1974     65    -21       O  
ATOM   2517  CB  ALA A 259      29.114  10.725  20.053  1.00 92.85           C  
ANISOU 2517  CB  ALA A 259     4307  15101  15870   1911    251     56       C  
ATOM   2518  N   ALA A 260      30.241  11.806  17.235  1.00 90.09           N  
ANISOU 2518  N   ALA A 260     4131  14852  15245   1879     33     -1       N  
ATOM   2519  CA  ALA A 260      31.163  11.650  16.115  1.00 89.88           C  
ANISOU 2519  CA  ALA A 260     4185  14820  15144   1861    -64     11       C  
ATOM   2520  C   ALA A 260      32.040  12.884  15.944  1.00 99.26           C  
ANISOU 2520  C   ALA A 260     5517  16041  16155   1893    -80     27       C  
ATOM   2521  O   ALA A 260      33.235  12.766  15.643  1.00109.59           O  
ANISOU 2521  O   ALA A 260     6913  17327  17397   1901   -131     52       O  
ATOM   2522  CB  ALA A 260      30.386  11.359  14.832  1.00 89.14           C  
ANISOU 2522  CB  ALA A 260     4073  14684  15114   1786   -118     15       C  
ATOM   2523  N   VAL A 261      31.468  14.076  16.129  1.00 87.66           N  
ANISOU 2523  N   VAL A 261     4072  14613  14624   1907    -30     25       N  
ATOM   2524  CA  VAL A 261      32.256  15.303  16.018  1.00 92.17           C  
ANISOU 2524  CA  VAL A 261     4767  15195  15057   1935    -25     69       C  
ATOM   2525  C   VAL A 261      33.315  15.354  17.112  1.00 86.39           C  
ANISOU 2525  C   VAL A 261     4081  14477  14265   1987     12     84       C  
ATOM   2526  O   VAL A 261      34.499  15.605  16.846  1.00 97.32           O  
ANISOU 2526  O   VAL A 261     5563  15815  15601   1994    -17    155       O  
ATOM   2527  CB  VAL A 261      31.338  16.538  16.062  1.00 86.91           C  
ANISOU 2527  CB  VAL A 261     4098  14567  14356   1943     34     63       C  
ATOM   2528  CG1 VAL A 261      32.161  17.806  16.236  1.00 87.70           C  
ANISOU 2528  CG1 VAL A 261     4308  14659  14355   1977     70    129       C  
ATOM   2529  CG2 VAL A 261      30.498  16.620  14.798  1.00 86.71           C  
ANISOU 2529  CG2 VAL A 261     4051  14533  14364   1897    -13     68       C  
ATOM   2530  N   VAL A 262      32.907  15.102  18.360  1.00 87.39           N  
ANISOU 2530  N   VAL A 262     4131  14649  14424   2020     78     18       N  
ATOM   2531  CA  VAL A 262      33.847  15.185  19.477  1.00 87.39           C  
ANISOU 2531  CA  VAL A 262     4166  14684  14353   2075    117     16       C  
ATOM   2532  C   VAL A 262      34.963  14.158  19.316  1.00104.21           C  
ANISOU 2532  C   VAL A 262     6325  16781  16489   2081     54     45       C  
ATOM   2533  O   VAL A 262      36.152  14.483  19.431  1.00 89.09           O  
ANISOU 2533  O   VAL A 262     4500  14840  14509   2103     53    154       O  
ATOM   2534  CB  VAL A 262      33.108  15.013  20.815  1.00 88.68           C  
ANISOU 2534  CB  VAL A 262     4224  14873  14599   2101    193   -110       C  
ATOM   2535  CG1 VAL A 262      34.094  15.034  21.971  1.00 88.81           C  
ANISOU 2535  CG1 VAL A 262     4265  14914  14563   2154    216   -193       C  
ATOM   2536  CG2 VAL A 262      32.066  16.105  20.981  1.00130.07           C  
ANISOU 2536  CG2 VAL A 262     9443  20141  19838   2092    259   -135       C  
ATOM   2537  N   LEU A 263      34.596  12.902  19.040  1.00102.57           N  
ANISOU 2537  N   LEU A 263     6032  16533  16409   2055     14      0       N  
ATOM   2538  CA  LEU A 263      35.608  11.861  18.878  1.00 91.45           C  
ANISOU 2538  CA  LEU A 263     4641  15089  15019   2061    -45     16       C  
ATOM   2539  C   LEU A 263      36.522  12.154  17.695  1.00 92.86           C  
ANISOU 2539  C   LEU A 263     4934  15219  15128   2029   -120     97       C  
ATOM   2540  O   LEU A 263      37.724  11.868  17.745  1.00100.34           O  
ANISOU 2540  O   LEU A 263     5944  16139  16040   2046   -153    140       O  
ATOM   2541  CB  LEU A 263      34.943  10.494  18.716  1.00 88.49           C  
ANISOU 2541  CB  LEU A 263     4137  14656  14829   2029    -55      0       C  
ATOM   2542  CG  LEU A 263      34.367   9.866  19.985  1.00 89.93           C  
ANISOU 2542  CG  LEU A 263     4189  14826  15154   2062     31    -15       C  
ATOM   2543  CD1 LEU A 263      33.890   8.449  19.711  1.00 90.88           C  
ANISOU 2543  CD1 LEU A 263     4237  14824  15467   2009     32     44       C  
ATOM   2544  CD2 LEU A 263      35.394   9.883  21.106  1.00 89.99           C  
ANISOU 2544  CD2 LEU A 263     4231  14855  15108   2131     53    -51       C  
ATOM   2545  N   ALA A 264      35.972  12.726  16.622  1.00 85.59           N  
ANISOU 2545  N   ALA A 264     4037  14271  14213   1980   -149    115       N  
ATOM   2546  CA  ALA A 264      36.796  13.077  15.470  1.00 84.32           C  
ANISOU 2546  CA  ALA A 264     3978  14037  14024   1945   -220    162       C  
ATOM   2547  C   ALA A 264      37.836  14.127  15.843  1.00 84.58           C  
ANISOU 2547  C   ALA A 264     4112  14016  14008   1971   -192    231       C  
ATOM   2548  O   ALA A 264      39.032  13.961  15.567  1.00 87.37           O  
ANISOU 2548  O   ALA A 264     4535  14294  14367   1966   -243    246       O  
ATOM   2549  CB  ALA A 264      35.913  13.572  14.324  1.00 84.13           C  
ANISOU 2549  CB  ALA A 264     3948  14003  14013   1897   -247    153       C  
ATOM   2550  N   PHE A 265      37.398  15.210  16.490  1.00 83.58           N  
ANISOU 2550  N   PHE A 265     3988  13903  13865   1995   -109    263       N  
ATOM   2551  CA  PHE A 265      38.324  16.278  16.856  1.00 82.81           C  
ANISOU 2551  CA  PHE A 265     3968  13698  13800   2007    -73    309       C  
ATOM   2552  C   PHE A 265      39.389  15.779  17.826  1.00 97.58           C  
ANISOU 2552  C   PHE A 265     5843  15514  15721   2036    -62    328       C  
ATOM   2553  O   PHE A 265      40.588  16.012  17.625  1.00 94.36           O  
ANISOU 2553  O   PHE A 265     5503  15011  15340   2031   -108    293       O  
ATOM   2554  CB  PHE A 265      37.554  17.453  17.458  1.00 83.19           C  
ANISOU 2554  CB  PHE A 265     3996  13756  13857   2024     26    332       C  
ATOM   2555  CG  PHE A 265      38.422  18.621  17.831  1.00 82.53           C  
ANISOU 2555  CG  PHE A 265     3971  13545  13841   2032     66    317       C  
ATOM   2556  CD1 PHE A 265      38.838  19.527  16.869  1.00 81.50           C  
ANISOU 2556  CD1 PHE A 265     3915  13362  13688   2015     31    278       C  
ATOM   2557  CD2 PHE A 265      38.814  18.819  19.145  1.00 83.02           C  
ANISOU 2557  CD2 PHE A 265     4003  13554  13986   2061    139    302       C  
ATOM   2558  CE1 PHE A 265      39.633  20.605  17.209  1.00 80.96           C  
ANISOU 2558  CE1 PHE A 265     3891  13225  13643   2033     68    216       C  
ATOM   2559  CE2 PHE A 265      39.609  19.895  19.491  1.00 82.49           C  
ANISOU 2559  CE2 PHE A 265     3976  13425  13943   2077    170    215       C  
ATOM   2560  CZ  PHE A 265      40.019  20.789  18.522  1.00 81.46           C  
ANISOU 2560  CZ  PHE A 265     3920  13272  13757   2065    136    175       C  
ATOM   2561  N   ILE A 266      38.969  15.080  18.885  1.00 91.39           N  
ANISOU 2561  N   ILE A 266     4981  14807  14934   2072     -6    360       N  
ATOM   2562  CA  ILE A 266      39.920  14.623  19.898  1.00 84.34           C  
ANISOU 2562  CA  ILE A 266     4080  13820  14146   2097     15    390       C  
ATOM   2563  C   ILE A 266      40.911  13.636  19.294  1.00 83.82           C  
ANISOU 2563  C   ILE A 266     4051  13752  14043   2092    -84    369       C  
ATOM   2564  O   ILE A 266      42.130  13.773  19.457  1.00 94.43           O  
ANISOU 2564  O   ILE A 266     5444  14986  15450   2096   -119    327       O  
ATOM   2565  CB  ILE A 266      39.177  14.010  21.098  1.00 85.80           C  
ANISOU 2565  CB  ILE A 266     4169  14094  14337   2139    103    451       C  
ATOM   2566  CG1 ILE A 266      38.328  15.070  21.798  1.00 89.24           C  
ANISOU 2566  CG1 ILE A 266     4567  14429  14910   2126    209    467       C  
ATOM   2567  CG2 ILE A 266      40.166  13.384  22.071  1.00 86.21           C  
ANISOU 2567  CG2 ILE A 266     4190  13849  14717   2128    101    398       C  
ATOM   2568  CD1 ILE A 266      37.607  14.559  23.026  1.00 91.36           C  
ANISOU 2568  CD1 ILE A 266     4713  14229  15770   2047    217     41       C  
ATOM   2569  N   ILE A 267      40.400  12.626  18.584  1.00 84.10           N  
ANISOU 2569  N   ILE A 267     4055  13924  13975   2088   -140    326       N  
ATOM   2570  CA  ILE A 267      41.268  11.596  18.018  1.00 90.38           C  
ANISOU 2570  CA  ILE A 267     4874  14701  14767   2079   -227    298       C  
ATOM   2571  C   ILE A 267      42.248  12.203  17.025  1.00 82.28           C  
ANISOU 2571  C   ILE A 267     3953  13550  13761   2036   -302    284       C  
ATOM   2572  O   ILE A 267      43.436  11.855  17.010  1.00 81.76           O  
ANISOU 2572  O   ILE A 267     3934  13425  13706   2042   -351    274       O  
ATOM   2573  CB  ILE A 267      40.423  10.480  17.373  1.00 92.19           C  
ANISOU 2573  CB  ILE A 267     5023  15002  15004   2059   -274    201       C  
ATOM   2574  CG1 ILE A 267      39.830   9.569  18.450  1.00 99.21           C  
ANISOU 2574  CG1 ILE A 267     5794  15974  15926   2110   -227    119       C  
ATOM   2575  CG2 ILE A 267      41.253   9.674  16.383  1.00 83.73           C  
ANISOU 2575  CG2 ILE A 267     3988  13861  13965   2023   -370    184       C  
ATOM   2576  CD1 ILE A 267      39.021   8.416  17.897  1.00 97.56           C  
ANISOU 2576  CD1 ILE A 267     5475  15719  15877   2067   -255     66       C  
ATOM   2577  N   CYS A 268      41.778  13.132  16.192  1.00 81.66           N  
ANISOU 2577  N   CYS A 268     3909  13447  13670   1999   -312    262       N  
ATOM   2578  CA  CYS A 268      42.635  13.671  15.142  1.00 80.34           C  
ANISOU 2578  CA  CYS A 268     3838  13200  13488   1965   -385    219       C  
ATOM   2579  C   CYS A 268      43.665  14.646  15.704  1.00 82.24           C  
ANISOU 2579  C   CYS A 268     4139  13370  13738   1991   -365    187       C  
ATOM   2580  O   CYS A 268      44.875  14.445  15.552  1.00 96.08           O  
ANISOU 2580  O   CYS A 268     5948  15084  15474   1995   -424    144       O  
ATOM   2581  CB  CYS A 268      41.783  14.341  14.068  1.00 80.01           C  
ANISOU 2581  CB  CYS A 268     3807  13165  13427   1926   -397    207       C  
ATOM   2582  SG  CYS A 268      40.910  13.186  12.987  1.00102.95           S  
ANISOU 2582  SG  CYS A 268     6651  16124  16342   1879   -462    184       S  
ATOM   2583  N   TRP A 269      43.207  15.713  16.356  1.00 80.81           N  
ANISOU 2583  N   TRP A 269     3942  13183  13580   2009   -283    185       N  
ATOM   2584  CA  TRP A 269      44.107  16.773  16.795  1.00 79.37           C  
ANISOU 2584  CA  TRP A 269     3806  12957  13392   2035   -262    109       C  
ATOM   2585  C   TRP A 269      44.727  16.521  18.164  1.00 79.93           C  
ANISOU 2585  C   TRP A 269     3836  13038  13496   2083   -225     77       C  
ATOM   2586  O   TRP A 269      45.443  17.392  18.669  1.00 79.61           O  
ANISOU 2586  O   TRP A 269     3841  12997  13410   2107   -201    -23       O  
ATOM   2587  CB  TRP A 269      43.376  18.119  16.807  1.00 80.23           C  
ANISOU 2587  CB  TRP A 269     3914  13064  13505   2035   -187     99       C  
ATOM   2588  CG  TRP A 269      43.335  18.793  15.469  1.00 78.37           C  
ANISOU 2588  CG  TRP A 269     3746  12806  13226   2003   -229     87       C  
ATOM   2589  CD1 TRP A 269      42.245  18.962  14.668  1.00 78.51           C  
ANISOU 2589  CD1 TRP A 269     3751  12844  13237   1975   -225    138       C  
ATOM   2590  CD2 TRP A 269      44.440  19.383  14.773  1.00 81.80           C  
ANISOU 2590  CD2 TRP A 269     4285  13192  13603   1994   -280      6       C  
ATOM   2591  NE1 TRP A 269      42.600  19.625  13.518  1.00 77.56           N  
ANISOU 2591  NE1 TRP A 269     3701  12688  13079   1956   -268    109       N  
ATOM   2592  CE2 TRP A 269      43.943  19.894  13.558  1.00 79.80           C  
ANISOU 2592  CE2 TRP A 269     4061  12926  13334   1966   -300     30       C  
ATOM   2593  CE3 TRP A 269      45.801  19.530  15.061  1.00 86.11           C  
ANISOU 2593  CE3 TRP A 269     4918  13707  14093   2006   -311    -96       C  
ATOM   2594  CZ2 TRP A 269      44.758  20.542  12.631  1.00 86.45           C  
ANISOU 2594  CZ2 TRP A 269     5011  13715  14120   1950   -344    -34       C  
ATOM   2595  CZ3 TRP A 269      46.608  20.173  14.139  1.00 75.51           C  
ANISOU 2595  CZ3 TRP A 269     3687  12318  12685   1987   -355   -167       C  
ATOM   2596  CH2 TRP A 269      46.084  20.671  12.939  1.00 78.62           C  
ANISOU 2596  CH2 TRP A 269     4105  12689  13078   1960   -369   -132       C  
ATOM   2597  N   LEU A 270      44.482  15.360  18.779  1.00 80.87           N  
ANISOU 2597  N   LEU A 270     3891  13172  13663   2097   -218    135       N  
ATOM   2598  CA  LEU A 270      45.082  15.100  20.087  1.00 84.02           C  
ANISOU 2598  CA  LEU A 270     4242  13584  14097   2150   -186     91       C  
ATOM   2599  C   LEU A 270      46.575  14.799  19.995  1.00 84.02           C  
ANISOU 2599  C   LEU A 270     4313  13588  14023   2169   -265     19       C  
ATOM   2600  O   LEU A 270      47.355  15.425  20.737  1.00 80.79           O  
ANISOU 2600  O   LEU A 270     3951  13222  13523   2203   -247    -95       O  
ATOM   2601  CB  LEU A 270      44.316  13.981  20.800  1.00 90.04           C  
ANISOU 2601  CB  LEU A 270     4914  14342  14956   2160   -145    170       C  
ATOM   2602  CG  LEU A 270      44.777  13.642  22.219  1.00 83.85           C  
ANISOU 2602  CG  LEU A 270     4058  13585  14217   2225   -108     99       C  
ATOM   2603  CD1 LEU A 270      44.618  14.845  23.136  1.00 84.15           C  
ANISOU 2603  CD1 LEU A 270     4060  13696  14217   2263    -22     12       C  
ATOM   2604  CD2 LEU A 270      44.014  12.444  22.760  1.00 85.17           C  
ANISOU 2604  CD2 LEU A 270     4134  13705  14521   2228    -79    139       C  
ATOM   2605  N   PRO A 271      47.048  13.881  19.139  1.00 80.36           N  
ANISOU 2605  N   PRO A 271     3884  13100  13551   2145   -350     62       N  
ATOM   2606  CA  PRO A 271      48.488  13.572  19.142  1.00 79.78           C  
ANISOU 2606  CA  PRO A 271     3896  13022  13393   2160   -421    -16       C  
ATOM   2607  C   PRO A 271      49.371  14.751  18.778  1.00 78.63           C  
ANISOU 2607  C   PRO A 271     3882  12871  13123   2148   -446   -145       C  
ATOM   2608  O   PRO A 271      50.482  14.866  19.313  1.00 78.45           O  
ANISOU 2608  O   PRO A 271     3916  12885  13007   2181   -467   -237       O  
ATOM   2609  CB  PRO A 271      48.606  12.442  18.108  1.00 79.45           C  
ANISOU 2609  CB  PRO A 271     3864  12954  13371   2126   -498     58       C  
ATOM   2610  CG  PRO A 271      47.247  11.852  18.033  1.00 80.36           C  
ANISOU 2610  CG  PRO A 271     3890  13091  13552   2110   -453    164       C  
ATOM   2611  CD  PRO A 271      46.321  13.010  18.197  1.00 80.45           C  
ANISOU 2611  CD  PRO A 271     3884  13107  13575   2101   -382    154       C  
ATOM   2612  N   PHE A 272      48.916  15.632  17.884  1.00 77.91           N  
ANISOU 2612  N   PHE A 272     3837  12745  13021   2106   -442   -155       N  
ATOM   2613  CA  PHE A 272      49.733  16.781  17.508  1.00 76.88           C  
ANISOU 2613  CA  PHE A 272     3823  12599  12788   2096   -455   -274       C  
ATOM   2614  C   PHE A 272      49.985  17.695  18.700  1.00 77.32           C  
ANISOU 2614  C   PHE A 272     3874  12722  12784   2142   -380   -369       C  
ATOM   2615  O   PHE A 272      51.104  18.184  18.890  1.00 99.85           O  
ANISOU 2615  O   PHE A 272     6810  15602  15526   2157   -399   -484       O  
ATOM   2616  CB  PHE A 272      49.069  17.558  16.372  1.00 76.22           C  
ANISOU 2616  CB  PHE A 272     3773  12468  12720   2052   -452   -254       C  
ATOM   2617  CG  PHE A 272      49.790  18.825  16.005  1.00 75.29           C  
ANISOU 2617  CG  PHE A 272     3761  12328  12517   2046   -447   -366       C  
ATOM   2618  CD1 PHE A 272      49.415  20.039  16.560  1.00 84.77           C  
ANISOU 2618  CD1 PHE A 272     4947  13551  13709   2066   -358   -411       C  
ATOM   2619  CD2 PHE A 272      50.847  18.802  15.112  1.00 74.21           C  
ANISOU 2619  CD2 PHE A 272     3735  12147  12313   2022   -526   -427       C  
ATOM   2620  CE1 PHE A 272      50.080  21.204  16.230  1.00 74.78           C  
ANISOU 2620  CE1 PHE A 272     3772  12267  12373   2064   -345   -513       C  
ATOM   2621  CE2 PHE A 272      51.514  19.965  14.777  1.00 73.41           C  
ANISOU 2621  CE2 PHE A 272     3726  12024  12141   2020   -514   -528       C  
ATOM   2622  CZ  PHE A 272      51.130  21.166  15.337  1.00 73.71           C  
ANISOU 2622  CZ  PHE A 272     3744  12086  12176   2042   -423   -570       C  
ATOM   2623  N   HIS A 273      48.956  17.942  19.511  1.00 78.32           N  
ANISOU 2623  N   HIS A 273     3901  12885  12971   2163   -291   -329       N  
ATOM   2624  CA  HIS A 273      49.117  18.821  20.660  1.00 78.86           C  
ANISOU 2624  CA  HIS A 273     3958  13036  12968   2205   -211   -425       C  
ATOM   2625  C   HIS A 273      49.750  18.118  21.852  1.00 85.50           C  
ANISOU 2625  C   HIS A 273     4764  13978  13743   2261   -210   -460       C  
ATOM   2626  O   HIS A 273      50.322  18.793  22.717  1.00 90.11           O  
ANISOU 2626  O   HIS A 273     5370  14662  14206   2299   -168   -570       O  
ATOM   2627  CB  HIS A 273      47.769  19.423  21.054  1.00 79.61           C  
ANISOU 2627  CB  HIS A 273     3966  13137  13146   2204   -110   -375       C  
ATOM   2628  CG  HIS A 273      47.257  20.431  20.072  1.00 78.89           C  
ANISOU 2628  CG  HIS A 273     3915  12979  13080   2165    -93   -364       C  
ATOM   2629  ND1 HIS A 273      47.510  21.780  20.192  1.00 78.58           N  
ANISOU 2629  ND1 HIS A 273     3927  12953  12976   2170    -37   -462       N  
ATOM   2630  CD2 HIS A 273      46.522  20.284  18.945  1.00 88.43           C  
ANISOU 2630  CD2 HIS A 273     5118  14121  14360   2124   -122   -265       C  
ATOM   2631  CE1 HIS A 273      46.945  22.422  19.185  1.00 78.02           C  
ANISOU 2631  CE1 HIS A 273     3879  12816  12949   2138    -30   -417       C  
ATOM   2632  NE2 HIS A 273      46.339  21.538  18.414  1.00 94.36           N  
ANISOU 2632  NE2 HIS A 273     5916  14845  15090   2111    -85   -300       N  
ATOM   2633  N   VAL A 274      49.666  16.789  21.923  1.00 85.92           N  
ANISOU 2633  N   VAL A 274     4761  14019  13865   2272   -251   -370       N  
ATOM   2634  CA  VAL A 274      50.441  16.061  22.924  1.00 81.24           C  
ANISOU 2634  CA  VAL A 274     4148  13528  13192   2333   -262   -397       C  
ATOM   2635  C   VAL A 274      51.929  16.161  22.610  1.00 79.99           C  
ANISOU 2635  C   VAL A 274     4107  13387  12898   2338   -340   -493       C  
ATOM   2636  O   VAL A 274      52.733  16.581  23.453  1.00 80.25           O  
ANISOU 2636  O   VAL A 274     4170  13541  12781   2384   -322   -594       O  
ATOM   2637  CB  VAL A 274      49.977  14.596  23.005  1.00 81.70           C  
ANISOU 2637  CB  VAL A 274     4113  13552  13378   2345   -283   -272       C  
ATOM   2638  CG1 VAL A 274      50.942  13.784  23.854  1.00 82.33           C  
ANISOU 2638  CG1 VAL A 274     4188  13734  13361   2413   -308   -292       C  
ATOM   2639  CG2 VAL A 274      48.570  14.517  23.573  1.00 82.82           C  
ANISOU 2639  CG2 VAL A 274     4131  13696  13642   2352   -193   -202       C  
ATOM   2640  N   LEU A 275      52.313  15.790  21.384  1.00 78.93           N  
ANISOU 2640  N   LEU A 275     4041  13144  12805   2288   -425   -465       N  
ATOM   2641  CA  LEU A 275      53.712  15.884  20.979  1.00 77.98           C  
ANISOU 2641  CA  LEU A 275     4037  13024  12567   2285   -500   -556       C  
ATOM   2642  C   LEU A 275      54.215  17.320  21.023  1.00 79.00           C  
ANISOU 2642  C   LEU A 275     4247  13187  12581   2281   -469   -697       C  
ATOM   2643  O   LEU A 275      55.386  17.557  21.340  1.00 81.64           O  
ANISOU 2643  O   LEU A 275     4650  13586  12783   2306   -496   -804       O  
ATOM   2644  CB  LEU A 275      53.894  15.301  19.579  1.00 76.97           C  
ANISOU 2644  CB  LEU A 275     3966  12773  12504   2226   -586   -501       C  
ATOM   2645  CG  LEU A 275      53.691  13.793  19.434  1.00 77.48           C  
ANISOU 2645  CG  LEU A 275     3964  12804  12671   2228   -628   -378       C  
ATOM   2646  CD1 LEU A 275      53.730  13.396  17.970  1.00 76.49           C  
ANISOU 2646  CD1 LEU A 275     3897  12577  12590   2162   -700   -336       C  
ATOM   2647  CD2 LEU A 275      54.745  13.035  20.225  1.00 77.95           C  
ANISOU 2647  CD2 LEU A 275     4026  12933  12659   2286   -660   -401       C  
ATOM   2648  N   THR A 276      53.354  18.289  20.705  1.00 77.20           N  
ANISOU 2648  N   THR A 276     4009  12917  12405   2251   -410   -697       N  
ATOM   2649  CA  THR A 276      53.745  19.688  20.828  1.00 76.80           C  
ANISOU 2649  CA  THR A 276     4020  12897  12263   2251   -363   -828       C  
ATOM   2650  C   THR A 276      53.907  20.092  22.287  1.00 80.27           C  
ANISOU 2650  C   THR A 276     4412  13487  12598   2309   -290   -910       C  
ATOM   2651  O   THR A 276      54.774  20.913  22.611  1.00 77.64           O  
ANISOU 2651  O   THR A 276     4139  13218  12141   2323   -276  -1047       O  
ATOM   2652  CB  THR A 276      52.718  20.586  20.136  1.00 82.69           C  
ANISOU 2652  CB  THR A 276     4758  13562  13100   2211   -311   -791       C  
ATOM   2653  OG1 THR A 276      52.541  20.154  18.781  1.00 94.20           O  
ANISOU 2653  OG1 THR A 276     6253  14906  14631   2161   -381   -711       O  
ATOM   2654  CG2 THR A 276      53.182  22.036  20.138  1.00 76.03           C  
ANISOU 2654  CG2 THR A 276     3980  12730  12178   2209   -262   -923       C  
ATOM   2655  N   PHE A 277      53.095  19.521  23.179  1.00 91.04           N  
ANISOU 2655  N   PHE A 277     5668  14920  14005   2344   -239   -832       N  
ATOM   2656  CA  PHE A 277      53.212  19.834  24.599  1.00 91.15           C  
ANISOU 2656  CA  PHE A 277     5632  15103  13900   2403   -166   -903       C  
ATOM   2657  C   PHE A 277      54.519  19.304  25.174  1.00100.27           C  
ANISOU 2657  C   PHE A 277     6824  16376  14898   2453   -220   -969       C  
ATOM   2658  O   PHE A 277      55.340  20.070  25.692  1.00 80.42           O  
ANISOU 2658  O   PHE A 277     4355  13966  12234   2475   -202  -1107       O  
ATOM   2659  CB  PHE A 277      52.019  19.267  25.368  1.00 84.63           C  
ANISOU 2659  CB  PHE A 277     4680  14322  13155   2430    -98   -794       C  
ATOM   2660  CG  PHE A 277      52.217  19.252  26.858  1.00 88.03           C  
ANISOU 2660  CG  PHE A 277     5055  14953  13441   2503    -34   -841       C  
ATOM   2661  CD1 PHE A 277      52.427  18.059  27.531  1.00 86.49           C  
ANISOU 2661  CD1 PHE A 277     4806  14853  13204   2561    -55   -767       C  
ATOM   2662  CD2 PHE A 277      52.209  20.432  27.583  1.00 83.23           C  
ANISOU 2662  CD2 PHE A 277     4446  14447  12730   2515     51   -955       C  
ATOM   2663  CE1 PHE A 277      52.613  18.042  28.900  1.00 85.02           C  
ANISOU 2663  CE1 PHE A 277     4569  14876  12858   2635      6   -796       C  
ATOM   2664  CE2 PHE A 277      52.396  20.422  28.953  1.00 84.53           C  
ANISOU 2664  CE2 PHE A 277     4559  14818  12741   2582    110   -998       C  
ATOM   2665  CZ  PHE A 277      52.598  19.225  29.612  1.00 85.43           C  
ANISOU 2665  CZ  PHE A 277     4622  15042  12796   2644     88   -914       C  
ATOM   2666  N   LEU A 278      54.731  17.985  25.099  1.00 80.58           N  
ANISOU 2666  N   LEU A 278     4308  13871  12437   2473   -285   -872       N  
ATOM   2667  CA  LEU A 278      55.956  17.432  25.670  1.00 93.86           C  
ANISOU 2667  CA  LEU A 278     6021  15673  13968   2528   -334   -919       C  
ATOM   2668  C   LEU A 278      57.190  17.885  24.899  1.00 91.22           C  
ANISOU 2668  C   LEU A 278     5813  15287  13560   2496   -408  -1032       C  
ATOM   2669  O   LEU A 278      58.291  17.920  25.461  1.00 84.79           O  
ANISOU 2669  O   LEU A 278     5037  14594  12584   2539   -431  -1124       O  
ATOM   2670  CB  LEU A 278      55.879  15.903  25.739  1.00 81.41           C  
ANISOU 2670  CB  LEU A 278     4388  14085  12461   2559   -380   -779       C  
ATOM   2671  CG  LEU A 278      55.276  15.085  24.595  1.00 80.81           C  
ANISOU 2671  CG  LEU A 278     4299  13819  12588   2501   -432   -657       C  
ATOM   2672  CD1 LEU A 278      56.211  15.007  23.407  1.00 79.39           C  
ANISOU 2672  CD1 LEU A 278     4232  13523  12410   2451   -530   -694       C  
ATOM   2673  CD2 LEU A 278      54.916  13.691  25.084  1.00 81.92           C  
ANISOU 2673  CD2 LEU A 278     4342  13983  12802   2548   -432   -524       C  
ATOM   2674  N   ASP A 279      57.030  18.239  23.621  1.00 93.31           N  
ANISOU 2674  N   ASP A 279     6141  15382  13930   2425   -443  -1026       N  
ATOM   2675  CA  ASP A 279      58.120  18.882  22.894  1.00 92.83           C  
ANISOU 2675  CA  ASP A 279     6202  15273  13798   2394   -494  -1144       C  
ATOM   2676  C   ASP A 279      58.448  20.238  23.504  1.00 77.27           C  
ANISOU 2676  C   ASP A 279     4254  13396  11709   2407   -427  -1302       C  
ATOM   2677  O   ASP A 279      59.622  20.571  23.704  1.00 77.01           O  
ANISOU 2677  O   ASP A 279     4287  13431  11542   2423   -454  -1429       O  
ATOM   2678  CB  ASP A 279      57.753  19.029  21.418  1.00 91.53           C  
ANISOU 2678  CB  ASP A 279     6091  14924  13761   2320   -532  -1094       C  
ATOM   2679  CG  ASP A 279      58.785  19.816  20.640  1.00 83.82           C  
ANISOU 2679  CG  ASP A 279     5238  13894  12716   2288   -570  -1216       C  
ATOM   2680  OD1 ASP A 279      59.871  19.265  20.362  1.00 74.15           O  
ANISOU 2680  OD1 ASP A 279     4081  12664  11430   2291   -647  -1248       O  
ATOM   2681  OD2 ASP A 279      58.513  20.990  20.310  1.00 80.41           O  
ANISOU 2681  OD2 ASP A 279     4834  13423  12296   2262   -519  -1278       O  
ATOM   2682  N   ALA A 280      57.418  21.031  23.812  1.00 80.09           N  
ANISOU 2682  N   ALA A 280     4553  13758  12118   2399   -335  -1298       N  
ATOM   2683  CA  ALA A 280      57.639  22.296  24.503  1.00 84.71           C  
ANISOU 2683  CA  ALA A 280     5145  14440  12602   2411   -257  -1445       C  
ATOM   2684  C   ALA A 280      58.282  22.081  25.865  1.00 84.02           C  
ANISOU 2684  C   ALA A 280     5020  14564  12340   2480   -240  -1521       C  
ATOM   2685  O   ALA A 280      59.049  22.931  26.330  1.00 82.94           O  
ANISOU 2685  O   ALA A 280     4919  14522  12073   2491   -216  -1679       O  
ATOM   2686  CB  ALA A 280      56.321  23.055  24.648  1.00 87.48           C  
ANISOU 2686  CB  ALA A 280     5429  14758  13052   2393   -156  -1407       C  
ATOM   2687  N   LEU A 281      57.981  20.956  26.521  1.00 81.67           N  
ANISOU 2687  N   LEU A 281     4648  14352  12033   2528   -249  -1410       N  
ATOM   2688  CA  LEU A 281      58.694  20.610  27.745  1.00 89.19           C  
ANISOU 2688  CA  LEU A 281     5569  15521  12798   2603   -244  -1462       C  
ATOM   2689  C   LEU A 281      60.154  20.285  27.464  1.00102.05           C  
ANISOU 2689  C   LEU A 281     7285  17171  14317   2615   -337  -1537       C  
ATOM   2690  O   LEU A 281      61.021  20.559  28.301  1.00110.75           O  
ANISOU 2690  O   LEU A 281     8395  18449  15235   2661   -332  -1653       O  
ATOM   2691  CB  LEU A 281      58.015  19.432  28.443  1.00 94.79           C  
ANISOU 2691  CB  LEU A 281     6177  16309  13531   2658   -228  -1304       C  
ATOM   2692  CG  LEU A 281      56.679  19.716  29.130  1.00104.80           C  
ANISOU 2692  CG  LEU A 281     7343  17623  14855   2668   -120  -1246       C  
ATOM   2693  CD1 LEU A 281      56.148  18.459  29.800  1.00110.20           C  
ANISOU 2693  CD1 LEU A 281     7932  18387  15552   2729   -108  -1087       C  
ATOM   2694  CD2 LEU A 281      56.825  20.845  30.139  1.00101.36           C  
ANISOU 2694  CD2 LEU A 281     6891  17357  14264   2692    -35  -1392       C  
ATOM   2695  N   ALA A 282      60.445  19.702  26.298  1.00106.16           N  
ANISOU 2695  N   ALA A 282     7870  17522  14942   2573   -423  -1474       N  
ATOM   2696  CA  ALA A 282      61.834  19.439  25.938  1.00 95.49           C  
ANISOU 2696  CA  ALA A 282     6611  16174  13498   2576   -510  -1548       C  
ATOM   2697  C   ALA A 282      62.583  20.725  25.615  1.00 77.99           C  
ANISOU 2697  C   ALA A 282     4481  13941  11212   2541   -502  -1732       C  
ATOM   2698  O   ALA A 282      63.803  20.792  25.803  1.00 84.56           O  
ANISOU 2698  O   ALA A 282     5370  14852  11908   2562   -545  -1844       O  
ATOM   2699  CB  ALA A 282      61.900  18.473  24.755  1.00 86.53           C  
ANISOU 2699  CB  ALA A 282     5520  14859  12499   2536   -597  -1431       C  
ATOM   2700  N   TRP A 283      61.878  21.752  25.134  1.00 77.53           N  
ANISOU 2700  N   TRP A 283     4430  13781  11248   2490   -444  -1764       N  
ATOM   2701  CA  TRP A 283      62.539  23.016  24.823  1.00 76.87           C  
ANISOU 2701  CA  TRP A 283     4421  13671  11115   2458   -425  -1934       C  
ATOM   2702  C   TRP A 283      62.987  23.738  26.088  1.00 77.97           C  
ANISOU 2702  C   TRP A 283     4527  14013  11087   2501   -365  -2089       C  
ATOM   2703  O   TRP A 283      64.065  24.343  26.113  1.00 94.99           O  
ANISOU 2703  O   TRP A 283     6744  16209  13137   2497   -382  -2248       O  
ATOM   2704  CB  TRP A 283      61.612  23.910  23.999  1.00 83.00           C  
ANISOU 2704  CB  TRP A 283     5206  14289  12040   2399   -371  -1908       C  
ATOM   2705  CG  TRP A 283      61.534  23.529  22.553  1.00 93.69           C  
ANISOU 2705  CG  TRP A 283     6626  15450  13522   2347   -438  -1813       C  
ATOM   2706  CD1 TRP A 283      60.547  22.809  21.946  1.00 98.15           C  
ANISOU 2706  CD1 TRP A 283     7154  15911  14226   2326   -455  -1645       C  
ATOM   2707  CD2 TRP A 283      62.485  23.847  21.530  1.00 94.13           C  
ANISOU 2707  CD2 TRP A 283     6794  15402  13569   2310   -496  -1885       C  
ATOM   2708  NE1 TRP A 283      60.824  22.660  20.609  1.00 90.01           N  
ANISOU 2708  NE1 TRP A 283     6206  14730  13265   2277   -521  -1609       N  
ATOM   2709  CE2 TRP A 283      62.008  23.288  20.328  1.00 85.18           C  
ANISOU 2709  CE2 TRP A 283     5687  14113  12565   2268   -545  -1752       C  
ATOM   2710  CE3 TRP A 283      63.693  24.551  21.514  1.00101.53           C  
ANISOU 2710  CE3 TRP A 283     7808  16368  14402   2308   -509  -2053       C  
ATOM   2711  CZ2 TRP A 283      62.696  23.411  19.123  1.00 85.51           C  
ANISOU 2711  CZ2 TRP A 283     5833  14033  12625   2227   -605  -1777       C  
ATOM   2712  CZ3 TRP A 283      64.375  24.672  20.317  1.00101.41           C  
ANISOU 2712  CZ3 TRP A 283     7895  16219  14416   2267   -567  -2076       C  
ATOM   2713  CH2 TRP A 283      63.875  24.104  19.138  1.00 96.11           C  
ANISOU 2713  CH2 TRP A 283     7250  15400  13866   2228   -613  -1937       C  
ATOM   2714  N   MET A 284      62.180  23.688  27.144  1.00 79.30           N  
ANISOU 2714  N   MET A 284     4593  14311  11224   2540   -291  -2050       N  
ATOM   2715  CA  MET A 284      62.480  24.388  28.385  1.00 80.50           C  
ANISOU 2715  CA  MET A 284     4703  14670  11213   2578   -225  -2194       C  
ATOM   2716  C   MET A 284      63.383  23.587  29.317  1.00 81.41           C  
ANISOU 2716  C   MET A 284     4798  14998  11136   2652   -272  -2218       C  
ATOM   2717  O   MET A 284      63.554  23.974  30.478  1.00 82.67           O  
ANISOU 2717  O   MET A 284     4905  15367  11139   2695   -219  -2316       O  
ATOM   2718  CB  MET A 284      61.180  24.761  29.105  1.00 81.56           C  
ANISOU 2718  CB  MET A 284     4739  14857  11395   2586   -117  -2144       C  
ATOM   2719  CG  MET A 284      60.269  23.584  29.404  1.00 98.60           C  
ANISOU 2719  CG  MET A 284     6815  17036  13612   2623   -117  -1947       C  
ATOM   2720  SD  MET A 284      58.607  24.102  29.876  1.00106.57           S  
ANISOU 2720  SD  MET A 284     7724  18034  14733   2612      9  -1874       S  
ATOM   2721  CE  MET A 284      58.968  25.202  31.243  1.00105.99           C  
ANISOU 2721  CE  MET A 284     7615  18192  14465   2641    102  -2070       C  
ATOM   2722  N   GLY A 285      63.963  22.488  28.839  1.00 87.36           N  
ANISOU 2722  N   GLY A 285     5591  15709  11894   2668   -366  -2129       N  
ATOM   2723  CA  GLY A 285      64.917  21.722  29.612  1.00 95.07           C  
ANISOU 2723  CA  GLY A 285     6557  16875  12690   2741   -415  -2142       C  
ATOM   2724  C   GLY A 285      64.333  20.632  30.485  1.00 95.80           C  
ANISOU 2724  C   GLY A 285     6551  17104  12744   2815   -398  -1979       C  
ATOM   2725  O   GLY A 285      65.101  19.888  31.109  1.00 83.71           O  
ANISOU 2725  O   GLY A 285     5009  15735  11064   2885   -439  -1961       O  
ATOM   2726  N   VAL A 286      63.006  20.510  30.552  1.00101.32           N  
ANISOU 2726  N   VAL A 286     7178  17747  13572   2806   -336  -1856       N  
ATOM   2727  CA  VAL A 286      62.398  19.476  31.385  1.00 95.12           C  
ANISOU 2727  CA  VAL A 286     6295  17086  12759   2878   -310  -1693       C  
ATOM   2728  C   VAL A 286      62.720  18.092  30.835  1.00 89.65           C  
ANISOU 2728  C   VAL A 286     5621  16306  12135   2897   -398  -1540       C  
ATOM   2729  O   VAL A 286      63.153  17.198  31.572  1.00 85.32           O  
ANISOU 2729  O   VAL A 286     5035  15917  11467   2978   -415  -1465       O  
ATOM   2730  CB  VAL A 286      60.879  19.702  31.497  1.00 96.66           C  
ANISOU 2730  CB  VAL A 286     6412  17219  13095   2855   -221  -1602       C  
ATOM   2731  CG1 VAL A 286      60.236  18.598  32.325  1.00 91.97           C  
ANISOU 2731  CG1 VAL A 286     5716  16745  12482   2930   -189  -1426       C  
ATOM   2732  CG2 VAL A 286      60.590  21.067  32.102  1.00 85.61           C  
ANISOU 2732  CG2 VAL A 286     4993  15910  11627   2838   -127  -1754       C  
ATOM   2733  N   ILE A 287      62.520  17.896  29.537  1.00 93.97           N  
ANISOU 2733  N   ILE A 287     6224  16605  12875   2823   -451  -1489       N  
ATOM   2734  CA  ILE A 287      62.796  16.627  28.875  1.00100.30           C  
ANISOU 2734  CA  ILE A 287     7047  17294  13770   2825   -534  -1354       C  
ATOM   2735  C   ILE A 287      64.135  16.759  28.163  1.00101.17           C  
ANISOU 2735  C   ILE A 287     7273  17344  13825   2797   -621  -1463       C  
ATOM   2736  O   ILE A 287      64.243  17.450  27.144  1.00 97.21           O  
ANISOU 2736  O   ILE A 287     6850  16679  13409   2720   -644  -1539       O  
ATOM   2737  CB  ILE A 287      61.677  16.241  27.899  1.00100.24           C  
ANISOU 2737  CB  ILE A 287     7019  17061  14008   2760   -537  -1223       C  
ATOM   2738  CG1 ILE A 287      60.346  16.098  28.641  1.00 90.65           C  
ANISOU 2738  CG1 ILE A 287     5687  15908  12849   2790   -446  -1119       C  
ATOM   2739  CG2 ILE A 287      62.028  14.954  27.165  1.00 99.80           C  
ANISOU 2739  CG2 ILE A 287     6985  16881  14052   2754   -625  -1102       C  
ATOM   2740  CD1 ILE A 287      59.185  15.723  27.748  1.00 82.45           C  
ANISOU 2740  CD1 ILE A 287     4616  14662  12050   2728   -444   -995       C  
ATOM   2741  N   ASN A 288      65.160  16.097  28.697  1.00102.41           N  
ANISOU 2741  N   ASN A 288     7439  17637  13834   2863   -667  -1463       N  
ATOM   2742  CA  ASN A 288      66.494  16.124  28.114  1.00 96.73           C  
ANISOU 2742  CA  ASN A 288     6825  16876  13051   2845   -749  -1562       C  
ATOM   2743  C   ASN A 288      66.934  14.772  27.572  1.00 96.39           C  
ANISOU 2743  C   ASN A 288     6803  16738  13084   2855   -830  -1426       C  
ATOM   2744  O   ASN A 288      68.081  14.642  27.132  1.00104.19           O  
ANISOU 2744  O   ASN A 288     7876  17696  14016   2846   -900  -1492       O  
ATOM   2745  CB  ASN A 288      67.513  16.624  29.145  1.00101.43           C  
ANISOU 2745  CB  ASN A 288     7426  17715  13397   2908   -739  -1710       C  
ATOM   2746  CG  ASN A 288      67.277  18.068  29.545  1.00109.90           C  
ANISOU 2746  CG  ASN A 288     8493  18863  14402   2884   -666  -1881       C  
ATOM   2747  OD1 ASN A 288      66.681  18.843  28.796  1.00109.40           O  
ANISOU 2747  OD1 ASN A 288     8458  18634  14476   2808   -639  -1920       O  
ATOM   2748  ND2 ASN A 288      67.749  18.438  30.730  1.00114.05           N  
ANISOU 2748  ND2 ASN A 288     8978  19644  14713   2950   -630  -1983       N  
ATOM   2749  N   SER A 289      66.063  13.766  27.593  1.00 92.68           N  
ANISOU 2749  N   SER A 289     6256  16215  12743   2873   -820  -1243       N  
ATOM   2750  CA  SER A 289      66.407  12.467  27.032  1.00 92.19           C  
ANISOU 2750  CA  SER A 289     6205  16043  12779   2877   -891  -1112       C  
ATOM   2751  C   SER A 289      66.529  12.572  25.516  1.00 87.45           C  
ANISOU 2751  C   SER A 289     5698  15193  12338   2772   -954  -1137       C  
ATOM   2752  O   SER A 289      65.622  13.073  24.843  1.00 83.94           O  
ANISOU 2752  O   SER A 289     5251  14614  12028   2703   -928  -1132       O  
ATOM   2753  CB  SER A 289      65.354  11.429  27.414  1.00 95.30           C  
ANISOU 2753  CB  SER A 289     6485  16435  13291   2918   -853   -919       C  
ATOM   2754  OG  SER A 289      65.679  10.152  26.894  1.00 90.82           O  
ANISOU 2754  OG  SER A 289     5919  15757  12831   2923   -915   -796       O  
ATOM   2755  N   CYS A 290      67.654  12.098  24.979  1.00 92.51           N  
ANISOU 2755  N   CYS A 290     6418  15779  12953   2763  -1032  -1158       N  
ATOM   2756  CA  CYS A 290      67.938  12.295  23.560  1.00 95.75           C  
ANISOU 2756  CA  CYS A 290     6929  15979  13473   2667  -1089  -1199       C  
ATOM   2757  C   CYS A 290      66.996  11.474  22.685  1.00 82.82           C  
ANISOU 2757  C   CYS A 290     5253  14158  12057   2615  -1104  -1048       C  
ATOM   2758  O   CYS A 290      66.385  12.003  21.748  1.00 76.99           O  
ANISOU 2758  O   CYS A 290     4547  13281  11427   2536  -1099  -1062       O  
ATOM   2759  CB  CYS A 290      69.397  11.946  23.261  1.00112.12           C  
ANISOU 2759  CB  CYS A 290     9093  18049  15458   2674  -1165  -1257       C  
ATOM   2760  SG  CYS A 290      69.758  10.174  23.195  1.00138.08           S  
ANISOU 2760  SG  CYS A 290    12344  21294  18825   2715  -1224  -1081       S  
ATOM   2761  N   GLU A 291      66.866  10.176  22.974  1.00 81.37           N  
ANISOU 2761  N   GLU A 291     4997  13979  11942   2660  -1120   -902       N  
ATOM   2762  CA  GLU A 291      66.029   9.322  22.138  1.00 81.54           C  
ANISOU 2762  CA  GLU A 291     4973  13828  12178   2610  -1135   -767       C  
ATOM   2763  C   GLU A 291      64.559   9.711  22.228  1.00 83.51           C  
ANISOU 2763  C   GLU A 291     5141  14054  12534   2588  -1065   -718       C  
ATOM   2764  O   GLU A 291      63.803   9.487  21.276  1.00 86.61           O  
ANISOU 2764  O   GLU A 291     5523  14294  13090   2519  -1074   -655       O  
ATOM   2765  CB  GLU A 291      66.217   7.851  22.517  1.00 96.40           C  
ANISOU 2765  CB  GLU A 291     6783  15724  14120   2672  -1156   -625       C  
ATOM   2766  CG  GLU A 291      65.659   7.461  23.878  1.00113.56           C  
ANISOU 2766  CG  GLU A 291     8836  18062  16248   2774  -1087   -540       C  
ATOM   2767  CD  GLU A 291      66.590   7.816  25.021  1.00121.42           C  
ANISOU 2767  CD  GLU A 291     9851  19284  16998   2864  -1074   -612       C  
ATOM   2768  OE1 GLU A 291      67.762   8.152  24.753  1.00120.40           O  
ANISOU 2768  OE1 GLU A 291     9823  19169  16756   2852  -1129   -719       O  
ATOM   2769  OE2 GLU A 291      66.148   7.757  26.188  1.00128.28           O  
ANISOU 2769  OE2 GLU A 291    10634  20328  17779   2948  -1006   -560       O  
ATOM   2770  N   VAL A 292      64.138  10.296  23.351  1.00 84.04           N  
ANISOU 2770  N   VAL A 292     5150  14280  12504   2646   -993   -749       N  
ATOM   2771  CA  VAL A 292      62.755  10.746  23.479  1.00 87.05           C  
ANISOU 2771  CA  VAL A 292     5455  14642  12980   2625   -921   -711       C  
ATOM   2772  C   VAL A 292      62.490  11.919  22.543  1.00 83.99           C  
ANISOU 2772  C   VAL A 292     5144  14147  12622   2537   -919   -807       C  
ATOM   2773  O   VAL A 292      61.507  11.926  21.792  1.00 77.13           O  
ANISOU 2773  O   VAL A 292     4249  13150  11905   2478   -907   -744       O  
ATOM   2774  CB  VAL A 292      62.443  11.106  24.943  1.00 80.26           C  
ANISOU 2774  CB  VAL A 292     4517  13993  11986   2710   -839   -724       C  
ATOM   2775  CG1 VAL A 292      61.075  11.758  25.050  1.00 86.78           C  
ANISOU 2775  CG1 VAL A 292     5277  14798  12899   2682   -759   -708       C  
ATOM   2776  CG2 VAL A 292      62.510   9.862  25.815  1.00 81.72           C  
ANISOU 2776  CG2 VAL A 292     4614  14282  12152   2803   -828   -594       C  
ATOM   2777  N   ILE A 293      63.368  12.926  22.570  1.00 82.97           N  
ANISOU 2777  N   ILE A 293     5106  14072  12346   2532   -927   -960       N  
ATOM   2778  CA  ILE A 293      63.237  14.057  21.655  1.00 76.11           C  
ANISOU 2778  CA  ILE A 293     4317  13101  11501   2457   -922  -1053       C  
ATOM   2779  C   ILE A 293      63.321  13.581  20.210  1.00 74.40           C  
ANISOU 2779  C   ILE A 293     4164  12700  11402   2382   -990  -1002       C  
ATOM   2780  O   ILE A 293      62.630  14.103  19.325  1.00 73.67           O  
ANISOU 2780  O   ILE A 293     4093  12500  11398   2319   -978   -993       O  
ATOM   2781  CB  ILE A 293      64.306  15.121  21.968  1.00 76.05           C  
ANISOU 2781  CB  ILE A 293     4393  13186  11318   2471   -919  -1233       C  
ATOM   2782  CG1 ILE A 293      64.179  15.596  23.416  1.00 83.04           C  
ANISOU 2782  CG1 ILE A 293     5206  14275  12070   2544   -846  -1288       C  
ATOM   2783  CG2 ILE A 293      64.181  16.299  21.021  1.00 74.00           C  
ANISOU 2783  CG2 ILE A 293     4210  12814  11091   2400   -906  -1324       C  
ATOM   2784  CD1 ILE A 293      65.205  16.637  23.809  1.00 76.32           C  
ANISOU 2784  CD1 ILE A 293     4422  13532  11043   2559   -838  -1476       C  
ATOM   2785  N   ALA A 294      64.163  12.577  19.951  1.00 74.23           N  
ANISOU 2785  N   ALA A 294     4174  12651  11378   2391  -1060   -964       N  
ATOM   2786  CA  ALA A 294      64.215  11.984  18.619  1.00 80.15           C  
ANISOU 2786  CA  ALA A 294     4975  13242  12236   2322  -1121   -907       C  
ATOM   2787  C   ALA A 294      62.865  11.396  18.227  1.00 96.11           C  
ANISOU 2787  C   ALA A 294     6905  15185  14427   2291  -1099   -768       C  
ATOM   2788  O   ALA A 294      62.395  11.600  17.102  1.00109.17           O  
ANISOU 2788  O   ALA A 294     8595  16731  16154   2221  -1113   -753       O  
ATOM   2789  CB  ALA A 294      65.307  10.917  18.560  1.00 73.22           C  
ANISOU 2789  CB  ALA A 294     4129  12360  11332   2344  -1190   -880       C  
ATOM   2790  N   VAL A 295      62.220  10.673  19.148  1.00 94.81           N  
ANISOU 2790  N   VAL A 295     6619  15084  14321   2346  -1061   -667       N  
ATOM   2791  CA  VAL A 295      60.898  10.113  18.869  1.00 90.00           C  
ANISOU 2791  CA  VAL A 295     5909  14408  13878   2321  -1031   -538       C  
ATOM   2792  C   VAL A 295      59.895  11.226  18.592  1.00 75.20           C  
ANISOU 2792  C   VAL A 295     4031  12513  12028   2280   -977   -568       C  
ATOM   2793  O   VAL A 295      59.031  11.099  17.714  1.00 74.89           O  
ANISOU 2793  O   VAL A 295     3973  12386  12097   2223   -977   -502       O  
ATOM   2794  CB  VAL A 295      60.443   9.210  20.031  1.00 77.13           C  
ANISOU 2794  CB  VAL A 295     4146  12857  12302   2398   -989   -436       C  
ATOM   2795  CG1 VAL A 295      58.974   8.851  19.891  1.00 77.77           C  
ANISOU 2795  CG1 VAL A 295     4115  12882  12552   2375   -940   -322       C  
ATOM   2796  CG2 VAL A 295      61.287   7.948  20.080  1.00105.15           C  
ANISOU 2796  CG2 VAL A 295     7687  16396  15870   2433  -1043   -374       C  
ATOM   2797  N   ILE A 296      59.995  12.335  19.329  1.00 75.32           N  
ANISOU 2797  N   ILE A 296     4063  12620  11936   2310   -928   -669       N  
ATOM   2798  CA  ILE A 296      59.135  13.487  19.066  1.00 75.00           C  
ANISOU 2798  CA  ILE A 296     4025  12557  11916   2274   -872   -706       C  
ATOM   2799  C   ILE A 296      59.324  13.972  17.634  1.00 73.59           C  
ANISOU 2799  C   ILE A 296     3949  12260  11751   2198   -916   -743       C  
ATOM   2800  O   ILE A 296      58.356  14.141  16.879  1.00 73.34           O  
ANISOU 2800  O   ILE A 296     3898  12157  11812   2151   -901   -685       O  
ATOM   2801  CB  ILE A 296      59.421  14.612  20.077  1.00 75.35           C  
ANISOU 2801  CB  ILE A 296     4078  12725  11827   2318   -812   -827       C  
ATOM   2802  CG1 ILE A 296      59.210  14.116  21.507  1.00 76.86           C  
ANISOU 2802  CG1 ILE A 296     4166  13060  11979   2399   -764   -789       C  
ATOM   2803  CG2 ILE A 296      58.546  15.821  19.788  1.00 75.05           C  
ANISOU 2803  CG2 ILE A 296     4040  12654  11823   2282   -748   -861       C  
ATOM   2804  CD1 ILE A 296      59.703  15.083  22.561  1.00 77.32           C  
ANISOU 2804  CD1 ILE A 296     4236  13275  11866   2449   -712   -919       C  
ATOM   2805  N   ASP A 297      60.580  14.192  17.237  1.00 72.68           N  
ANISOU 2805  N   ASP A 297     3946  12132  11537   2190   -970   -841       N  
ATOM   2806  CA  ASP A 297      60.870  14.664  15.888  1.00 71.35           C  
ANISOU 2806  CA  ASP A 297     3882  11859  11369   2125  -1009   -886       C  
ATOM   2807  C   ASP A 297      60.481  13.648  14.822  1.00 71.06           C  
ANISOU 2807  C   ASP A 297     3838  11728  11432   2075  -1061   -781       C  
ATOM   2808  O   ASP A 297      60.299  14.027  13.659  1.00 70.17           O  
ANISOU 2808  O   ASP A 297     3786  11538  11338   2020  -1080   -792       O  
ATOM   2809  CB  ASP A 297      62.356  15.008  15.763  1.00 84.62           C  
ANISOU 2809  CB  ASP A 297     5678  13548  12925   2130  -1053  -1013       C  
ATOM   2810  CG  ASP A 297      62.819  15.986  16.826  1.00 95.17           C  
ANISOU 2810  CG  ASP A 297     7019  14996  14144   2179  -1003  -1134       C  
ATOM   2811  OD1 ASP A 297      62.004  16.830  17.256  1.00 97.62           O  
ANISOU 2811  OD1 ASP A 297     7280  15342  14468   2188   -930  -1148       O  
ATOM   2812  OD2 ASP A 297      63.998  15.910  17.235  1.00 97.86           O  
ANISOU 2812  OD2 ASP A 297     7412  15396  14376   2210  -1034  -1219       O  
ATOM   2813  N   LEU A 298      60.352  12.371  15.185  1.00 74.43           N  
ANISOU 2813  N   LEU A 298     4189  12169  11922   2097  -1081   -682       N  
ATOM   2814  CA  LEU A 298      59.924  11.366  14.217  1.00 74.76           C  
ANISOU 2814  CA  LEU A 298     4210  12136  12057   2050  -1122   -589       C  
ATOM   2815  C   LEU A 298      58.407  11.326  14.083  1.00 75.52           C  
ANISOU 2815  C   LEU A 298     4207  12226  12259   2031  -1074   -495       C  
ATOM   2816  O   LEU A 298      57.885  11.094  12.987  1.00 80.09           O  
ANISOU 2816  O   LEU A 298     4798  12751  12884   1975  -1099   -464       O  
ATOM   2817  CB  LEU A 298      60.450   9.985  14.615  1.00 84.20           C  
ANISOU 2817  CB  LEU A 298     5362  13346  13285   2082  -1159   -522       C  
ATOM   2818  CG  LEU A 298      61.963   9.758  14.616  1.00108.33           C  
ANISOU 2818  CG  LEU A 298     8512  16402  16247   2098  -1217   -595       C  
ATOM   2819  CD1 LEU A 298      62.296   8.341  15.063  1.00116.53           C  
ANISOU 2819  CD1 LEU A 298     9482  17455  17340   2138  -1241   -502       C  
ATOM   2820  CD2 LEU A 298      62.560  10.045  13.249  1.00123.51           C  
ANISOU 2820  CD2 LEU A 298    10560  18237  18130   2031  -1272   -668       C  
ATOM   2821  N   ALA A 299      57.686  11.553  15.180  1.00 78.35           N  
ANISOU 2821  N   ALA A 299     4469  12650  12650   2076  -1005   -458       N  
ATOM   2822  CA  ALA A 299      56.240  11.382  15.195  1.00 74.13           C  
ANISOU 2822  CA  ALA A 299     3826  12117  12223   2065   -954   -358       C  
ATOM   2823  C   ALA A 299      55.468  12.671  14.946  1.00 73.80           C  
ANISOU 2823  C   ALA A 299     3797  12069  12172   2042   -904   -393       C  
ATOM   2824  O   ALA A 299      54.255  12.608  14.721  1.00 85.20           O  
ANISOU 2824  O   ALA A 299     5166  13510  13697   2023   -869   -316       O  
ATOM   2825  CB  ALA A 299      55.796  10.775  16.530  1.00 75.56           C  
ANISOU 2825  CB  ALA A 299     3880  12365  12465   2130   -900   -282       C  
ATOM   2826  N   LEU A 300      56.125  13.831  14.983  1.00 73.07           N  
ANISOU 2826  N   LEU A 300     3795  11983  11986   2046   -896   -507       N  
ATOM   2827  CA  LEU A 300      55.413  15.084  14.733  1.00 72.81           C  
ANISOU 2827  CA  LEU A 300     3771  11940  11953   2029   -841   -536       C  
ATOM   2828  C   LEU A 300      54.810  15.171  13.333  1.00 81.59           C  
ANISOU 2828  C   LEU A 300     4911  12983  13105   1969   -869   -497       C  
ATOM   2829  O   LEU A 300      53.624  15.532  13.222  1.00 97.35           O  
ANISOU 2829  O   LEU A 300     6842  14984  15162   1958   -820   -438       O  
ATOM   2830  CB  LEU A 300      56.341  16.270  15.017  1.00 86.62           C  
ANISOU 2830  CB  LEU A 300     5610  13711  13592   2047   -824   -674       C  
ATOM   2831  CG  LEU A 300      56.327  16.793  16.454  1.00 89.43           C  
ANISOU 2831  CG  LEU A 300     5912  14165  13904   2106   -753   -724       C  
ATOM   2832  CD1 LEU A 300      57.422  17.827  16.661  1.00 89.23           C  
ANISOU 2832  CD1 LEU A 300     5980  14171  13753   2121   -747   -875       C  
ATOM   2833  CD2 LEU A 300      54.963  17.380  16.787  1.00 73.76           C  
ANISOU 2833  CD2 LEU A 300     3838  12194  11994   2108   -668   -670       C  
ATOM   2834  N   PRO A 301      55.534  14.873  12.241  1.00 71.22           N  
ANISOU 2834  N   PRO A 301     3689  11614  11757   1929   -942   -530       N  
ATOM   2835  CA  PRO A 301      54.913  15.021  10.910  1.00 90.90           C  
ANISOU 2835  CA  PRO A 301     6204  14057  14276   1876   -964   -502       C  
ATOM   2836  C   PRO A 301      53.675  14.162  10.713  1.00 85.99           C  
ANISOU 2836  C   PRO A 301     5475  13453  13743   1858   -958   -394       C  
ATOM   2837  O   PRO A 301      52.706  14.612  10.087  1.00 76.93           O  
ANISOU 2837  O   PRO A 301     4302  12302  12626   1833   -937   -360       O  
ATOM   2838  CB  PRO A 301      56.043  14.617   9.952  1.00 78.80           C  
ANISOU 2838  CB  PRO A 301     4782  12471  12689   1844  -1045   -561       C  
ATOM   2839  CG  PRO A 301      57.291  14.851  10.719  1.00 69.44           C  
ANISOU 2839  CG  PRO A 301     3656  11300  11428   1881  -1051   -646       C  
ATOM   2840  CD  PRO A 301      56.953  14.489  12.130  1.00 70.58           C  
ANISOU 2840  CD  PRO A 301     3699  11514  11603   1932  -1005   -602       C  
ATOM   2841  N   PHE A 302      53.681  12.931  11.231  1.00 81.54           N  
ANISOU 2841  N   PHE A 302     4845  12914  13222   1872   -974   -340       N  
ATOM   2842  CA  PHE A 302      52.502  12.079  11.121  1.00 79.03           C  
ANISOU 2842  CA  PHE A 302     4416  12625  12987   1859   -961   -248       C  
ATOM   2843  C   PHE A 302      51.311  12.694  11.846  1.00 74.00           C  
ANISOU 2843  C   PHE A 302     3684  12035  12396   1884   -876   -191       C  
ATOM   2844  O   PHE A 302      50.168  12.579  11.388  1.00 74.43           O  
ANISOU 2844  O   PHE A 302     3675  12109  12496   1859   -859   -140       O  
ATOM   2845  CB  PHE A 302      52.805  10.687  11.674  1.00 80.54           C  
ANISOU 2845  CB  PHE A 302     4546  12839  13216   1882   -980   -201       C  
ATOM   2846  CG  PHE A 302      53.923   9.982  10.961  1.00 73.24           C  
ANISOU 2846  CG  PHE A 302     3706  11867  12255   1856  -1061   -252       C  
ATOM   2847  CD1 PHE A 302      53.676   9.252   9.810  1.00 73.09           C  
ANISOU 2847  CD1 PHE A 302     3694  11816  12259   1801  -1112   -260       C  
ATOM   2848  CD2 PHE A 302      55.219  10.046  11.443  1.00 72.79           C  
ANISOU 2848  CD2 PHE A 302     3720  11799  12140   1887  -1084   -302       C  
ATOM   2849  CE1 PHE A 302      54.701   8.600   9.153  1.00 72.48           C  
ANISOU 2849  CE1 PHE A 302     3693  11689  12155   1776  -1182   -311       C  
ATOM   2850  CE2 PHE A 302      56.249   9.397  10.789  1.00 87.67           C  
ANISOU 2850  CE2 PHE A 302     5681  13638  13991   1864  -1156   -346       C  
ATOM   2851  CZ  PHE A 302      55.990   8.674   9.642  1.00 90.69           C  
ANISOU 2851  CZ  PHE A 302     6071  13983  14404   1808  -1202   -348       C  
ATOM   2852  N   ALA A 303      51.560  13.355  12.979  1.00 74.25           N  
ANISOU 2852  N   ALA A 303     3705  12091  12416   1932   -821   -211       N  
ATOM   2853  CA  ALA A 303      50.481  14.026  13.694  1.00 75.00           C  
ANISOU 2853  CA  ALA A 303     3715  12224  12556   1955   -734   -169       C  
ATOM   2854  C   ALA A 303      49.975  15.234  12.917  1.00 84.62           C  
ANISOU 2854  C   ALA A 303     4978  13419  13755   1927   -713   -195       C  
ATOM   2855  O   ALA A 303      48.770  15.522  12.916  1.00 86.50           O  
ANISOU 2855  O   ALA A 303     5141  13682  14042   1924   -662   -133       O  
ATOM   2856  CB  ALA A 303      50.953  14.436  15.087  1.00 75.46           C  
ANISOU 2856  CB  ALA A 303     3756  12318  12596   2013   -681   -209       C  
ATOM   2857  N   ILE A 304      50.881  15.956  12.251  1.00 78.15           N  
ANISOU 2857  N   ILE A 304     4276  12553  12862   1911   -749   -283       N  
ATOM   2858  CA  ILE A 304      50.460  17.057  11.387  1.00 84.12           C  
ANISOU 2858  CA  ILE A 304     5074  13283  13605   1889   -731   -298       C  
ATOM   2859  C   ILE A 304      49.546  16.537  10.283  1.00 92.11           C  
ANISOU 2859  C   ILE A 304     6051  14293  14655   1846   -765   -229       C  
ATOM   2860  O   ILE A 304      48.488  17.114  10.000  1.00104.83           O  
ANISOU 2860  O   ILE A 304     7614  15920  16295   1841   -722   -182       O  
ATOM   2861  CB  ILE A 304      51.686  17.788  10.810  1.00 71.56           C  
ANISOU 2861  CB  ILE A 304     3614  11644  11932   1881   -765   -402       C  
ATOM   2862  CG1 ILE A 304      52.607  18.255  11.935  1.00 71.56           C  
ANISOU 2862  CG1 ILE A 304     3644  11666  11880   1924   -734   -489       C  
ATOM   2863  CG2 ILE A 304      51.252  18.979   9.981  1.00 71.08           C  
ANISOU 2863  CG2 ILE A 304     3586  11557  11865   1868   -735   -408       C  
ATOM   2864  CD1 ILE A 304      53.833  18.991  11.448  1.00 73.86           C  
ANISOU 2864  CD1 ILE A 304     4060  11920  12085   1919   -762   -601       C  
ATOM   2865  N   LEU A 305      49.936  15.425   9.652  1.00 90.01           N  
ANISOU 2865  N   LEU A 305     5805  14011  14384   1815   -841   -230       N  
ATOM   2866  CA  LEU A 305      49.068  14.792   8.667  1.00 83.96           C  
ANISOU 2866  CA  LEU A 305     4995  13255  13649   1772   -875   -185       C  
ATOM   2867  C   LEU A 305      47.793  14.239   9.289  1.00 74.15           C  
ANISOU 2867  C   LEU A 305     3618  12078  12476   1784   -827   -104       C  
ATOM   2868  O   LEU A 305      46.819  14.004   8.567  1.00 74.51           O  
ANISOU 2868  O   LEU A 305     3615  12149  12548   1753   -836    -74       O  
ATOM   2869  CB  LEU A 305      49.815  13.674   7.939  1.00 82.80           C  
ANISOU 2869  CB  LEU A 305     4896  13077  13487   1737   -961   -220       C  
ATOM   2870  CG  LEU A 305      50.692  14.111   6.766  1.00 86.92           C  
ANISOU 2870  CG  LEU A 305     5540  13538  13947   1705  -1019   -289       C  
ATOM   2871  CD1 LEU A 305      51.447  12.922   6.200  1.00 91.26           C  
ANISOU 2871  CD1 LEU A 305     6130  14057  14489   1672  -1097   -325       C  
ATOM   2872  CD2 LEU A 305      49.845  14.774   5.690  1.00 71.23           C  
ANISOU 2872  CD2 LEU A 305     3549  11554  11963   1678  -1015   -269       C  
ATOM   2873  N   LEU A 306      47.778  14.020  10.605  1.00 74.85           N  
ANISOU 2873  N   LEU A 306     3645  12201  12593   1828   -775    -74       N  
ATOM   2874  CA  LEU A 306      46.552  13.589  11.267  1.00 76.06           C  
ANISOU 2874  CA  LEU A 306     3668  12424  12807   1846   -717      3       C  
ATOM   2875  C   LEU A 306      45.579  14.751  11.429  1.00 76.27           C  
ANISOU 2875  C   LEU A 306     3660  12474  12847   1858   -644     33       C  
ATOM   2876  O   LEU A 306      44.370  14.586  11.226  1.00 76.97           O  
ANISOU 2876  O   LEU A 306     3665  12615  12964   1847   -620     81       O  
ATOM   2877  CB  LEU A 306      46.880  12.962  12.622  1.00 76.80           C  
ANISOU 2877  CB  LEU A 306     3702  12550  12931   1896   -681     34       C  
ATOM   2878  CG  LEU A 306      45.827  12.026  13.215  1.00 78.13           C  
ANISOU 2878  CG  LEU A 306     3733  12797  13155   1915   -637    108       C  
ATOM   2879  CD1 LEU A 306      45.501  10.915  12.234  1.00 78.32           C  
ANISOU 2879  CD1 LEU A 306     3738  12828  13190   1869   -700     88       C  
ATOM   2880  CD2 LEU A 306      46.312  11.449  14.533  1.00 78.84           C  
ANISOU 2880  CD2 LEU A 306     3778  12909  13269   1971   -599    143       C  
ATOM   2881  N   GLY A 307      46.087  15.932  11.788  1.00 75.74           N  
ANISOU 2881  N   GLY A 307     3651  12373  12754   1880   -607     -6       N  
ATOM   2882  CA  GLY A 307      45.239  17.114  11.786  1.00 75.86           C  
ANISOU 2882  CA  GLY A 307     3643  12400  12781   1890   -538     15       C  
ATOM   2883  C   GLY A 307      44.745  17.464  10.395  1.00 75.41           C  
ANISOU 2883  C   GLY A 307     3615  12333  12706   1852   -573     24       C  
ATOM   2884  O   GLY A 307      43.575  17.816  10.207  1.00 75.95           O  
ANISOU 2884  O   GLY A 307     3615  12444  12798   1851   -532     79       O  
ATOM   2885  N   PHE A 308      45.629  17.370   9.398  1.00 74.48           N  
ANISOU 2885  N   PHE A 308     3594  12163  12542   1822   -649    -30       N  
ATOM   2886  CA  PHE A 308      45.193  17.544   8.017  1.00 77.80           C  
ANISOU 2886  CA  PHE A 308     4035  12578  12949   1786   -690    -19       C  
ATOM   2887  C   PHE A 308      44.166  16.491   7.626  1.00 74.97           C  
ANISOU 2887  C   PHE A 308     3585  12275  12625   1756   -717     26       C  
ATOM   2888  O   PHE A 308      43.285  16.757   6.800  1.00 80.04           O  
ANISOU 2888  O   PHE A 308     4195  12944  13272   1737   -720     56       O  
ATOM   2889  CB  PHE A 308      46.396  17.497   7.075  1.00 83.93           C  
ANISOU 2889  CB  PHE A 308     4928  13290  13670   1760   -766    -87       C  
ATOM   2890  CG  PHE A 308      47.356  18.638   7.258  1.00 72.24           C  
ANISOU 2890  CG  PHE A 308     3540  11761  12146   1785   -739   -147       C  
ATOM   2891  CD1 PHE A 308      46.938  19.828   7.830  1.00 74.18           C  
ANISOU 2891  CD1 PHE A 308     3763  12017  12406   1821   -652   -134       C  
ATOM   2892  CD2 PHE A 308      48.676  18.521   6.858  1.00 75.00           C  
ANISOU 2892  CD2 PHE A 308     3996  12058  12441   1774   -797   -224       C  
ATOM   2893  CE1 PHE A 308      47.819  20.881   7.999  1.00 71.77           C  
ANISOU 2893  CE1 PHE A 308     3538  11671  12061   1844   -622   -204       C  
ATOM   2894  CE2 PHE A 308      49.561  19.570   7.022  1.00 78.15           C  
ANISOU 2894  CE2 PHE A 308     4477  12421  12795   1797   -770   -292       C  
ATOM   2895  CZ  PHE A 308      49.131  20.751   7.595  1.00 70.86           C  
ANISOU 2895  CZ  PHE A 308     3528  11509  11887   1832   -682   -286       C  
ATOM   2896  N   THR A 309      44.258  15.295   8.212  1.00 92.21           N  
ANISOU 2896  N   THR A 309     5723  14479  14835   1753   -736     25       N  
ATOM   2897  CA  THR A 309      43.233  14.282   7.988  1.00 87.54           C  
ANISOU 2897  CA  THR A 309     5033  13943  14284   1727   -750     48       C  
ATOM   2898  C   THR A 309      41.910  14.699   8.616  1.00 87.57           C  
ANISOU 2898  C   THR A 309     4933  14022  14318   1753   -669    106       C  
ATOM   2899  O   THR A 309      40.839  14.410   8.068  1.00 85.15           O  
ANISOU 2899  O   THR A 309     4557  13762  14033   1727   -675    117       O  
ATOM   2900  CB  THR A 309      43.696  12.932   8.539  1.00 87.87           C  
ANISOU 2900  CB  THR A 309     5046  13988  14353   1727   -777     30       C  
ATOM   2901  OG1 THR A 309      44.976  12.604   7.986  1.00 88.64           O  
ANISOU 2901  OG1 THR A 309     5245  14016  14417   1707   -848    -25       O  
ATOM   2902  CG2 THR A 309      42.704  11.836   8.178  1.00 88.93           C  
ANISOU 2902  CG2 THR A 309     5085  14163  14543   1692   -795     25       C  
ATOM   2903  N   ASN A 310      41.960  15.383   9.764  1.00 91.01           N  
ANISOU 2903  N   ASN A 310     5363  14463  14754   1800   -592    131       N  
ATOM   2904  CA  ASN A 310      40.743  15.978  10.311  1.00 94.51           C  
ANISOU 2904  CA  ASN A 310     5746  14956  15209   1817   -510    169       C  
ATOM   2905  C   ASN A 310      40.150  16.984   9.335  1.00 78.04           C  
ANISOU 2905  C   ASN A 310     3685  12864  13102   1802   -506    181       C  
ATOM   2906  O   ASN A 310      38.936  16.990   9.098  1.00 78.76           O  
ANISOU 2906  O   ASN A 310     3712  13012  13200   1790   -485    203       O  
ATOM   2907  CB  ASN A 310      41.031  16.650  11.654  1.00 92.26           C  
ANISOU 2907  CB  ASN A 310     5466  14660  14931   1865   -427    182       C  
ATOM   2908  CG  ASN A 310      39.766  16.944  12.448  1.00 95.77           C  
ANISOU 2908  CG  ASN A 310     5832  15169  15390   1886   -338    221       C  
ATOM   2909  OD1 ASN A 310      38.679  17.081  11.887  1.00 79.95           O  
ANISOU 2909  OD1 ASN A 310     3787  13211  13378   1868   -333    233       O  
ATOM   2910  ND2 ASN A 310      39.907  17.041  13.765  1.00 99.62           N  
ANISOU 2910  ND2 ASN A 310     6292  15661  15897   1924   -269    236       N  
ATOM   2911  N   SER A 311      40.993  17.842   8.755  1.00 95.49           N  
ANISOU 2911  N   SER A 311     5983  15013  15286   1804   -525    163       N  
ATOM   2912  CA  SER A 311      40.508  18.767   7.737  1.00 95.63           C  
ANISOU 2912  CA  SER A 311     6026  15026  15283   1795   -522    181       C  
ATOM   2913  C   SER A 311      40.001  18.043   6.496  1.00 91.26           C  
ANISOU 2913  C   SER A 311     5447  14501  14728   1749   -596    183       C  
ATOM   2914  O   SER A 311      39.226  18.621   5.726  1.00 78.59           O  
ANISOU 2914  O   SER A 311     3831  12918  13113   1741   -588    213       O  
ATOM   2915  CB  SER A 311      41.611  19.754   7.353  1.00103.89           C  
ANISOU 2915  CB  SER A 311     7169  16002  16302   1810   -526    151       C  
ATOM   2916  OG  SER A 311      42.025  20.513   8.475  1.00115.15           O  
ANISOU 2916  OG  SER A 311     8608  17406  17737   1851   -452    134       O  
ATOM   2917  N   CYS A 312      40.418  16.793   6.286  1.00 94.92           N  
ANISOU 2917  N   CYS A 312     5895  14964  15206   1719   -666    151       N  
ATOM   2918  CA  CYS A 312      39.961  16.027   5.131  1.00 92.74           C  
ANISOU 2918  CA  CYS A 312     5582  14712  14941   1670   -736    140       C  
ATOM   2919  C   CYS A 312      38.583  15.418   5.375  1.00 94.11           C  
ANISOU 2919  C   CYS A 312     5642  14960  15156   1656   -712    153       C  
ATOM   2920  O   CYS A 312      37.640  15.661   4.615  1.00 78.89           O  
ANISOU 2920  O   CYS A 312     3675  13069  13230   1637   -716    172       O  
ATOM   2921  CB  CYS A 312      40.982  14.936   4.793  1.00 82.64           C  
ANISOU 2921  CB  CYS A 312     4356  13382  13663   1635   -815     78       C  
ATOM   2922  SG  CYS A 312      40.423  13.736   3.562  1.00 86.91           S  
ANISOU 2922  SG  CYS A 312     4848  13937  14238   1564   -897     39       S  
ATOM   2923  N   VAL A 313      38.452  14.619   6.439  1.00 93.16           N  
ANISOU 2923  N   VAL A 313     5461  14864  15073   1668   -685    141       N  
ATOM   2924  CA  VAL A 313      37.194  13.932   6.728  1.00 87.13           C  
ANISOU 2924  CA  VAL A 313     4579  14166  14360   1654   -662    135       C  
ATOM   2925  C   VAL A 313      36.149  14.848   7.345  1.00 89.26           C  
ANISOU 2925  C   VAL A 313     4815  14487  14615   1686   -577    170       C  
ATOM   2926  O   VAL A 313      34.974  14.467   7.426  1.00 81.94           O  
ANISOU 2926  O   VAL A 313     3790  13617  13728   1673   -557    160       O  
ATOM   2927  CB  VAL A 313      37.455  12.729   7.657  1.00 85.18           C  
ANISOU 2927  CB  VAL A 313     4277  13923  14166   1660   -658    105       C  
ATOM   2928  CG1 VAL A 313      36.298  11.736   7.610  1.00 88.17           C  
ANISOU 2928  CG1 VAL A 313     4541  14332  14629   1623   -657     71       C  
ATOM   2929  CG2 VAL A 313      38.759  12.042   7.280  1.00 84.18           C  
ANISOU 2929  CG2 VAL A 313     4232  13718  14033   1638   -728     66       C  
ATOM   2930  N   ASN A 314      36.537  16.051   7.766  1.00 96.48           N  
ANISOU 2930  N   ASN A 314     5800  15376  15481   1726   -525    203       N  
ATOM   2931  CA  ASN A 314      35.597  16.938   8.449  1.00 91.48           C  
ANISOU 2931  CA  ASN A 314     5133  14790  14833   1760   -437    231       C  
ATOM   2932  C   ASN A 314      34.406  17.331   7.581  1.00 94.68           C  
ANISOU 2932  C   ASN A 314     5494  15246  15232   1742   -438    246       C  
ATOM   2933  O   ASN A 314      33.269  17.293   8.085  1.00 96.68           O  
ANISOU 2933  O   ASN A 314     5665  15567  15501   1750   -391    238       O  
ATOM   2934  CB  ASN A 314      36.347  18.166   8.977  1.00 83.76           C  
ANISOU 2934  CB  ASN A 314     4241  13761  13824   1801   -381    257       C  
ATOM   2935  CG  ASN A 314      35.503  19.004   9.911  1.00 80.75           C  
ANISOU 2935  CG  ASN A 314     3821  13426  13433   1839   -281    280       C  
ATOM   2936  OD1 ASN A 314      34.944  20.024   9.513  1.00 82.50           O  
ANISOU 2936  OD1 ASN A 314     4054  13660  13631   1850   -246    305       O  
ATOM   2937  ND2 ASN A 314      35.403  18.575  11.163  1.00 81.36           N  
ANISOU 2937  ND2 ASN A 314     3851  13536  13525   1862   -232    271       N  
ATOM   2938  N   PRO A 315      34.567  17.718   6.308  1.00101.19           N  
ANISOU 2938  N   PRO A 315     6366  16046  16036   1720   -488    264       N  
ATOM   2939  CA  PRO A 315      33.372  17.961   5.481  1.00 97.69           C  
ANISOU 2939  CA  PRO A 315     5867  15662  15589   1704   -493    283       C  
ATOM   2940  C   PRO A 315      32.520  16.721   5.274  1.00 97.02           C  
ANISOU 2940  C   PRO A 315     5672  15628  15563   1660   -532    244       C  
ATOM   2941  O   PRO A 315      31.294  16.836   5.154  1.00 83.38           O  
ANISOU 2941  O   PRO A 315     3867  13967  13848   1655   -508    247       O  
ATOM   2942  CB  PRO A 315      33.958  18.471   4.157  1.00 90.02           C  
ANISOU 2942  CB  PRO A 315     4971  14645  14587   1690   -546    311       C  
ATOM   2943  CG  PRO A 315      35.281  19.030   4.525  1.00 86.79           C  
ANISOU 2943  CG  PRO A 315     4664  14154  14157   1716   -534    309       C  
ATOM   2944  CD  PRO A 315      35.796  18.132   5.606  1.00 97.48           C  
ANISOU 2944  CD  PRO A 315     6000  15497  15540   1717   -532    269       C  
ATOM   2945  N   PHE A 316      33.133  15.535   5.225  1.00107.23           N  
ANISOU 2945  N   PHE A 316     6950  16890  16903   1627   -589    203       N  
ATOM   2946  CA  PHE A 316      32.356  14.307   5.098  1.00114.00           C  
ANISOU 2946  CA  PHE A 316     7691  17782  17843   1582   -617    160       C  
ATOM   2947  C   PHE A 316      31.464  14.093   6.315  1.00109.21           C  
ANISOU 2947  C   PHE A 316     6993  17218  17283   1603   -544    140       C  
ATOM   2948  O   PHE A 316      30.340  13.594   6.192  1.00113.25           O  
ANISOU 2948  O   PHE A 316     7396  17772  17862   1574   -538    118       O  
ATOM   2949  CB  PHE A 316      33.293  13.114   4.897  1.00123.75           C  
ANISOU 2949  CB  PHE A 316     8929  18966  19123   1548   -684    117       C  
ATOM   2950  CG  PHE A 316      32.603  11.779   4.954  1.00132.09           C  
ANISOU 2950  CG  PHE A 316     9881  20019  20289   1497   -700     60       C  
ATOM   2951  CD1 PHE A 316      31.906  11.297   3.859  1.00137.83           C  
ANISOU 2951  CD1 PHE A 316    10552  20757  21061   1438   -750     38       C  
ATOM   2952  CD2 PHE A 316      32.662  11.003   6.100  1.00133.88           C  
ANISOU 2952  CD2 PHE A 316    10070  20217  20584   1507   -660     29       C  
ATOM   2953  CE1 PHE A 316      31.272  10.068   3.909  1.00141.70           C  
ANISOU 2953  CE1 PHE A 316    10951  21217  21672   1382   -758    -20       C  
ATOM   2954  CE2 PHE A 316      32.030   9.773   6.156  1.00136.39           C  
ANISOU 2954  CE2 PHE A 316    10297  20498  21028   1454   -665    -22       C  
ATOM   2955  CZ  PHE A 316      31.335   9.305   5.059  1.00138.45           C  
ANISOU 2955  CZ  PHE A 316    10504  20759  21343   1389   -712    -50       C  
ATOM   2956  N   LEU A 317      31.948  14.472   7.499  1.00 99.46           N  
ANISOU 2956  N   LEU A 317     5798  15972  16020   1652   -484    146       N  
ATOM   2957  CA  LEU A 317      31.160  14.312   8.715  1.00 97.02           C  
ANISOU 2957  CA  LEU A 317     5405  15702  15755   1676   -409    123       C  
ATOM   2958  C   LEU A 317      30.110  15.409   8.854  1.00 95.28           C  
ANISOU 2958  C   LEU A 317     5167  15538  15498   1700   -348    138       C  
ATOM   2959  O   LEU A 317      28.979  15.139   9.271  1.00 95.78           O  
ANISOU 2959  O   LEU A 317     5126  15641  15626   1692   -310    108       O  
ATOM   2960  CB  LEU A 317      32.081  14.301   9.936  1.00 88.47           C  
ANISOU 2960  CB  LEU A 317     4367  14597  14651   1721   -368    123       C  
ATOM   2961  CG  LEU A 317      31.411  14.285  11.311  1.00 85.74           C  
ANISOU 2961  CG  LEU A 317     3946  14292  14338   1756   -282    100       C  
ATOM   2962  CD1 LEU A 317      30.603  13.011  11.505  1.00 86.95           C  
ANISOU 2962  CD1 LEU A 317     3964  14446  14628   1722   -282     60       C  
ATOM   2963  CD2 LEU A 317      32.446  14.444  12.412  1.00 85.31           C  
ANISOU 2963  CD2 LEU A 317     3952  14226  14238   1806   -244    111       C  
ATOM   2964  N   TYR A 318      30.463  16.647   8.504  1.00 93.16           N  
ANISOU 2964  N   TYR A 318     4993  15266  15139   1728   -335    182       N  
ATOM   2965  CA  TYR A 318      29.555  17.769   8.719  1.00 95.90           C  
ANISOU 2965  CA  TYR A 318     5327  15665  15446   1759   -269    191       C  
ATOM   2966  C   TYR A 318      28.511  17.876   7.612  1.00104.68           C  
ANISOU 2966  C   TYR A 318     6387  16823  16564   1731   -300    199       C  
ATOM   2967  O   TYR A 318      27.312  17.989   7.891  1.00108.93           O  
ANISOU 2967  O   TYR A 318     6840  17417  17132   1732   -261    170       O  
ATOM   2968  CB  TYR A 318      30.352  19.068   8.836  1.00 84.10           C  
ANISOU 2968  CB  TYR A 318     3944  14140  13870   1803   -231    239       C  
ATOM   2969  CG  TYR A 318      30.723  19.429  10.256  1.00 85.95           C  
ANISOU 2969  CG  TYR A 318     4194  14371  14093   1846   -154    228       C  
ATOM   2970  CD1 TYR A 318      29.963  20.336  10.982  1.00 84.59           C  
ANISOU 2970  CD1 TYR A 318     3994  14249  13895   1882    -71    212       C  
ATOM   2971  CD2 TYR A 318      31.829  18.858  10.873  1.00 86.57           C  
ANISOU 2971  CD2 TYR A 318     4309  14399  14185   1851   -165    230       C  
ATOM   2972  CE1 TYR A 318      30.296  20.670  12.282  1.00 92.06           C  
ANISOU 2972  CE1 TYR A 318     4949  15198  14830   1918      3    203       C  
ATOM   2973  CE2 TYR A 318      32.170  19.185  12.173  1.00 87.33           C  
ANISOU 2973  CE2 TYR A 318     4414  14498  14269   1891    -92    230       C  
ATOM   2974  CZ  TYR A 318      31.400  20.091  12.872  1.00 91.49           C  
ANISOU 2974  CZ  TYR A 318     4914  15079  14771   1923     -7    219       C  
ATOM   2975  OH  TYR A 318      31.734  20.419  14.166  1.00 84.96           O  
ANISOU 2975  OH  TYR A 318     4090  14258  13932   1961     69    221       O  
ATOM   2976  N   CYS A 319      28.945  17.847   6.350  1.00106.30           N  
ANISOU 2976  N   CYS A 319     6638  17004  16746   1705   -370    235       N  
ATOM   2977  CA  CYS A 319      28.003  18.003   5.247  1.00 99.03           C  
ANISOU 2977  CA  CYS A 319     5671  16136  15821   1682   -399    254       C  
ATOM   2978  C   CYS A 319      27.182  16.738   5.024  1.00110.59           C  
ANISOU 2978  C   CYS A 319     7012  17626  17381   1626   -437    211       C  
ATOM   2979  O   CYS A 319      25.968  16.814   4.806  1.00119.51           O  
ANISOU 2979  O   CYS A 319     8057  18819  18534   1616   -422    203       O  
ATOM   2980  CB  CYS A 319      28.749  18.391   3.970  1.00 84.76           C  
ANISOU 2980  CB  CYS A 319     3948  14290  13966   1672   -457    310       C  
ATOM   2981  SG  CYS A 319      27.681  18.881   2.597  1.00 85.40           S  
ANISOU 2981  SG  CYS A 319     3986  14443  14019   1661   -481    360       S  
ATOM   2982  N   PHE A 320      27.820  15.572   5.076  1.00122.59           N  
ANISOU 2982  N   PHE A 320     8517  19098  18966   1589   -484    180       N  
ATOM   2983  CA  PHE A 320      27.115  14.305   4.904  1.00130.87           C  
ANISOU 2983  CA  PHE A 320     9441  20158  20128   1533   -514    137       C  
ATOM   2984  C   PHE A 320      27.179  13.460   6.173  1.00129.08           C  
ANISOU 2984  C   PHE A 320     9154  19900  19992   1535   -472     91       C  
ATOM   2985  O   PHE A 320      26.280  12.665   6.447  1.00124.95           O  
ANISOU 2985  O   PHE A 320     8509  19385  19582   1502   -454     59       O  
ATOM   2986  CB  PHE A 320      27.692  13.523   3.722  1.00132.31           C  
ANISOU 2986  CB  PHE A 320     9631  20310  20331   1479   -606    132       C  
ATOM   2987  CG  PHE A 320      27.431  14.160   2.387  1.00132.99           C  
ANISOU 2987  CG  PHE A 320     9744  20430  20355   1468   -649    179       C  
ATOM   2988  CD1 PHE A 320      26.259  13.897   1.696  1.00129.22           C  
ANISOU 2988  CD1 PHE A 320     9163  20014  19920   1431   -666    178       C  
ATOM   2989  CD2 PHE A 320      28.357  15.022   1.823  1.00134.53           C  
ANISOU 2989  CD2 PHE A 320    10063  20593  20459   1495   -669    228       C  
ATOM   2990  CE1 PHE A 320      26.015  14.482   0.468  1.00120.84           C  
ANISOU 2990  CE1 PHE A 320     8122  18989  18802   1426   -704    231       C  
ATOM   2991  CE2 PHE A 320      28.118  15.610   0.594  1.00136.08           C  
ANISOU 2991  CE2 PHE A 320    10279  20814  20610   1489   -703    280       C  
ATOM   2992  CZ  PHE A 320      26.945  15.339  -0.084  1.00129.35           C  
ANISOU 2992  CZ  PHE A 320     9325  20031  19793   1456   -721    286       C  
TER    2993      PHE A 320                                                      
ATOM   2994  N   ASP H   1      72.394  -1.462  -1.535  1.00 97.16           N  
ANISOU 2994  N   ASP H   1     8958  13857  14102   -982   -221   -595       N  
ATOM   2995  CA  ASP H   1      73.419  -1.348  -2.566  1.00 69.20           C  
ANISOU 2995  CA  ASP H   1     5557  10284  10451   -991   -309   -686       C  
ATOM   2996  C   ASP H   1      73.385   0.029  -3.222  1.00 59.24           C  
ANISOU 2996  C   ASP H   1     4306   9114   9087   -853   -479   -755       C  
ATOM   2997  O   ASP H   1      72.521   0.314  -4.051  1.00 59.61           O  
ANISOU 2997  O   ASP H   1     4261   9231   9156   -826   -676   -862       O  
ATOM   2998  CB  ASP H   1      73.241  -2.441  -3.622  1.00 59.90           C  
ANISOU 2998  CB  ASP H   1     4364   9064   9331  -1128   -412   -822       C  
ATOM   2999  CG  ASP H   1      74.291  -2.374  -4.716  1.00 67.12           C  
ANISOU 2999  CG  ASP H   1     5431   9954  10119  -1144   -503   -923       C  
ATOM   3000  OD1 ASP H   1      75.481  -2.610  -4.416  1.00 66.56           O  
ANISOU 3000  OD1 ASP H   1     5505   9805   9979  -1169   -357   -851       O  
ATOM   3001  OD2 ASP H   1      73.927  -2.088  -5.876  1.00 71.18           O  
ANISOU 3001  OD2 ASP H   1     5930  10526  10589  -1126   -725  -1067       O  
ATOM   3002  N   VAL H   2      74.331   0.881  -2.839  1.00 45.36           N  
ANISOU 3002  N   VAL H   2     2669   7356   7211   -757   -407   -684       N  
ATOM   3003  CA  VAL H   2      74.461   2.225  -3.390  1.00 44.64           C  
ANISOU 3003  CA  VAL H   2     2614   7346   7000   -609   -549   -728       C  
ATOM   3004  C   VAL H   2      75.582   2.216  -4.418  1.00 55.98           C  
ANISOU 3004  C   VAL H   2     4201   8776   8293   -621   -628   -804       C  
ATOM   3005  O   VAL H   2      76.701   1.774  -4.125  1.00 66.83           O  
ANISOU 3005  O   VAL H   2     5692  10079   9623   -684   -480   -751       O  
ATOM   3006  CB  VAL H   2      74.733   3.256  -2.281  1.00 46.68           C  
ANISOU 3006  CB  VAL H   2     2908   7611   7219   -486   -419   -605       C  
ATOM   3007  CG1 VAL H   2      74.963   4.633  -2.879  1.00 52.55           C  
ANISOU 3007  CG1 VAL H   2     3710   8427   7832   -326   -558   -641       C  
ATOM   3008  CG2 VAL H   2      73.578   3.286  -1.291  1.00 47.30           C  
ANISOU 3008  CG2 VAL H   2     2839   7702   7429   -471   -348   -534       C  
ATOM   3009  N   GLN H   3      75.287   2.701  -5.622  1.00 44.26           N  
ANISOU 3009  N   GLN H   3     2726   7365   6726   -555   -863   -917       N  
ATOM   3010  CA  GLN H   3      76.241   2.712  -6.725  1.00 43.14           C  
ANISOU 3010  CA  GLN H   3     2736   7231   6424   -553   -975   -997       C  
ATOM   3011  C   GLN H   3      76.403   4.133  -7.243  1.00 49.45           C  
ANISOU 3011  C   GLN H   3     3674   8069   7046   -346  -1104   -956       C  
ATOM   3012  O   GLN H   3      75.432   4.746  -7.704  1.00 52.52           O  
ANISOU 3012  O   GLN H   3     3948   8562   7446   -249  -1297  -1020       O  
ATOM   3013  CB  GLN H   3      75.790   1.779  -7.851  1.00 58.44           C  
ANISOU 3013  CB  GLN H   3     4668   9155   8380   -660  -1141  -1142       C  
ATOM   3014  CG  GLN H   3      75.953   0.301  -7.538  1.00 71.66           C  
ANISOU 3014  CG  GLN H   3     6320  10720  10187   -862   -986  -1153       C  
ATOM   3015  CD  GLN H   3      77.407  -0.133  -7.520  1.00 64.10           C  
ANISOU 3015  CD  GLN H   3     5582   9644   9129   -924   -823  -1088       C  
ATOM   3016  OE1 GLN H   3      78.285   0.572  -8.019  1.00 64.71           O  
ANISOU 3016  OE1 GLN H   3     5904   9677   9005   -813   -844  -1026       O  
ATOM   3017  NE2 GLN H   3      77.667  -1.300  -6.943  1.00 46.58           N  
ANISOU 3017  NE2 GLN H   3     3305   7345   7049  -1090   -642  -1074       N  
ATOM   3018  N   LEU H   4      77.628   4.650  -7.166  1.00 50.41           N  
ANISOU 3018  N   LEU H   4     4035   8102   7015   -278   -996   -846       N  
ATOM   3019  CA  LEU H   4      77.993   5.948  -7.719  1.00 47.64           C  
ANISOU 3019  CA  LEU H   4     3857   7755   6491    -89  -1091   -793       C  
ATOM   3020  C   LEU H   4      79.100   5.726  -8.739  1.00 57.59           C  
ANISOU 3020  C   LEU H   4     5417   8897   7568    -94  -1104   -774       C  
ATOM   3021  O   LEU H   4      80.150   5.168  -8.403  1.00 73.64           O  
ANISOU 3021  O   LEU H   4     7578  10818   9583   -181   -927   -710       O  
ATOM   3022  CB  LEU H   4      78.455   6.907  -6.620  1.00 34.63           C  
ANISOU 3022  CB  LEU H   4     2212   6102   4844     10   -936   -675       C  
ATOM   3023  CG  LEU H   4      77.490   7.147  -5.458  1.00 35.16           C  
ANISOU 3023  CG  LEU H   4     2000   6275   5084     20   -878   -679       C  
ATOM   3024  CD1 LEU H   4      78.191   7.873  -4.324  1.00 33.34           C  
ANISOU 3024  CD1 LEU H   4     1815   6017   4837     86   -694   -567       C  
ATOM   3025  CD2 LEU H   4      76.284   7.936  -5.927  1.00 37.08           C  
ANISOU 3025  CD2 LEU H   4     2096   6635   5356    146  -1083   -744       C  
ATOM   3026  N   VAL H   5      78.867   6.153  -9.977  1.00 36.83           N  
ANISOU 3026  N   VAL H   5     2900   6292   4800      4  -1308   -825       N  
ATOM   3027  CA  VAL H   5      79.800   5.921 -11.075  1.00 36.54           C  
ANISOU 3027  CA  VAL H   5     3150   6153   4579      7  -1335   -820       C  
ATOM   3028  C   VAL H   5      80.184   7.265 -11.680  1.00 45.16           C  
ANISOU 3028  C   VAL H   5     4426   7238   5496    214  -1412   -741       C  
ATOM   3029  O   VAL H   5      79.327   7.977 -12.217  1.00 42.21           O  
ANISOU 3029  O   VAL H   5     3989   6965   5083    339  -1605   -780       O  
ATOM   3030  CB  VAL H   5      79.204   4.994 -12.146  1.00 38.60           C  
ANISOU 3030  CB  VAL H   5     3404   6443   4820    -82  -1510   -967       C  
ATOM   3031  CG1 VAL H   5      80.234   4.706 -13.226  1.00 48.39           C  
ANISOU 3031  CG1 VAL H   5     4955   7568   5862    -81  -1509   -959       C  
ATOM   3032  CG2 VAL H   5      78.710   3.704 -11.515  1.00 39.06           C  
ANISOU 3032  CG2 VAL H   5     3251   6506   5086   -285  -1434  -1049       C  
ATOM   3033  N   GLU H   6      81.467   7.605 -11.603  1.00 46.56           N  
ANISOU 3033  N   GLU H   6     4824   7291   5575    251  -1260   -627       N  
ATOM   3034  CA  GLU H   6      81.960   8.817 -12.236  1.00 34.20           C  
ANISOU 3034  CA  GLU H   6     3456   5692   3848    439  -1309   -544       C  
ATOM   3035  C   GLU H   6      82.255   8.569 -13.712  1.00 44.10           C  
ANISOU 3035  C   GLU H   6     4940   6904   4912    470  -1431   -581       C  
ATOM   3036  O   GLU H   6      82.392   7.429 -14.166  1.00 41.32           O  
ANISOU 3036  O   GLU H   6     4638   6516   4546    333  -1432   -658       O  
ATOM   3037  CB  GLU H   6      83.223   9.325 -11.536  1.00 31.89           C  
ANISOU 3037  CB  GLU H   6     3295   5277   3544    467  -1095   -408       C  
ATOM   3038  CG  GLU H   6      82.996   9.895 -10.144  1.00 30.92           C  
ANISOU 3038  CG  GLU H   6     2985   5198   3564    487   -989   -361       C  
ATOM   3039  CD  GLU H   6      82.943   8.828  -9.068  1.00 36.75           C  
ANISOU 3039  CD  GLU H   6     3560   5945   4459    307   -847   -385       C  
ATOM   3040  OE1 GLU H   6      82.942   7.626  -9.410  1.00 37.99           O  
ANISOU 3040  OE1 GLU H   6     3720   6078   4636    163   -844   -447       O  
ATOM   3041  OE2 GLU H   6      82.911   9.193  -7.874  1.00 37.48           O  
ANISOU 3041  OE2 GLU H   6     3524   6064   4651    314   -733   -340       O  
ATOM   3042  N   SER H   7      82.356   9.663 -14.463  1.00 60.82           N  
ANISOU 3042  N   SER H   7     7204   9024   6880    656  -1528   -524       N  
ATOM   3043  CA  SER H   7      82.674   9.608 -15.884  1.00 36.94           C  
ANISOU 3043  CA  SER H   7     4424   5965   3647    720  -1639   -540       C  
ATOM   3044  C   SER H   7      83.068  11.005 -16.342  1.00 36.85           C  
ANISOU 3044  C   SER H   7     4577   5921   3503    937  -1658   -419       C  
ATOM   3045  O   SER H   7      82.757  12.001 -15.684  1.00 36.49           O  
ANISOU 3045  O   SER H   7     4415   5914   3535   1042  -1649   -359       O  
ATOM   3046  CB  SER H   7      81.494   9.081 -16.707  1.00 39.51           C  
ANISOU 3046  CB  SER H   7     4651   6421   3939    699  -1887   -690       C  
ATOM   3047  OG  SER H   7      80.312   9.811 -16.431  1.00 40.73           O  
ANISOU 3047  OG  SER H   7     4582   6718   4176    797  -2039   -715       O  
ATOM   3048  N   GLY H   8      83.764  11.063 -17.472  1.00 43.63           N  
ANISOU 3048  N   GLY H   8     5712   6702   4163   1005  -1675   -383       N  
ATOM   3049  CA  GLY H   8      84.151  12.325 -18.065  1.00 40.54           C  
ANISOU 3049  CA  GLY H   8     5499   6270   3634   1215  -1693   -264       C  
ATOM   3050  C   GLY H   8      85.585  12.754 -17.847  1.00 42.12           C  
ANISOU 3050  C   GLY H   8     5899   6293   3812   1243  -1463   -122       C  
ATOM   3051  O   GLY H   8      85.924  13.897 -18.176  1.00 35.52           O  
ANISOU 3051  O   GLY H   8     5188   5410   2900   1417  -1452    -11       O  
ATOM   3052  N   GLY H   9      86.437  11.885 -17.306  1.00 46.58           N  
ANISOU 3052  N   GLY H   9     6494   6755   4451   1081  -1279   -117       N  
ATOM   3053  CA  GLY H   9      87.830  12.230 -17.126  1.00 41.56           C  
ANISOU 3053  CA  GLY H   9     6040   5947   3804   1100  -1066     15       C  
ATOM   3054  C   GLY H   9      88.636  12.084 -18.403  1.00 43.81           C  
ANISOU 3054  C   GLY H   9     6627   6126   3891   1153  -1043     57       C  
ATOM   3055  O   GLY H   9      88.157  11.599 -19.429  1.00 35.63           O  
ANISOU 3055  O   GLY H   9     5673   5151   2713   1161  -1190    -26       O  
ATOM   3056  N   GLY H  10      89.888  12.517 -18.331  1.00 47.48           N  
ANISOU 3056  N   GLY H  10     7260   6431   4351   1191   -854    187       N  
ATOM   3057  CA  GLY H  10      90.771  12.424 -19.477  1.00 31.61           C  
ANISOU 3057  CA  GLY H  10     5544   4301   2166   1246   -794    246       C  
ATOM   3058  C   GLY H  10      91.869  13.471 -19.396  1.00 30.47           C  
ANISOU 3058  C   GLY H  10     5544   4003   2030   1363   -627    411       C  
ATOM   3059  O   GLY H  10      92.183  13.980 -18.321  1.00 33.07           O  
ANISOU 3059  O   GLY H  10     5752   4293   2522   1349   -521    467       O  
ATOM   3060  N   LEU H  11      92.438  13.770 -20.560  1.00 31.38           N  
ANISOU 3060  N   LEU H  11     5889   4026   2007   1456   -592    471       N  
ATOM   3061  CA  LEU H  11      93.531  14.725 -20.684  1.00 30.60           C  
ANISOU 3061  CA  LEU H  11     5845   3759   2024   1497   -395    577       C  
ATOM   3062  C   LEU H  11      92.986  16.040 -21.226  1.00 32.00           C  
ANISOU 3062  C   LEU H  11     6001   3978   2180   1656   -481    606       C  
ATOM   3063  O   LEU H  11      92.358  16.065 -22.290  1.00 51.03           O  
ANISOU 3063  O   LEU H  11     8488   6461   4440   1734   -618    572       O  
ATOM   3064  CB  LEU H  11      94.629  14.176 -21.595  1.00 30.69           C  
ANISOU 3064  CB  LEU H  11     6036   3626   1999   1441   -249    591       C  
ATOM   3065  CG  LEU H  11      95.868  15.057 -21.770  1.00 35.30           C  
ANISOU 3065  CG  LEU H  11     6647   4048   2717   1462    -50    662       C  
ATOM   3066  CD1 LEU H  11      96.489  15.364 -20.420  1.00 44.07           C  
ANISOU 3066  CD1 LEU H  11     7599   5106   4040   1380     79    691       C  
ATOM   3067  CD2 LEU H  11      96.881  14.393 -22.692  1.00 30.21           C  
ANISOU 3067  CD2 LEU H  11     6157   3282   2038   1412     75    655       C  
ATOM   3068  N   VAL H  12      93.224  17.126 -20.494  1.00 38.83           N  
ANISOU 3068  N   VAL H  12     6761   4798   3196   1697   -398    664       N  
ATOM   3069  CA  VAL H  12      92.750  18.456 -20.858  1.00 46.93           C  
ANISOU 3069  CA  VAL H  12     7755   5850   4226   1835   -452    697       C  
ATOM   3070  C   VAL H  12      93.947  19.393 -20.916  1.00 60.96           C  
ANISOU 3070  C   VAL H  12     9575   7468   6118   1835   -247    764       C  
ATOM   3071  O   VAL H  12      94.802  19.372 -20.023  1.00 71.51           O  
ANISOU 3071  O   VAL H  12    10847   8723   7603   1735   -102    775       O  
ATOM   3072  CB  VAL H  12      91.701  18.980 -19.860  1.00 32.14           C  
ANISOU 3072  CB  VAL H  12     5679   4100   2432   1884   -572    677       C  
ATOM   3073  CG1 VAL H  12      91.090  20.279 -20.364  1.00 33.71           C  
ANISOU 3073  CG1 VAL H  12     5853   4332   2623   2026   -641    707       C  
ATOM   3074  CG2 VAL H  12      90.625  17.936 -19.616  1.00 42.21           C  
ANISOU 3074  CG2 VAL H  12     6861   5547   3629   1850   -767    585       C  
ATOM   3075  N   GLN H  13      94.008  20.209 -21.965  1.00 45.21           N  
ANISOU 3075  N   GLN H  13     7678   5445   4055   1939   -244    801       N  
ATOM   3076  CA  GLN H  13      95.037  21.230 -22.048  1.00 37.15           C  
ANISOU 3076  CA  GLN H  13     6674   4302   3139   1944    -71    853       C  
ATOM   3077  C   GLN H  13      94.706  22.380 -21.096  1.00 36.12           C  
ANISOU 3077  C   GLN H  13     6390   4191   3143   1974    -71    874       C  
ATOM   3078  O   GLN H  13      93.532  22.650 -20.824  1.00 36.32           O  
ANISOU 3078  O   GLN H  13     6329   4326   3145   2050   -221    862       O  
ATOM   3079  CB  GLN H  13      95.165  21.744 -23.479  1.00 38.94           C  
ANISOU 3079  CB  GLN H  13     7056   4499   3241   2054    -66    891       C  
ATOM   3080  CG  GLN H  13      95.649  20.691 -24.466  1.00 57.21           C  
ANISOU 3080  CG  GLN H  13     9535   6772   5429   2026    -40    869       C  
ATOM   3081  CD  GLN H  13      95.628  21.176 -25.903  1.00 74.70           C  
ANISOU 3081  CD  GLN H  13    11910   8975   7499   2155    -55    906       C  
ATOM   3082  OE1 GLN H  13      95.011  22.194 -26.218  1.00 95.46           O  
ANISOU 3082  OE1 GLN H  13    14525  11651  10095   2274   -124    947       O  
ATOM   3083  NE2 GLN H  13      96.304  20.447 -26.784  1.00 69.73           N  
ANISOU 3083  NE2 GLN H  13    11433   8279   6782   2134     13    894       N  
ATOM   3084  N   PRO H  14      95.723  23.060 -20.563  1.00 38.40           N  
ANISOU 3084  N   PRO H  14     6628   4384   3578   1907     87    895       N  
ATOM   3085  CA  PRO H  14      95.467  24.137 -19.598  1.00 30.33           C  
ANISOU 3085  CA  PRO H  14     5465   3371   2687   1920     91    907       C  
ATOM   3086  C   PRO H  14      94.559  25.214 -20.173  1.00 53.32           C  
ANISOU 3086  C   PRO H  14     8384   6330   5546   2071     -5    945       C  
ATOM   3087  O   PRO H  14      94.604  25.530 -21.364  1.00 58.43           O  
ANISOU 3087  O   PRO H  14     9155   6959   6087   2157     -9    983       O  
ATOM   3088  CB  PRO H  14      96.866  24.686 -19.300  1.00 29.16           C  
ANISOU 3088  CB  PRO H  14     5297   3113   2670   1822    267    919       C  
ATOM   3089  CG  PRO H  14      97.775  23.535 -19.564  1.00 43.12           C  
ANISOU 3089  CG  PRO H  14     7130   4837   4417   1719    348    893       C  
ATOM   3090  CD  PRO H  14      97.164  22.798 -20.724  1.00 45.54           C  
ANISOU 3090  CD  PRO H  14     7581   5179   4543   1802    258    894       C  
ATOM   3091  N   GLY H  15      93.722  25.777 -19.300  1.00 36.15           N  
ANISOU 3091  N   GLY H  15     6070   4217   3449   2107    -82    934       N  
ATOM   3092  CA  GLY H  15      92.733  26.754 -19.696  1.00 33.96           C  
ANISOU 3092  CA  GLY H  15     5766   3995   3141   2246   -186    963       C  
ATOM   3093  C   GLY H  15      91.441  26.178 -20.227  1.00 36.02           C  
ANISOU 3093  C   GLY H  15     6024   4398   3266   2338   -385    937       C  
ATOM   3094  O   GLY H  15      90.440  26.903 -20.298  1.00 36.86           O  
ANISOU 3094  O   GLY H  15     6056   4577   3372   2442   -495    947       O  
ATOM   3095  N   GLY H  16      91.421  24.901 -20.592  1.00 35.37           N  
ANISOU 3095  N   GLY H  16     6007   4359   3071   2294   -440    897       N  
ATOM   3096  CA  GLY H  16      90.240  24.285 -21.151  1.00 49.10           C  
ANISOU 3096  CA  GLY H  16     7737   6246   4674   2359   -647    855       C  
ATOM   3097  C   GLY H  16      89.173  24.027 -20.101  1.00 56.63           C  
ANISOU 3097  C   GLY H  16     8486   7330   5701   2348   -777    791       C  
ATOM   3098  O   GLY H  16      89.202  24.535 -18.979  1.00 54.85           O  
ANISOU 3098  O   GLY H  16     8129   7084   5627   2321   -714    790       O  
ATOM   3099  N   SER H  17      88.204  23.202 -20.492  1.00 52.98           N  
ANISOU 3099  N   SER H  17     7988   7013   5129   2361   -967    727       N  
ATOM   3100  CA  SER H  17      87.073  22.877 -19.639  1.00 48.65           C  
ANISOU 3100  CA  SER H  17     7223   6615   4646   2348  -1112    649       C  
ATOM   3101  C   SER H  17      86.787  21.385 -19.721  1.00 50.03           C  
ANISOU 3101  C   SER H  17     7386   6891   4731   2256  -1225    560       C  
ATOM   3102  O   SER H  17      87.338  20.665 -20.558  1.00 54.25           O  
ANISOU 3102  O   SER H  17     8094   7385   5135   2219  -1210    558       O  
ATOM   3103  CB  SER H  17      85.830  23.688 -20.026  1.00 49.61           C  
ANISOU 3103  CB  SER H  17     7241   6845   4764   2465  -1268    645       C  
ATOM   3104  OG  SER H  17      86.057  25.076 -19.849  1.00 60.88           O  
ANISOU 3104  OG  SER H  17     8667   8179   6286   2542  -1162    723       O  
ATOM   3105  N   ARG H  18      85.911  20.927 -18.832  1.00 43.99           N  
ANISOU 3105  N   ARG H  18     6405   6260   4048   2213  -1333    477       N  
ATOM   3106  CA  ARG H  18      85.522  19.526 -18.762  1.00 37.49           C  
ANISOU 3106  CA  ARG H  18     5523   5551   3169   2108  -1450    372       C  
ATOM   3107  C   ARG H  18      84.180  19.452 -18.048  1.00 49.26           C  
ANISOU 3107  C   ARG H  18     6730   7214   4772   2098  -1601    278       C  
ATOM   3108  O   ARG H  18      83.741  20.412 -17.413  1.00 65.83           O  
ANISOU 3108  O   ARG H  18     8692   9322   7000   2161  -1577    305       O  
ATOM   3109  CB  ARG H  18      86.582  18.687 -18.041  1.00 35.22           C  
ANISOU 3109  CB  ARG H  18     5293   5181   2909   1994  -1302    382       C  
ATOM   3110  CG  ARG H  18      86.605  17.221 -18.439  1.00 35.39           C  
ANISOU 3110  CG  ARG H  18     5374   5258   2813   1880  -1379    294       C  
ATOM   3111  CD  ARG H  18      87.094  17.052 -19.866  1.00 36.56           C  
ANISOU 3111  CD  ARG H  18     5775   5329   2787   1901  -1373    320       C  
ATOM   3112  NE  ARG H  18      87.292  15.649 -20.215  1.00 36.58           N  
ANISOU 3112  NE  ARG H  18     5865   5352   2680   1778  -1411    234       N  
ATOM   3113  CZ  ARG H  18      87.873  15.235 -21.335  1.00 49.60           C  
ANISOU 3113  CZ  ARG H  18     7740   6922   4183   1763  -1373    242       C  
ATOM   3114  NH1 ARG H  18      88.319  16.118 -22.218  1.00 46.00           N  
ANISOU 3114  NH1 ARG H  18     7435   6369   3675   1869  -1300    335       N  
ATOM   3115  NH2 ARG H  18      88.012  13.937 -21.573  1.00 55.21           N  
ANISOU 3115  NH2 ARG H  18     8519   7648   4812   1636  -1399    147       N  
ATOM   3116  N   LYS H  19      83.526  18.297 -18.164  1.00 46.53           N  
ANISOU 3116  N   LYS H  19     6290   6999   4391   2005  -1749    159       N  
ATOM   3117  CA  LYS H  19      82.221  18.080 -17.538  1.00 41.27           C  
ANISOU 3117  CA  LYS H  19     5332   6495   3854   1965  -1885     54       C  
ATOM   3118  C   LYS H  19      82.223  16.679 -16.934  1.00 46.02           C  
ANISOU 3118  C   LYS H  19     5821   7158   4507   1785  -1887    -58       C  
ATOM   3119  O   LYS H  19      82.106  15.684 -17.656  1.00 51.02           O  
ANISOU 3119  O   LYS H  19     6514   7824   5047   1694  -1977   -142       O  
ATOM   3120  CB  LYS H  19      81.087  18.256 -18.541  1.00 52.93           C  
ANISOU 3120  CB  LYS H  19     6767   8072   5271   2017  -2082      7       C  
ATOM   3121  CG  LYS H  19      79.705  18.357 -17.909  1.00 50.66           C  
ANISOU 3121  CG  LYS H  19     6177   7922   5150   1997  -2193    -70       C  
ATOM   3122  CD  LYS H  19      78.638  18.644 -18.957  1.00 59.73           C  
ANISOU 3122  CD  LYS H  19     7301   9156   6236   2063  -2383    -94       C  
ATOM   3123  CE  LYS H  19      77.277  18.876 -18.317  1.00 62.37           C  
ANISOU 3123  CE  LYS H  19     7341   9606   6752   2051  -2471   -148       C  
ATOM   3124  NZ  LYS H  19      76.226  19.182 -19.329  1.00 50.59           N  
ANISOU 3124  NZ  LYS H  19     5819   8198   5205   2120  -2661   -162       N  
ATOM   3125  N   LEU H  20      82.358  16.609 -15.613  1.00 42.86           N  
ANISOU 3125  N   LEU H  20     5260   6736   4291   1687  -1734    -60       N  
ATOM   3126  CA  LEU H  20      82.373  15.339 -14.904  1.00 36.25           C  
ANISOU 3126  CA  LEU H  20     4300   5912   3562   1467  -1655   -148       C  
ATOM   3127  C   LEU H  20      80.960  14.951 -14.491  1.00 37.62           C  
ANISOU 3127  C   LEU H  20     4177   6251   3865   1413  -1796   -266       C  
ATOM   3128  O   LEU H  20      80.193  15.780 -13.992  1.00 57.80           O  
ANISOU 3128  O   LEU H  20     6561   8884   6515   1514  -1845   -257       O  
ATOM   3129  CB  LEU H  20      83.280  15.421 -13.676  1.00 35.21           C  
ANISOU 3129  CB  LEU H  20     4152   5675   3550   1390  -1414    -84       C  
ATOM   3130  CG  LEU H  20      84.726  15.836 -13.956  1.00 42.94           C  
ANISOU 3130  CG  LEU H  20     5398   6479   4439   1436  -1258     36       C  
ATOM   3131  CD1 LEU H  20      85.548  15.822 -12.677  1.00 64.48           C  
ANISOU 3131  CD1 LEU H  20     8082   9121   7298   1346  -1041     82       C  
ATOM   3132  CD2 LEU H  20      85.352  14.936 -15.010  1.00 32.69           C  
ANISOU 3132  CD2 LEU H  20     4314   5114   2993   1367  -1263     24       C  
ATOM   3133  N   SER H  21      80.625  13.681 -14.703  1.00 38.23           N  
ANISOU 3133  N   SER H  21     4193   6375   3958   1251  -1852   -377       N  
ATOM   3134  CA  SER H  21      79.298  13.155 -14.429  1.00 47.85           C  
ANISOU 3134  CA  SER H  21     5132   7742   5308   1180  -1990   -499       C  
ATOM   3135  C   SER H  21      79.368  12.094 -13.339  1.00 58.86           C  
ANISOU 3135  C   SER H  21     6369   9121   6874    971  -1834   -548       C  
ATOM   3136  O   SER H  21      80.360  11.368 -13.213  1.00 53.62           O  
ANISOU 3136  O   SER H  21     5841   8346   6185    850  -1680   -526       O  
ATOM   3137  CB  SER H  21      78.669  12.562 -15.693  1.00 47.48           C  
ANISOU 3137  CB  SER H  21     5122   7773   5145   1172  -2223   -604       C  
ATOM   3138  OG  SER H  21      78.697  13.499 -16.755  1.00 53.54           O  
ANISOU 3138  OG  SER H  21     6063   8550   5728   1372  -2359   -545       O  
ATOM   3139  N   CYS H  22      78.294  12.009 -12.554  1.00 39.26           N  
ANISOU 3139  N   CYS H  22     3597   6751   4569    934  -1869   -609       N  
ATOM   3140  CA  CYS H  22      78.197  11.072 -11.435  1.00 38.38           C  
ANISOU 3140  CA  CYS H  22     3306   6641   4636    751  -1720   -648       C  
ATOM   3141  C   CYS H  22      76.809  10.441 -11.490  1.00 59.76           C  
ANISOU 3141  C   CYS H  22     5746   9483   7478    678  -1876   -778       C  
ATOM   3142  O   CYS H  22      75.826  11.052 -11.062  1.00 66.67           O  
ANISOU 3142  O   CYS H  22     6407  10462   8463    759  -1946   -792       O  
ATOM   3143  CB  CYS H  22      78.438  11.777 -10.105  1.00 36.81           C  
ANISOU 3143  CB  CYS H  22     3019   6424   4542    790  -1537   -563       C  
ATOM   3144  SG  CYS H  22      78.198  10.758  -8.626  1.00 50.69           S  
ANISOU 3144  SG  CYS H  22     4540   8206   6515    595  -1350   -594       S  
ATOM   3145  N   ALA H  23      76.735   9.226 -12.029  1.00 63.89           N  
ANISOU 3145  N   ALA H  23     6278   9997   8000    527  -1930   -875       N  
ATOM   3146  CA  ALA H  23      75.482   8.488 -12.083  1.00 43.32           C  
ANISOU 3146  CA  ALA H  23     3414   7502   5543    431  -2070  -1010       C  
ATOM   3147  C   ALA H  23      75.239   7.787 -10.753  1.00 42.55           C  
ANISOU 3147  C   ALA H  23     3091   7406   5670    279  -1884  -1017       C  
ATOM   3148  O   ALA H  23      76.115   7.077 -10.246  1.00 45.69           O  
ANISOU 3148  O   ALA H  23     3575   7702   6084    154  -1687   -978       O  
ATOM   3149  CB  ALA H  23      75.507   7.473 -13.224  1.00 44.63           C  
ANISOU 3149  CB  ALA H  23     3687   7650   5618    329  -2205  -1124       C  
ATOM   3150  N   ALA H  24      74.051   7.988 -10.191  1.00 43.85           N  
ANISOU 3150  N   ALA H  24     3027   7630   6003    283  -1898  -1023       N  
ATOM   3151  CA  ALA H  24      73.687   7.441  -8.893  1.00 53.11           C  
ANISOU 3151  CA  ALA H  24     4013   8783   7382    160  -1701   -996       C  
ATOM   3152  C   ALA H  24      72.542   6.452  -9.047  1.00 54.34           C  
ANISOU 3152  C   ALA H  24     4000   8952   7693     22  -1766  -1079       C  
ATOM   3153  O   ALA H  24      71.583   6.707  -9.782  1.00 47.76           O  
ANISOU 3153  O   ALA H  24     3115   8170   6860     73  -1952  -1123       O  
ATOM   3154  CB  ALA H  24      73.286   8.552  -7.918  1.00 47.94           C  
ANISOU 3154  CB  ALA H  24     3282   8140   6793    278  -1599   -892       C  
ATOM   3155  N   SER H  25      72.646   5.326  -8.346  1.00 51.33           N  
ANISOU 3155  N   SER H  25     3537   8518   7447   -151  -1605  -1089       N  
ATOM   3156  CA  SER H  25      71.603   4.312  -8.374  1.00 47.17           C  
ANISOU 3156  CA  SER H  25     2850   7988   7086   -289  -1636  -1154       C  
ATOM   3157  C   SER H  25      71.581   3.583  -7.039  1.00 46.37           C  
ANISOU 3157  C   SER H  25     2643   7825   7151   -409  -1383  -1080       C  
ATOM   3158  O   SER H  25      72.595   3.505  -6.341  1.00 51.87           O  
ANISOU 3158  O   SER H  25     3427   8468   7815   -430  -1200  -1008       O  
ATOM   3159  CB  SER H  25      71.811   3.321  -9.524  1.00 48.16           C  
ANISOU 3159  CB  SER H  25     3053   8090   7154   -399  -1774  -1286       C  
ATOM   3160  OG  SER H  25      73.102   2.739  -9.471  1.00 46.18           O  
ANISOU 3160  OG  SER H  25     2941   7769   6835   -482  -1653  -1291       O  
ATOM   3161  N   GLY H  26      70.411   3.052  -6.692  1.00 59.13           N  
ANISOU 3161  N   GLY H  26     4080   9450   8938   -481  -1375  -1087       N  
ATOM   3162  CA  GLY H  26      70.233   2.319  -5.457  1.00 49.79           C  
ANISOU 3162  CA  GLY H  26     2803   8211   7904   -583  -1147  -1002       C  
ATOM   3163  C   GLY H  26      69.549   3.081  -4.344  1.00 48.05           C  
ANISOU 3163  C   GLY H  26     2473   8024   7758   -493  -1039   -889       C  
ATOM   3164  O   GLY H  26      69.317   2.501  -3.276  1.00 65.91           O  
ANISOU 3164  O   GLY H  26     4665  10250  10129   -563   -854   -805       O  
ATOM   3165  N   PHE H  27      69.218   4.352  -4.553  1.00 48.31           N  
ANISOU 3165  N   PHE H  27     2501   8124   7732   -337  -1146   -879       N  
ATOM   3166  CA  PHE H  27      68.555   5.146  -3.528  1.00 55.74           C  
ANISOU 3166  CA  PHE H  27     3343   9093   8743   -248  -1046   -780       C  
ATOM   3167  C   PHE H  27      67.820   6.295  -4.202  1.00 49.93           C  
ANISOU 3167  C   PHE H  27     2561   8434   7974   -103  -1237   -810       C  
ATOM   3168  O   PHE H  27      67.945   6.518  -5.409  1.00 50.48           O  
ANISOU 3168  O   PHE H  27     2702   8535   7944    -61  -1437   -890       O  
ATOM   3169  CB  PHE H  27      69.554   5.666  -2.488  1.00 53.96           C  
ANISOU 3169  CB  PHE H  27     3239   8817   8447   -191   -846   -674       C  
ATOM   3170  CG  PHE H  27      70.579   6.614  -3.048  1.00 63.79           C  
ANISOU 3170  CG  PHE H  27     4656  10063   9518    -76   -915   -688       C  
ATOM   3171  CD1 PHE H  27      70.387   7.985  -2.977  1.00 74.01           C  
ANISOU 3171  CD1 PHE H  27     5967  11393  10762     88   -960   -655       C  
ATOM   3172  CD2 PHE H  27      71.734   6.136  -3.644  1.00 66.49           C  
ANISOU 3172  CD2 PHE H  27     5145  10369   9748   -128   -928   -730       C  
ATOM   3173  CE1 PHE H  27      71.327   8.860  -3.490  1.00 42.98           C  
ANISOU 3173  CE1 PHE H  27     2201   7462   6669    202  -1018   -657       C  
ATOM   3174  CE2 PHE H  27      72.678   7.006  -4.160  1.00 41.60           C  
ANISOU 3174  CE2 PHE H  27     2150   7227   6430    -15   -988   -733       C  
ATOM   3175  CZ  PHE H  27      72.474   8.369  -4.081  1.00 41.60           C  
ANISOU 3175  CZ  PHE H  27     2169   7260   6377    153  -1033   -692       C  
ATOM   3176  N   THR H  28      67.047   7.025  -3.402  1.00 63.39           N  
ANISOU 3176  N   THR H  28     4156  10168   9760    -23  -1168   -735       N  
ATOM   3177  CA  THR H  28      66.342   8.209  -3.880  1.00 58.21           C  
ANISOU 3177  CA  THR H  28     3455   9576   9085    125  -1318   -739       C  
ATOM   3178  C   THR H  28      67.332   9.365  -3.957  1.00 58.72           C  
ANISOU 3178  C   THR H  28     3701   9619   8992    267  -1311   -702       C  
ATOM   3179  O   THR H  28      67.743   9.911  -2.928  1.00 60.24           O  
ANISOU 3179  O   THR H  28     3935   9774   9180    317  -1138   -622       O  
ATOM   3180  CB  THR H  28      65.169   8.545  -2.965  1.00 53.32           C  
ANISOU 3180  CB  THR H  28     2649   8992   8618    155  -1232   -672       C  
ATOM   3181  OG1 THR H  28      64.250   7.446  -2.942  1.00 55.27           O  
ANISOU 3181  OG1 THR H  28     2726   9264   9010     23  -1241   -706       O  
ATOM   3182  CG2 THR H  28      64.449   9.791  -3.461  1.00 57.60           C  
ANISOU 3182  CG2 THR H  28     3142   9594   9149    310  -1379   -668       C  
ATOM   3183  N   PHE H  29      67.712   9.741  -5.180  1.00 63.06           N  
ANISOU 3183  N   PHE H  29     4366  10190   9404    336  -1500   -759       N  
ATOM   3184  CA  PHE H  29      68.769  10.730  -5.359  1.00 63.84           C  
ANISOU 3184  CA  PHE H  29     4656  10262   9338    466  -1494   -723       C  
ATOM   3185  C   PHE H  29      68.305  12.137  -5.008  1.00 61.77           C  
ANISOU 3185  C   PHE H  29     4371  10013   9087    628  -1486   -655       C  
ATOM   3186  O   PHE H  29      69.115  12.963  -4.573  1.00 64.56           O  
ANISOU 3186  O   PHE H  29     4849  10323   9359    718  -1388   -601       O  
ATOM   3187  CB  PHE H  29      69.281  10.682  -6.799  1.00 60.38           C  
ANISOU 3187  CB  PHE H  29     4361   9841   8738    499  -1696   -790       C  
ATOM   3188  CG  PHE H  29      70.369  11.675  -7.092  1.00 46.66           C  
ANISOU 3188  CG  PHE H  29     2829   8074   6823    639  -1696   -744       C  
ATOM   3189  CD1 PHE H  29      71.672  11.431  -6.695  1.00 44.25           C  
ANISOU 3189  CD1 PHE H  29     2659   7715   6438    604  -1558   -721       C  
ATOM   3190  CD2 PHE H  29      70.090  12.849  -7.773  1.00 47.57           C  
ANISOU 3190  CD2 PHE H  29     3005   8212   6856    806  -1830   -714       C  
ATOM   3191  CE1 PHE H  29      72.676  12.340  -6.966  1.00 42.79           C  
ANISOU 3191  CE1 PHE H  29     2661   7500   6096    735  -1554   -672       C  
ATOM   3192  CE2 PHE H  29      71.089  13.762  -8.047  1.00 46.11           C  
ANISOU 3192  CE2 PHE H  29     3017   7987   6515    938  -1819   -659       C  
ATOM   3193  CZ  PHE H  29      72.384  13.508  -7.643  1.00 58.51           C  
ANISOU 3193  CZ  PHE H  29     4718   9504   8010    903  -1682   -640       C  
ATOM   3194  N   SER H  30      67.017  12.428  -5.178  1.00 50.88           N  
ANISOU 3194  N   SER H  30     2830   8689   7812    664  -1584   -658       N  
ATOM   3195  CA  SER H  30      66.514  13.787  -5.011  1.00 67.98           C  
ANISOU 3195  CA  SER H  30     4971  10868   9992    823  -1599   -598       C  
ATOM   3196  C   SER H  30      66.233  14.130  -3.552  1.00 76.25           C  
ANISOU 3196  C   SER H  30     5929  11885  11156    828  -1384   -529       C  
ATOM   3197  O   SER H  30      65.387  14.983  -3.267  1.00 87.02           O  
ANISOU 3197  O   SER H  30     7191  13271  12600    922  -1386   -489       O  
ATOM   3198  CB  SER H  30      65.246  13.979  -5.846  1.00 54.40           C  
ANISOU 3198  CB  SER H  30     3113   9225   8333    866  -1799   -625       C  
ATOM   3199  OG  SER H  30      64.280  12.989  -5.539  1.00 77.57           O  
ANISOU 3199  OG  SER H  30     5848  12198  11428    736  -1789   -657       O  
ATOM   3200  N   GLY H  31      66.940  13.490  -2.623  1.00 72.55           N  
ANISOU 3200  N   GLY H  31     5504  11366  10696    732  -1196   -511       N  
ATOM   3201  CA  GLY H  31      66.690  13.726  -1.214  1.00 68.95           C  
ANISOU 3201  CA  GLY H  31     4981  10880  10337    732   -990   -444       C  
ATOM   3202  C   GLY H  31      67.913  14.108  -0.405  1.00 67.02           C  
ANISOU 3202  C   GLY H  31     4905  10559   9999    756   -821   -406       C  
ATOM   3203  O   GLY H  31      67.791  14.758   0.638  1.00 64.45           O  
ANISOU 3203  O   GLY H  31     4568  10204   9717    809   -680   -356       O  
ATOM   3204  N   PHE H  32      69.098  13.719  -0.869  1.00 58.56           N  
ANISOU 3204  N   PHE H  32     3993   9458   8800    717   -836   -432       N  
ATOM   3205  CA  PHE H  32      70.334  13.934  -0.132  1.00 43.25           C  
ANISOU 3205  CA  PHE H  32     2213   7450   6771    721   -679   -397       C  
ATOM   3206  C   PHE H  32      71.285  14.801  -0.943  1.00 41.22           C  
ANISOU 3206  C   PHE H  32     2132   7176   6355    832   -769   -407       C  
ATOM   3207  O   PHE H  32      71.344  14.693  -2.171  1.00 41.74           O  
ANISOU 3207  O   PHE H  32     2235   7275   6351    854   -941   -446       O  
ATOM   3208  CB  PHE H  32      71.011  12.602   0.206  1.00 41.18           C  
ANISOU 3208  CB  PHE H  32     1985   7157   6505    567   -576   -397       C  
ATOM   3209  CG  PHE H  32      70.061  11.546   0.685  1.00 42.57           C  
ANISOU 3209  CG  PHE H  32     1993   7351   6831    449   -521   -386       C  
ATOM   3210  CD1 PHE H  32      69.662  11.505   2.010  1.00 50.23           C  
ANISOU 3210  CD1 PHE H  32     2898   8293   7893    433   -344   -319       C  
ATOM   3211  CD2 PHE H  32      69.567  10.593  -0.190  1.00 43.85           C  
ANISOU 3211  CD2 PHE H  32     2068   7554   7039    356   -647   -443       C  
ATOM   3212  CE1 PHE H  32      68.788  10.533   2.453  1.00 57.44           C  
ANISOU 3212  CE1 PHE H  32     3660   9226   8938    334   -286   -290       C  
ATOM   3213  CE2 PHE H  32      68.692   9.618   0.248  1.00 48.48           C  
ANISOU 3213  CE2 PHE H  32     2500   8155   7766    247   -592   -428       C  
ATOM   3214  CZ  PHE H  32      68.302   9.587   1.571  1.00 49.38           C  
ANISOU 3214  CZ  PHE H  32     2547   8249   7966    239   -408   -343       C  
ATOM   3215  N   GLY H  33      72.032  15.656  -0.249  1.00 39.79           N  
ANISOU 3215  N   GLY H  33     2066   6939   6114    903   -652   -368       N  
ATOM   3216  CA  GLY H  33      73.038  16.457  -0.912  1.00 56.72           C  
ANISOU 3216  CA  GLY H  33     4386   9052   8113   1005   -708   -360       C  
ATOM   3217  C   GLY H  33      74.198  15.619  -1.413  1.00 49.45           C  
ANISOU 3217  C   GLY H  33     3586   8120   7084    930   -713   -372       C  
ATOM   3218  O   GLY H  33      74.413  14.479  -0.997  1.00 36.54           O  
ANISOU 3218  O   GLY H  33     1917   6483   5483    792   -629   -380       O  
ATOM   3219  N   MET H  34      74.965  16.202  -2.332  1.00 45.88           N  
ANISOU 3219  N   MET H  34     3282   7650   6500   1028   -805   -364       N  
ATOM   3220  CA  MET H  34      76.077  15.512  -2.966  1.00 35.18           C  
ANISOU 3220  CA  MET H  34     2049   6287   5031    981   -826   -371       C  
ATOM   3221  C   MET H  34      77.341  16.353  -2.862  1.00 50.83           C  
ANISOU 3221  C   MET H  34     4215   8196   6901   1074   -753   -314       C  
ATOM   3222  O   MET H  34      77.289  17.586  -2.847  1.00 65.14           O  
ANISOU 3222  O   MET H  34     6085   9967   8699   1204   -761   -282       O  
ATOM   3223  CB  MET H  34      75.775  15.201  -4.439  1.00 36.76           C  
ANISOU 3223  CB  MET H  34     2267   6537   5165   1006  -1040   -416       C  
ATOM   3224  CG  MET H  34      74.498  14.405  -4.662  1.00 46.30           C  
ANISOU 3224  CG  MET H  34     3293   7810   6487    914  -1135   -479       C  
ATOM   3225  SD  MET H  34      74.511  12.790  -3.859  1.00 37.88           S  
ANISOU 3225  SD  MET H  34     2114   6747   5532    693   -997   -511       S  
ATOM   3226  CE  MET H  34      75.931  12.030  -4.645  1.00 36.31           C  
ANISOU 3226  CE  MET H  34     2077   6534   5185    636  -1020   -534       C  
ATOM   3227  N   HIS H  35      78.480  15.669  -2.800  1.00 44.52           N  
ANISOU 3227  N   HIS H  35     3505   7376   6035   1003   -676   -298       N  
ATOM   3228  CA  HIS H  35      79.782  16.304  -2.666  1.00 30.17           C  
ANISOU 3228  CA  HIS H  35     1859   5480   4122   1073   -593   -236       C  
ATOM   3229  C   HIS H  35      80.706  15.867  -3.795  1.00 39.13           C  
ANISOU 3229  C   HIS H  35     3177   6559   5131   1062   -656   -211       C  
ATOM   3230  O   HIS H  35      80.613  14.742  -4.298  1.00 34.16           O  
ANISOU 3230  O   HIS H  35     2545   5940   4492    938   -697   -244       O  
ATOM   3231  CB  HIS H  35      80.443  15.957  -1.325  1.00 28.69           C  
ANISOU 3231  CB  HIS H  35     1677   5253   3973    970   -389   -208       C  
ATOM   3232  CG  HIS H  35      79.663  16.396  -0.126  1.00 29.24           C  
ANISOU 3232  CG  HIS H  35     1656   5310   4144    956   -299   -216       C  
ATOM   3233  ND1 HIS H  35      80.046  17.463   0.659  1.00 28.65           N  
ANISOU 3233  ND1 HIS H  35     1657   5166   4063   1024   -211   -191       N  
ATOM   3234  CD2 HIS H  35      78.533  15.904   0.434  1.00 40.83           C  
ANISOU 3234  CD2 HIS H  35     2969   6820   5724    883   -281   -246       C  
ATOM   3235  CE1 HIS H  35      79.182  17.613   1.646  1.00 35.08           C  
ANISOU 3235  CE1 HIS H  35     2369   5991   4970    999   -147   -209       C  
ATOM   3236  NE2 HIS H  35      78.253  16.680   1.533  1.00 36.34           N  
ANISOU 3236  NE2 HIS H  35     2388   6215   5204    919   -183   -235       N  
ATOM   3237  N   TRP H  36      81.601  16.771  -4.184  1.00 30.87           N  
ANISOU 3237  N   TRP H  36     2331   5404   3994   1168   -642   -144       N  
ATOM   3238  CA  TRP H  36      82.731  16.459  -5.049  1.00 27.86           C  
ANISOU 3238  CA  TRP H  36     2193   4898   3493   1135   -632    -91       C  
ATOM   3239  C   TRP H  36      84.003  16.577  -4.220  1.00 35.45           C  
ANISOU 3239  C   TRP H  36     3265   5752   4454   1091   -449    -27       C  
ATOM   3240  O   TRP H  36      84.252  17.625  -3.610  1.00 41.66           O  
ANISOU 3240  O   TRP H  36     4056   6508   5265   1190   -389      0       O  
ATOM   3241  CB  TRP H  36      82.792  17.393  -6.258  1.00 28.66           C  
ANISOU 3241  CB  TRP H  36     2447   4951   3493   1297   -758    -54       C  
ATOM   3242  CG  TRP H  36      81.837  17.042  -7.359  1.00 39.72           C  
ANISOU 3242  CG  TRP H  36     3806   6438   4850   1320   -954   -109       C  
ATOM   3243  CD1 TRP H  36      80.698  17.711  -7.699  1.00 43.30           C  
ANISOU 3243  CD1 TRP H  36     4133   6991   5330   1448  -1107   -141       C  
ATOM   3244  CD2 TRP H  36      81.942  15.939  -8.268  1.00 40.24           C  
ANISOU 3244  CD2 TRP H  36     3955   6497   4838   1214  -1025   -142       C  
ATOM   3245  NE1 TRP H  36      80.086  17.093  -8.763  1.00 47.90           N  
ANISOU 3245  NE1 TRP H  36     4712   7638   5852   1428  -1280   -194       N  
ATOM   3246  CE2 TRP H  36      80.829  16.002  -9.130  1.00 46.79           C  
ANISOU 3246  CE2 TRP H  36     4702   7432   5643   1283  -1232   -202       C  
ATOM   3247  CE3 TRP H  36      82.867  14.904  -8.435  1.00 29.76           C  
ANISOU 3247  CE3 TRP H  36     2761   5084   3463   1069   -934   -131       C  
ATOM   3248  CZ2 TRP H  36      80.617  15.071 -10.145  1.00 44.18           C  
ANISOU 3248  CZ2 TRP H  36     4425   7126   5235   1209  -1356   -261       C  
ATOM   3249  CZ3 TRP H  36      82.655  13.980  -9.443  1.00 30.73           C  
ANISOU 3249  CZ3 TRP H  36     2939   5224   3514    996  -1044   -187       C  
ATOM   3250  CH2 TRP H  36      81.539  14.070 -10.285  1.00 47.04           C  
ANISOU 3250  CH2 TRP H  36     4926   7398   5549   1065  -1256   -256       C  
ATOM   3251  N   VAL H  37      84.791  15.501  -4.193  1.00 40.98           N  
ANISOU 3251  N   VAL H  37     4045   6393   5131    944   -363     -7       N  
ATOM   3252  CA  VAL H  37      86.031  15.422  -3.424  1.00 35.39           C  
ANISOU 3252  CA  VAL H  37     3433   5587   4426    884   -196     55       C  
ATOM   3253  C   VAL H  37      87.095  14.798  -4.316  1.00 22.42           C  
ANISOU 3253  C   VAL H  37     2002   3819   2698    819   -172    106       C  
ATOM   3254  O   VAL H  37      86.933  13.662  -4.772  1.00 27.58           O  
ANISOU 3254  O   VAL H  37     2651   4488   3340    705   -195     77       O  
ATOM   3255  CB  VAL H  37      85.868  14.590  -2.137  1.00 34.65           C  
ANISOU 3255  CB  VAL H  37     3179   5566   4420    753    -79     34       C  
ATOM   3256  CG1 VAL H  37      87.213  14.401  -1.453  1.00 20.98           C  
ANISOU 3256  CG1 VAL H  37     1559   3735   2678    687     76    103       C  
ATOM   3257  CG2 VAL H  37      84.863  15.240  -1.192  1.00 23.44           C  
ANISOU 3257  CG2 VAL H  37     1558   4266   3081    824    -80    -14       C  
ATOM   3258  N   ARG H  38      88.183  15.523  -4.554  1.00 21.54           N  
ANISOU 3258  N   ARG H  38     2070   3576   2538    889   -116    179       N  
ATOM   3259  CA  ARG H  38      89.260  15.058  -5.418  1.00 26.40           C  
ANISOU 3259  CA  ARG H  38     2896   4058   3076    845    -77    238       C  
ATOM   3260  C   ARG H  38      90.464  14.624  -4.591  1.00 19.26           C  
ANISOU 3260  C   ARG H  38     2040   3065   2212    744     90    296       C  
ATOM   3261  O   ARG H  38      90.508  14.785  -3.369  1.00 18.66           O  
ANISOU 3261  O   ARG H  38     1851   3031   2209    720    167    292       O  
ATOM   3262  CB  ARG H  38      89.667  16.146  -6.419  1.00 21.24           C  
ANISOU 3262  CB  ARG H  38     2421   3306   2343   1000   -128    292       C  
ATOM   3263  CG  ARG H  38      90.344  17.354  -5.792  1.00 20.48           C  
ANISOU 3263  CG  ARG H  38     2362   3128   2292   1096    -46    345       C  
ATOM   3264  CD  ARG H  38      90.624  18.424  -6.834  1.00 21.08           C  
ANISOU 3264  CD  ARG H  38     2603   3106   2302   1256    -96    403       C  
ATOM   3265  NE  ARG H  38      91.146  19.649  -6.236  1.00 37.61           N  
ANISOU 3265  NE  ARG H  38     4712   5119   4461   1353    -25    441       N  
ATOM   3266  CZ  ARG H  38      91.470  20.739  -6.926  1.00 36.54           C  
ANISOU 3266  CZ  ARG H  38     4704   4880   4300   1499    -37    501       C  
ATOM   3267  NH1 ARG H  38      91.329  20.760  -8.244  1.00 22.02           N  
ANISOU 3267  NH1 ARG H  38     2999   3014   2355   1573   -119    538       N  
ATOM   3268  NH2 ARG H  38      91.937  21.809  -6.296  1.00 20.67           N  
ANISOU 3268  NH2 ARG H  38     2693   2790   2371   1555     34    517       N  
ATOM   3269  N   GLN H  39      91.454  14.065  -5.285  1.00 18.65           N  
ANISOU 3269  N   GLN H  39     2137   2865   2084    688    144    351       N  
ATOM   3270  CA  GLN H  39      92.673  13.583  -4.641  1.00 36.37           C  
ANISOU 3270  CA  GLN H  39     4438   5013   4368    592    297    416       C  
ATOM   3271  C   GLN H  39      93.809  13.675  -5.649  1.00 30.26           C  
ANISOU 3271  C   GLN H  39     3893   4072   3532    618    340    493       C  
ATOM   3272  O   GLN H  39      93.815  12.946  -6.646  1.00 17.25           O  
ANISOU 3272  O   GLN H  39     2345   2393   1818    577    311    487       O  
ATOM   3273  CB  GLN H  39      92.502  12.153  -4.136  1.00 33.03           C  
ANISOU 3273  CB  GLN H  39     3915   4647   3990    426    352    392       C  
ATOM   3274  CG  GLN H  39      93.718  11.608  -3.406  1.00 15.60           C  
ANISOU 3274  CG  GLN H  39     1749   2350   1827    329    507    467       C  
ATOM   3275  CD  GLN H  39      93.515  10.190  -2.912  1.00 25.77           C  
ANISOU 3275  CD  GLN H  39     2936   3691   3165    173    569    454       C  
ATOM   3276  OE1 GLN H  39      92.655   9.464  -3.410  1.00 22.59           O  
ANISOU 3276  OE1 GLN H  39     2475   3351   2757    119    503    391       O  
ATOM   3277  NE2 GLN H  39      94.305   9.791  -1.923  1.00 24.45           N  
ANISOU 3277  NE2 GLN H  39     2743   3495   3051     99    695    514       N  
ATOM   3278  N   ALA H  40      94.762  14.566  -5.386  1.00 33.33           N  
ANISOU 3278  N   ALA H  40     4365   4351   3946    685    414    559       N  
ATOM   3279  CA  ALA H  40      95.889  14.751  -6.283  1.00 21.35           C  
ANISOU 3279  CA  ALA H  40     3060   2663   2389    718    474    642       C  
ATOM   3280  C   ALA H  40      96.773  13.504  -6.299  1.00 25.17           C  
ANISOU 3280  C   ALA H  40     3607   3071   2887    574    585    685       C  
ATOM   3281  O   ALA H  40      96.798  12.740  -5.330  1.00 44.12           O  
ANISOU 3281  O   ALA H  40     5887   5526   5351    460    642    672       O  
ATOM   3282  CB  ALA H  40      96.711  15.965  -5.860  1.00 32.19           C  
ANISOU 3282  CB  ALA H  40     4478   3932   3820    809    537    699       C  
ATOM   3283  N   PRO H  41      97.498  13.269  -7.393  1.00 39.87           N  
ANISOU 3283  N   PRO H  41     5658   4802   4687    583    624    740       N  
ATOM   3284  CA  PRO H  41      98.389  12.102  -7.450  1.00 26.73           C  
ANISOU 3284  CA  PRO H  41     3991   3081   3086    424    678    696       C  
ATOM   3285  C   PRO H  41      99.437  12.150  -6.348  1.00 25.99           C  
ANISOU 3285  C   PRO H  41     3774   2971   3131    350    698    637       C  
ATOM   3286  O   PRO H  41     100.080  13.178  -6.124  1.00 33.91           O  
ANISOU 3286  O   PRO H  41     4764   3941   4178    406    697    615       O  
ATOM   3287  CB  PRO H  41      99.024  12.210  -8.841  1.00 14.63           C  
ANISOU 3287  CB  PRO H  41     2598   1456   1506    452    654    669       C  
ATOM   3288  CG  PRO H  41      98.048  13.007  -9.638  1.00 15.93           C  
ANISOU 3288  CG  PRO H  41     2875   1644   1534    608    582    717       C  
ATOM   3289  CD  PRO H  41      97.452  13.990  -8.677  1.00 15.84           C  
ANISOU 3289  CD  PRO H  41     2765   1701   1553    706    557    748       C  
ATOM   3290  N   GLU H  42      99.592  11.023  -5.653  1.00 25.85           N  
ANISOU 3290  N   GLU H  42     3666   2989   3164    230    702    605       N  
ATOM   3291  CA  GLU H  42     100.541  10.864  -4.551  1.00 32.02           C  
ANISOU 3291  CA  GLU H  42     4352   3779   4036    177    676    548       C  
ATOM   3292  C   GLU H  42     100.271  11.831  -3.402  1.00 21.55           C  
ANISOU 3292  C   GLU H  42     2949   2491   2747    234    689    563       C  
ATOM   3293  O   GLU H  42     101.175  12.127  -2.614  1.00 18.83           O  
ANISOU 3293  O   GLU H  42     2565   2128   2461    237    674    525       O  
ATOM   3294  CB  GLU H  42     101.989  11.013  -5.035  1.00 36.29           C  
ANISOU 3294  CB  GLU H  42     4943   4226   4620    227    713    510       C  
ATOM   3295  CG  GLU H  42     102.415   9.969  -6.054  1.00 52.67           C  
ANISOU 3295  CG  GLU H  42     7089   6250   6673    196    740    496       C  
ATOM   3296  CD  GLU H  42     103.823  10.198  -6.568  1.00 75.82           C  
ANISOU 3296  CD  GLU H  42    10069   9104   9636    264    817    462       C  
ATOM   3297  OE1 GLU H  42     104.343  11.322  -6.399  1.00 80.49           O  
ANISOU 3297  OE1 GLU H  42    10651   9685  10248    331    846    457       O  
ATOM   3298  OE2 GLU H  42     104.411   9.255  -7.138  1.00 82.03           O  
ANISOU 3298  OE2 GLU H  42    10899   9848  10423    246    858    440       O  
ATOM   3299  N   LYS H  43      99.042  12.329  -3.285  1.00 16.29           N  
ANISOU 3299  N   LYS H  43     2257   1894   2039    297    725    626       N  
ATOM   3300  CA  LYS H  43      98.657  13.251  -2.225  1.00 11.77           C  
ANISOU 3300  CA  LYS H  43     1595   1385   1493    364    745    648       C  
ATOM   3301  C   LYS H  43      97.316  12.815  -1.643  1.00 14.90           C  
ANISOU 3301  C   LYS H  43     1847   1959   1857    339    769    654       C  
ATOM   3302  O   LYS H  43      96.739  11.799  -2.044  1.00 12.80           O  
ANISOU 3302  O   LYS H  43     1552   1751   1563    266    777    649       O  
ATOM   3303  CB  LYS H  43      98.598  14.695  -2.739  1.00 12.53           C  
ANISOU 3303  CB  LYS H  43     1767   1434   1561    519    760    697       C  
ATOM   3304  CG  LYS H  43      99.959  15.287  -3.075  1.00 11.66           C  
ANISOU 3304  CG  LYS H  43     1719   1208   1503    519    751    633       C  
ATOM   3305  CD  LYS H  43      99.837  16.719  -3.568  1.00 40.15           C  
ANISOU 3305  CD  LYS H  43     5386   4788   5080    631    748    648       C  
ATOM   3306  CE  LYS H  43      99.212  17.619  -2.514  1.00 55.13           C  
ANISOU 3306  CE  LYS H  43     7206   6737   7002    716    754    678       C  
ATOM   3307  NZ  LYS H  43      99.063  19.022  -2.993  1.00 61.35           N  
ANISOU 3307  NZ  LYS H  43     8040   7496   7775    798    696    651       N  
ATOM   3308  N   GLY H  44      96.815  13.599  -0.689  1.00 22.23           N  
ANISOU 3308  N   GLY H  44     2654   2991   2803    403    774    633       N  
ATOM   3309  CA  GLY H  44      95.627  13.247   0.059  1.00 15.81           C  
ANISOU 3309  CA  GLY H  44     1661   2350   1998    373    741    564       C  
ATOM   3310  C   GLY H  44      94.349  13.781  -0.561  1.00 17.75           C  
ANISOU 3310  C   GLY H  44     1854   2679   2212    463    618    490       C  
ATOM   3311  O   GLY H  44      94.329  14.322  -1.668  1.00 25.42           O  
ANISOU 3311  O   GLY H  44     2937   3582   3139    546    550    494       O  
ATOM   3312  N   LEU H  45      93.261  13.623   0.188  1.00 14.93           N  
ANISOU 3312  N   LEU H  45     1320   2474   1879    451    592    426       N  
ATOM   3313  CA  LEU H  45      91.939  14.013  -0.279  1.00 16.19           C  
ANISOU 3313  CA  LEU H  45     1392   2731   2027    525    474    352       C  
ATOM   3314  C   LEU H  45      91.728  15.516  -0.137  1.00 16.55           C  
ANISOU 3314  C   LEU H  45     1436   2776   2077    680    426    328       C  
ATOM   3315  O   LEU H  45      92.323  16.173   0.721  1.00 15.97           O  
ANISOU 3315  O   LEU H  45     1365   2673   2029    711    490    340       O  
ATOM   3316  CB  LEU H  45      90.856  13.266   0.500  1.00 16.82           C  
ANISOU 3316  CB  LEU H  45     1270   2966   2153    452    480    298       C  
ATOM   3317  CG  LEU H  45      90.889  11.740   0.410  1.00 22.75           C  
ANISOU 3317  CG  LEU H  45     1997   3725   2923    297    531    314       C  
ATOM   3318  CD1 LEU H  45      89.904  11.126   1.389  1.00 32.82           C  
ANISOU 3318  CD1 LEU H  45     3063   5144   4262    233    566    273       C  
ATOM   3319  CD2 LEU H  45      90.592  11.284  -1.010  1.00 19.41           C  
ANISOU 3319  CD2 LEU H  45     1654   3262   2461    282    435    290       C  
ATOM   3320  N   GLU H  46      90.861  16.056  -0.992  1.00 43.44           N  
ANISOU 3320  N   GLU H  46     4835   6213   5458    777    308    291       N  
ATOM   3321  CA  GLU H  46      90.545  17.480  -0.995  1.00 18.21           C  
ANISOU 3321  CA  GLU H  46     1636   3012   2273    934    256    270       C  
ATOM   3322  C   GLU H  46      89.078  17.655  -1.350  1.00 19.69           C  
ANISOU 3322  C   GLU H  46     1691   3325   2465   1000    134    204       C  
ATOM   3323  O   GLU H  46      88.650  17.258  -2.438  1.00 48.21           O  
ANISOU 3323  O   GLU H  46     5341   6946   6030   1002     38    199       O  
ATOM   3324  CB  GLU H  46      91.430  18.243  -1.985  1.00 17.98           C  
ANISOU 3324  CB  GLU H  46     1807   2823   2203   1024    245    334       C  
ATOM   3325  CG  GLU H  46      91.122  19.730  -2.072  1.00 46.26           C  
ANISOU 3325  CG  GLU H  46     5392   6380   5805   1192    197    322       C  
ATOM   3326  CD  GLU H  46      91.923  20.433  -3.153  1.00 49.18           C  
ANISOU 3326  CD  GLU H  46     5959   6588   6137   1284    191    396       C  
ATOM   3327  OE1 GLU H  46      92.534  19.736  -3.991  1.00 42.62           O  
ANISOU 3327  OE1 GLU H  46     5262   5683   5249   1226    205    449       O  
ATOM   3328  OE2 GLU H  46      91.941  21.682  -3.164  1.00 19.09           O  
ANISOU 3328  OE2 GLU H  46     2174   2720   2360   1412    183    401       O  
ATOM   3329  N   TRP H  47      88.313  18.245  -0.437  1.00 47.64           N  
ANISOU 3329  N   TRP H  47     5077   6964   6062   1057    137    151       N  
ATOM   3330  CA  TRP H  47      86.907  18.520  -0.699  1.00 21.73           C  
ANISOU 3330  CA  TRP H  47     1652   3800   2806   1132     26     91       C  
ATOM   3331  C   TRP H  47      86.778  19.639  -1.725  1.00 22.51           C  
ANISOU 3331  C   TRP H  47     1847   3835   2871   1293    -76    110       C  
ATOM   3332  O   TRP H  47      87.384  20.704  -1.576  1.00 39.14           O  
ANISOU 3332  O   TRP H  47     4039   5847   4986   1390    -36    138       O  
ATOM   3333  CB  TRP H  47      86.196  18.897   0.601  1.00 22.13           C  
ANISOU 3333  CB  TRP H  47     1547   3930   2931   1129     77     34       C  
ATOM   3334  CG  TRP H  47      84.783  19.342   0.413  1.00 23.74           C  
ANISOU 3334  CG  TRP H  47     1633   4207   3181   1188    -23    -21       C  
ATOM   3335  CD1 TRP H  47      83.670  18.553   0.389  1.00 38.14           C  
ANISOU 3335  CD1 TRP H  47     3301   6142   5048   1128    -73    -65       C  
ATOM   3336  CD2 TRP H  47      84.326  20.686   0.228  1.00 24.64           C  
ANISOU 3336  CD2 TRP H  47     1772   4272   3317   1311    -77    -33       C  
ATOM   3337  NE1 TRP H  47      82.548  19.322   0.198  1.00 26.23           N  
ANISOU 3337  NE1 TRP H  47     1718   4661   3587   1212   -159    -99       N  
ATOM   3338  CE2 TRP H  47      82.924  20.636   0.095  1.00 26.18           C  
ANISOU 3338  CE2 TRP H  47     1820   4561   3566   1326   -160    -78       C  
ATOM   3339  CE3 TRP H  47      84.966  21.926   0.158  1.00 24.38           C  
ANISOU 3339  CE3 TRP H  47     1869   4116   3278   1399    -58     -8       C  
ATOM   3340  CZ2 TRP H  47      82.152  21.778  -0.103  1.00 35.29           C  
ANISOU 3340  CZ2 TRP H  47     2952   5696   4760   1435   -221    -91       C  
ATOM   3341  CZ3 TRP H  47      84.198  23.059  -0.038  1.00 37.69           C  
ANISOU 3341  CZ3 TRP H  47     3533   5781   5005   1500   -115    -25       C  
ATOM   3342  CH2 TRP H  47      82.806  22.978  -0.166  1.00 33.78           C  
ANISOU 3342  CH2 TRP H  47     2890   5388   4556   1521   -194    -62       C  
ATOM   3343  N   VAL H  48      85.989  19.397  -2.771  1.00 23.68           N  
ANISOU 3343  N   VAL H  48     1980   4033   2983   1324   -210     94       N  
ATOM   3344  CA  VAL H  48      85.839  20.371  -3.848  1.00 31.94           C  
ANISOU 3344  CA  VAL H  48     3127   5026   3981   1482   -315    125       C  
ATOM   3345  C   VAL H  48      84.540  21.147  -3.687  1.00 26.11           C  
ANISOU 3345  C   VAL H  48     2229   4388   3305   1591   -403     74       C  
ATOM   3346  O   VAL H  48      84.560  22.370  -3.507  1.00 44.75           O  
ANISOU 3346  O   VAL H  48     4644   6661   5700   1659   -375     88       O  
ATOM   3347  CB  VAL H  48      85.901  19.697  -5.231  1.00 27.53           C  
ANISOU 3347  CB  VAL H  48     2695   4445   3320   1457   -416    148       C  
ATOM   3348  CG1 VAL H  48      85.567  20.699  -6.325  1.00 26.35           C  
ANISOU 3348  CG1 VAL H  48     2632   4268   3112   1636   -537    182       C  
ATOM   3349  CG2 VAL H  48      87.272  19.097  -5.460  1.00 23.65           C  
ANISOU 3349  CG2 VAL H  48     2391   3821   2774   1359   -312    209       C  
ATOM   3350  N   ALA H  49      83.402  20.458  -3.753  1.00 27.20           N  
ANISOU 3350  N   ALA H  49     2198   4664   3471   1546   -493     13       N  
ATOM   3351  CA  ALA H  49      82.131  21.168  -3.797  1.00 28.87           C  
ANISOU 3351  CA  ALA H  49     2303   4920   3745   1603   -575    -24       C  
ATOM   3352  C   ALA H  49      81.053  20.385  -3.062  1.00 29.55           C  
ANISOU 3352  C   ALA H  49     2174   5129   3925   1495   -572    -94       C  
ATOM   3353  O   ALA H  49      81.232  19.220  -2.698  1.00 51.22           O  
ANISOU 3353  O   ALA H  49     4854   7931   6677   1372   -526   -117       O  
ATOM   3354  CB  ALA H  49      81.698  21.440  -5.242  1.00 30.25           C  
ANISOU 3354  CB  ALA H  49     2548   5100   3845   1708   -743     -2       C  
ATOM   3355  N   TYR H  50      79.924  21.056  -2.840  1.00 30.99           N  
ANISOU 3355  N   TYR H  50     2248   5338   4187   1540   -610   -120       N  
ATOM   3356  CA  TYR H  50      78.727  20.440  -2.286  1.00 39.38           C  
ANISOU 3356  CA  TYR H  50     3111   6499   5353   1457   -619   -175       C  
ATOM   3357  C   TYR H  50      77.503  21.145  -2.852  1.00 35.35           C  
ANISOU 3357  C   TYR H  50     2517   6021   4892   1551   -744   -183       C  
ATOM   3358  O   TYR H  50      77.483  22.375  -2.963  1.00 34.51           O  
ANISOU 3358  O   TYR H  50     2474   5851   4788   1667   -748   -151       O  
ATOM   3359  CB  TYR H  50      78.692  20.504  -0.754  1.00 31.46           C  
ANISOU 3359  CB  TYR H  50     2042   5478   4431   1384   -452   -188       C  
ATOM   3360  CG  TYR H  50      77.307  20.270  -0.181  1.00 44.36           C  
ANISOU 3360  CG  TYR H  50     3486   7183   6186   1342   -453   -225       C  
ATOM   3361  CD1 TYR H  50      76.763  18.994  -0.130  1.00 60.89           C  
ANISOU 3361  CD1 TYR H  50     5457   9350   8329   1221   -465   -253       C  
ATOM   3362  CD2 TYR H  50      76.540  21.326   0.295  1.00 48.60           C  
ANISOU 3362  CD2 TYR H  50     3965   7702   6799   1422   -435   -226       C  
ATOM   3363  CE1 TYR H  50      75.498  18.773   0.386  1.00 34.87           C  
ANISOU 3363  CE1 TYR H  50     1988   6103   5156   1185   -457   -275       C  
ATOM   3364  CE2 TYR H  50      75.273  21.115   0.811  1.00 42.30           C  
ANISOU 3364  CE2 TYR H  50     2991   6963   6119   1392   -427   -249       C  
ATOM   3365  CZ  TYR H  50      74.758  19.836   0.853  1.00 35.92           C  
ANISOU 3365  CZ  TYR H  50     2066   6222   5360   1275   -438   -270       C  
ATOM   3366  OH  TYR H  50      73.499  19.618   1.365  1.00 68.68           O  
ANISOU 3366  OH  TYR H  50     6040  10418   9639   1246   -422   -282       O  
ATOM   3367  N   ILE H  51      76.486  20.357  -3.200  1.00 44.70           N  
ANISOU 3367  N   ILE H  51     3557   7300   6126   1495   -844   -225       N  
ATOM   3368  CA  ILE H  51      75.202  20.878  -3.648  1.00 51.09           C  
ANISOU 3368  CA  ILE H  51     4255   8155   7004   1567   -963   -233       C  
ATOM   3369  C   ILE H  51      74.100  20.185  -2.856  1.00 50.79           C  
ANISOU 3369  C   ILE H  51     4006   8186   7106   1464   -926   -275       C  
ATOM   3370  O   ILE H  51      74.210  19.008  -2.497  1.00 37.99           O  
ANISOU 3370  O   ILE H  51     2329   6599   5508   1330   -877   -305       O  
ATOM   3371  CB  ILE H  51      74.995  20.693  -5.171  1.00 43.65           C  
ANISOU 3371  CB  ILE H  51     3364   7249   5971   1621  -1164   -235       C  
ATOM   3372  CG1 ILE H  51      73.806  21.519  -5.662  1.00 40.96           C  
ANISOU 3372  CG1 ILE H  51     2937   6938   5688   1724  -1282   -222       C  
ATOM   3373  CG2 ILE H  51      74.802  19.224  -5.524  1.00 38.96           C  
ANISOU 3373  CG2 ILE H  51     2695   6734   5373   1487  -1235   -295       C  
ATOM   3374  CD1 ILE H  51      73.572  21.418  -7.152  1.00 42.33           C  
ANISOU 3374  CD1 ILE H  51     3176   7148   5760   1783  -1484   -219       C  
ATOM   3375  N   SER H  52      73.038  20.933  -2.570  1.00 56.32           N  
ANISOU 3375  N   SER H  52     4590   8899   7909   1529   -938   -269       N  
ATOM   3376  CA  SER H  52      71.924  20.415  -1.792  1.00 53.92           C  
ANISOU 3376  CA  SER H  52     4086   8649   7750   1451   -892   -292       C  
ATOM   3377  C   SER H  52      71.047  19.512  -2.657  1.00 45.53           C  
ANISOU 3377  C   SER H  52     2901   7672   6726   1394  -1050   -327       C  
ATOM   3378  O   SER H  52      71.294  19.310  -3.849  1.00 56.60           O  
ANISOU 3378  O   SER H  52     4379   9095   8030   1418  -1201   -340       O  
ATOM   3379  CB  SER H  52      71.113  21.564  -1.200  1.00 67.25           C  
ANISOU 3379  CB  SER H  52     5694  10319   9539   1549   -846   -269       C  
ATOM   3380  OG  SER H  52      70.006  21.076  -0.465  1.00 87.85           O  
ANISOU 3380  OG  SER H  52     8109  12977  12292   1483   -795   -281       O  
ATOM   3381  N   SER H  53      69.998  18.957  -2.043  1.00 44.11           N  
ANISOU 3381  N   SER H  53     2532   7539   6689   1317  -1013   -342       N  
ATOM   3382  CA  SER H  53      69.090  18.086  -2.782  1.00 45.87           C  
ANISOU 3382  CA  SER H  53     2620   7839   6970   1251  -1159   -380       C  
ATOM   3383  C   SER H  53      68.181  18.880  -3.712  1.00 53.03           C  
ANISOU 3383  C   SER H  53     3471   8787   7892   1371  -1337   -371       C  
ATOM   3384  O   SER H  53      67.748  18.358  -4.745  1.00 49.34           O  
ANISOU 3384  O   SER H  53     2966   8377   7403   1348  -1512   -407       O  
ATOM   3385  CB  SER H  53      68.257  17.247  -1.813  1.00 46.63           C  
ANISOU 3385  CB  SER H  53     2531   7962   7224   1133  -1051   -385       C  
ATOM   3386  OG  SER H  53      67.519  18.067  -0.925  1.00 52.32           O  
ANISOU 3386  OG  SER H  53     3154   8673   8053   1202   -955   -345       O  
ATOM   3387  N   GLY H  54      67.884  20.130  -3.367  1.00 61.44           N  
ANISOU 3387  N   GLY H  54     4529   9821   8993   1496  -1296   -325       N  
ATOM   3388  CA  GLY H  54      67.050  20.971  -4.201  1.00 50.52           C  
ANISOU 3388  CA  GLY H  54     3096   8470   7629   1620  -1452   -301       C  
ATOM   3389  C   GLY H  54      67.823  22.107  -4.835  1.00 49.87           C  
ANISOU 3389  C   GLY H  54     3205   8325   7417   1762  -1492   -259       C  
ATOM   3390  O   GLY H  54      67.233  23.086  -5.304  1.00 51.40           O  
ANISOU 3390  O   GLY H  54     3375   8519   7634   1887  -1575   -218       O  
ATOM   3391  N   SER H  55      69.151  21.987  -4.840  1.00 47.67           N  
ANISOU 3391  N   SER H  55     3116   7987   7010   1744  -1425   -260       N  
ATOM   3392  CA  SER H  55      70.061  22.965  -5.434  1.00 46.85           C  
ANISOU 3392  CA  SER H  55     3217   7808   6778   1866  -1442   -213       C  
ATOM   3393  C   SER H  55      69.934  24.346  -4.798  1.00 47.01           C  
ANISOU 3393  C   SER H  55     3240   7759   6864   1979  -1342   -165       C  
ATOM   3394  O   SER H  55      70.322  25.349  -5.406  1.00 47.13           O  
ANISOU 3394  O   SER H  55     3384   7713   6811   2101  -1379   -115       O  
ATOM   3395  CB  SER H  55      69.857  23.064  -6.951  1.00 48.30           C  
ANISOU 3395  CB  SER H  55     3466   8026   6859   1942  -1653   -198       C  
ATOM   3396  OG  SER H  55      69.953  21.790  -7.564  1.00 48.32           O  
ANISOU 3396  OG  SER H  55     3469   8091   6798   1835  -1753   -254       O  
ATOM   3397  N   SER H  56      69.405  24.422  -3.578  1.00 47.11           N  
ANISOU 3397  N   SER H  56     3118   7771   7010   1940  -1208   -178       N  
ATOM   3398  CA  SER H  56      69.216  25.698  -2.901  1.00 47.42           C  
ANISOU 3398  CA  SER H  56     3150   7745   7125   2039  -1107   -146       C  
ATOM   3399  C   SER H  56      70.430  26.133  -2.094  1.00 52.95           C  
ANISOU 3399  C   SER H  56     4004   8347   7769   2031   -941   -146       C  
ATOM   3400  O   SER H  56      70.497  27.297  -1.684  1.00 65.16           O  
ANISOU 3400  O   SER H  56     5586   9819   9354   2120   -867   -124       O  
ATOM   3401  CB  SER H  56      67.994  25.635  -1.977  1.00 48.84           C  
ANISOU 3401  CB  SER H  56     3112   7970   7475   2012  -1040   -157       C  
ATOM   3402  OG  SER H  56      68.225  24.763  -0.885  1.00 47.64           O  
ANISOU 3402  OG  SER H  56     2922   7826   7354   1883   -896   -193       O  
ATOM   3403  N   LEU H  57      71.385  25.236  -1.858  1.00 45.03           N  
ANISOU 3403  N   LEU H  57     3088   7338   6681   1925   -883   -172       N  
ATOM   3404  CA  LEU H  57      72.578  25.555  -1.082  1.00 41.38           C  
ANISOU 3404  CA  LEU H  57     2770   6790   6165   1906   -733   -173       C  
ATOM   3405  C   LEU H  57      73.781  24.926  -1.764  1.00 39.76           C  
ANISOU 3405  C   LEU H  57     2725   6565   5817   1864   -767   -167       C  
ATOM   3406  O   LEU H  57      73.832  23.704  -1.929  1.00 39.37           O  
ANISOU 3406  O   LEU H  57     2639   6578   5740   1761   -799   -193       O  
ATOM   3407  CB  LEU H  57      72.448  25.055   0.359  1.00 40.79           C  
ANISOU 3407  CB  LEU H  57     2609   6728   6162   1803   -573   -208       C  
ATOM   3408  CG  LEU H  57      73.512  25.543   1.341  1.00 41.22           C  
ANISOU 3408  CG  LEU H  57     2791   6695   6175   1789   -417   -214       C  
ATOM   3409  CD1 LEU H  57      73.495  27.061   1.437  1.00 39.70           C  
ANISOU 3409  CD1 LEU H  57     2648   6421   6017   1914   -391   -198       C  
ATOM   3410  CD2 LEU H  57      73.300  24.915   2.706  1.00 47.49           C  
ANISOU 3410  CD2 LEU H  57     3504   7516   7025   1685   -274   -245       C  
ATOM   3411  N   ILE H  58      74.742  25.758  -2.158  1.00 38.92           N  
ANISOU 3411  N   ILE H  58     2794   6363   5631   1943   -754   -129       N  
ATOM   3412  CA  ILE H  58      75.936  25.314  -2.866  1.00 45.72           C  
ANISOU 3412  CA  ILE H  58     3825   7189   6359   1926   -779   -107       C  
ATOM   3413  C   ILE H  58      77.162  25.880  -2.164  1.00 35.75           C  
ANISOU 3413  C   ILE H  58     2702   5813   5068   1921   -634    -93       C  
ATOM   3414  O   ILE H  58      77.183  27.056  -1.784  1.00 36.04           O  
ANISOU 3414  O   ILE H  58     2769   5771   5155   1993   -575    -79       O  
ATOM   3415  CB  ILE H  58      75.911  25.746  -4.348  1.00 38.50           C  
ANISOU 3415  CB  ILE H  58     3007   6258   5362   2036   -931    -58       C  
ATOM   3416  CG1 ILE H  58      74.735  25.093  -5.076  1.00 40.31           C  
ANISOU 3416  CG1 ILE H  58     3100   6606   5611   2027  -1093    -82       C  
ATOM   3417  CG2 ILE H  58      77.219  25.396  -5.033  1.00 37.03           C  
ANISOU 3417  CG2 ILE H  58     3018   6013   5038   2029   -933    -25       C  
ATOM   3418  CD1 ILE H  58      74.683  25.409  -6.554  1.00 74.03           C  
ANISOU 3418  CD1 ILE H  58     7474  10874   9781   2128  -1254    -36       C  
ATOM   3419  N   TYR H  59      78.182  25.041  -1.989  1.00 34.04           N  
ANISOU 3419  N   TYR H  59     2568   5586   4780   1833   -577    -97       N  
ATOM   3420  CA  TYR H  59      79.444  25.459  -1.391  1.00 32.39           C  
ANISOU 3420  CA  TYR H  59     2497   5270   4541   1816   -451    -81       C  
ATOM   3421  C   TYR H  59      80.595  25.015  -2.281  1.00 48.01           C  
ANISOU 3421  C   TYR H  59     4639   7200   6405   1814   -479    -36       C  
ATOM   3422  O   TYR H  59      80.632  23.864  -2.726  1.00 53.42           O  
ANISOU 3422  O   TYR H  59     5303   7958   7036   1755   -532    -43       O  
ATOM   3423  CB  TYR H  59      79.617  24.881   0.018  1.00 31.42           C  
ANISOU 3423  CB  TYR H  59     2307   5173   4458   1697   -318   -125       C  
ATOM   3424  CG  TYR H  59      78.756  25.539   1.072  1.00 32.37           C  
ANISOU 3424  CG  TYR H  59     2315   5303   4682   1709   -251   -160       C  
ATOM   3425  CD1 TYR H  59      79.061  26.805   1.554  1.00 32.41           C  
ANISOU 3425  CD1 TYR H  59     2383   5211   4720   1774   -186   -161       C  
ATOM   3426  CD2 TYR H  59      77.647  24.890   1.597  1.00 43.22           C  
ANISOU 3426  CD2 TYR H  59     3519   6775   6128   1653   -247   -193       C  
ATOM   3427  CE1 TYR H  59      78.282  27.410   2.522  1.00 33.37           C  
ANISOU 3427  CE1 TYR H  59     2405   5341   4933   1791   -120   -196       C  
ATOM   3428  CE2 TYR H  59      76.861  25.486   2.566  1.00 42.30           C  
ANISOU 3428  CE2 TYR H  59     3306   6662   6105   1672   -176   -219       C  
ATOM   3429  CZ  TYR H  59      77.183  26.747   3.024  1.00 44.00           C  
ANISOU 3429  CZ  TYR H  59     3589   6787   6340   1745   -113   -222       C  
ATOM   3430  OH  TYR H  59      76.404  27.346   3.988  1.00 37.40           O  
ANISOU 3430  OH  TYR H  59     2660   5955   5595   1770    -38   -251       O  
ATOM   3431  N   TYR H  60      81.530  25.928  -2.534  1.00 51.33           N  
ANISOU 3431  N   TYR H  60     5219   7487   6795   1875   -436     11       N  
ATOM   3432  CA  TYR H  60      82.727  25.638  -3.310  1.00 37.79           C  
ANISOU 3432  CA  TYR H  60     3681   5696   4982   1876   -434     66       C  
ATOM   3433  C   TYR H  60      83.963  25.778  -2.433  1.00 50.79           C  
ANISOU 3433  C   TYR H  60     5415   7242   6640   1809   -292     70       C  
ATOM   3434  O   TYR H  60      83.996  26.588  -1.501  1.00 61.32           O  
ANISOU 3434  O   TYR H  60     6725   8526   8049   1802   -213     41       O  
ATOM   3435  CB  TYR H  60      82.863  26.576  -4.517  1.00 30.42           C  
ANISOU 3435  CB  TYR H  60     2884   4671   4004   1995   -502    133       C  
ATOM   3436  CG  TYR H  60      81.790  26.415  -5.566  1.00 32.15           C  
ANISOU 3436  CG  TYR H  60     3049   4982   4185   2065   -661    140       C  
ATOM   3437  CD1 TYR H  60      81.844  25.380  -6.489  1.00 32.22           C  
ANISOU 3437  CD1 TYR H  60     3100   5054   4089   2050   -759    149       C  
ATOM   3438  CD2 TYR H  60      80.734  27.310  -5.647  1.00 52.70           C  
ANISOU 3438  CD2 TYR H  60     5560   7605   6857   2147   -717    136       C  
ATOM   3439  CE1 TYR H  60      80.868  25.233  -7.454  1.00 33.96           C  
ANISOU 3439  CE1 TYR H  60     3274   5360   4270   2105   -919    145       C  
ATOM   3440  CE2 TYR H  60      79.755  27.174  -6.610  1.00 53.83           C  
ANISOU 3440  CE2 TYR H  60     5651   7833   6967   2208   -870    144       C  
ATOM   3441  CZ  TYR H  60      79.825  26.133  -7.510  1.00 53.67           C  
ANISOU 3441  CZ  TYR H  60     5675   7879   6838   2184   -975    145       C  
ATOM   3442  OH  TYR H  60      78.848  25.994  -8.470  1.00 66.79           O  
ANISOU 3442  OH  TYR H  60     7287   9628   8464   2236  -1140    143       O  
ATOM   3443  N   ALA H  61      84.981  24.979  -2.739  1.00 50.64           N  
ANISOU 3443  N   ALA H  61     5499   7192   6549   1759   -262    105       N  
ATOM   3444  CA  ALA H  61      86.282  25.170  -2.120  1.00 43.49           C  
ANISOU 3444  CA  ALA H  61     4701   6171   5653   1700   -141    124       C  
ATOM   3445  C   ALA H  61      86.966  26.391  -2.721  1.00 53.39           C  
ANISOU 3445  C   ALA H  61     6111   7263   6914   1767   -126    175       C  
ATOM   3446  O   ALA H  61      86.760  26.732  -3.890  1.00 57.47           O  
ANISOU 3446  O   ALA H  61     6702   7749   7384   1850   -201    224       O  
ATOM   3447  CB  ALA H  61      87.156  23.930  -2.303  1.00 32.89           C  
ANISOU 3447  CB  ALA H  61     3418   4835   4243   1626   -106    158       C  
ATOM   3448  N   ASP H  62      87.787  27.057  -1.905  1.00 40.09           N  
ANISOU 3448  N   ASP H  62     4469   5474   5288   1720    -30    160       N  
ATOM   3449  CA  ASP H  62      88.434  28.288  -2.350  1.00 42.28           C  
ANISOU 3449  CA  ASP H  62     4868   5597   5601   1761     -8    197       C  
ATOM   3450  C   ASP H  62      89.314  28.058  -3.572  1.00 40.52           C  
ANISOU 3450  C   ASP H  62     4812   5282   5301   1765    -13    282       C  
ATOM   3451  O   ASP H  62      89.511  28.977  -4.376  1.00 25.13           O  
ANISOU 3451  O   ASP H  62     2954   3235   3358   1820    -24    328       O  
ATOM   3452  CB  ASP H  62      89.256  28.889  -1.210  1.00 44.62           C  
ANISOU 3452  CB  ASP H  62     5169   5809   5977   1689     85    151       C  
ATOM   3453  CG  ASP H  62      88.402  29.293  -0.025  1.00 50.38           C  
ANISOU 3453  CG  ASP H  62     5753   6609   6778   1692    101     67       C  
ATOM   3454  OD1 ASP H  62      87.185  29.011  -0.044  1.00 58.32           O  
ANISOU 3454  OD1 ASP H  62     6646   7735   7779   1735     49     47       O  
ATOM   3455  OD2 ASP H  62      88.947  29.895   0.924  1.00 53.87           O  
ANISOU 3455  OD2 ASP H  62     6194   6988   7285   1648    165     18       O  
ATOM   3456  N   THR H  63      89.842  26.844  -3.736  1.00 55.03           N  
ANISOU 3456  N   THR H  63     6693   7148   7070   1705      5    308       N  
ATOM   3457  CA  THR H  63      90.721  26.567  -4.866  1.00 37.76           C  
ANISOU 3457  CA  THR H  63     4675   4865   4808   1698     16    388       C  
ATOM   3458  C   THR H  63      89.956  26.577  -6.184  1.00 43.42           C  
ANISOU 3458  C   THR H  63     5434   5621   5440   1801    -89    428       C  
ATOM   3459  O   THR H  63      90.462  27.076  -7.197  1.00 68.43           O  
ANISOU 3459  O   THR H  63     8743   8689   8569   1828    -83    489       O  
ATOM   3460  CB  THR H  63      91.421  25.224  -4.667  1.00 41.63           C  
ANISOU 3460  CB  THR H  63     5193   5372   5252   1610     67    406       C  
ATOM   3461  OG1 THR H  63      90.437  24.193  -4.509  1.00 63.02           O  
ANISOU 3461  OG1 THR H  63     7775   8247   7925   1629      0    373       O  
ATOM   3462  CG2 THR H  63      92.304  25.265  -3.431  1.00 38.86           C  
ANISOU 3462  CG2 THR H  63     4817   4974   4975   1505    167    376       C  
ATOM   3463  N   VAL H  64      88.735  26.037  -6.193  1.00 37.50           N  
ANISOU 3463  N   VAL H  64     4558   5026   4665   1851   -191    388       N  
ATOM   3464  CA  VAL H  64      87.954  25.927  -7.419  1.00 47.69           C  
ANISOU 3464  CA  VAL H  64     5878   6377   5866   1943   -318    415       C  
ATOM   3465  C   VAL H  64      86.839  26.957  -7.500  1.00 46.11           C  
ANISOU 3465  C   VAL H  64     5584   6220   5717   2036   -393    394       C  
ATOM   3466  O   VAL H  64      86.145  27.022  -8.524  1.00 46.87           O  
ANISOU 3466  O   VAL H  64     5700   6364   5744   2118   -507    417       O  
ATOM   3467  CB  VAL H  64      87.366  24.511  -7.576  1.00 45.82           C  
ANISOU 3467  CB  VAL H  64     5560   6290   5560   1923   -410    382       C  
ATOM   3468  CG1 VAL H  64      88.457  23.464  -7.418  1.00 53.94           C  
ANISOU 3468  CG1 VAL H  64     6672   7271   6550   1833   -324    410       C  
ATOM   3469  CG2 VAL H  64      86.243  24.288  -6.574  1.00 34.23           C  
ANISOU 3469  CG2 VAL H  64     3856   4975   4174   1902   -449    294       C  
ATOM   3470  N   LYS H  65      86.640  27.761  -6.458  1.00 47.09           N  
ANISOU 3470  N   LYS H  65     5609   6325   5957   2026   -334    351       N  
ATOM   3471  CA  LYS H  65      85.562  28.741  -6.473  1.00 45.74           C  
ANISOU 3471  CA  LYS H  65     5344   6186   5849   2114   -393    335       C  
ATOM   3472  C   LYS H  65      85.825  29.804  -7.531  1.00 36.23           C  
ANISOU 3472  C   LYS H  65     4273   4868   4623   2198   -404    411       C  
ATOM   3473  O   LYS H  65      86.951  30.282  -7.692  1.00 59.71           O  
ANISOU 3473  O   LYS H  65     7379   7702   7604   2165   -314    453       O  
ATOM   3474  CB  LYS H  65      85.403  29.389  -5.099  1.00 37.69           C  
ANISOU 3474  CB  LYS H  65     4211   5154   4958   2078   -312    271       C  
ATOM   3475  CG  LYS H  65      84.176  30.277  -4.984  1.00 40.09           C  
ANISOU 3475  CG  LYS H  65     4393   5500   5339   2164   -366    249       C  
ATOM   3476  CD  LYS H  65      83.757  30.476  -3.537  1.00 60.75           C  
ANISOU 3476  CD  LYS H  65     6867   8154   8062   2117   -297    168       C  
ATOM   3477  CE  LYS H  65      82.416  31.192  -3.453  1.00 78.50           C  
ANISOU 3477  CE  LYS H  65     8980  10457  10388   2201   -351    148       C  
ATOM   3478  NZ  LYS H  65      81.906  31.278  -2.057  1.00 80.70           N  
ANISOU 3478  NZ  LYS H  65     9120  10782  10761   2154   -280     69       N  
ATOM   3479  N   GLY H  66      84.773  30.171  -8.259  1.00 32.55           N  
ANISOU 3479  N   GLY H  66     3764   4467   4138   2300   -516    429       N  
ATOM   3480  CA  GLY H  66      84.891  31.082  -9.374  1.00 33.78           C  
ANISOU 3480  CA  GLY H  66     4040   4537   4257   2390   -538    509       C  
ATOM   3481  C   GLY H  66      85.187  30.421 -10.701  1.00 34.12           C  
ANISOU 3481  C   GLY H  66     4227   4591   4145   2414   -602    566       C  
ATOM   3482  O   GLY H  66      85.128  31.096 -11.738  1.00 35.45           O  
ANISOU 3482  O   GLY H  66     4491   4714   4264   2500   -636    634       O  
ATOM   3483  N   ARG H  67      85.501  29.127 -10.704  1.00 33.06           N  
ANISOU 3483  N   ARG H  67     4116   4515   3932   2343   -617    542       N  
ATOM   3484  CA  ARG H  67      85.788  28.384 -11.925  1.00 33.40           C  
ANISOU 3484  CA  ARG H  67     4301   4568   3820   2356   -678    583       C  
ATOM   3485  C   ARG H  67      84.880  27.178 -12.099  1.00 33.91           C  
ANISOU 3485  C   ARG H  67     4268   4802   3815   2347   -824    525       C  
ATOM   3486  O   ARG H  67      84.269  27.016 -13.161  1.00 67.57           O  
ANISOU 3486  O   ARG H  67     8567   9131   7976   2412   -956    538       O  
ATOM   3487  CB  ARG H  67      87.256  27.931 -11.937  1.00 31.67           C  
ANISOU 3487  CB  ARG H  67     4236   4229   3570   2262   -545    616       C  
ATOM   3488  CG  ARG H  67      88.264  29.047 -11.744  1.00 31.13           C  
ANISOU 3488  CG  ARG H  67     4247   3996   3585   2237   -403    660       C  
ATOM   3489  CD  ARG H  67      89.673  28.498 -11.821  1.00 29.58           C  
ANISOU 3489  CD  ARG H  67     4183   3695   3361   2130   -283    686       C  
ATOM   3490  NE  ARG H  67      89.857  27.373 -10.910  1.00 34.84           N  
ANISOU 3490  NE  ARG H  67     4781   4413   4042   2038   -262    635       N  
ATOM   3491  CZ  ARG H  67      90.868  26.513 -10.981  1.00 38.19           C  
ANISOU 3491  CZ  ARG H  67     5300   4782   4428   1943   -185    652       C  
ATOM   3492  NH1 ARG H  67      91.788  26.646 -11.926  1.00 45.07           N  
ANISOU 3492  NH1 ARG H  67     6331   5548   5244   1921   -120    708       N  
ATOM   3493  NH2 ARG H  67      90.955  25.517 -10.110  1.00 38.75           N  
ANISOU 3493  NH2 ARG H  67     5297   4906   4519   1870   -167    612       N  
ATOM   3494  N   PHE H  68      84.775  26.324 -11.086  1.00 32.75           N  
ANISOU 3494  N   PHE H  68     3992   4730   3722   2261   -808    455       N  
ATOM   3495  CA  PHE H  68      83.961  25.124 -11.194  1.00 33.71           C  
ANISOU 3495  CA  PHE H  68     3999   5013   3795   2227   -942    388       C  
ATOM   3496  C   PHE H  68      82.501  25.444 -10.895  1.00 34.78           C  
ANISOU 3496  C   PHE H  68     3923   5276   4014   2265  -1050    331       C  
ATOM   3497  O   PHE H  68      82.186  26.368 -10.139  1.00 41.60           O  
ANISOU 3497  O   PHE H  68     4697   6113   4997   2291   -988    326       O  
ATOM   3498  CB  PHE H  68      84.461  24.034 -10.242  1.00 36.14           C  
ANISOU 3498  CB  PHE H  68     4242   5354   4136   2111   -869    342       C  
ATOM   3499  CG  PHE H  68      85.786  23.426 -10.637  1.00 36.08           C  
ANISOU 3499  CG  PHE H  68     4432   5239   4038   2063   -785    398       C  
ATOM   3500  CD1 PHE H  68      86.588  24.016 -11.602  1.00 36.46           C  
ANISOU 3500  CD1 PHE H  68     4698   5145   4010   2107   -736    481       C  
ATOM   3501  CD2 PHE H  68      86.220  22.252 -10.044  1.00 28.75           C  
ANISOU 3501  CD2 PHE H  68     3464   4351   3110   1967   -744    370       C  
ATOM   3502  CE1 PHE H  68      87.800  23.456 -11.958  1.00 29.14           C  
ANISOU 3502  CE1 PHE H  68     3949   4107   3015   2047   -641    531       C  
ATOM   3503  CE2 PHE H  68      87.430  21.685 -10.398  1.00 35.22           C  
ANISOU 3503  CE2 PHE H  68     4469   5057   3856   1916   -656    430       C  
ATOM   3504  CZ  PHE H  68      88.220  22.287 -11.357  1.00 30.79           C  
ANISOU 3504  CZ  PHE H  68     4129   4345   3225   1954   -602    509       C  
ATOM   3505  N   THR H  69      81.607  24.666 -11.501  1.00 36.06           N  
ANISOU 3505  N   THR H  69     4009   5573   4120   2259  -1212    284       N  
ATOM   3506  CA  THR H  69      80.167  24.871 -11.364  1.00 37.79           C  
ANISOU 3506  CA  THR H  69     4026   5913   4421   2285  -1326    232       C  
ATOM   3507  C   THR H  69      79.513  23.513 -11.160  1.00 42.13           C  
ANISOU 3507  C   THR H  69     4418   6609   4982   2176  -1421    136       C  
ATOM   3508  O   THR H  69      79.434  22.714 -12.099  1.00 58.52           O  
ANISOU 3508  O   THR H  69     6553   8738   6944   2156  -1544    114       O  
ATOM   3509  CB  THR H  69      79.584  25.573 -12.592  1.00 39.94           C  
ANISOU 3509  CB  THR H  69     4366   6189   4619   2403  -1454    282       C  
ATOM   3510  OG1 THR H  69      80.264  26.816 -12.805  1.00 56.85           O  
ANISOU 3510  OG1 THR H  69     6656   8186   6759   2491  -1351    374       O  
ATOM   3511  CG2 THR H  69      78.100  25.839 -12.396  1.00 41.80           C  
ANISOU 3511  CG2 THR H  69     4384   6539   4958   2431  -1564    238       C  
ATOM   3512  N   ILE H  70      79.044  23.254  -9.945  1.00 37.44           N  
ANISOU 3512  N   ILE H  70     3625   6074   4527   2098  -1356     74       N  
ATOM   3513  CA  ILE H  70      78.395  21.991  -9.617  1.00 43.22           C  
ANISOU 3513  CA  ILE H  70     4181   6935   5304   1974  -1417    -18       C  
ATOM   3514  C   ILE H  70      76.899  22.125  -9.873  1.00 45.81           C  
ANISOU 3514  C   ILE H  70     4335   7365   5707   1993  -1555    -59       C  
ATOM   3515  O   ILE H  70      76.263  23.090  -9.429  1.00 40.70           O  
ANISOU 3515  O   ILE H  70     3600   6705   5160   2059  -1526    -39       O  
ATOM   3516  CB  ILE H  70      78.686  21.584  -8.161  1.00 36.72           C  
ANISOU 3516  CB  ILE H  70     3241   6117   4593   1867  -1255    -54       C  
ATOM   3517  CG1 ILE H  70      77.937  20.302  -7.792  1.00 42.46           C  
ANISOU 3517  CG1 ILE H  70     3772   6970   5392   1726  -1298   -145       C  
ATOM   3518  CG2 ILE H  70      78.345  22.713  -7.197  1.00 36.06           C  
ANISOU 3518  CG2 ILE H  70     3083   5989   4630   1914  -1148    -38       C  
ATOM   3519  CD1 ILE H  70      78.288  19.774  -6.417  1.00 39.08           C  
ANISOU 3519  CD1 ILE H  70     3246   6546   5056   1609  -1126   -170       C  
ATOM   3520  N   SER H  71      76.339  21.169 -10.609  1.00 55.55           N  
ANISOU 3520  N   SER H  71     5518   8692   6895   1935  -1707   -118       N  
ATOM   3521  CA  SER H  71      74.926  21.170 -10.957  1.00 51.27           C  
ANISOU 3521  CA  SER H  71     4809   8247   6423   1943  -1854   -159       C  
ATOM   3522  C   SER H  71      74.341  19.786 -10.701  1.00 55.92           C  
ANISOU 3522  C   SER H  71     5228   8936   7082   1783  -1904   -261       C  
ATOM   3523  O   SER H  71      75.063  18.816 -10.450  1.00 56.14           O  
ANISOU 3523  O   SER H  71     5288   8961   7081   1674  -1845   -300       O  
ATOM   3524  CB  SER H  71      74.709  21.596 -12.416  1.00 49.15           C  
ANISOU 3524  CB  SER H  71     4673   7983   6017   2053  -2022   -120       C  
ATOM   3525  OG  SER H  71      75.668  21.003 -13.273  1.00 44.73           O  
ANISOU 3525  OG  SER H  71     4323   7389   5284   2039  -2055   -115       O  
ATOM   3526  N   ARG H  72      73.015  19.700 -10.774  1.00 45.85           N  
ANISOU 3526  N   ARG H  72     3765   7745   5912   1765  -2011   -302       N  
ATOM   3527  CA  ARG H  72      72.298  18.504 -10.358  1.00 56.24           C  
ANISOU 3527  CA  ARG H  72     4885   9141   7343   1607  -2032   -393       C  
ATOM   3528  C   ARG H  72      71.116  18.252 -11.282  1.00 75.29           C  
ANISOU 3528  C   ARG H  72     7198  11640   9769   1608  -2240   -438       C  
ATOM   3529  O   ARG H  72      70.471  19.194 -11.750  1.00 93.72           O  
ANISOU 3529  O   ARG H  72     9520  13987  12101   1731  -2330   -390       O  
ATOM   3530  CB  ARG H  72      71.819  18.646  -8.908  1.00 53.41           C  
ANISOU 3530  CB  ARG H  72     4341   8781   7172   1556  -1869   -391       C  
ATOM   3531  CG  ARG H  72      71.232  17.392  -8.298  1.00 46.19           C  
ANISOU 3531  CG  ARG H  72     3237   7924   6389   1383  -1836   -466       C  
ATOM   3532  CD  ARG H  72      71.224  17.509  -6.786  1.00 45.03           C  
ANISOU 3532  CD  ARG H  72     2988   7746   6375   1335  -1623   -443       C  
ATOM   3533  NE  ARG H  72      70.693  16.314  -6.143  1.00 60.05           N  
ANISOU 3533  NE  ARG H  72     4722   9687   8408   1170  -1564   -495       N  
ATOM   3534  CZ  ARG H  72      70.964  15.962  -4.891  1.00 60.31           C  
ANISOU 3534  CZ  ARG H  72     4706   9689   8522   1085  -1367   -481       C  
ATOM   3535  NH1 ARG H  72      71.771  16.709  -4.149  1.00 55.72           N  
ANISOU 3535  NH1 ARG H  72     4228   9044   7900   1146  -1220   -429       N  
ATOM   3536  NH2 ARG H  72      70.436  14.857  -4.382  1.00 70.37           N  
ANISOU 3536  NH2 ARG H  72     5834  10989   9914    939  -1312   -515       N  
ATOM   3537  N   ASP H  73      70.839  16.972 -11.540  1.00 69.59           N  
ANISOU 3537  N   ASP H  73     6401  10974   9066   1465  -2316   -531       N  
ATOM   3538  CA  ASP H  73      69.704  16.539 -12.357  1.00 52.40           C  
ANISOU 3538  CA  ASP H  73     4112   8882   6916   1434  -2514   -592       C  
ATOM   3539  C   ASP H  73      69.023  15.394 -11.610  1.00 52.77           C  
ANISOU 3539  C   ASP H  73     3936   8971   7144   1256  -2468   -673       C  
ATOM   3540  O   ASP H  73      69.426  14.233 -11.730  1.00 78.13           O  
ANISOU 3540  O   ASP H  73     7167  12181  10337   1119  -2467   -748       O  
ATOM   3541  CB  ASP H  73      70.157  16.121 -13.756  1.00 65.42           C  
ANISOU 3541  CB  ASP H  73     5953  10541   8364   1446  -2678   -628       C  
ATOM   3542  CG  ASP H  73      69.007  16.033 -14.745  1.00 72.35           C  
ANISOU 3542  CG  ASP H  73     6751  11505   9235   1463  -2901   -671       C  
ATOM   3543  OD1 ASP H  73      67.863  15.772 -14.318  1.00 75.99           O  
ANISOU 3543  OD1 ASP H  73     6974  12026   9872   1399  -2933   -709       O  
ATOM   3544  OD2 ASP H  73      69.248  16.225 -15.956  1.00 70.88           O  
ANISOU 3544  OD2 ASP H  73     6742  11325   8864   1541  -3040   -663       O  
ATOM   3545  N   ASN H  74      67.991  15.730 -10.835  1.00 53.79           N  
ANISOU 3545  N   ASN H  74     3856   9129   7453   1258  -2420   -652       N  
ATOM   3546  CA  ASN H  74      67.247  14.760 -10.037  1.00 54.34           C  
ANISOU 3546  CA  ASN H  74     3706   9228   7712   1102  -2352   -705       C  
ATOM   3547  C   ASN H  74      66.376  13.836 -10.889  1.00 65.46           C  
ANISOU 3547  C   ASN H  74     5011  10707   9153   1008  -2540   -796       C  
ATOM   3548  O   ASN H  74      66.335  12.629 -10.615  1.00 56.66           O  
ANISOU 3548  O   ASN H  74     3817   9591   8119    843  -2497   -867       O  
ATOM   3549  CB  ASN H  74      66.390  15.475  -8.988  1.00 70.83           C  
ANISOU 3549  CB  ASN H  74     5618  11322   9972   1148  -2240   -643       C  
ATOM   3550  CG  ASN H  74      67.214  16.035  -7.846  1.00 52.45           C  
ANISOU 3550  CG  ASN H  74     3360   8920   7650   1181  -2015   -578       C  
ATOM   3551  OD1 ASN H  74      68.289  15.525  -7.534  1.00 50.34           O  
ANISOU 3551  OD1 ASN H  74     3206   8604   7315   1115  -1906   -588       O  
ATOM   3552  ND2 ASN H  74      66.709  17.086  -7.211  1.00 52.85           N  
ANISOU 3552  ND2 ASN H  74     3340   8959   7782   1283  -1943   -513       N  
ATOM   3553  N   PRO H  75      65.653  14.333 -11.903  1.00 59.46           N  
ANISOU 3553  N   PRO H  75     4244  10006   8341   1101  -2743   -798       N  
ATOM   3554  CA  PRO H  75      64.884  13.411 -12.758  1.00 61.48           C  
ANISOU 3554  CA  PRO H  75     4414  10329   8616   1005  -2932   -897       C  
ATOM   3555  C   PRO H  75      65.732  12.354 -13.445  1.00 60.76           C  
ANISOU 3555  C   PRO H  75     4478  10214   8393    899  -2982   -987       C  
ATOM   3556  O   PRO H  75      65.191  11.320 -13.854  1.00 62.37           O  
ANISOU 3556  O   PRO H  75     4592  10454   8653    770  -3083  -1088       O  
ATOM   3557  CB  PRO H  75      64.225  14.346 -13.779  1.00 64.27           C  
ANISOU 3557  CB  PRO H  75     4789  10743   8887   1158  -3134   -863       C  
ATOM   3558  CG  PRO H  75      64.101  15.632 -13.067  1.00 75.77           C  
ANISOU 3558  CG  PRO H  75     6213  12175  10401   1298  -3022   -748       C  
ATOM   3559  CD  PRO H  75      65.336  15.739 -12.224  1.00 59.95           C  
ANISOU 3559  CD  PRO H  75     4342  10080   8358   1290  -2806   -710       C  
ATOM   3560  N   LYS H  76      67.038  12.574 -13.588  1.00 58.50           N  
ANISOU 3560  N   LYS H  76     4421   9865   7940    947  -2913   -956       N  
ATOM   3561  CA  LYS H  76      67.928  11.594 -14.191  1.00 57.68           C  
ANISOU 3561  CA  LYS H  76     4477   9730   7708    850  -2941  -1035       C  
ATOM   3562  C   LYS H  76      68.933  11.017 -13.205  1.00 62.43           C  
ANISOU 3562  C   LYS H  76     5107  10260   8353    748  -2723  -1030       C  
ATOM   3563  O   LYS H  76      69.765  10.195 -13.603  1.00 65.23           O  
ANISOU 3563  O   LYS H  76     5593  10579   8611    662  -2722  -1090       O  
ATOM   3564  CB  LYS H  76      68.663  12.214 -15.386  1.00 57.69           C  
ANISOU 3564  CB  LYS H  76     4749   9719   7451    988  -3060  -1003       C  
ATOM   3565  CG  LYS H  76      67.735  12.642 -16.511  1.00 67.15           C  
ANISOU 3565  CG  LYS H  76     5940  10993   8579   1078  -3288  -1013       C  
ATOM   3566  CD  LYS H  76      68.498  12.950 -17.787  1.00 65.78           C  
ANISOU 3566  CD  LYS H  76     6054  10804   8136   1182  -3399   -995       C  
ATOM   3567  CE  LYS H  76      67.544  13.229 -18.938  1.00 73.33           C  
ANISOU 3567  CE  LYS H  76     6999  11845   9019   1254  -3633  -1014       C  
ATOM   3568  NZ  LYS H  76      68.262  13.401 -20.231  1.00 79.76           N  
ANISOU 3568  NZ  LYS H  76     8102  12645   9560   1343  -3733  -1000       N  
ATOM   3569  N   ASN H  77      68.872  11.420 -11.932  1.00 58.97           N  
ANISOU 3569  N   ASN H  77     4553   9799   8055    755  -2535   -959       N  
ATOM   3570  CA  ASN H  77      69.741  10.890 -10.878  1.00 59.02           C  
ANISOU 3570  CA  ASN H  77     4565   9744   8115    657  -2315   -944       C  
ATOM   3571  C   ASN H  77      71.217  11.054 -11.241  1.00 57.47           C  
ANISOU 3571  C   ASN H  77     4619   9495   7723    709  -2278   -920       C  
ATOM   3572  O   ASN H  77      72.011  10.114 -11.156  1.00 47.68           O  
ANISOU 3572  O   ASN H  77     3436   8219   6459    589  -2207   -965       O  
ATOM   3573  CB  ASN H  77      69.413   9.424 -10.578  1.00 51.60           C  
ANISOU 3573  CB  ASN H  77     3490   8801   7316    449  -2271  -1032       C  
ATOM   3574  CG  ASN H  77      67.938   9.196 -10.311  1.00 65.07           C  
ANISOU 3574  CG  ASN H  77     4953  10557   9213    397  -2316  -1053       C  
ATOM   3575  OD1 ASN H  77      67.322   8.302 -10.892  1.00 55.84           O  
ANISOU 3575  OD1 ASN H  77     3706   9414   8097    290  -2434  -1146       O  
ATOM   3576  ND2 ASN H  77      67.364  10.005  -9.429  1.00 74.05           N  
ANISOU 3576  ND2 ASN H  77     5972  11707  10457    474  -2220   -969       N  
ATOM   3577  N   THR H  78      71.588  12.266 -11.648  1.00 61.20           N  
ANISOU 3577  N   THR H  78     5240   9955   8060    889  -2318   -841       N  
ATOM   3578  CA  THR H  78      72.937  12.532 -12.124  1.00 46.89           C  
ANISOU 3578  CA  THR H  78     3681   8086   6048    961  -2296   -801       C  
ATOM   3579  C   THR H  78      73.479  13.805 -11.493  1.00 45.36           C  
ANISOU 3579  C   THR H  78     3560   7843   5833   1108  -2166   -683       C  
ATOM   3580  O   THR H  78      72.767  14.807 -11.380  1.00 46.37           O  
ANISOU 3580  O   THR H  78     3624   7984   6011   1218  -2190   -631       O  
ATOM   3581  CB  THR H  78      72.973  12.655 -13.655  1.00 48.41           C  
ANISOU 3581  CB  THR H  78     4058   8291   6045   1041  -2502   -823       C  
ATOM   3582  OG1 THR H  78      72.334  11.515 -14.242  1.00 56.20           O  
ANISOU 3582  OG1 THR H  78     4967   9325   7063    903  -2633   -945       O  
ATOM   3583  CG2 THR H  78      74.408  12.726 -14.151  1.00 51.87           C  
ANISOU 3583  CG2 THR H  78     4774   8657   6276   1095  -2462   -781       C  
ATOM   3584  N   LEU H  79      74.742  13.753 -11.082  1.00 43.02           N  
ANISOU 3584  N   LEU H  79     3393   7486   5467   1104  -2027   -643       N  
ATOM   3585  CA  LEU H  79      75.462  14.912 -10.576  1.00 41.49           C  
ANISOU 3585  CA  LEU H  79     3304   7227   5234   1237  -1901   -535       C  
ATOM   3586  C   LEU H  79      76.441  15.396 -11.637  1.00 41.06           C  
ANISOU 3586  C   LEU H  79     3529   7109   4963   1359  -1963   -476       C  
ATOM   3587  O   LEU H  79      77.032  14.590 -12.361  1.00 40.87           O  
ANISOU 3587  O   LEU H  79     3634   7077   4816   1305  -2023   -516       O  
ATOM   3588  CB  LEU H  79      76.205  14.566  -9.284  1.00 39.27           C  
ANISOU 3588  CB  LEU H  79     2971   6915   5035   1150  -1684   -516       C  
ATOM   3589  CG  LEU H  79      76.964  15.686  -8.570  1.00 37.66           C  
ANISOU 3589  CG  LEU H  79     2858   6636   4815   1264  -1532   -416       C  
ATOM   3590  CD1 LEU H  79      76.002  16.748  -8.065  1.00 38.72           C  
ANISOU 3590  CD1 LEU H  79     2881   6773   5058   1348  -1516   -386       C  
ATOM   3591  CD2 LEU H  79      77.790  15.116  -7.430  1.00 35.60           C  
ANISOU 3591  CD2 LEU H  79     2570   6347   4610   1152  -1328   -402       C  
ATOM   3592  N   PHE H  80      76.604  16.714 -11.738  1.00 41.02           N  
ANISOU 3592  N   PHE H  80     3625   7045   4915   1520  -1936   -379       N  
ATOM   3593  CA  PHE H  80      77.470  17.306 -12.748  1.00 53.60           C  
ANISOU 3593  CA  PHE H  80     5492   8556   6316   1645  -1969   -300       C  
ATOM   3594  C   PHE H  80      78.458  18.267 -12.103  1.00 48.75           C  
ANISOU 3594  C   PHE H  80     4990   7830   5702   1735  -1791   -193       C  
ATOM   3595  O   PHE H  80      78.145  18.939 -11.115  1.00 52.05           O  
ANISOU 3595  O   PHE H  80     5281   8241   6256   1755  -1689   -174       O  
ATOM   3596  CB  PHE H  80      76.662  18.049 -13.821  1.00 60.06           C  
ANISOU 3596  CB  PHE H  80     6354   9396   7070   1762  -2128   -276       C  
ATOM   3597  CG  PHE H  80      75.828  17.151 -14.688  1.00 58.54           C  
ANISOU 3597  CG  PHE H  80     6102   9299   6841   1687  -2320   -375       C  
ATOM   3598  CD1 PHE H  80      76.399  16.467 -15.748  1.00 57.07           C  
ANISOU 3598  CD1 PHE H  80     6111   9097   6476   1662  -2403   -404       C  
ATOM   3599  CD2 PHE H  80      74.472  17.000 -14.451  1.00 59.26           C  
ANISOU 3599  CD2 PHE H  80     5950   9487   7081   1640  -2411   -439       C  
ATOM   3600  CE1 PHE H  80      75.634  15.643 -16.551  1.00 61.10           C  
ANISOU 3600  CE1 PHE H  80     6572   9689   6952   1586  -2580   -506       C  
ATOM   3601  CE2 PHE H  80      73.701  16.177 -15.251  1.00 49.02           C  
ANISOU 3601  CE2 PHE H  80     4594   8269   5760   1565  -2588   -533       C  
ATOM   3602  CZ  PHE H  80      74.283  15.499 -16.303  1.00 61.14           C  
ANISOU 3602  CZ  PHE H  80     6324   9792   7115   1536  -2676   -572       C  
ATOM   3603  N   LEU H  81      79.656  18.330 -12.685  1.00 55.33           N  
ANISOU 3603  N   LEU H  81     6075   8565   6385   1783  -1747   -125       N  
ATOM   3604  CA  LEU H  81      80.695  19.261 -12.249  1.00 56.69           C  
ANISOU 3604  CA  LEU H  81     6386   8603   6552   1865  -1578    -17       C  
ATOM   3605  C   LEU H  81      81.386  19.816 -13.487  1.00 53.34           C  
ANISOU 3605  C   LEU H  81     6241   8068   5958   1971  -1599     72       C  
ATOM   3606  O   LEU H  81      82.150  19.103 -14.145  1.00 66.07           O  
ANISOU 3606  O   LEU H  81     8030   9638   7434   1937  -1605     82       O  
ATOM   3607  CB  LEU H  81      81.704  18.580 -11.323  1.00 46.00           C  
ANISOU 3607  CB  LEU H  81     5057   7174   5248   1719  -1384    -12       C  
ATOM   3608  CG  LEU H  81      82.860  19.454 -10.833  1.00 32.41           C  
ANISOU 3608  CG  LEU H  81     3478   5303   3534   1781  -1205     91       C  
ATOM   3609  CD1 LEU H  81      82.335  20.681 -10.104  1.00 33.13           C  
ANISOU 3609  CD1 LEU H  81     3439   5412   3737   1902  -1182    107       C  
ATOM   3610  CD2 LEU H  81      83.796  18.658  -9.940  1.00 30.38           C  
ANISOU 3610  CD2 LEU H  81     3239   4971   3332   1605  -1017     90       C  
ATOM   3611  N   GLN H  82      81.119  21.081 -13.803  1.00 42.03           N  
ANISOU 3611  N   GLN H  82     4849   6583   4536   2093  -1597    138       N  
ATOM   3612  CA  GLN H  82      81.717  21.738 -14.958  1.00 41.02           C  
ANISOU 3612  CA  GLN H  82     4969   6347   4269   2193  -1593    230       C  
ATOM   3613  C   GLN H  82      82.988  22.457 -14.522  1.00 45.67           C  
ANISOU 3613  C   GLN H  82     5703   6765   4884   2218  -1387    325       C  
ATOM   3614  O   GLN H  82      82.932  23.405 -13.732  1.00 50.18           O  
ANISOU 3614  O   GLN H  82     6193   7291   5581   2253  -1296    350       O  
ATOM   3615  CB  GLN H  82      80.729  22.715 -15.594  1.00 50.53           C  
ANISOU 3615  CB  GLN H  82     6131   7591   5477   2306  -1702    253       C  
ATOM   3616  CG  GLN H  82      79.455  22.058 -16.101  1.00 72.66           C  
ANISOU 3616  CG  GLN H  82     8791  10554   8263   2278  -1911    162       C  
ATOM   3617  CD  GLN H  82      78.430  23.062 -16.590  1.00 83.57           C  
ANISOU 3617  CD  GLN H  82    10105  11977   9671   2393  -2014    194       C  
ATOM   3618  OE1 GLN H  82      78.651  24.272 -16.530  1.00 91.81           O  
ANISOU 3618  OE1 GLN H  82    11203  12931  10748   2495  -1928    282       O  
ATOM   3619  NE2 GLN H  82      77.299  22.564 -17.076  1.00 84.55           N  
ANISOU 3619  NE2 GLN H  82    10103  12235   9788   2371  -2200    121       N  
ATOM   3620  N   MET H  83      84.128  22.007 -15.039  1.00 50.22           N  
ANISOU 3620  N   MET H  83     6493   7238   5350   2189  -1310    373       N  
ATOM   3621  CA  MET H  83      85.433  22.540 -14.666  1.00 44.83           C  
ANISOU 3621  CA  MET H  83     5949   6381   4704   2182  -1106    458       C  
ATOM   3622  C   MET H  83      85.919  23.475 -15.769  1.00 49.80           C  
ANISOU 3622  C   MET H  83     6776   6890   5254   2268  -1062    546       C  
ATOM   3623  O   MET H  83      86.220  23.029 -16.880  1.00 60.13           O  
ANISOU 3623  O   MET H  83     8252   8179   6417   2275  -1099    565       O  
ATOM   3624  CB  MET H  83      86.427  21.406 -14.431  1.00 36.08           C  
ANISOU 3624  CB  MET H  83     4933   5224   3552   2076  -1020    459       C  
ATOM   3625  CG  MET H  83      85.947  20.357 -13.442  1.00 31.43           C  
ANISOU 3625  CG  MET H  83     4142   4767   3034   1974  -1062    369       C  
ATOM   3626  SD  MET H  83      87.235  19.175 -12.998  1.00 29.32           S  
ANISOU 3626  SD  MET H  83     3972   4385   2783   1761   -872    370       S  
ATOM   3627  CE  MET H  83      87.609  18.455 -14.591  1.00 30.29           C  
ANISOU 3627  CE  MET H  83     4343   4467   2699   1760   -942    385       C  
ATOM   3628  N   THR H  84      86.001  24.766 -15.461  1.00 37.87           N  
ANISOU 3628  N   THR H  84     5246   5302   3842   2328   -979    594       N  
ATOM   3629  CA  THR H  84      86.478  25.767 -16.402  1.00 37.38           C  
ANISOU 3629  CA  THR H  84     5344   5127   3731   2405   -921    679       C  
ATOM   3630  C   THR H  84      87.812  26.333 -15.934  1.00 45.05           C  
ANISOU 3630  C   THR H  84     6404   5926   4789   2347   -711    730       C  
ATOM   3631  O   THR H  84      88.096  26.386 -14.734  1.00 45.08           O  
ANISOU 3631  O   THR H  84     6306   5904   4919   2279   -627    703       O  
ATOM   3632  CB  THR H  84      85.466  26.904 -16.566  1.00 37.59           C  
ANISOU 3632  CB  THR H  84     5276   5201   3806   2519  -1004    694       C  
ATOM   3633  OG1 THR H  84      85.327  27.604 -15.324  1.00 70.32           O  
ANISOU 3633  OG1 THR H  84     9272   9323   8122   2503   -929    676       O  
ATOM   3634  CG2 THR H  84      84.113  26.353 -16.987  1.00 39.33           C  
ANISOU 3634  CG2 THR H  84     5382   5600   3963   2559  -1218    634       C  
ATOM   3635  N   SER H  85      88.627  26.759 -16.903  1.00 41.93           N  
ANISOU 3635  N   SER H  85     7492   4326   4113   2304   -936   1014       N  
ATOM   3636  CA  SER H  85      89.958  27.311 -16.643  1.00 46.89           C  
ANISOU 3636  CA  SER H  85     8510   4727   4580   2184   -753    939       C  
ATOM   3637  C   SER H  85      90.819  26.318 -15.863  1.00 52.87           C  
ANISOU 3637  C   SER H  85     9189   5615   5285   1945   -828    742       C  
ATOM   3638  O   SER H  85      91.365  26.629 -14.802  1.00 57.33           O  
ANISOU 3638  O   SER H  85     9979   6020   5783   1849   -697    677       O  
ATOM   3639  CB  SER H  85      89.865  28.653 -15.913  1.00 44.74           C  
ANISOU 3639  CB  SER H  85     8614   4059   4328   2293   -432    998       C  
ATOM   3640  OG  SER H  85      89.069  29.573 -16.638  1.00 55.36           O  
ANISOU 3640  OG  SER H  85     9999   5289   5747   2549   -327   1214       O  
ATOM   3641  N   LEU H  86      90.938  25.108 -16.403  1.00 35.78           N  
ANISOU 3641  N   LEU H  86     6727   3729   3139   1834  -1006    673       N  
ATOM   3642  CA  LEU H  86      91.699  24.062 -15.736  1.00 56.18           C  
ANISOU 3642  CA  LEU H  86     9164   6461   5719   1640  -1042    530       C  
ATOM   3643  C   LEU H  86      93.186  24.392 -15.724  1.00 51.49           C  
ANISOU 3643  C   LEU H  86     8796   5834   4933   1485   -931    532       C  
ATOM   3644  O   LEU H  86      93.723  24.994 -16.658  1.00 57.38           O  
ANISOU 3644  O   LEU H  86     9748   6500   5552   1482   -866    607       O  
ATOM   3645  CB  LEU H  86      91.467  22.714 -16.416  1.00 31.69           C  
ANISOU 3645  CB  LEU H  86     5774   3578   2688   1569  -1162    479       C  
ATOM   3646  CG  LEU H  86      90.145  22.022 -16.082  1.00 31.44           C  
ANISOU 3646  CG  LEU H  86     5492   3647   2809   1603  -1266    454       C  
ATOM   3647  CD1 LEU H  86      89.994  20.736 -16.875  1.00 55.22           C  
ANISOU 3647  CD1 LEU H  86     8367   6807   5807   1516  -1354    413       C  
ATOM   3648  CD2 LEU H  86      90.061  21.744 -14.589  1.00 29.69           C  
ANISOU 3648  CD2 LEU H  86     5172   3423   2687   1555  -1232    365       C  
ATOM   3649  N   ARG H  87      93.850  23.995 -14.642  1.00 59.59           N  
ANISOU 3649  N   ARG H  87     9754   6972   5917   1323   -902    471       N  
ATOM   3650  CA  ARG H  87      95.274  24.220 -14.456  1.00 67.43           C  
ANISOU 3650  CA  ARG H  87    10850   8080   6691   1078   -784    493       C  
ATOM   3651  C   ARG H  87      95.920  22.934 -13.956  1.00 70.53           C  
ANISOU 3651  C   ARG H  87    10832   8820   7145    951   -821    464       C  
ATOM   3652  O   ARG H  87      95.239  21.984 -13.561  1.00 68.59           O  
ANISOU 3652  O   ARG H  87    10336   8631   7093   1034   -906    416       O  
ATOM   3653  CB  ARG H  87      95.532  25.377 -13.480  1.00 72.48           C  
ANISOU 3653  CB  ARG H  87    11880   8563   7095    881   -602    483       C  
ATOM   3654  CG  ARG H  87      94.882  26.685 -13.905  1.00 98.17           C  
ANISOU 3654  CG  ARG H  87    15626  11355  10318   1037   -447    566       C  
ATOM   3655  CD  ARG H  87      95.159  27.812 -12.925  1.00121.99           C  
ANISOU 3655  CD  ARG H  87    18881  14167  13303    673    -80    423       C  
ATOM   3656  NE  ARG H  87      94.490  29.047 -13.326  1.00135.67           N  
ANISOU 3656  NE  ARG H  87    21053  15384  15112    866    165    505       N  
ATOM   3657  CZ  ARG H  87      94.617  30.209 -12.693  1.00128.71           C  
ANISOU 3657  CZ  ARG H  87    20538  14165  14203    591    577    388       C  
ATOM   3658  NH1 ARG H  87      95.392  30.302 -11.622  1.00131.20           N  
ANISOU 3658  NH1 ARG H  87    20804  14669  14378     40    752    157       N  
ATOM   3659  NH2 ARG H  87      93.968  31.279 -13.133  1.00120.85           N  
ANISOU 3659  NH2 ARG H  87    19969  12651  13299    858    841    514       N  
ATOM   3660  N   SER H  88      97.256  22.912 -13.981  1.00 62.86           N  
ANISOU 3660  N   SER H  88     9793   8095   5998    738   -721    515       N  
ATOM   3661  CA  SER H  88      97.986  21.716 -13.571  1.00 28.50           C  
ANISOU 3661  CA  SER H  88     5063   4083   1683    659   -722    561       C  
ATOM   3662  C   SER H  88      97.684  21.337 -12.128  1.00 48.31           C  
ANISOU 3662  C   SER H  88     7379   6742   4235    577   -749    532       C  
ATOM   3663  O   SER H  88      97.756  20.156 -11.769  1.00 62.32           O  
ANISOU 3663  O   SER H  88     8900   8633   6147    615   -780    571       O  
ATOM   3664  CB  SER H  88      99.488  21.925 -13.758  1.00 29.86           C  
ANISOU 3664  CB  SER H  88     5167   4567   1613    426   -605    657       C  
ATOM   3665  OG  SER H  88      99.813  22.073 -15.129  1.00 82.98           O  
ANISOU 3665  OG  SER H  88    12037  11176   8314    515   -580    690       O  
ATOM   3666  N   GLU H  89      97.342  22.317 -11.289  1.00 45.09           N  
ANISOU 3666  N   GLU H  89     7163   6274   3695    455   -711    454       N  
ATOM   3667  CA  GLU H  89      97.001  22.024  -9.903  1.00 37.37           C  
ANISOU 3667  CA  GLU H  89     6019   5455   2723    357   -733    402       C  
ATOM   3668  C   GLU H  89      95.685  21.270  -9.779  1.00 30.46           C  
ANISOU 3668  C   GLU H  89     5050   4367   2157    633   -866    362       C  
ATOM   3669  O   GLU H  89      95.420  20.683  -8.725  1.00 28.19           O  
ANISOU 3669  O   GLU H  89     4549   4228   1935    584   -894    347       O  
ATOM   3670  CB  GLU H  89      96.934  23.317  -9.087  1.00 59.21           C  
ANISOU 3670  CB  GLU H  89     9124   8123   5252     57   -593    267       C  
ATOM   3671  CG  GLU H  89      98.284  23.977  -8.835  1.00 81.19           C  
ANISOU 3671  CG  GLU H  89    11849  11208   7792   -400   -385    249       C  
ATOM   3672  CD  GLU H  89      98.855  24.645 -10.070  1.00 83.00           C  
ANISOU 3672  CD  GLU H  89    12334  11272   7932   -409   -295    296       C  
ATOM   3673  OE1 GLU H  89      98.067  25.011 -10.969  1.00 79.75           O  
ANISOU 3673  OE1 GLU H  89    12284  10416   7601   -133   -336    313       O  
ATOM   3674  OE2 GLU H  89     100.092  24.799 -10.145  1.00 86.73           O  
ANISOU 3674  OE2 GLU H  89    12627  12048   8280   -648   -188    331       O  
ATOM   3675  N   ASP H  90      94.860  21.271 -10.824  1.00 30.61           N  
ANISOU 3675  N   ASP H  90     5192   4092   2347    873   -930    343       N  
ATOM   3676  CA  ASP H  90      93.581  20.575 -10.804  1.00 31.71           C  
ANISOU 3676  CA  ASP H  90     5202   4106   2741   1041  -1016    284       C  
ATOM   3677  C   ASP H  90      93.687  19.123 -11.250  1.00 23.78           C  
ANISOU 3677  C   ASP H  90     3973   3193   1869   1042  -1005    298       C  
ATOM   3678  O   ASP H  90      92.683  18.404 -11.206  1.00 51.05           O  
ANISOU 3678  O   ASP H  90     7339   6586   5470   1098  -1048    240       O  
ATOM   3679  CB  ASP H  90      92.564  21.313 -11.681  1.00 30.28           C  
ANISOU 3679  CB  ASP H  90     5223   3665   2615   1227  -1068    264       C  
ATOM   3680  CG  ASP H  90      92.187  22.671 -11.119  1.00 27.60           C  
ANISOU 3680  CG  ASP H  90     5212   3109   2165   1313  -1042    276       C  
ATOM   3681  OD1 ASP H  90      92.164  22.819  -9.879  1.00 27.40           O  
ANISOU 3681  OD1 ASP H  90     5232   3118   2059   1239  -1032    236       O  
ATOM   3682  OD2 ASP H  90      91.911  23.591 -11.917  1.00 32.53           O  
ANISOU 3682  OD2 ASP H  90     6093   3512   2755   1447   -998    341       O  
ATOM   3683  N   THR H  91      94.866  18.678 -11.679  1.00 23.92           N  
ANISOU 3683  N   THR H  91     3945   3345   1797    982   -939    378       N  
ATOM   3684  CA  THR H  91      95.062  17.280 -12.045  1.00 23.52           C  
ANISOU 3684  CA  THR H  91     3796   3323   1817   1037   -906    395       C  
ATOM   3685  C   THR H  91      94.902  16.404 -10.812  1.00 22.72           C  
ANISOU 3685  C   THR H  91     3510   3316   1807   1008   -888    418       C  
ATOM   3686  O   THR H  91      95.676  16.524  -9.856  1.00 22.85           O  
ANISOU 3686  O   THR H  91     3403   3523   1756    903   -857    504       O  
ATOM   3687  CB  THR H  91      96.445  17.078 -12.660  1.00 24.36           C  
ANISOU 3687  CB  THR H  91     3915   3552   1790   1031   -824    496       C  
ATOM   3688  OG1 THR H  91      96.523  17.764 -13.916  1.00 54.82           O  
ANISOU 3688  OG1 THR H  91     7962   7303   5563   1063   -837    474       O  
ATOM   3689  CG2 THR H  91      96.718  15.597 -12.870  1.00 24.52           C  
ANISOU 3689  CG2 THR H  91     3895   3579   1843   1167   -755    521       C  
ATOM   3690  N   ALA H  92      93.909  15.521 -10.830  1.00 22.29           N  
ANISOU 3690  N   ALA H  92     3450   3150   1870   1080   -917    344       N  
ATOM   3691  CA  ALA H  92      93.601  14.705  -9.659  1.00 24.49           C  
ANISOU 3691  CA  ALA H  92     3582   3488   2236   1060   -901    366       C  
ATOM   3692  C   ALA H  92      92.598  13.628 -10.055  1.00 23.39           C  
ANISOU 3692  C   ALA H  92     3516   3213   2159   1151   -938    279       C  
ATOM   3693  O   ALA H  92      92.169  13.538 -11.210  1.00 23.64           O  
ANISOU 3693  O   ALA H  92     3707   3132   2144   1212   -997    197       O  
ATOM   3694  CB  ALA H  92      93.060  15.561  -8.511  1.00 21.80           C  
ANISOU 3694  CB  ALA H  92     3152   3198   1932    958   -946    341       C  
ATOM   3695  N   MET H  93      92.233  12.807  -9.073  1.00 27.09           N  
ANISOU 3695  N   MET H  93     3885   3708   2699   1152   -921    301       N  
ATOM   3696  CA  MET H  93      91.168  11.821  -9.204  1.00 23.09           C  
ANISOU 3696  CA  MET H  93     3460   3086   2226   1220   -986    211       C  
ATOM   3697  C   MET H  93      89.927  12.369  -8.512  1.00 24.53           C  
ANISOU 3697  C   MET H  93     3533   3274   2514   1123  -1076    134       C  
ATOM   3698  O   MET H  93      89.961  12.660  -7.312  1.00 33.25           O  
ANISOU 3698  O   MET H  93     4485   4470   3680   1050  -1037    187       O  
ATOM   3699  CB  MET H  93      91.585  10.486  -8.587  1.00 24.96           C  
ANISOU 3699  CB  MET H  93     3694   3329   2461   1332   -884    310       C  
ATOM   3700  CG  MET H  93      90.543   9.390  -8.702  1.00 25.87           C  
ANISOU 3700  CG  MET H  93     3975   3285   2568   1427   -963    216       C  
ATOM   3701  SD  MET H  93      90.502   8.653 -10.343  1.00 33.17           S  
ANISOU 3701  SD  MET H  93     5329   3979   3293   1592  -1019    113       S  
ATOM   3702  CE  MET H  93      92.157   7.981 -10.455  1.00 28.44           C  
ANISOU 3702  CE  MET H  93     4798   3377   2630   1795   -683    326       C  
ATOM   3703  N   TYR H  94      88.839  12.509  -9.262  1.00 32.41           N  
ANISOU 3703  N   TYR H  94     4603   4196   3514   1131  -1203     25       N  
ATOM   3704  CA  TYR H  94      87.629  13.155  -8.770  1.00 36.02           C  
ANISOU 3704  CA  TYR H  94     4941   4680   4066   1080  -1274    -18       C  
ATOM   3705  C   TYR H  94      86.600  12.104  -8.369  1.00 25.53           C  
ANISOU 3705  C   TYR H  94     3568   3351   2780   1070  -1370    -85       C  
ATOM   3706  O   TYR H  94      86.223  11.253  -9.183  1.00 26.18           O  
ANISOU 3706  O   TYR H  94     3776   3387   2785   1095  -1495   -158       O  
ATOM   3707  CB  TYR H  94      87.056  14.099  -9.826  1.00 44.69           C  
ANISOU 3707  CB  TYR H  94     6085   5762   5133   1108  -1358    -32       C  
ATOM   3708  CG  TYR H  94      87.851  15.376  -9.984  1.00 42.02           C  
ANISOU 3708  CG  TYR H  94     5798   5403   4763   1131  -1287     21       C  
ATOM   3709  CD1 TYR H  94      89.035  15.398 -10.711  1.00 31.54           C  
ANISOU 3709  CD1 TYR H  94     4587   4058   3340   1140  -1231     54       C  
ATOM   3710  CD2 TYR H  94      87.419  16.560  -9.400  1.00 41.86           C  
ANISOU 3710  CD2 TYR H  94     5741   5371   4792   1170  -1288     33       C  
ATOM   3711  CE1 TYR H  94      89.764  16.565 -10.854  1.00 27.51           C  
ANISOU 3711  CE1 TYR H  94     4144   3534   2776   1153  -1188     97       C  
ATOM   3712  CE2 TYR H  94      88.141  17.731  -9.537  1.00 26.79           C  
ANISOU 3712  CE2 TYR H  94     3954   3409   2817   1220  -1253     62       C  
ATOM   3713  CZ  TYR H  94      89.312  17.729 -10.264  1.00 26.97           C  
ANISOU 3713  CZ  TYR H  94     4084   3431   2735   1193  -1206     95       C  
ATOM   3714  OH  TYR H  94      90.030  18.894 -10.400  1.00 27.14           O  
ANISOU 3714  OH  TYR H  94     4259   3399   2655   1232  -1181    127       O  
ATOM   3715  N   PHE H  95      86.158  12.168  -7.116  1.00 22.17           N  
ANISOU 3715  N   PHE H  95     2988   2983   2453   1023  -1335    -72       N  
ATOM   3716  CA  PHE H  95      85.101  11.323  -6.584  1.00 22.89           C  
ANISOU 3716  CA  PHE H  95     3000   3097   2601    994  -1431   -137       C  
ATOM   3717  C   PHE H  95      83.863  12.162  -6.295  1.00 44.82           C  
ANISOU 3717  C   PHE H  95     5614   5957   5459    960  -1481   -155       C  
ATOM   3718  O   PHE H  95      83.960  13.340  -5.939  1.00 23.05           O  
ANISOU 3718  O   PHE H  95     2814   3205   2738    989  -1410   -113       O  
ATOM   3719  CB  PHE H  95      85.525  10.628  -5.285  1.00 22.12           C  
ANISOU 3719  CB  PHE H  95     2832   3025   2547    989  -1343    -79       C  
ATOM   3720  CG  PHE H  95      86.818   9.873  -5.378  1.00 22.66           C  
ANISOU 3720  CG  PHE H  95     3017   3053   2540   1082  -1243     26       C  
ATOM   3721  CD1 PHE H  95      86.829   8.529  -5.711  1.00 26.86           C  
ANISOU 3721  CD1 PHE H  95     3736   3455   3016   1216  -1296     13       C  
ATOM   3722  CD2 PHE H  95      88.021  10.499  -5.097  1.00 21.09           C  
ANISOU 3722  CD2 PHE H  95     2761   2938   2315   1058  -1103    157       C  
ATOM   3723  CE1 PHE H  95      88.017   7.829  -5.783  1.00 25.11           C  
ANISOU 3723  CE1 PHE H  95     3641   3170   2728   1374  -1116    173       C  
ATOM   3724  CE2 PHE H  95      89.212   9.805  -5.167  1.00 21.49           C  
ANISOU 3724  CE2 PHE H  95     2861   2998   2307   1152   -989    297       C  
ATOM   3725  CZ  PHE H  95      89.210   8.467  -5.510  1.00 34.86           C  
ANISOU 3725  CZ  PHE H  95     4727   4557   3961   1329   -956    322       C  
ATOM   3726  N   CYS H  96      82.697  11.542  -6.439  1.00 41.77           N  
ANISOU 3726  N   CYS H  96     5140   5645   5086    910  -1620   -219       N  
ATOM   3727  CA  CYS H  96      81.448  12.097  -5.933  1.00 44.78           C  
ANISOU 3727  CA  CYS H  96     5309   6154   5552    892  -1655   -204       C  
ATOM   3728  C   CYS H  96      81.033  11.276  -4.722  1.00 39.61           C  
ANISOU 3728  C   CYS H  96     4539   5533   4976    812  -1646   -259       C  
ATOM   3729  O   CYS H  96      80.856  10.057  -4.824  1.00 43.86           O  
ANISOU 3729  O   CYS H  96     5110   6073   5483    724  -1749   -350       O  
ATOM   3730  CB  CYS H  96      80.351  12.100  -6.998  1.00 57.35           C  
ANISOU 3730  CB  CYS H  96     6802   7913   7075    853  -1825   -190       C  
ATOM   3731  SG  CYS H  96      80.063  10.537  -7.853  1.00 72.04           S  
ANISOU 3731  SG  CYS H  96     8748   9848   8776    657  -2019   -336       S  
ATOM   3732  N   ALA H  97      80.898  11.939  -3.578  1.00 25.13           N  
ANISOU 3732  N   ALA H  97     2595   3717   3235    836  -1541   -228       N  
ATOM   3733  CA  ALA H  97      80.623  11.265  -2.320  1.00 30.80           C  
ANISOU 3733  CA  ALA H  97     3200   4480   4024    760  -1509   -264       C  
ATOM   3734  C   ALA H  97      79.506  11.984  -1.582  1.00 37.49           C  
ANISOU 3734  C   ALA H  97     3842   5431   4972    775  -1494   -268       C  
ATOM   3735  O   ALA H  97      79.424  13.215  -1.606  1.00 38.96           O  
ANISOU 3735  O   ALA H  97     4016   5598   5189    900  -1454   -237       O  
ATOM   3736  CB  ALA H  97      81.877  11.198  -1.441  1.00 32.75           C  
ANISOU 3736  CB  ALA H  97     3518   4676   4248    766  -1380   -207       C  
ATOM   3737  N   THR H  98      78.648  11.207  -0.928  1.00 32.55           N  
ANISOU 3737  N   THR H  98     3055   4909   4406    666  -1530   -319       N  
ATOM   3738  CA  THR H  98      77.542  11.731  -0.143  1.00 40.94           C  
ANISOU 3738  CA  THR H  98     3891   6089   5575    681  -1503   -324       C  
ATOM   3739  C   THR H  98      77.513  11.027   1.208  1.00 38.59           C  
ANISOU 3739  C   THR H  98     3507   5823   5333    560  -1430   -379       C  
ATOM   3740  O   THR H  98      78.302  10.117   1.479  1.00 41.67           O  
ANISOU 3740  O   THR H  98     3995   6157   5682    484  -1418   -387       O  
ATOM   3741  CB  THR H  98      76.203  11.556  -0.872  1.00 51.44           C  
ANISOU 3741  CB  THR H  98     5029   7605   6912    633  -1639   -298       C  
ATOM   3742  OG1 THR H  98      75.135  12.019  -0.035  1.00 39.10           O  
ANISOU 3742  OG1 THR H  98     3215   6169   5473    677  -1593   -280       O  
ATOM   3743  CG2 THR H  98      75.974  10.091  -1.216  1.00 60.25           C  
ANISOU 3743  CG2 THR H  98     6147   8789   7957    392  -1758   -391       C  
ATOM   3744  N   SER H  99      76.589  11.461   2.064  1.00 42.16           N  
ANISOU 3744  N   SER H  99     3755   6378   5886    568  -1376   -403       N  
ATOM   3745  CA  SER H  99      76.391  10.851   3.368  1.00 35.12           C  
ANISOU 3745  CA  SER H  99     2749   5549   5047    433  -1294   -455       C  
ATOM   3746  C   SER H  99      75.105  10.047   3.464  1.00 48.90           C  
ANISOU 3746  C   SER H  99     4289   7441   6850    275  -1350   -491       C  
ATOM   3747  O   SER H  99      74.918   9.332   4.456  1.00 66.47           O  
ANISOU 3747  O   SER H  99     6431   9711   9113    123  -1282   -537       O  
ATOM   3748  CB  SER H  99      76.389  11.925   4.464  1.00 37.48           C  
ANISOU 3748  CB  SER H  99     2958   5874   5407    523  -1154   -506       C  
ATOM   3749  OG  SER H  99      75.326  12.844   4.277  1.00 31.14           O  
ANISOU 3749  OG  SER H  99     1985   5138   4708    686  -1139   -516       O  
ATOM   3750  N   LEU H 100      74.225  10.141   2.464  1.00 50.97           N  
ANISOU 3750  N   LEU H 100     4451   7810   7105    280  -1475   -458       N  
ATOM   3751  CA  LEU H 100      72.913   9.494   2.496  1.00 35.74           C  
ANISOU 3751  CA  LEU H 100     2285   6077   5216     94  -1547   -482       C  
ATOM   3752  C   LEU H 100      72.147   9.894   3.753  1.00 52.44           C  
ANISOU 3752  C   LEU H 100     4180   8286   7458    125  -1406   -489       C  
ATOM   3753  O   LEU H 100      71.493   9.074   4.401  1.00 55.68           O  
ANISOU 3753  O   LEU H 100     4462   8792   7904    -88  -1378   -548       O  
ATOM   3754  CB  LEU H 100      73.042   7.974   2.392  1.00 36.07           C  
ANISOU 3754  CB  LEU H 100     2406   6103   5195   -212  -1609   -603       C  
ATOM   3755  CG  LEU H 100      71.914   7.265   1.644  1.00 61.34           C  
ANISOU 3755  CG  LEU H 100     5469   9486   8350   -475  -1761   -660       C  
ATOM   3756  CD1 LEU H 100      71.990   7.590   0.161  1.00 43.50           C  
ANISOU 3756  CD1 LEU H 100     3286   7267   5975   -423  -1938   -609       C  
ATOM   3757  CD2 LEU H 100      71.967   5.764   1.876  1.00 79.14           C  
ANISOU 3757  CD2 LEU H 100     7818  11690  10560   -845  -1732   -850       C  
ATOM   3758  N   TYR H 101      72.234  11.178   4.101  1.00 36.42           N  
ANISOU 3758  N   TYR H 101     2115   6226   5497    386  -1295   -453       N  
ATOM   3759  CA  TYR H 101      71.650  11.678   5.337  1.00 37.42           C  
ANISOU 3759  CA  TYR H 101     2052   6429   5736    445  -1119   -499       C  
ATOM   3760  C   TYR H 101      71.492  13.192   5.273  1.00 38.50           C  
ANISOU 3760  C   TYR H 101     2114   6548   5966    787  -1010   -464       C  
ATOM   3761  O   TYR H 101      72.369  13.931   5.734  1.00 36.94           O  
ANISOU 3761  O   TYR H 101     2059   6209   5766    903   -884   -554       O  
ATOM   3762  CB  TYR H 101      72.519  11.271   6.529  1.00 35.19           C  
ANISOU 3762  CB  TYR H 101     1901   6054   5417    302   -988   -600       C  
ATOM   3763  CG  TYR H 101      71.873  11.481   7.879  1.00 36.47           C  
ANISOU 3763  CG  TYR H 101     1871   6326   5658    260   -796   -675       C  
ATOM   3764  CD1 TYR H 101      70.963  10.564   8.386  1.00 38.10           C  
ANISOU 3764  CD1 TYR H 101     1923   6660   5895     50   -782   -676       C  
ATOM   3765  CD2 TYR H 101      72.185  12.589   8.653  1.00 44.72           C  
ANISOU 3765  CD2 TYR H 101     2895   7354   6741    402   -603   -776       C  
ATOM   3766  CE1 TYR H 101      70.374  10.751   9.622  1.00 39.41           C  
ANISOU 3766  CE1 TYR H 101     1928   6930   6117      2   -586   -739       C  
ATOM   3767  CE2 TYR H 101      71.603  12.785   9.889  1.00 40.15           C  
ANISOU 3767  CE2 TYR H 101     2151   6885   6217    340   -384   -870       C  
ATOM   3768  CZ  TYR H 101      70.699  11.863  10.368  1.00 39.25           C  
ANISOU 3768  CZ  TYR H 101     1897   6893   6123    150   -384   -832       C  
ATOM   3769  OH  TYR H 101      70.118  12.058  11.599  1.00 57.06           O  
ANISOU 3769  OH  TYR H 101     4008   9256   8417     82   -152   -917       O  
ATOM   3770  N   TYR H 102      70.392  13.655   4.671  1.00 54.89           N  
ANISOU 3770  N   TYR H 102     3956   8768   8132    953  -1052   -331       N  
ATOM   3771  CA  TYR H 102      70.032  15.070   4.585  1.00 56.07           C  
ANISOU 3771  CA  TYR H 102     4004   8883   8416   1342   -899   -246       C  
ATOM   3772  C   TYR H 102      70.997  15.888   3.730  1.00 57.73           C  
ANISOU 3772  C   TYR H 102     4478   8882   8575   1545   -920   -201       C  
ATOM   3773  O   TYR H 102      70.568  16.769   2.977  1.00 81.64           O  
ANISOU 3773  O   TYR H 102     7446  11883  11692   1829   -905    -41       O  
ATOM   3774  CB  TYR H 102      69.936  15.690   5.983  1.00 44.35           C  
ANISOU 3774  CB  TYR H 102     2452   7361   7036   1454   -586   -382       C  
ATOM   3775  CG  TYR H 102      68.807  15.145   6.827  1.00 56.39           C  
ANISOU 3775  CG  TYR H 102     3686   9102   8640   1320   -510   -391       C  
ATOM   3776  CD1 TYR H 102      67.518  15.647   6.702  1.00 62.67           C  
ANISOU 3776  CD1 TYR H 102     4169  10042   9603   1545   -430   -246       C  
ATOM   3777  CD2 TYR H 102      69.032  14.137   7.756  1.00 44.76           C  
ANISOU 3777  CD2 TYR H 102     2250   7673   7084    972   -506   -534       C  
ATOM   3778  CE1 TYR H 102      66.482  15.156   7.474  1.00 63.59           C  
ANISOU 3778  CE1 TYR H 102     4007  10367   9788   1415   -355   -261       C  
ATOM   3779  CE2 TYR H 102      68.002  13.640   8.533  1.00 48.83           C  
ANISOU 3779  CE2 TYR H 102     2520   8372   7660    834   -423   -541       C  
ATOM   3780  CZ  TYR H 102      66.730  14.153   8.388  1.00 58.95           C  
ANISOU 3780  CZ  TYR H 102     3483   9820   9094   1050   -351   -411       C  
ATOM   3781  OH  TYR H 102      65.701  13.662   9.157  1.00 53.44           O  
ANISOU 3781  OH  TYR H 102     2530   9319   8455    906   -265   -422       O  
ATOM   3782  N   GLY H 103      72.292  15.616   3.838  1.00 39.01           N  
ANISOU 3782  N   GLY H 103     2394   6352   6077   1404   -948   -333       N  
ATOM   3783  CA  GLY H 103      73.296  16.426   3.178  1.00 57.48           C  
ANISOU 3783  CA  GLY H 103     4995   8482   8364   1575   -941   -323       C  
ATOM   3784  C   GLY H 103      74.376  16.848   4.151  1.00 47.65           C  
ANISOU 3784  C   GLY H 103     3913   7086   7107   1563   -783   -542       C  
ATOM   3785  O   GLY H 103      75.007  17.897   3.989  1.00 41.27           O  
ANISOU 3785  O   GLY H 103     3283   6083   6314   1778   -660   -593       O  
ATOM   3786  N   THR H 104      74.585  16.024   5.178  1.00 40.99           N  
ANISOU 3786  N   THR H 104     3005   6339   6230   1290   -767   -674       N  
ATOM   3787  CA  THR H 104      75.571  16.309   6.202  1.00 33.00           C  
ANISOU 3787  CA  THR H 104     2130   5259   5151   1143   -595   -848       C  
ATOM   3788  C   THR H 104      76.976  16.317   5.598  1.00 33.41           C  
ANISOU 3788  C   THR H 104     2468   5192   5034   1060   -704   -814       C  
ATOM   3789  O   THR H 104      77.214  15.715   4.548  1.00 39.02           O  
ANISOU 3789  O   THR H 104     3206   5912   5707   1095   -946   -708       O  
ATOM   3790  CB  THR H 104      75.470  15.275   7.322  1.00 45.42           C  
ANISOU 3790  CB  THR H 104     3568   7010   6680    833   -576   -907       C  
ATOM   3791  OG1 THR H 104      75.581  13.956   6.773  1.00 39.69           O  
ANISOU 3791  OG1 THR H 104     2882   6319   5878    677   -801   -771       O  
ATOM   3792  CG2 THR H 104      74.143  15.409   8.050  1.00 34.87           C  
ANISOU 3792  CG2 THR H 104     1961   5793   5494    890   -409   -959       C  
ATOM   3793  N   PRO H 105      77.931  17.005   6.244  1.00 31.86           N  
ANISOU 3793  N   PRO H 105     2518   4892   4695    897   -494   -897       N  
ATOM   3794  CA  PRO H 105      79.277  17.140   5.664  1.00 39.53           C  
ANISOU 3794  CA  PRO H 105     3728   5800   5490    815   -575   -852       C  
ATOM   3795  C   PRO H 105      80.209  15.988   6.041  1.00 45.96           C  
ANISOU 3795  C   PRO H 105     4500   6822   6141    564   -709   -781       C  
ATOM   3796  O   PRO H 105      81.284  16.185   6.618  1.00 58.31           O  
ANISOU 3796  O   PRO H 105     6175   8485   7495    331   -615   -788       O  
ATOM   3797  CB  PRO H 105      79.745  18.485   6.233  1.00 46.14           C  
ANISOU 3797  CB  PRO H 105     4833   6469   6228    707   -246   -986       C  
ATOM   3798  CG  PRO H 105      78.943  18.694   7.495  1.00 31.95           C  
ANISOU 3798  CG  PRO H 105     2947   4708   4485    604     14  -1121       C  
ATOM   3799  CD  PRO H 105      77.835  17.686   7.547  1.00 31.83           C  
ANISOU 3799  CD  PRO H 105     2587   4861   4646    726   -157  -1050       C  
ATOM   3800  N   TRP H 106      79.792  14.767   5.714  1.00 25.86           N  
ANISOU 3800  N   TRP H 106     1791   4363   3672    604   -905   -694       N  
ATOM   3801  CA  TRP H 106      80.677  13.613   5.753  1.00 24.41           C  
ANISOU 3801  CA  TRP H 106     1654   4260   3360    468   -982   -547       C  
ATOM   3802  C   TRP H 106      80.367  12.734   4.550  1.00 24.31           C  
ANISOU 3802  C   TRP H 106     1759   4072   3406    540  -1085   -416       C  
ATOM   3803  O   TRP H 106      79.361  12.919   3.860  1.00 24.99           O  
ANISOU 3803  O   TRP H 106     1810   4093   3594    636  -1137   -446       O  
ATOM   3804  CB  TRP H 106      80.566  12.833   7.075  1.00 24.73           C  
ANISOU 3804  CB  TRP H 106     1562   4478   3354    264   -886   -518       C  
ATOM   3805  CG  TRP H 106      79.262  12.130   7.322  1.00 40.00           C  
ANISOU 3805  CG  TRP H 106     3370   6379   5448    249   -881   -537       C  
ATOM   3806  CD1 TRP H 106      78.824  10.980   6.730  1.00 40.81           C  
ANISOU 3806  CD1 TRP H 106     3499   6391   5617    249   -971   -447       C  
ATOM   3807  CD2 TRP H 106      78.250  12.506   8.263  1.00 43.97           C  
ANISOU 3807  CD2 TRP H 106     3676   6990   6039    191   -761   -678       C  
ATOM   3808  NE1 TRP H 106      77.592  10.630   7.229  1.00 40.92           N  
ANISOU 3808  NE1 TRP H 106     3343   6464   5741    174   -937   -512       N  
ATOM   3809  CE2 TRP H 106      77.218  11.551   8.172  1.00 49.67           C  
ANISOU 3809  CE2 TRP H 106     4320   7679   6872    159   -803   -628       C  
ATOM   3810  CE3 TRP H 106      78.110  13.565   9.166  1.00 39.83           C  
ANISOU 3810  CE3 TRP H 106     3105   6537   5490    127   -559   -831       C  
ATOM   3811  CZ2 TRP H 106      76.064  11.622   8.950  1.00 61.59           C  
ANISOU 3811  CZ2 TRP H 106     5634   9285   8482    104   -696   -716       C  
ATOM   3812  CZ3 TRP H 106      76.966  13.632   9.940  1.00 29.98           C  
ANISOU 3812  CZ3 TRP H 106     1682   5350   4358     94   -419   -929       C  
ATOM   3813  CH2 TRP H 106      75.957  12.668   9.825  1.00 30.57           C  
ANISOU 3813  CH2 TRP H 106     1592   5462   4562    101   -512   -873       C  
ATOM   3814  N   PHE H 107      81.252  11.774   4.289  1.00 23.07           N  
ANISOU 3814  N   PHE H 107     1709   3895   3162    490  -1104   -277       N  
ATOM   3815  CA  PHE H 107      81.219  10.996   3.052  1.00 22.97           C  
ANISOU 3815  CA  PHE H 107     1813   3758   3157    546  -1185   -223       C  
ATOM   3816  C   PHE H 107      81.172   9.510   3.395  1.00 49.77           C  
ANISOU 3816  C   PHE H 107     5153   7189   6569    494  -1211   -183       C  
ATOM   3817  O   PHE H 107      82.209   8.891   3.652  1.00 42.30           O  
ANISOU 3817  O   PHE H 107     4247   6279   5545    539  -1176    -51       O  
ATOM   3818  CB  PHE H 107      82.424  11.331   2.180  1.00 21.99           C  
ANISOU 3818  CB  PHE H 107     1871   3559   2928    616  -1179   -142       C  
ATOM   3819  CG  PHE H 107      82.796  12.785   2.207  1.00 37.47           C  
ANISOU 3819  CG  PHE H 107     3864   5525   4846    655  -1154   -196       C  
ATOM   3820  CD1 PHE H 107      81.971  13.735   1.628  1.00 38.13           C  
ANISOU 3820  CD1 PHE H 107     3951   5531   5006    774  -1195   -293       C  
ATOM   3821  CD2 PHE H 107      83.966  13.204   2.818  1.00 21.33           C  
ANISOU 3821  CD2 PHE H 107     1830   3605   2669    589  -1105   -155       C  
ATOM   3822  CE1 PHE H 107      82.308  15.075   1.656  1.00 42.86           C  
ANISOU 3822  CE1 PHE H 107     4589   6117   5580    882  -1195   -378       C  
ATOM   3823  CE2 PHE H 107      84.308  14.542   2.850  1.00 21.65           C  
ANISOU 3823  CE2 PHE H 107     1896   3703   2628    616  -1111   -272       C  
ATOM   3824  CZ  PHE H 107      83.479  15.478   2.267  1.00 45.31           C  
ANISOU 3824  CZ  PHE H 107     4922   6559   5735    796  -1168   -404       C  
ATOM   3825  N   ALA H 108      79.967   8.941   3.385  1.00 52.36           N  
ANISOU 3825  N   ALA H 108     5366   7531   6997    420  -1275   -292       N  
ATOM   3826  CA  ALA H 108      79.763   7.532   3.688  1.00 25.71           C  
ANISOU 3826  CA  ALA H 108     1947   4152   3668    334  -1295   -313       C  
ATOM   3827  C   ALA H 108      79.635   6.662   2.446  1.00 26.74           C  
ANISOU 3827  C   ALA H 108     2286   4096   3778    291  -1350   -362       C  
ATOM   3828  O   ALA H 108      79.632   5.433   2.570  1.00 54.85           O  
ANISOU 3828  O   ALA H 108     6006   7504   7332    171  -1205   -326       O  
ATOM   3829  CB  ALA H 108      78.515   7.353   4.561  1.00 35.59           C  
ANISOU 3829  CB  ALA H 108     2978   5524   5021    158  -1259   -413       C  
ATOM   3830  N   TYR H 109      79.525   7.259   1.262  1.00 26.67           N  
ANISOU 3830  N   TYR H 109     2311   4084   3739    368  -1524   -443       N  
ATOM   3831  CA  TYR H 109      79.398   6.506   0.017  1.00 35.66           C  
ANISOU 3831  CA  TYR H 109     3662   5083   4804    273  -1580   -521       C  
ATOM   3832  C   TYR H 109      80.231   7.208  -1.045  1.00 30.35           C  
ANISOU 3832  C   TYR H 109     3128   4363   4042    472  -1680   -481       C  
ATOM   3833  O   TYR H 109      79.900   8.323  -1.459  1.00 26.64           O  
ANISOU 3833  O   TYR H 109     2580   3988   3556    522  -1690   -454       O  
ATOM   3834  CB  TYR H 109      77.937   6.392  -0.421  1.00 42.68           C  
ANISOU 3834  CB  TYR H 109     4371   6140   5706     46  -1738   -693       C  
ATOM   3835  CG  TYR H 109      77.074   5.607   0.539  1.00 43.47           C  
ANISOU 3835  CG  TYR H 109     4347   6290   5878   -205  -1626   -749       C  
ATOM   3836  CD1 TYR H 109      76.376   6.244   1.556  1.00 31.67           C  
ANISOU 3836  CD1 TYR H 109     2522   5013   4497   -180  -1636   -745       C  
ATOM   3837  CD2 TYR H 109      76.960   4.228   0.431  1.00 46.40           C  
ANISOU 3837  CD2 TYR H 109     4970   6462   6198   -479  -1465   -812       C  
ATOM   3838  CE1 TYR H 109      75.588   5.530   2.436  1.00 33.17           C  
ANISOU 3838  CE1 TYR H 109     2595   5265   4744   -421  -1524   -794       C  
ATOM   3839  CE2 TYR H 109      76.172   3.505   1.306  1.00 52.45           C  
ANISOU 3839  CE2 TYR H 109     5649   7257   7022   -736  -1339   -861       C  
ATOM   3840  CZ  TYR H 109      75.488   4.162   2.307  1.00 46.29           C  
ANISOU 3840  CZ  TYR H 109     4498   6740   6351   -707  -1387   -847       C  
ATOM   3841  OH  TYR H 109      74.703   3.448   3.184  1.00 36.77           O  
ANISOU 3841  OH  TYR H 109     3199   5579   5193   -973  -1254   -892       O  
ATOM   3842  N   TRP H 110      81.305   6.559  -1.480  1.00 37.87           N  
ANISOU 3842  N   TRP H 110     4366   5111   4911    544  -1545   -393       N  
ATOM   3843  CA  TRP H 110      82.201   7.098  -2.489  1.00 38.84           C  
ANISOU 3843  CA  TRP H 110     4643   5181   4933    718  -1604   -346       C  
ATOM   3844  C   TRP H 110      81.995   6.376  -3.814  1.00 39.06           C  
ANISOU 3844  C   TRP H 110     4931   5060   4849    592  -1630   -469       C  
ATOM   3845  O   TRP H 110      81.494   5.249  -3.865  1.00 33.85           O  
ANISOU 3845  O   TRP H 110     4420   4265   4175    367  -1515   -568       O  
ATOM   3846  CB  TRP H 110      83.664   6.971  -2.050  1.00 37.49           C  
ANISOU 3846  CB  TRP H 110     4572   4952   4721    910  -1411   -130       C  
ATOM   3847  CG  TRP H 110      84.019   7.787  -0.843  1.00 23.21           C  
ANISOU 3847  CG  TRP H 110     2531   3349   2941    940  -1359    -16       C  
ATOM   3848  CD1 TRP H 110      83.606   7.577   0.441  1.00 23.34           C  
ANISOU 3848  CD1 TRP H 110     2362   3481   3024    872  -1318      9       C  
ATOM   3849  CD2 TRP H 110      84.879   8.932  -0.805  1.00 31.32           C  
ANISOU 3849  CD2 TRP H 110     3535   4454   3909    897  -1221     83       C  
ATOM   3850  NE1 TRP H 110      84.147   8.526   1.274  1.00 22.25           N  
ANISOU 3850  NE1 TRP H 110     2110   3495   2847    798  -1194    111       N  
ATOM   3851  CE2 TRP H 110      84.934   9.369   0.534  1.00 34.00           C  
ANISOU 3851  CE2 TRP H 110     3707   4944   4269    802  -1151    146       C  
ATOM   3852  CE3 TRP H 110      85.605   9.633  -1.773  1.00 24.90           C  
ANISOU 3852  CE3 TRP H 110     2838   3594   3029    914  -1185    101       C  
ATOM   3853  CZ2 TRP H 110      85.685  10.474   0.928  1.00 42.67           C  
ANISOU 3853  CZ2 TRP H 110     4779   6122   5311    724  -1091    191       C  
ATOM   3854  CZ3 TRP H 110      86.351  10.729  -1.380  1.00 20.45           C  
ANISOU 3854  CZ3 TRP H 110     2222   3118   2429    841  -1106    167       C  
ATOM   3855  CH2 TRP H 110      86.385  11.139  -0.042  1.00 49.78           C  
ANISOU 3855  CH2 TRP H 110     5797   6964   6151    747  -1078    197       C  
ATOM   3856  N   GLY H 111      82.393   7.046  -4.895  1.00 27.39           N  
ANISOU 3856  N   GLY H 111     3538   3602   3267    701  -1760   -475       N  
ATOM   3857  CA  GLY H 111      82.333   6.475  -6.220  1.00 32.15           C  
ANISOU 3857  CA  GLY H 111     4411   4094   3712    570  -1783   -595       C  
ATOM   3858  C   GLY H 111      83.667   5.880  -6.649  1.00 38.46           C  
ANISOU 3858  C   GLY H 111     5550   4625   4436    717  -1534   -499       C  
ATOM   3859  O   GLY H 111      84.648   5.859  -5.909  1.00 27.82           O  
ANISOU 3859  O   GLY H 111     4188   3228   3155    932  -1357   -305       O  
ATOM   3860  N   GLN H 112      83.682   5.386  -7.889  1.00 51.15           N  
ANISOU 3860  N   GLN H 112     7453   6102   5877    587  -1513   -630       N  
ATOM   3861  CA  GLN H 112      84.903   4.801  -8.434  1.00 45.85           C  
ANISOU 3861  CA  GLN H 112     7135   5159   5128    746  -1236   -549       C  
ATOM   3862  C   GLN H 112      85.966   5.860  -8.688  1.00 42.19           C  
ANISOU 3862  C   GLN H 112     6582   4813   4637   1045  -1308   -375       C  
ATOM   3863  O   GLN H 112      87.164   5.558  -8.643  1.00 38.89           O  
ANISOU 3863  O   GLN H 112     6297   4269   4209   1272  -1062   -202       O  
ATOM   3864  CB  GLN H 112      84.593   4.044  -9.726  1.00 59.28           C  
ANISOU 3864  CB  GLN H 112     9213   6686   6624    476  -1170   -778       C  
ATOM   3865  CG  GLN H 112      83.496   2.997  -9.591  1.00 92.57           C  
ANISOU 3865  CG  GLN H 112    13556  10803  10812     65  -1086   -999       C  
ATOM   3866  CD  GLN H 112      83.890   1.841  -8.690  1.00116.05           C  
ANISOU 3866  CD  GLN H 112    16754  13416  13922    126   -663   -907       C  
ATOM   3867  OE1 GLN H 112      85.073   1.578  -8.474  1.00118.68           O  
ANISOU 3867  OE1 GLN H 112    17241  13534  14318    475   -376   -685       O  
ATOM   3868  NE2 GLN H 112      82.893   1.144  -8.156  1.00122.57           N  
ANISOU 3868  NE2 GLN H 112    17583  14201  14785   -204   -609  -1048       N  
ATOM   3869  N   GLY H 113      85.554   7.097  -8.952  1.00 40.71           N  
ANISOU 3869  N   GLY H 113     6168   4871   4429   1056  -1613   -397       N  
ATOM   3870  CA  GLY H 113      86.488   8.168  -9.234  1.00 30.21           C  
ANISOU 3870  CA  GLY H 113     4783   3629   3067   1262  -1644   -261       C  
ATOM   3871  C   GLY H 113      86.938   8.182 -10.679  1.00 38.31           C  
ANISOU 3871  C   GLY H 113     6092   4579   3886   1286  -1676   -308       C  
ATOM   3872  O   GLY H 113      87.166   7.123 -11.272  1.00 62.63           O  
ANISOU 3872  O   GLY H 113     9475   7450   6871   1209  -1480   -387       O  
ATOM   3873  N   THR H 114      87.065   9.371 -11.260  1.00 34.48           N  
ANISOU 3873  N   THR H 114     5435   4203   3462   1234  -1640   -274       N  
ATOM   3874  CA  THR H 114      87.527   9.526 -12.632  1.00 42.32           C  
ANISOU 3874  CA  THR H 114     6646   5154   4281   1250  -1657   -296       C  
ATOM   3875  C   THR H 114      88.761  10.420 -12.654  1.00 31.08           C  
ANISOU 3875  C   THR H 114     5132   3754   2923   1332  -1457   -167       C  
ATOM   3876  O   THR H 114      88.829  11.420 -11.933  1.00 30.46           O  
ANISOU 3876  O   THR H 114     4797   3778   3000   1269  -1375    -98       O  
ATOM   3877  CB  THR H 114      86.422  10.101 -13.534  1.00 54.39           C  
ANISOU 3877  CB  THR H 114     8061   6837   5766   1081  -1826   -350       C  
ATOM   3878  OG1 THR H 114      86.906  10.218 -14.877  1.00 56.71           O  
ANISOU 3878  OG1 THR H 114     8563   7112   5870   1075  -1834   -358       O  
ATOM   3879  CG2 THR H 114      85.958  11.467 -13.039  1.00 57.08           C  
ANISOU 3879  CG2 THR H 114     8068   7315   6305   1079  -1780   -236       C  
ATOM   3880  N   LEU H 115      89.741  10.046 -13.471  1.00 41.03           N  
ANISOU 3880  N   LEU H 115     6647   4923   4020   1444  -1370   -144       N  
ATOM   3881  CA  LEU H 115      91.032  10.722 -13.488  1.00 35.38           C  
ANISOU 3881  CA  LEU H 115     5833   4275   3336   1489  -1181    -26       C  
ATOM   3882  C   LEU H 115      91.007  11.896 -14.458  1.00 26.43           C  
ANISOU 3882  C   LEU H 115     4676   3186   2180   1408  -1244    -35       C  
ATOM   3883  O   LEU H 115      90.600  11.748 -15.616  1.00 32.93           O  
ANISOU 3883  O   LEU H 115     5690   3961   2860   1399  -1359   -100       O  
ATOM   3884  CB  LEU H 115      92.145   9.746 -13.869  1.00 27.99           C  
ANISOU 3884  CB  LEU H 115     5154   3240   2242   1689   -992     49       C  
ATOM   3885  CG  LEU H 115      93.570  10.295 -13.800  1.00 26.94           C  
ANISOU 3885  CG  LEU H 115     4852   3253   2132   1724   -796    198       C  
ATOM   3886  CD1 LEU H 115      93.894  10.732 -12.384  1.00 35.51           C  
ANISOU 3886  CD1 LEU H 115     5572   4529   3390   1618   -739    312       C  
ATOM   3887  CD2 LEU H 115      94.570   9.261 -14.285  1.00 28.85           C  
ANISOU 3887  CD2 LEU H 115     5336   3403   2224   1969   -546    301       C  
ATOM   3888  N   VAL H 116      91.447  13.058 -13.983  1.00 25.13           N  
ANISOU 3888  N   VAL H 116     4311   3115   2120   1338  -1169     43       N  
ATOM   3889  CA  VAL H 116      91.547  14.266 -14.793  1.00 30.20           C  
ANISOU 3889  CA  VAL H 116     4974   3772   2730   1302  -1197     70       C  
ATOM   3890  C   VAL H 116      92.996  14.731 -14.761  1.00 35.70           C  
ANISOU 3890  C   VAL H 116     5662   4522   3379   1307  -1058    161       C  
ATOM   3891  O   VAL H 116      93.513  15.105 -13.698  1.00 32.10           O  
ANISOU 3891  O   VAL H 116     5053   4158   2987   1250   -987    228       O  
ATOM   3892  CB  VAL H 116      90.605  15.374 -14.295  1.00 25.21           C  
ANISOU 3892  CB  VAL H 116     4202   3167   2209   1246  -1260     81       C  
ATOM   3893  CG1 VAL H 116      90.874  16.672 -15.041  1.00 25.99           C  
ANISOU 3893  CG1 VAL H 116     4377   3250   2249   1265  -1263    140       C  
ATOM   3894  CG2 VAL H 116      89.155  14.951 -14.463  1.00 26.26           C  
ANISOU 3894  CG2 VAL H 116     4293   3319   2366   1239  -1409     31       C  
ATOM   3895  N   THR H 117      93.650  14.700 -15.919  1.00 34.93           N  
ANISOU 3895  N   THR H 117     5731   4396   3145   1362  -1033    174       N  
ATOM   3896  CA  THR H 117      95.030  15.144 -16.066  1.00 26.27           C  
ANISOU 3896  CA  THR H 117     4627   3380   1973   1364   -912    274       C  
ATOM   3897  C   THR H 117      95.042  16.423 -16.891  1.00 45.32           C  
ANISOU 3897  C   THR H 117     7124   5766   4328   1312   -960    291       C  
ATOM   3898  O   THR H 117      94.550  16.438 -18.024  1.00 35.94           O  
ANISOU 3898  O   THR H 117     6086   4507   3064   1344  -1037    252       O  
ATOM   3899  CB  THR H 117      95.889  14.070 -16.733  1.00 27.45           C  
ANISOU 3899  CB  THR H 117     4929   3518   1984   1512   -797    299       C  
ATOM   3900  OG1 THR H 117      95.832  12.862 -15.964  1.00 44.22           O  
ANISOU 3900  OG1 THR H 117     7027   5635   4141   1621   -722    310       O  
ATOM   3901  CG2 THR H 117      97.335  14.534 -16.831  1.00 27.90           C  
ANISOU 3901  CG2 THR H 117     4919   3720   1960   1513   -665    432       C  
ATOM   3902  N   VAL H 118      95.598  17.489 -16.325  1.00 53.76           N  
ANISOU 3902  N   VAL H 118     8128   6901   5395   1232   -921    362       N  
ATOM   3903  CA  VAL H 118      95.677  18.786 -16.987  1.00 60.52           C  
ANISOU 3903  CA  VAL H 118     9127   7700   6168   1210   -941    395       C  
ATOM   3904  C   VAL H 118      97.128  19.009 -17.388  1.00 28.35           C  
ANISOU 3904  C   VAL H 118     5095   3738   1940   1155   -834    486       C  
ATOM   3905  O   VAL H 118      97.997  19.212 -16.531  1.00 28.13           O  
ANISOU 3905  O   VAL H 118     4954   3876   1858   1048   -764    559       O  
ATOM   3906  CB  VAL H 118      95.167  19.919 -16.088  1.00 27.45           C  
ANISOU 3906  CB  VAL H 118     4953   3457   2019   1182   -967    399       C  
ATOM   3907  CG1 VAL H 118      95.165  21.235 -16.851  1.00 51.52           C  
ANISOU 3907  CG1 VAL H 118     8246   6375   4954   1217   -967    449       C  
ATOM   3908  CG2 VAL H 118      93.776  19.595 -15.563  1.00 26.86           C  
ANISOU 3908  CG2 VAL H 118     4784   3322   2099   1238  -1056    327       C  
ATOM   3909  N   SER H 119      97.393  18.975 -18.692  1.00 36.69           N  
ANISOU 3909  N   SER H 119     5887   5879   2174   2568   -160    223       N  
ATOM   3910  CA  SER H 119      98.747  19.148 -19.195  1.00 54.37           C  
ANISOU 3910  CA  SER H 119     8227   7929   4503   2236   -297    246       C  
ATOM   3911  C   SER H 119      98.693  19.492 -20.675  1.00 52.69           C  
ANISOU 3911  C   SER H 119     7921   7756   4344   2153   -428    347       C  
ATOM   3912  O   SER H 119      97.747  19.127 -21.377  1.00 58.77           O  
ANISOU 3912  O   SER H 119     8476   8730   5125   2243   -417    391       O  
ATOM   3913  CB  SER H 119      99.594  17.890 -18.978  1.00 40.95           C  
ANISOU 3913  CB  SER H 119     6381   6279   2899   1913   -231    221       C  
ATOM   3914  OG  SER H 119     100.851  18.003 -19.622  1.00 31.67           O  
ANISOU 3914  OG  SER H 119     5247   4992   1795   1627   -341    279       O  
ATOM   3915  N   ALA H 120      99.721  20.200 -21.135  1.00 42.24           N  
ANISOU 3915  N   ALA H 120     6754   6240   3055   1962   -562    401       N  
ATOM   3916  CA  ALA H 120      99.881  20.515 -22.546  1.00 46.31           C  
ANISOU 3916  CA  ALA H 120     7202   6777   3617   1820   -678    509       C  
ATOM   3917  C   ALA H 120     100.620  19.425 -23.310  1.00 52.68           C  
ANISOU 3917  C   ALA H 120     7823   7708   4484   1508   -634    540       C  
ATOM   3918  O   ALA H 120     100.858  19.582 -24.512  1.00 50.44           O  
ANISOU 3918  O   ALA H 120     7504   7449   4213   1369   -710    629       O  
ATOM   3919  CB  ALA H 120     100.614  21.850 -22.711  1.00 49.07           C  
ANISOU 3919  CB  ALA H 120     7801   6877   3965   1766   -840    581       C  
ATOM   3920  N   ALA H 121     100.987  18.332 -22.646  1.00 31.71           N  
ANISOU 3920  N   ALA H 121     5073   5117   1859   1406   -514    468       N  
ATOM   3921  CA  ALA H 121     101.681  17.245 -23.313  1.00 30.08           C  
ANISOU 3921  CA  ALA H 121     4724   4997   1709   1152   -467    480       C  
ATOM   3922  C   ALA H 121     100.720  16.453 -24.195  1.00 30.08           C  
ANISOU 3922  C   ALA H 121     4541   5175   1714   1180   -440    470       C  
ATOM   3923  O   ALA H 121      99.495  16.522 -24.052  1.00 51.15           O  
ANISOU 3923  O   ALA H 121     7131   7948   4354   1387   -438    456       O  
ATOM   3924  CB  ALA H 121     102.341  16.320 -22.292  1.00 28.58           C  
ANISOU 3924  CB  ALA H 121     4502   4792   1566   1046   -371    409       C  
ATOM   3925  N   LYS H 122     101.295  15.690 -25.116  1.00 29.23           N  
ANISOU 3925  N   LYS H 122     4374   5102   1629    982   -428    485       N  
ATOM   3926  CA  LYS H 122     100.537  14.888 -26.062  1.00 29.41           C  
ANISOU 3926  CA  LYS H 122     4273   5258   1644    965   -433    478       C  
ATOM   3927  C   LYS H 122     100.392  13.461 -25.550  1.00 49.71           C  
ANISOU 3927  C   LYS H 122     6711   7908   4268    919   -334    391       C  
ATOM   3928  O   LYS H 122     101.274  12.932 -24.869  1.00 59.23           O  
ANISOU 3928  O   LYS H 122     7934   9044   5525    824   -261    347       O  
ATOM   3929  CB  LYS H 122     101.220  14.884 -27.431  1.00 29.65           C  
ANISOU 3929  CB  LYS H 122     4372   5256   1636    801   -478    536       C  
ATOM   3930  CG  LYS H 122     101.552  16.272 -27.948  1.00 36.11           C  
ANISOU 3930  CG  LYS H 122     5330   5986   2406    797   -585    646       C  
ATOM   3931  CD  LYS H 122     102.487  16.220 -29.143  1.00 37.69           C  
ANISOU 3931  CD  LYS H 122     5612   6159   2549    621   -592    712       C  
ATOM   3932  CE  LYS H 122     102.888  17.621 -29.579  1.00 32.56           C  
ANISOU 3932  CE  LYS H 122     5097   5423   1852    587   -710    848       C  
ATOM   3933  NZ  LYS H 122     103.898  17.598 -30.673  1.00 51.25           N  
ANISOU 3933  NZ  LYS H 122     7558   7773   4141    427   -694    925       N  
ATOM   3934  N   THR H 123      99.261  12.842 -25.882  1.00 28.79           N  
ANISOU 3934  N   THR H 123     3928   5406   1605    977   -357    383       N  
ATOM   3935  CA  THR H 123      99.029  11.449 -25.521  1.00 32.82           C  
ANISOU 3935  CA  THR H 123     4316   5998   2157    914   -295    321       C  
ATOM   3936  C   THR H 123     100.013  10.558 -26.271  1.00 28.25           C  
ANISOU 3936  C   THR H 123     3803   5334   1595    726   -276    289       C  
ATOM   3937  O   THR H 123     100.022  10.533 -27.507  1.00 47.77           O  
ANISOU 3937  O   THR H 123     6336   7804   4008    666   -339    317       O  
ATOM   3938  CB  THR H 123      97.590  11.049 -25.836  1.00 29.25           C  
ANISOU 3938  CB  THR H 123     3702   5741   1671    997   -361    353       C  
ATOM   3939  OG1 THR H 123      96.689  11.920 -25.142  1.00 30.47           O  
ANISOU 3939  OG1 THR H 123     3781   5998   1798   1226   -360    398       O  
ATOM   3940  CG2 THR H 123      97.328   9.615 -25.402  1.00 28.62           C  
ANISOU 3940  CG2 THR H 123     3500   5750   1624    913   -317    304       C  
ATOM   3941  N   THR H 124     100.842   9.833 -25.526  1.00 25.70           N  
ANISOU 3941  N   THR H 124     3484   4941   1340    649   -191    235       N  
ATOM   3942  CA  THR H 124     101.887   9.009 -26.097  1.00 25.05           C  
ANISOU 3942  CA  THR H 124     3464   4782   1270    522   -154    208       C  
ATOM   3943  C   THR H 124     101.715   7.563 -25.652  1.00 24.39           C  
ANISOU 3943  C   THR H 124     3308   4724   1233    475   -122    143       C  
ATOM   3944  O   THR H 124     101.610   7.299 -24.446  1.00 37.98           O  
ANISOU 3944  O   THR H 124     4967   6446   3016    493    -83    118       O  
ATOM   3945  CB  THR H 124     103.275   9.522 -25.677  1.00 24.34           C  
ANISOU 3945  CB  THR H 124     3455   4579   1215    476   -103    231       C  
ATOM   3946  OG1 THR H 124     103.386  10.914 -25.995  1.00 43.48           O  
ANISOU 3946  OG1 THR H 124     5959   6977   3586    510   -155    306       O  
ATOM   3947  CG2 THR H 124     104.373   8.753 -26.399  1.00 24.16           C  
ANISOU 3947  CG2 THR H 124     3475   4520   1182    390    -49    223       C  
ATOM   3948  N   PRO H 125     101.680   6.609 -26.577  1.00 39.66           N  
ANISOU 3948  N   PRO H 125     5277   6670   3123    414   -145    115       N  
ATOM   3949  CA  PRO H 125     101.617   5.199 -26.190  1.00 24.36           C  
ANISOU 3949  CA  PRO H 125     3304   4736   1216    362   -131     57       C  
ATOM   3950  C   PRO H 125     102.930   4.753 -25.572  1.00 37.40           C  
ANISOU 3950  C   PRO H 125     4991   6282   2938    323    -45     30       C  
ATOM   3951  O   PRO H 125     103.990   5.329 -25.859  1.00 23.09           O  
ANISOU 3951  O   PRO H 125     3241   4408   1124    318      2     58       O  
ATOM   3952  CB  PRO H 125     101.349   4.481 -27.520  1.00 25.54           C  
ANISOU 3952  CB  PRO H 125     3548   4895   1259    313   -199     37       C  
ATOM   3953  CG  PRO H 125     101.922   5.391 -28.551  1.00 26.18           C  
ANISOU 3953  CG  PRO H 125     3742   4934   1271    319   -189     77       C  
ATOM   3954  CD  PRO H 125     101.690   6.786 -28.039  1.00 45.30           C  
ANISOU 3954  CD  PRO H 125     6098   7381   3732    387   -196    138       C  
ATOM   3955  N   PRO H 126     102.904   3.732 -24.721  1.00 45.09           N  
ANISOU 3955  N   PRO H 126     5917   7249   3964    293    -30    -10       N  
ATOM   3956  CA  PRO H 126     104.122   3.325 -24.016  1.00 21.66           C  
ANISOU 3956  CA  PRO H 126     2973   4193   1063    265     34    -24       C  
ATOM   3957  C   PRO H 126     105.056   2.499 -24.885  1.00 27.37           C  
ANISOU 3957  C   PRO H 126     3776   4881   1743    242     71    -52       C  
ATOM   3958  O   PRO H 126     104.633   1.781 -25.794  1.00 33.69           O  
ANISOU 3958  O   PRO H 126     4639   5701   2461    228     39    -89       O  
ATOM   3959  CB  PRO H 126     103.581   2.489 -22.853  1.00 23.62           C  
ANISOU 3959  CB  PRO H 126     3153   4462   1360    241     22    -51       C  
ATOM   3960  CG  PRO H 126     102.323   1.900 -23.391  1.00 37.62           C  
ANISOU 3960  CG  PRO H 126     4881   6342   3070    230    -46    -65       C  
ATOM   3961  CD  PRO H 126     101.731   2.945 -24.301  1.00 41.36           C  
ANISOU 3961  CD  PRO H 126     5356   6875   3485    280    -82    -29       C  
ATOM   3962  N   SER H 127     106.350   2.608 -24.583  1.00 43.73           N  
ANISOU 3962  N   SER H 127     5852   6912   3850    244    138    -31       N  
ATOM   3963  CA  SER H 127     107.383   1.795 -25.217  1.00 34.07           C  
ANISOU 3963  CA  SER H 127     4675   5687   2584    251    207    -53       C  
ATOM   3964  C   SER H 127     107.805   0.716 -24.226  1.00 21.63           C  
ANISOU 3964  C   SER H 127     3064   4091   1063    237    214    -88       C  
ATOM   3965  O   SER H 127     108.409   1.016 -23.191  1.00 31.93           O  
ANISOU 3965  O   SER H 127     4310   5384   2437    229    222    -49       O  
ATOM   3966  CB  SER H 127     108.575   2.651 -25.642  1.00 22.66           C  
ANISOU 3966  CB  SER H 127     3222   4266   1122    276    284     19       C  
ATOM   3967  OG  SER H 127     108.176   3.663 -26.549  1.00 23.72           O  
ANISOU 3967  OG  SER H 127     3403   4417   1191    280    267     57       O  
ATOM   3968  N   VAL H 128     107.484  -0.535 -24.540  1.00 22.17           N  
ANISOU 3968  N   VAL H 128     3189   4155   1081    227    197   -159       N  
ATOM   3969  CA  VAL H 128     107.693  -1.655 -23.631  1.00 34.54           C  
ANISOU 3969  CA  VAL H 128     4739   5705   2681    208    180   -197       C  
ATOM   3970  C   VAL H 128     108.962  -2.388 -24.044  1.00 42.29           C  
ANISOU 3970  C   VAL H 128     5752   6699   3616    264    271   -226       C  
ATOM   3971  O   VAL H 128     109.075  -2.862 -25.181  1.00 23.96           O  
ANISOU 3971  O   VAL H 128     3530   4380   1193    299    314   -278       O  
ATOM   3972  CB  VAL H 128     106.486  -2.604 -23.625  1.00 22.16           C  
ANISOU 3972  CB  VAL H 128     3216   4134   1070    160     83   -253       C  
ATOM   3973  CG1 VAL H 128     106.611  -3.610 -22.491  1.00 33.12           C  
ANISOU 3973  CG1 VAL H 128     4580   5509   2497    122     48   -277       C  
ATOM   3974  CG2 VAL H 128     105.193  -1.812 -23.513  1.00 21.94           C  
ANISOU 3974  CG2 VAL H 128     3127   4147   1060    137     20   -215       C  
ATOM   3975  N   TYR H 129     109.913  -2.490 -23.118  1.00 36.69           N  
ANISOU 3975  N   TYR H 129     4962   6012   2968    281    304   -192       N  
ATOM   3976  CA  TYR H 129     111.175  -3.176 -23.355  1.00 23.13           C  
ANISOU 3976  CA  TYR H 129     3228   4343   1217    370    408   -204       C  
ATOM   3977  C   TYR H 129     111.278  -4.373 -22.420  1.00 30.42           C  
ANISOU 3977  C   TYR H 129     4153   5259   2146    364    356   -259       C  
ATOM   3978  O   TYR H 129     111.154  -4.207 -21.193  1.00 21.84           O  
ANISOU 3978  O   TYR H 129     3008   4169   1123    290    281   -216       O  
ATOM   3979  CB  TYR H 129     112.359  -2.229 -23.151  1.00 30.80           C  
ANISOU 3979  CB  TYR H 129     4077   5389   2236    412    493    -81       C  
ATOM   3980  CG  TYR H 129     112.310  -1.003 -24.035  1.00 34.17           C  
ANISOU 3980  CG  TYR H 129     4510   5828   2647    408    528    -18       C  
ATOM   3981  CD1 TYR H 129     112.591  -1.092 -25.393  1.00 25.03           C  
ANISOU 3981  CD1 TYR H 129     3412   4693   1406    473    634    -37       C  
ATOM   3982  CD2 TYR H 129     111.985   0.243 -23.514  1.00 22.50           C  
ANISOU 3982  CD2 TYR H 129     3000   4332   1216    344    455     55       C  
ATOM   3983  CE1 TYR H 129     112.546   0.024 -26.207  1.00 25.50           C  
ANISOU 3983  CE1 TYR H 129     3487   4771   1430    458    659     26       C  
ATOM   3984  CE2 TYR H 129     111.938   1.365 -24.320  1.00 34.01           C  
ANISOU 3984  CE2 TYR H 129     4476   5805   2643    343    475    112       C  
ATOM   3985  CZ  TYR H 129     112.220   1.249 -25.666  1.00 32.96           C  
ANISOU 3985  CZ  TYR H 129     4390   5707   2427    394    574    103       C  
ATOM   3986  OH  TYR H 129     112.177   2.360 -26.477  1.00 29.90           O  
ANISOU 3986  OH  TYR H 129     4029   5340   1992    384    589    168       O  
ATOM   3987  N   PRO H 130     111.491  -5.581 -22.938  1.00 26.80           N  
ANISOU 3987  N   PRO H 130     3785   4789   1609    439    386   -360       N  
ATOM   3988  CA  PRO H 130     111.558  -6.758 -22.065  1.00 24.26           C  
ANISOU 3988  CA  PRO H 130     3489   4453   1276    436    309   -426       C  
ATOM   3989  C   PRO H 130     112.869  -6.813 -21.295  1.00 24.35           C  
ANISOU 3989  C   PRO H 130     3376   4532   1343    527    379   -360       C  
ATOM   3990  O   PRO H 130     113.946  -6.560 -21.841  1.00 26.52           O  
ANISOU 3990  O   PRO H 130     3573   4832   1670    658    534   -297       O  
ATOM   3991  CB  PRO H 130     111.434  -7.928 -23.046  1.00 26.02           C  
ANISOU 3991  CB  PRO H 130     3887   4611   1388    520    317   -566       C  
ATOM   3992  CG  PRO H 130     111.986  -7.393 -24.323  1.00 27.23           C  
ANISOU 3992  CG  PRO H 130     4057   4787   1503    628    479   -550       C  
ATOM   3993  CD  PRO H 130     111.609  -5.937 -24.363  1.00 25.96           C  
ANISOU 3993  CD  PRO H 130     3798   4664   1402    526    474   -431       C  
ATOM   3994  N   LEU H 131     112.768  -7.159 -20.015  1.00 23.50           N  
ANISOU 3994  N   LEU H 131     3232   4336   1361    402    241   -324       N  
ATOM   3995  CA  LEU H 131     113.911  -7.220 -19.107  1.00 23.62           C  
ANISOU 3995  CA  LEU H 131     3124   4260   1590    395    225   -207       C  
ATOM   3996  C   LEU H 131     114.189  -8.681 -18.765  1.00 24.61           C  
ANISOU 3996  C   LEU H 131     3308   4227   1818    420    146   -273       C  
ATOM   3997  O   LEU H 131     113.524  -9.266 -17.904  1.00 40.76           O  
ANISOU 3997  O   LEU H 131     5421   6195   3869    282    -12   -299       O  
ATOM   3998  CB  LEU H 131     113.649  -6.397 -17.851  1.00 22.16           C  
ANISOU 3998  CB  LEU H 131     2892   4077   1450    230    111   -104       C  
ATOM   3999  CG  LEU H 131     113.406  -4.907 -18.090  1.00 26.57           C  
ANISOU 3999  CG  LEU H 131     3417   4756   1921    212    164    -36       C  
ATOM   4000  CD1 LEU H 131     113.094  -4.197 -16.783  1.00 27.79           C  
ANISOU 4000  CD1 LEU H 131     3587   4878   2093     70     45     39       C  
ATOM   4001  CD2 LEU H 131     114.609  -4.281 -18.779  1.00 24.06           C  
ANISOU 4001  CD2 LEU H 131     2980   4477   1685    314    292     75       C  
ATOM   4002  N   ALA H 132     115.177  -9.259 -19.445  1.00 26.36           N  
ANISOU 4002  N   ALA H 132     3503   4396   2115    606    264   -289       N  
ATOM   4003  CA  ALA H 132     115.680 -10.605 -19.238  1.00 29.81           C  
ANISOU 4003  CA  ALA H 132     3990   4661   2674    687    211   -344       C  
ATOM   4004  C   ALA H 132     117.151 -10.548 -18.838  1.00 28.86           C  
ANISOU 4004  C   ALA H 132     3664   4491   2809    783    272   -191       C  
ATOM   4005  O   ALA H 132     117.857  -9.602 -19.203  1.00 29.10           O  
ANISOU 4005  O   ALA H 132     3532   4639   2887    844    415    -69       O  
ATOM   4006  CB  ALA H 132     115.523 -11.453 -20.507  1.00 29.62           C  
ANISOU 4006  CB  ALA H 132     4150   4599   2504    871    308   -517       C  
ATOM   4007  N   PRO H 133     117.644 -11.535 -18.086  1.00 48.24           N  
ANISOU 4007  N   PRO H 133     6110   6773   5446    788    150   -172       N  
ATOM   4008  CA  PRO H 133     119.039 -11.487 -17.635  1.00 50.96           C  
ANISOU 4008  CA  PRO H 133     6229   7067   6069    867    174      3       C  
ATOM   4009  C   PRO H 133     120.015 -11.487 -18.803  1.00 59.67           C  
ANISOU 4009  C   PRO H 133     7210   8241   7221   1148    445     22       C  
ATOM   4010  O   PRO H 133     119.706 -11.928 -19.913  1.00 62.40           O  
ANISOU 4010  O   PRO H 133     7711   8609   7388   1319    596   -140       O  
ATOM   4011  CB  PRO H 133     119.186 -12.756 -16.786  1.00 42.91           C  
ANISOU 4011  CB  PRO H 133     5278   5828   5199    842    -19    -20       C  
ATOM   4012  CG  PRO H 133     118.084 -13.654 -17.245  1.00 31.71           C  
ANISOU 4012  CG  PRO H 133     4131   4342   3575    841    -69   -234       C  
ATOM   4013  CD  PRO H 133     116.952 -12.740 -17.595  1.00 29.79           C  
ANISOU 4013  CD  PRO H 133     3962   4272   3086    707    -38   -287       C  
ATOM   4014  N   GLY H 134     121.212 -10.971 -18.534  1.00 52.74           N  
ANISOU 4014  N   GLY H 134     6056   7400   6584   1188    501    238       N  
ATOM   4015  CA  GLY H 134     122.250 -10.880 -19.542  1.00 55.27           C  
ANISOU 4015  CA  GLY H 134     6198   7817   6987   1450    784    313       C  
ATOM   4016  C   GLY H 134     122.676 -12.224 -20.096  1.00 55.27           C  
ANISOU 4016  C   GLY H 134     6273   7695   7033   1740    904    186       C  
ATOM   4017  O   GLY H 134     122.452 -12.517 -21.275  1.00 41.07           O  
ANISOU 4017  O   GLY H 134     4634   5946   5025   1944   1118     27       O  
ATOM   4018  N   CYS H 135     123.289 -13.054 -19.253  1.00 51.90           N  
ANISOU 4018  N   CYS H 135     5761   7090   6870   1768    756    251       N  
ATOM   4019  CA  CYS H 135     123.730 -14.391 -19.608  1.00 43.16           C  
ANISOU 4019  CA  CYS H 135     4735   5819   5843   2051    828    136       C  
ATOM   4020  C   CYS H 135     122.806 -15.418 -18.943  1.00 42.08           C  
ANISOU 4020  C   CYS H 135     4899   5460   5632   1915    542    -39       C  
ATOM   4021  O   CYS H 135     121.663 -15.081 -18.585  1.00 41.41           O  
ANISOU 4021  O   CYS H 135     4984   5399   5351   1649    376   -112       O  
ATOM   4022  CB  CYS H 135     125.201 -14.540 -19.242  1.00 60.57           C  
ANISOU 4022  CB  CYS H 135     6584   7994   8434   2210    886    372       C  
ATOM   4023  SG  CYS H 135     126.337 -13.821 -20.458  1.00 60.56           S  
ANISOU 4023  SG  CYS H 135     6268   8244   8500   2502   1326    536       S  
ATOM   4024  N   GLY H 136     123.285 -16.646 -18.777  1.00 78.60           N  
ANISOU 4024  N   GLY H 136     9579   9869  10416   2096    485    -90       N  
ATOM   4025  CA  GLY H 136     122.446 -17.716 -18.278  1.00 86.79           C  
ANISOU 4025  CA  GLY H 136    10920  10678  11376   1983    220   -252       C  
ATOM   4026  C   GLY H 136     122.073 -17.652 -16.809  1.00 90.39           C  
ANISOU 4026  C   GLY H 136    11352  11052  11940   1638   -114   -133       C  
ATOM   4027  O   GLY H 136     120.942 -17.991 -16.445  1.00 83.03           O  
ANISOU 4027  O   GLY H 136    10665  10050  10831   1421   -308   -245       O  
ATOM   4028  N   ASP H 137     123.005 -17.219 -15.959  1.00 89.44           N  
ANISOU 4028  N   ASP H 137    10943  10939  12100   1578   -187    107       N  
ATOM   4029  CA  ASP H 137     122.848 -17.291 -14.505  1.00 91.07           C  
ANISOU 4029  CA  ASP H 137    11151  11029  12423   1283   -514    232       C  
ATOM   4030  C   ASP H 137     122.516 -18.724 -14.089  1.00 75.74           C  
ANISOU 4030  C   ASP H 137     9449   8818  10510   1285   -728    120       C  
ATOM   4031  O   ASP H 137     121.498 -19.010 -13.456  1.00 47.78           O  
ANISOU 4031  O   ASP H 137     6126   5210   6818   1029   -938     58       O  
ATOM   4032  CB  ASP H 137     121.792 -16.298 -14.011  1.00 89.47           C  
ANISOU 4032  CB  ASP H 137    11035  10969  11990    958   -603    236       C  
ATOM   4033  CG  ASP H 137     122.213 -14.856 -14.215  1.00 72.27           C  
ANISOU 4033  CG  ASP H 137     8629   9009   9821    926   -457    382       C  
ATOM   4034  OD1 ASP H 137     123.402 -14.550 -13.988  1.00 64.90           O  
ANISOU 4034  OD1 ASP H 137     7426   8078   9155    995   -445    585       O  
ATOM   4035  OD2 ASP H 137     121.360 -14.035 -14.613  1.00 57.54           O  
ANISOU 4035  OD2 ASP H 137     6847   7306   7707    828   -370    306       O  
ATOM   4036  N   THR H 138     123.419 -19.629 -14.467  1.00 83.75           N  
ANISOU 4036  N   THR H 138    10413   9679  11730   1590   -664    107       N  
ATOM   4037  CA  THR H 138     123.173 -21.063 -14.402  1.00 77.98           C  
ANISOU 4037  CA  THR H 138     9946   8669  11014   1675   -825    -36       C  
ATOM   4038  C   THR H 138     123.491 -21.647 -13.032  1.00 83.49           C  
ANISOU 4038  C   THR H 138    10619   9156  11949   1500  -1161    122       C  
ATOM   4039  O   THR H 138     124.257 -22.610 -12.926  1.00 67.69           O  
ANISOU 4039  O   THR H 138     8599   6934  10187   1710  -1234    146       O  
ATOM   4040  CB  THR H 138     123.995 -21.789 -15.465  1.00 79.62           C  
ANISOU 4040  CB  THR H 138    10148   8785  11319   2126   -589   -138       C  
ATOM   4041  OG1 THR H 138     125.390 -21.569 -15.216  1.00 63.70           O  
ANISOU 4041  OG1 THR H 138     7754   6792   9657   2311   -504     89       O  
ATOM   4042  CG2 THR H 138     123.647 -21.273 -16.857  1.00 92.45           C  
ANISOU 4042  CG2 THR H 138    11855  10607  12664   2298   -260   -303       C  
ATOM   4043  N   THR H 139     122.908 -21.074 -11.983  1.00 97.14           N  
ANISOU 4043  N   THR H 139    12362  10944  13604   1128  -1366    230       N  
ATOM   4044  CA  THR H 139     122.996 -21.630 -10.640  1.00 80.57           C  
ANISOU 4044  CA  THR H 139    10313   8646  11652    908  -1707    367       C  
ATOM   4045  C   THR H 139     121.706 -22.319 -10.217  1.00 64.90           C  
ANISOU 4045  C   THR H 139     8667   6553   9440    655  -1910    247       C  
ATOM   4046  O   THR H 139     121.559 -22.669  -9.042  1.00 57.22           O  
ANISOU 4046  O   THR H 139     7773   5450   8519    409  -2190    366       O  
ATOM   4047  CB  THR H 139     123.359 -20.537  -9.633  1.00 42.98           C  
ANISOU 4047  CB  THR H 139     5353   4004   6973    665  -1812    602       C  
ATOM   4048  OG1 THR H 139     122.544 -19.379  -9.862  1.00 40.23           O  
ANISOU 4048  OG1 THR H 139     5026   3907   6351    506  -1670    553       O  
ATOM   4049  CG2 THR H 139     124.826 -20.156  -9.759  1.00 44.94           C  
ANISOU 4049  CG2 THR H 139     5245   4278   7554    875  -1729    796       C  
ATOM   4050  N   GLY H 140     120.770 -22.514 -11.145  1.00 42.92           N  
ANISOU 4050  N   GLY H 140     6082   3822   6403    697  -1787     34       N  
ATOM   4051  CA  GLY H 140     119.506 -23.155 -10.849  1.00 42.40           C  
ANISOU 4051  CA  GLY H 140     6306   3672   6132    448  -1976    -58       C  
ATOM   4052  C   GLY H 140     118.562 -22.355  -9.983  1.00 39.51           C  
ANISOU 4052  C   GLY H 140     5944   3483   5583     82  -2051     34       C  
ATOM   4053  O   GLY H 140     117.461 -22.837  -9.692  1.00 39.07           O  
ANISOU 4053  O   GLY H 140     6091   3391   5362   -145  -2192     -9       O  
ATOM   4054  N   SER H 141     118.950 -21.156  -9.561  1.00 42.29           N  
ANISOU 4054  N   SER H 141     6086   4022   5961     19  -1962    166       N  
ATOM   4055  CA  SER H 141     118.098 -20.343  -8.711  1.00 58.78           C  
ANISOU 4055  CA  SER H 141     8203   6269   7863   -291  -2012    245       C  
ATOM   4056  C   SER H 141     116.872 -19.860  -9.482  1.00 59.91           C  
ANISOU 4056  C   SER H 141     8420   6617   7729   -339  -1846    102       C  
ATOM   4057  O   SER H 141     116.829 -19.881 -10.715  1.00 68.24           O  
ANISOU 4057  O   SER H 141     9477   7722   8730   -132  -1674    -43       O  
ATOM   4058  CB  SER H 141     118.878 -19.151  -8.160  1.00 64.56           C  
ANISOU 4058  CB  SER H 141     8728   7117   8686   -320  -1971    409       C  
ATOM   4059  OG  SER H 141     119.498 -18.427  -9.208  1.00 71.63           O  
ANISOU 4059  OG  SER H 141     9431   8150   9635    -79  -1724    374       O  
ATOM   4060  N   SER H 142     115.865 -19.422  -8.729  1.00 43.64           N  
ANISOU 4060  N   SER H 142     6424   4673   5485   -611  -1900    154       N  
ATOM   4061  CA  SER H 142     114.636 -18.928  -9.331  1.00 33.08           C  
ANISOU 4061  CA  SER H 142     5127   3538   3906   -677  -1765     53       C  
ATOM   4062  C   SER H 142     114.925 -17.719 -10.216  1.00 36.94           C  
ANISOU 4062  C   SER H 142     5460   4226   4349   -501  -1516      5       C  
ATOM   4063  O   SER H 142     115.842 -16.935  -9.958  1.00 31.65           O  
ANISOU 4063  O   SER H 142     4642   3595   3789   -435  -1460    102       O  
ATOM   4064  CB  SER H 142     113.625 -18.563  -8.244  1.00 30.18           C  
ANISOU 4064  CB  SER H 142     4813   3278   3375   -970  -1833    151       C  
ATOM   4065  OG  SER H 142     112.355 -18.286  -8.802  1.00 58.53           O  
ANISOU 4065  OG  SER H 142     8427   7047   6766  -1038  -1732     72       O  
ATOM   4066  N   VAL H 143     114.129 -17.576 -11.273  1.00 33.71           N  
ANISOU 4066  N   VAL H 143     5091   3937   3778   -442  -1390   -129       N  
ATOM   4067  CA  VAL H 143     114.359 -16.574 -12.308  1.00 28.97           C  
ANISOU 4067  CA  VAL H 143     4378   3511   3120   -262  -1159   -188       C  
ATOM   4068  C   VAL H 143     113.474 -15.364 -12.046  1.00 27.03           C  
ANISOU 4068  C   VAL H 143     4079   3489   2700   -405  -1079   -148       C  
ATOM   4069  O   VAL H 143     112.261 -15.502 -11.841  1.00 26.59           O  
ANISOU 4069  O   VAL H 143     4103   3501   2499   -570  -1132   -168       O  
ATOM   4070  CB  VAL H 143     114.092 -17.153 -13.708  1.00 30.10           C  
ANISOU 4070  CB  VAL H 143     4631   3629   3178    -88  -1078   -363       C  
ATOM   4071  CG1 VAL H 143     114.366 -16.106 -14.775  1.00 29.54           C  
ANISOU 4071  CG1 VAL H 143     4454   3741   3030     91   -834   -407       C  
ATOM   4072  CG2 VAL H 143     114.940 -18.393 -13.936  1.00 32.41           C  
ANISOU 4072  CG2 VAL H 143     5012   3673   3630     84  -1152   -417       C  
ATOM   4073  N   THR H 144     114.080 -14.180 -12.058  1.00 42.13           N  
ANISOU 4073  N   THR H 144     5853   5515   4639   -337   -955    -81       N  
ATOM   4074  CA  THR H 144     113.363 -12.917 -11.954  1.00 33.81           C  
ANISOU 4074  CA  THR H 144     4761   4659   3426   -416   -861    -57       C  
ATOM   4075  C   THR H 144     113.431 -12.201 -13.295  1.00 27.22           C  
ANISOU 4075  C   THR H 144     3858   3961   2524   -240   -669   -133       C  
ATOM   4076  O   THR H 144     114.514 -12.054 -13.870  1.00 24.98           O  
ANISOU 4076  O   THR H 144     3480   3654   2357    -71   -577   -115       O  
ATOM   4077  CB  THR H 144     113.952 -12.033 -10.851  1.00 39.73           C  
ANISOU 4077  CB  THR H 144     5456   5405   4233   -504   -906     88       C  
ATOM   4078  OG1 THR H 144     113.815 -12.689  -9.584  1.00 45.83           O  
ANISOU 4078  OG1 THR H 144     6328   6056   5030   -682  -1087    162       O  
ATOM   4079  CG2 THR H 144     113.231 -10.694 -10.803  1.00 22.56           C  
ANISOU 4079  CG2 THR H 144     3274   3412   1888   -549   -802     96       C  
ATOM   4080  N   LEU H 145     112.274 -11.770 -13.791  1.00 46.69           N  
ANISOU 4080  N   LEU H 145     6361   6573   4806   -280   -609   -201       N  
ATOM   4081  CA  LEU H 145     112.156 -11.093 -15.073  1.00 23.35           C  
ANISOU 4081  CA  LEU H 145     3372   3749   1751   -139   -451   -271       C  
ATOM   4082  C   LEU H 145     111.400  -9.787 -14.877  1.00 41.20           C  
ANISOU 4082  C   LEU H 145     5587   6181   3886   -210   -391   -227       C  
ATOM   4083  O   LEU H 145     110.832  -9.525 -13.812  1.00 40.99           O  
ANISOU 4083  O   LEU H 145     5573   6175   3826   -353   -457   -166       O  
ATOM   4084  CB  LEU H 145     111.441 -11.975 -16.105  1.00 24.33           C  
ANISOU 4084  CB  LEU H 145     3621   3854   1768    -97   -468   -411       C  
ATOM   4085  CG  LEU H 145     112.084 -13.332 -16.394  1.00 26.08           C  
ANISOU 4085  CG  LEU H 145     3945   3877   2086      1   -532   -485       C  
ATOM   4086  CD1 LEU H 145     111.154 -14.206 -17.219  1.00 27.17           C  
ANISOU 4086  CD1 LEU H 145     4266   3969   2090    -17   -615   -619       C  
ATOM   4087  CD2 LEU H 145     113.413 -13.145 -17.103  1.00 27.01           C  
ANISOU 4087  CD2 LEU H 145     3990   3975   2298    241   -368   -487       C  
ATOM   4088  N   GLY H 146     111.387  -8.964 -15.922  1.00 32.21           N  
ANISOU 4088  N   GLY H 146     4410   5162   2667    -95   -259   -258       N  
ATOM   4089  CA  GLY H 146     110.691  -7.697 -15.820  1.00 36.33           C  
ANISOU 4089  CA  GLY H 146     4898   5828   3079   -135   -208   -220       C  
ATOM   4090  C   GLY H 146     110.289  -7.165 -17.177  1.00 20.80           C  
ANISOU 4090  C   GLY H 146     2932   3946   1025    -29   -103   -276       C  
ATOM   4091  O   GLY H 146     110.597  -7.747 -18.219  1.00 26.52           O  
ANISOU 4091  O   GLY H 146     3702   4685   1691     76    -59   -359       O  
ATOM   4092  N   CYS H 147     109.574  -6.044 -17.142  1.00 20.01           N  
ANISOU 4092  N   CYS H 147     2805   3820    979    -45    -65   -221       N  
ATOM   4093  CA  CYS H 147     109.197  -5.289 -18.328  1.00 20.09           C  
ANISOU 4093  CA  CYS H 147     2813   3839    983     27      8   -231       C  
ATOM   4094  C   CYS H 147     109.260  -3.813 -17.975  1.00 30.41           C  
ANISOU 4094  C   CYS H 147     4073   5133   2349     33     45   -151       C  
ATOM   4095  O   CYS H 147     108.699  -3.391 -16.958  1.00 51.26           O  
ANISOU 4095  O   CYS H 147     6715   7734   5026    -21      9   -117       O  
ATOM   4096  CB  CYS H 147     107.794  -5.671 -18.826  1.00 27.33           C  
ANISOU 4096  CB  CYS H 147     3770   4741   1873    -10    -44   -273       C  
ATOM   4097  SG  CYS H 147     107.756  -7.195 -19.808  1.00 77.81           S  
ANISOU 4097  SG  CYS H 147    10290  11118   8157      3   -103   -388       S  
ATOM   4098  N   LEU H 148     109.961  -3.042 -18.801  1.00 20.66           N  
ANISOU 4098  N   LEU H 148     2811   3931   1106    102    116   -121       N  
ATOM   4099  CA  LEU H 148     110.151  -1.614 -18.577  1.00 19.08           C  
ANISOU 4099  CA  LEU H 148     2591   3717    943    103    128    -45       C  
ATOM   4100  C   LEU H 148     109.250  -0.836 -19.528  1.00 32.73           C  
ANISOU 4100  C   LEU H 148     4340   5431   2666    130    146    -60       C  
ATOM   4101  O   LEU H 148     109.416  -0.912 -20.750  1.00 27.46           O  
ANISOU 4101  O   LEU H 148     3682   4796   1956    176    194    -78       O  
ATOM   4102  CB  LEU H 148     111.615  -1.222 -18.776  1.00 24.86           C  
ANISOU 4102  CB  LEU H 148     3259   4527   1658    143    180     39       C  
ATOM   4103  CG  LEU H 148     111.954   0.270 -18.697  1.00 29.12           C  
ANISOU 4103  CG  LEU H 148     3792   5062   2212    132    173    136       C  
ATOM   4104  CD1 LEU H 148     111.617   0.834 -17.325  1.00 18.84           C  
ANISOU 4104  CD1 LEU H 148     2561   3665    932     59     76    158       C  
ATOM   4105  CD2 LEU H 148     113.419   0.508 -19.033  1.00 29.71           C  
ANISOU 4105  CD2 LEU H 148     3765   5258   2268    164    234    273       C  
ATOM   4106  N   VAL H 149     108.303  -0.096 -18.967  1.00 18.71           N  
ANISOU 4106  N   VAL H 149     2577   3615    915    108    112    -50       N  
ATOM   4107  CA  VAL H 149     107.365   0.713 -19.735  1.00 21.90           C  
ANISOU 4107  CA  VAL H 149     2984   4033   1305    137    113    -52       C  
ATOM   4108  C   VAL H 149     107.849   2.156 -19.674  1.00 29.80           C  
ANISOU 4108  C   VAL H 149     4007   5010   2307    157    121      8       C  
ATOM   4109  O   VAL H 149     107.749   2.813 -18.633  1.00 24.53           O  
ANISOU 4109  O   VAL H 149     3378   4293   1649    144     97     30       O  
ATOM   4110  CB  VAL H 149     105.935   0.571 -19.199  1.00 30.06           C  
ANISOU 4110  CB  VAL H 149     3993   5089   2340    122     81    -71       C  
ATOM   4111  CG1 VAL H 149     105.032   1.622 -19.807  1.00 33.13           C  
ANISOU 4111  CG1 VAL H 149     4362   5523   2704    168     78    -56       C  
ATOM   4112  CG2 VAL H 149     105.407  -0.821 -19.490  1.00 19.33           C  
ANISOU 4112  CG2 VAL H 149     2617   3776    953     88     51   -117       C  
ATOM   4113  N   LYS H 150     108.373   2.653 -20.791  1.00 30.96           N  
ANISOU 4113  N   LYS H 150     4153   5190   2421    187    152     36       N  
ATOM   4114  CA  LYS H 150     109.020   3.955 -20.843  1.00 31.22           C  
ANISOU 4114  CA  LYS H 150     4207   5217   2436    195    150    112       C  
ATOM   4115  C   LYS H 150     108.299   4.875 -21.819  1.00 20.08           C  
ANISOU 4115  C   LYS H 150     2823   3822    984    226    143    120       C  
ATOM   4116  O   LYS H 150     107.862   4.442 -22.891  1.00 20.56           O  
ANISOU 4116  O   LYS H 150     2879   3921   1010    243    160     87       O  
ATOM   4117  CB  LYS H 150     110.496   3.814 -21.249  1.00 33.11           C  
ANISOU 4117  CB  LYS H 150     4400   5521   2659    200    203    183       C  
ATOM   4118  CG  LYS H 150     111.189   5.128 -21.585  1.00 42.22           C  
ANISOU 4118  CG  LYS H 150     5564   6700   3779    197    200    299       C  
ATOM   4119  CD  LYS H 150     112.646   4.913 -21.961  1.00 35.65           C  
ANISOU 4119  CD  LYS H 150     4634   5975   2936    201    275    417       C  
ATOM   4120  CE  LYS H 150     113.460   4.470 -20.759  1.00 38.73           C  
ANISOU 4120  CE  LYS H 150     4970   6381   3366    156    236    487       C  
ATOM   4121  NZ  LYS H 150     113.434   5.496 -19.680  1.00 47.74           N  
ANISOU 4121  NZ  LYS H 150     6202   7425   4513     85    102    553       N  
ATOM   4122  N   GLY H 151     108.168   6.142 -21.427  1.00 45.46           N  
ANISOU 4122  N   GLY H 151     6088   7002   4181    231    102    166       N  
ATOM   4123  CA  GLY H 151     107.738   7.192 -22.330  1.00 43.72           C  
ANISOU 4123  CA  GLY H 151     5902   6803   3907    262     83    199       C  
ATOM   4124  C   GLY H 151     106.287   7.126 -22.755  1.00 34.03           C  
ANISOU 4124  C   GLY H 151     4650   5616   2664    304     63    148       C  
ATOM   4125  O   GLY H 151     105.993   6.943 -23.940  1.00 39.37           O  
ANISOU 4125  O   GLY H 151     5322   6341   3295    313     65    144       O  
ATOM   4126  N   TYR H 152     105.371   7.280 -21.803  1.00 21.08           N  
ANISOU 4126  N   TYR H 152     2994   3974   1040    336     42    121       N  
ATOM   4127  CA  TYR H 152     103.948   7.320 -22.098  1.00 24.52           C  
ANISOU 4127  CA  TYR H 152     3369   4500   1449    402     22    101       C  
ATOM   4128  C   TYR H 152     103.303   8.473 -21.340  1.00 39.92           C  
ANISOU 4128  C   TYR H 152     5345   6458   3367    492      7    119       C  
ATOM   4129  O   TYR H 152     103.905   9.084 -20.452  1.00 58.04           O  
ANISOU 4129  O   TYR H 152     7730   8665   5660    483      5    131       O  
ATOM   4130  CB  TYR H 152     103.257   5.993 -21.751  1.00 26.88           C  
ANISOU 4130  CB  TYR H 152     3580   4857   1777    382     34     51       C  
ATOM   4131  CG  TYR H 152     103.108   5.726 -20.272  1.00 26.02           C  
ANISOU 4131  CG  TYR H 152     3460   4724   1702    378     61     34       C  
ATOM   4132  CD1 TYR H 152     104.116   5.096 -19.555  1.00 27.44           C  
ANISOU 4132  CD1 TYR H 152     3689   4808   1928    304     78     21       C  
ATOM   4133  CD2 TYR H 152     101.953   6.092 -19.594  1.00 21.51           C  
ANISOU 4133  CD2 TYR H 152     2831   4245   1099    462     74     37       C  
ATOM   4134  CE1 TYR H 152     103.980   4.845 -18.203  1.00 20.61           C  
ANISOU 4134  CE1 TYR H 152     2845   3912   1075    288     95      9       C  
ATOM   4135  CE2 TYR H 152     101.810   5.849 -18.244  1.00 21.43           C  
ANISOU 4135  CE2 TYR H 152     2834   4213   1096    458    115     23       C  
ATOM   4136  CZ  TYR H 152     102.823   5.225 -17.553  1.00 20.55           C  
ANISOU 4136  CZ  TYR H 152     2801   3979   1028    357    120      7       C  
ATOM   4137  OH  TYR H 152     102.675   4.982 -16.207  1.00 20.65           O  
ANISOU 4137  OH  TYR H 152     2856   3962   1028    341    154     -3       O  
ATOM   4138  N   PHE H 153     102.054   8.753 -21.703  1.00 28.13           N  
ANISOU 4138  N   PHE H 153     3777   5082   1827    594    -12    125       N  
ATOM   4139  CA  PHE H 153     101.257   9.858 -21.188  1.00 24.01           C  
ANISOU 4139  CA  PHE H 153     3270   4605   1250    747    -17    144       C  
ATOM   4140  C   PHE H 153      99.841   9.670 -21.718  1.00 25.05           C  
ANISOU 4140  C   PHE H 153     3254   4929   1334    857    -34    161       C  
ATOM   4141  O   PHE H 153      99.676   9.411 -22.916  1.00 34.45           O  
ANISOU 4141  O   PHE H 153     4414   6169   2508    810    -91    181       O  
ATOM   4142  CB  PHE H 153     101.839  11.200 -21.643  1.00 24.46           C  
ANISOU 4142  CB  PHE H 153     3460   4572   1261    772    -72    194       C  
ATOM   4143  CG  PHE H 153     101.378  12.376 -20.830  1.00 38.09           C  
ANISOU 4143  CG  PHE H 153     5277   6272   2925    940    -81    202       C  
ATOM   4144  CD1 PHE H 153     102.187  12.917 -19.844  1.00 39.15           C  
ANISOU 4144  CD1 PHE H 153     5565   6261   3050    912    -88    195       C  
ATOM   4145  CD2 PHE H 153     100.141  12.949 -21.060  1.00 49.16           C  
ANISOU 4145  CD2 PHE H 153     6627   7790   4260   1146    -91    220       C  
ATOM   4146  CE1 PHE H 153     101.764  14.003 -19.100  1.00 45.77           C  
ANISOU 4146  CE1 PHE H 153     6541   7039   3809   1093   -101    187       C  
ATOM   4147  CE2 PHE H 153      99.715  14.031 -20.320  1.00 50.55           C  
ANISOU 4147  CE2 PHE H 153     6922   7925   4361   1357    -87    219       C  
ATOM   4148  CZ  PHE H 153     100.525  14.558 -19.340  1.00 49.62           C  
ANISOU 4148  CZ  PHE H 153     6996   7626   4230   1333    -90    192       C  
ATOM   4149  N   PRO H 154      98.789   9.787 -20.888  1.00 25.99           N  
ANISOU 4149  N   PRO H 154     3283   5179   1413   1009     11    166       N  
ATOM   4150  CA  PRO H 154      98.615  10.044 -19.448  1.00 37.25           C  
ANISOU 4150  CA  PRO H 154     4749   6582   2824   1107     96    143       C  
ATOM   4151  C   PRO H 154      98.936   8.879 -18.504  1.00 40.07           C  
ANISOU 4151  C   PRO H 154     5084   6899   3242    967    151    103       C  
ATOM   4152  O   PRO H 154      99.514   7.875 -18.910  1.00 57.59           O  
ANISOU 4152  O   PRO H 154     7281   9075   5525    797    120     86       O  
ATOM   4153  CB  PRO H 154      97.126  10.400 -19.338  1.00 39.71           C  
ANISOU 4153  CB  PRO H 154     4912   7130   3046   1347    138    192       C  
ATOM   4154  CG  PRO H 154      96.734  10.838 -20.698  1.00 40.31           C  
ANISOU 4154  CG  PRO H 154     4935   7296   3085   1394     35    249       C  
ATOM   4155  CD  PRO H 154      97.526   9.974 -21.616  1.00 27.51           C  
ANISOU 4155  CD  PRO H 154     3331   5586   1536   1142    -33    224       C  
ATOM   4156  N   GLU H 155      98.499   9.014 -17.248  1.00 47.34           N  
ANISOU 4156  N   GLU H 155     6026   7832   4130   1058    237     92       N  
ATOM   4157  CA  GLU H 155      99.185   8.345 -16.144  1.00 53.08           C  
ANISOU 4157  CA  GLU H 155     6845   8426   4898    917    272     53       C  
ATOM   4158  C   GLU H 155      98.887   6.851 -16.072  1.00 78.08           C  
ANISOU 4158  C   GLU H 155     9866  11690   8109    791    284     57       C  
ATOM   4159  O   GLU H 155      99.787   6.053 -15.782  1.00 84.68           O  
ANISOU 4159  O   GLU H 155    10772  12399   9003    630    261     31       O  
ATOM   4160  CB  GLU H 155      98.826   9.026 -14.820  1.00 55.99           C  
ANISOU 4160  CB  GLU H 155     7329   8753   5193   1048    363     35       C  
ATOM   4161  CG  GLU H 155      99.022   8.172 -13.555  1.00 63.15           C  
ANISOU 4161  CG  GLU H 155     8287   9602   6107    927    424     10       C  
ATOM   4162  CD  GLU H 155     100.477   7.851 -13.231  1.00 68.04           C  
ANISOU 4162  CD  GLU H 155     9063  10021   6769    721    349    -18       C  
ATOM   4163  OE1 GLU H 155     101.369   8.137 -14.057  1.00 73.21           O  
ANISOU 4163  OE1 GLU H 155     9754  10597   7466    653    260    -11       O  
ATOM   4164  OE2 GLU H 155     100.725   7.304 -12.134  1.00 69.76           O  
ANISOU 4164  OE2 GLU H 155     9362  10178   6967    628    383    -36       O  
ATOM   4165  N   SER H 156      97.640   6.447 -16.305  1.00 66.55           N  
ANISOU 4165  N   SER H 156     8201  10473   6613    868    314    105       N  
ATOM   4166  CA  SER H 156      97.209   5.096 -15.953  1.00 55.98           C  
ANISOU 4166  CA  SER H 156     6729   9254   5288    753    331    126       C  
ATOM   4167  C   SER H 156      97.598   4.088 -17.033  1.00 42.04           C  
ANISOU 4167  C   SER H 156     4913   7496   3563    597    223    113       C  
ATOM   4168  O   SER H 156      97.250   4.255 -18.208  1.00 36.10           O  
ANISOU 4168  O   SER H 156     4085   6846   2786    623    155    134       O  
ATOM   4169  CB  SER H 156      95.703   5.072 -15.710  1.00 66.54           C  
ANISOU 4169  CB  SER H 156     7837  10886   6559    881    414    215       C  
ATOM   4170  OG  SER H 156      94.988   5.422 -16.883  1.00 78.95           O  
ANISOU 4170  OG  SER H 156     9248  12666   8084    973    356    277       O  
ATOM   4171  N   VAL H 157      98.329   3.044 -16.626  1.00 27.92           N  
ANISOU 4171  N   VAL H 157     3192   5589   1825    446    206     78       N  
ATOM   4172  CA  VAL H 157      98.568   1.852 -17.433  1.00 28.22           C  
ANISOU 4172  CA  VAL H 157     3196   5643   1884    313    122     62       C  
ATOM   4173  C   VAL H 157      98.418   0.638 -16.526  1.00 23.61           C  
ANISOU 4173  C   VAL H 157     2570   5105   1295    198    134     74       C  
ATOM   4174  O   VAL H 157      98.512   0.737 -15.300  1.00 35.84           O  
ANISOU 4174  O   VAL H 157     4173   6600   2845    207    207     82       O  
ATOM   4175  CB  VAL H 157      99.961   1.835 -18.107  1.00 30.49           C  
ANISOU 4175  CB  VAL H 157     3649   5700   2236    265     82      7       C  
ATOM   4176  CG1 VAL H 157     100.074   2.930 -19.148  1.00 35.62           C  
ANISOU 4176  CG1 VAL H 157     4333   6328   2875    345     62     12       C  
ATOM   4177  CG2 VAL H 157     101.056   1.971 -17.066  1.00 32.06           C  
ANISOU 4177  CG2 VAL H 157     3990   5708   2485    239    121    -13       C  
ATOM   4178  N   THR H 158      98.177  -0.522 -17.139  1.00 23.91           N  
ANISOU 4178  N   THR H 158     2540   5231   1312     77     50     80       N  
ATOM   4179  CA  THR H 158      98.014  -1.770 -16.394  1.00 31.05           C  
ANISOU 4179  CA  THR H 158     3406   6193   2199    -64     33    105       C  
ATOM   4180  C   THR H 158      98.858  -2.862 -17.033  1.00 36.27           C  
ANISOU 4180  C   THR H 158     4188   6704   2890   -169    -66     40       C  
ATOM   4181  O   THR H 158      98.697  -3.157 -18.221  1.00 23.98           O  
ANISOU 4181  O   THR H 158     2644   5157   1311   -191   -157     19       O  
ATOM   4182  CB  THR H 158      96.547  -2.210 -16.346  1.00 26.16           C  
ANISOU 4182  CB  THR H 158     2551   5899   1490   -136     10    223       C  
ATOM   4183  OG1 THR H 158      96.080  -2.466 -17.676  1.00 68.79           O  
ANISOU 4183  OG1 THR H 158     7895  11383   6860   -185   -130    238       O  
ATOM   4184  CG2 THR H 158      95.679  -1.142 -15.701  1.00 39.81           C  
ANISOU 4184  CG2 THR H 158     4145   7796   3185     19    145    302       C  
ATOM   4185  N   VAL H 159      99.733  -3.478 -16.242  1.00 46.03           N  
ANISOU 4185  N   VAL H 159     5530   7796   4165   -221    -54     12       N  
ATOM   4186  CA  VAL H 159     100.574  -4.583 -16.695  1.00 22.43           C  
ANISOU 4186  CA  VAL H 159     2656   4672   1193   -291   -137    -46       C  
ATOM   4187  C   VAL H 159     100.051  -5.870 -16.074  1.00 23.37           C  
ANISOU 4187  C   VAL H 159     2731   4873   1274   -460   -213     -5       C  
ATOM   4188  O   VAL H 159     100.043  -6.018 -14.845  1.00 48.35           O  
ANISOU 4188  O   VAL H 159     5878   8058   4435   -514   -166     42       O  
ATOM   4189  CB  VAL H 159     102.050  -4.361 -16.339  1.00 23.60           C  
ANISOU 4189  CB  VAL H 159     2941   4618   1405   -228    -94    -88       C  
ATOM   4190  CG1 VAL H 159     102.822  -5.667 -16.448  1.00 26.26           C  
ANISOU 4190  CG1 VAL H 159     3368   4867   1740   -296   -170   -131       C  
ATOM   4191  CG2 VAL H 159     102.655  -3.321 -17.257  1.00 37.61           C  
ANISOU 4191  CG2 VAL H 159     4766   6313   3209   -114    -56   -112       C  
ATOM   4192  N   THR H 160      99.619  -6.799 -16.923  1.00 29.87           N  
ANISOU 4192  N   THR H 160     3565   5716   2067   -556   -350    -14       N  
ATOM   4193  CA  THR H 160      99.135  -8.105 -16.501  1.00 39.71           C  
ANISOU 4193  CA  THR H 160     4796   6994   3300   -751   -475     36       C  
ATOM   4194  C   THR H 160     100.075  -9.173 -17.040  1.00 35.60           C  
ANISOU 4194  C   THR H 160     4474   6250   2803   -759   -587    -66       C  
ATOM   4195  O   THR H 160     100.354  -9.209 -18.243  1.00 35.77           O  
ANISOU 4195  O   THR H 160     4603   6183   2804   -674   -639   -150       O  
ATOM   4196  CB  THR H 160      97.707  -8.354 -16.997  1.00 46.80           C  
ANISOU 4196  CB  THR H 160     5543   8073   4166   -879   -595    135       C  
ATOM   4197  OG1 THR H 160      96.855  -7.289 -16.555  1.00 43.73           O  
ANISOU 4197  OG1 THR H 160     4942   7939   3733   -829   -478    238       O  
ATOM   4198  CG2 THR H 160      97.177  -9.676 -16.460  1.00 53.37           C  
ANISOU 4198  CG2 THR H 160     6348   8909   5020  -1115   -743    225       C  
ATOM   4199  N   TRP H 161     100.558 -10.037 -16.152  1.00 39.24           N  
ANISOU 4199  N   TRP H 161     4994   6626   3290   -851   -624    -58       N  
ATOM   4200  CA  TRP H 161     101.543 -11.053 -16.498  1.00 48.03           C  
ANISOU 4200  CA  TRP H 161     6288   7539   4422   -835   -724   -155       C  
ATOM   4201  C   TRP H 161     100.857 -12.373 -16.818  1.00 27.49           C  
ANISOU 4201  C   TRP H 161     3743   4871   1831   -999   -930   -144       C  
ATOM   4202  O   TRP H 161     100.049 -12.868 -16.025  1.00 75.37           O  
ANISOU 4202  O   TRP H 161     9718  10996   7923  -1189   -992    -23       O  
ATOM   4203  CB  TRP H 161     102.543 -11.248 -15.358  1.00 57.42           C  
ANISOU 4203  CB  TRP H 161     7520   8646   5650   -840   -678   -147       C  
ATOM   4204  CG  TRP H 161     103.579 -10.177 -15.279  1.00 23.26           C  
ANISOU 4204  CG  TRP H 161     3200   4300   1336   -671   -532   -181       C  
ATOM   4205  CD1 TRP H 161     103.548  -9.057 -14.501  1.00 22.34           C  
ANISOU 4205  CD1 TRP H 161     3005   4247   1235   -625   -402   -121       C  
ATOM   4206  CD2 TRP H 161     104.810 -10.127 -16.006  1.00 22.83           C  
ANISOU 4206  CD2 TRP H 161     3244   4154   1277   -533   -512   -271       C  
ATOM   4207  NE1 TRP H 161     104.685  -8.311 -14.699  1.00 21.32           N  
ANISOU 4207  NE1 TRP H 161     2921   4043   1135   -488   -329   -157       N  
ATOM   4208  CE2 TRP H 161     105.476  -8.948 -15.619  1.00 26.13           C  
ANISOU 4208  CE2 TRP H 161     3617   4584   1727   -437   -382   -237       C  
ATOM   4209  CE3 TRP H 161     105.413 -10.965 -16.948  1.00 23.66           C  
ANISOU 4209  CE3 TRP H 161     3481   4174   1335   -483   -590   -376       C  
ATOM   4210  CZ2 TRP H 161     106.716  -8.586 -16.141  1.00 21.20           C  
ANISOU 4210  CZ2 TRP H 161     3034   3921   1099   -321   -327   -278       C  
ATOM   4211  CZ3 TRP H 161     106.642 -10.605 -17.464  1.00 23.30           C  
ANISOU 4211  CZ3 TRP H 161     3484   4110   1259   -343   -502   -435       C  
ATOM   4212  CH2 TRP H 161     107.281  -9.427 -17.060  1.00 22.07           C  
ANISOU 4212  CH2 TRP H 161     3239   3999   1148   -274   -370   -372       C  
ATOM   4213  N   ASN H 162     101.185 -12.938 -17.976  1.00 39.33           N  
ANISOU 4213  N   ASN H 162     5403   6241   3300   -928  -1035   -262       N  
ATOM   4214  CA  ASN H 162     100.716 -14.259 -18.391  1.00 58.77           C  
ANISOU 4214  CA  ASN H 162     7978   8575   5778  -1057  -1250   -280       C  
ATOM   4215  C   ASN H 162     101.939 -15.166 -18.481  1.00 59.10           C  
ANISOU 4215  C   ASN H 162     8220   8420   5815   -982  -1296   -409       C  
ATOM   4216  O   ASN H 162     102.647 -15.172 -19.494  1.00 45.29           O  
ANISOU 4216  O   ASN H 162     6615   6612   3983   -821  -1276   -551       O  
ATOM   4217  CB  ASN H 162      99.966 -14.188 -19.719  1.00 81.13           C  
ANISOU 4217  CB  ASN H 162    10851  11421   8552  -1037  -1351   -317       C  
ATOM   4218  CG  ASN H 162      98.698 -13.358 -19.630  1.00 91.96           C  
ANISOU 4218  CG  ASN H 162    12006  12994   9942  -1129  -1333   -172       C  
ATOM   4219  OD1 ASN H 162      98.037 -13.322 -18.591  1.00100.62           O  
ANISOU 4219  OD1 ASN H 162    12924  14212  11094  -1281  -1310    -22       O  
ATOM   4220  ND2 ASN H 162      98.352 -12.688 -20.723  1.00 80.33           N  
ANISOU 4220  ND2 ASN H 162    10542  11572   8409  -1036  -1342   -207       N  
ATOM   4221  N   SER H 163     102.191 -15.923 -17.413  1.00 70.30           N  
ANISOU 4221  N   SER H 163     9330   8939   8441   -581   -829  -1923       N  
ATOM   4222  CA  SER H 163     103.353 -16.799 -17.343  1.00 68.89           C  
ANISOU 4222  CA  SER H 163     9339   8603   8234   -556   -792  -1916       C  
ATOM   4223  C   SER H 163     102.928 -18.232 -17.059  1.00 85.67           C  
ANISOU 4223  C   SER H 163    11593  10562  10394   -739   -901  -1963       C  
ATOM   4224  O   SER H 163     101.859 -18.669 -17.498  1.00103.55           O  
ANISOU 4224  O   SER H 163    13831  12840  12673   -870  -1036  -2033       O  
ATOM   4225  CB  SER H 163     104.326 -16.314 -16.265  1.00 59.55           C  
ANISOU 4225  CB  SER H 163     8156   7378   7094   -486   -663  -1805       C  
ATOM   4226  OG  SER H 163     103.724 -16.338 -14.981  1.00 43.21           O  
ANISOU 4226  OG  SER H 163     6045   5260   5115   -593   -674  -1748       O  
ATOM   4227  N   GLY H 164     103.760 -18.971 -16.328  1.00 81.91           N  
ANISOU 4227  N   GLY H 164    11250   9935   9935   -761   -844  -1930       N  
ATOM   4228  CA  GLY H 164     103.377 -20.298 -15.900  1.00 85.18           C  
ANISOU 4228  CA  GLY H 164    11789  10187  10388   -953   -916  -1971       C  
ATOM   4229  C   GLY H 164     102.244 -20.265 -14.894  1.00 98.46           C  
ANISOU 4229  C   GLY H 164    13381  11838  12192  -1105  -1001  -1903       C  
ATOM   4230  O   GLY H 164     101.914 -19.230 -14.311  1.00118.34           O  
ANISOU 4230  O   GLY H 164    15738  14455  14770  -1049   -969  -1839       O  
ATOM   4231  N   SER H 165     101.632 -21.430 -14.691  1.00 91.67           N  
ANISOU 4231  N   SER H 165    12579  10857  11396  -1294  -1078  -1927       N  
ATOM   4232  CA  SER H 165     100.498 -21.543 -13.783  1.00 90.69           C  
ANISOU 4232  CA  SER H 165    12340  10680  11440  -1454  -1181  -1867       C  
ATOM   4233  C   SER H 165     100.912 -21.222 -12.351  1.00103.50           C  
ANISOU 4233  C   SER H 165    13942  12232  13152  -1381  -1107  -1766       C  
ATOM   4234  O   SER H 165     101.588 -22.027 -11.700  1.00117.28           O  
ANISOU 4234  O   SER H 165    15850  13821  14890  -1376  -1072  -1714       O  
ATOM   4235  CB  SER H 165      99.887 -22.943 -13.862  1.00 79.42           C  
ANISOU 4235  CB  SER H 165    10997   9119  10061  -1693  -1255  -1908       C  
ATOM   4236  OG  SER H 165      98.730 -23.038 -13.051  1.00 74.52           O  
ANISOU 4236  OG  SER H 165    10213   8431   9672  -1845  -1386  -1838       O  
ATOM   4237  N   LEU H 166     100.517 -20.049 -11.866  1.00 95.36           N  
ANISOU 4237  N   LEU H 166    12712  11340  12181  -1344  -1046  -1756       N  
ATOM   4238  CA  LEU H 166     100.819 -19.577 -10.506  1.00 89.98           C  
ANISOU 4238  CA  LEU H 166    11981  10645  11563  -1297   -916  -1693       C  
ATOM   4239  C   LEU H 166     102.340 -19.562 -10.324  1.00 82.49           C  
ANISOU 4239  C   LEU H 166    11232   9621  10488  -1101   -872  -1636       C  
ATOM   4240  O   LEU H 166     103.090 -19.439 -11.302  1.00 71.56           O  
ANISOU 4240  O   LEU H 166     9933   8293   8964  -1002   -838  -1642       O  
ATOM   4241  CB  LEU H 166     100.068 -20.414  -9.479  1.00 89.60           C  
ANISOU 4241  CB  LEU H 166    11880  10454  11710  -1503   -927  -1680       C  
ATOM   4242  CG  LEU H 166      98.607 -20.067  -9.174  1.00 80.91           C  
ANISOU 4242  CG  LEU H 166    10520   9493  10731  -1739   -834  -1669       C  
ATOM   4243  CD1 LEU H 166      97.694 -20.421 -10.338  1.00 70.96           C  
ANISOU 4243  CD1 LEU H 166     9153   8284   9525  -1852  -1007  -1721       C  
ATOM   4244  CD2 LEU H 166      98.149 -20.775  -7.908  1.00 77.98           C  
ANISOU 4244  CD2 LEU H 166    10147   8971  10509  -1956   -734  -1596       C  
ATOM   4245  N   SER H 167     102.796 -19.686  -9.075  1.00 95.59           N  
ANISOU 4245  N   SER H 167    12923  11184  12213  -1058   -832  -1587       N  
ATOM   4246  CA  SER H 167     104.222 -19.742  -8.741  1.00 87.10           C  
ANISOU 4246  CA  SER H 167    12000  10056  11039   -886   -793  -1504       C  
ATOM   4247  C   SER H 167     104.974 -18.528  -9.283  1.00 68.22           C  
ANISOU 4247  C   SER H 167     9590   7823   8506   -772   -671  -1470       C  
ATOM   4248  O   SER H 167     106.110 -18.635  -9.747  1.00 69.60           O  
ANISOU 4248  O   SER H 167     9848   8012   8587   -717   -577  -1451       O  
ATOM   4249  CB  SER H 167     104.858 -21.043  -9.239  1.00 92.30           C  
ANISOU 4249  CB  SER H 167    12892  10609  11570   -983   -740  -1489       C  
ATOM   4250  OG  SER H 167     104.849 -21.117 -10.655  1.00 91.46           O  
ANISOU 4250  OG  SER H 167    12753  10606  11393  -1018   -684  -1594       O  
ATOM   4251  N   SER H 168     104.336 -17.362  -9.221  1.00 43.59           N  
ANISOU 4251  N   SER H 168     6318   4839   5406   -766   -632  -1498       N  
ATOM   4252  CA  SER H 168     104.928 -16.129  -9.722  1.00 47.99           C  
ANISOU 4252  CA  SER H 168     6803   5544   5885   -636   -532  -1463       C  
ATOM   4253  C   SER H 168     104.673 -15.012  -8.724  1.00 41.98           C  
ANISOU 4253  C   SER H 168     5944   4863   5143   -609   -442  -1426       C  
ATOM   4254  O   SER H 168     103.549 -14.860  -8.236  1.00 50.41           O  
ANISOU 4254  O   SER H 168     6901   5990   6264   -720   -393  -1469       O  
ATOM   4255  CB  SER H 168     104.354 -15.752 -11.093  1.00 62.76           C  
ANISOU 4255  CB  SER H 168     8551   7561   7733   -629   -532  -1527       C  
ATOM   4256  OG  SER H 168     102.985 -15.401 -10.996  1.00 76.79           O  
ANISOU 4256  OG  SER H 168    10159   9447   9569   -730   -527  -1578       O  
ATOM   4257  N   SER H 169     105.710 -14.236  -8.422  1.00 29.50           N  
ANISOU 4257  N   SER H 169     4410   3289   3511   -495   -395  -1354       N  
ATOM   4258  CA  SER H 169     105.588 -13.081  -7.537  1.00 26.73           C  
ANISOU 4258  CA  SER H 169     4008   2999   3150   -456   -318  -1319       C  
ATOM   4259  C   SER H 169     105.710 -11.823  -8.389  1.00 34.01           C  
ANISOU 4259  C   SER H 169     4819   4064   4039   -380   -246  -1303       C  
ATOM   4260  O   SER H 169     106.787 -11.525  -8.917  1.00 45.94           O  
ANISOU 4260  O   SER H 169     6354   5569   5531   -306   -242  -1263       O  
ATOM   4261  CB  SER H 169     106.643 -13.109  -6.433  1.00 39.39           C  
ANISOU 4261  CB  SER H 169     5758   4477   4732   -392   -357  -1251       C  
ATOM   4262  OG  SER H 169     107.886 -12.612  -6.894  1.00 59.06           O  
ANISOU 4262  OG  SER H 169     8260   6989   7191   -336   -318  -1203       O  
ATOM   4263  N   VAL H 170     104.608 -11.091  -8.521  1.00 20.29           N  
ANISOU 4263  N   VAL H 170     2947   2464   2300   -413   -175  -1350       N  
ATOM   4264  CA  VAL H 170     104.541  -9.906  -9.368  1.00 22.91           C  
ANISOU 4264  CA  VAL H 170     3171   2933   2601   -337   -120  -1349       C  
ATOM   4265  C   VAL H 170     104.695  -8.662  -8.505  1.00 29.01           C  
ANISOU 4265  C   VAL H 170     3968   3714   3341   -281    -47  -1294       C  
ATOM   4266  O   VAL H 170     104.106  -8.562  -7.421  1.00 19.09           O  
ANISOU 4266  O   VAL H 170     2741   2446   2067   -324      4  -1307       O  
ATOM   4267  CB  VAL H 170     103.221  -9.871 -10.163  1.00 20.59           C  
ANISOU 4267  CB  VAL H 170     2718   2798   2307   -395   -109  -1448       C  
ATOM   4268  CG1 VAL H 170     103.102  -8.578 -10.952  1.00 20.04           C  
ANISOU 4268  CG1 VAL H 170     2551   2874   2191   -297    -60  -1446       C  
ATOM   4269  CG2 VAL H 170     103.140 -11.067 -11.093  1.00 21.70           C  
ANISOU 4269  CG2 VAL H 170     2871   2903   2470   -441   -214  -1501       C  
ATOM   4270  N   HIS H 171     105.500  -7.714  -8.982  1.00 25.87           N  
ANISOU 4270  N   HIS H 171     3572   3329   2930   -193    -33  -1240       N  
ATOM   4271  CA  HIS H 171     105.671  -6.418  -8.338  1.00 17.30           C  
ANISOU 4271  CA  HIS H 171     2529   2234   1812   -137     19  -1189       C  
ATOM   4272  C   HIS H 171     105.481  -5.334  -9.388  1.00 17.10           C  
ANISOU 4272  C   HIS H 171     2408   2323   1768    -77     67  -1193       C  
ATOM   4273  O   HIS H 171     106.255  -5.255 -10.347  1.00 16.88           O  
ANISOU 4273  O   HIS H 171     2351   2308   1756    -44     50  -1186       O  
ATOM   4274  CB  HIS H 171     107.050  -6.295  -7.682  1.00 16.78           C  
ANISOU 4274  CB  HIS H 171     2590   2031   1755   -112    -31  -1121       C  
ATOM   4275  CG  HIS H 171     107.303  -7.309  -6.611  1.00 17.14           C  
ANISOU 4275  CG  HIS H 171     2757   1957   1798   -148    -97  -1110       C  
ATOM   4276  ND1 HIS H 171     106.569  -7.360  -5.446  1.00 26.29           N  
ANISOU 4276  ND1 HIS H 171     3978   3089   2923   -152    -89  -1129       N  
ATOM   4277  CD2 HIS H 171     108.216  -8.305  -6.525  1.00 25.70           C  
ANISOU 4277  CD2 HIS H 171     3892   2960   2912   -179   -157  -1115       C  
ATOM   4278  CE1 HIS H 171     107.015  -8.348  -4.690  1.00 31.54           C  
ANISOU 4278  CE1 HIS H 171     4738   3646   3602   -164   -174  -1127       C  
ATOM   4279  NE2 HIS H 171     108.014  -8.937  -5.322  1.00 27.38           N  
ANISOU 4279  NE2 HIS H 171     4217   3078   3106   -191   -209  -1098       N  
ATOM   4280  N   THR H 172     104.454  -4.511  -9.212  1.00 22.15           N  
ANISOU 4280  N   THR H 172     3003   3052   2362    -51    136  -1209       N  
ATOM   4281  CA  THR H 172     104.175  -3.399 -10.111  1.00 21.66           C  
ANISOU 4281  CA  THR H 172     2875   3091   2264     27    180  -1201       C  
ATOM   4282  C   THR H 172     104.686  -2.114  -9.473  1.00 20.67           C  
ANISOU 4282  C   THR H 172     2869   2871   2113     90    225  -1131       C  
ATOM   4283  O   THR H 172     104.271  -1.760  -8.364  1.00 24.15           O  
ANISOU 4283  O   THR H 172     3398   3262   2517    107    265  -1114       O  
ATOM   4284  CB  THR H 172     102.680  -3.297 -10.412  1.00 22.55           C  
ANISOU 4284  CB  THR H 172     2854   3380   2333     37    224  -1268       C  
ATOM   4285  OG1 THR H 172     102.255  -4.468 -11.121  1.00 22.24           O  
ANISOU 4285  OG1 THR H 172     2704   3429   2317    -37    157  -1362       O  
ATOM   4286  CG2 THR H 172     102.389  -2.064 -11.256  1.00 29.07           C  
ANISOU 4286  CG2 THR H 172     3638   4301   3105    150    263  -1235       C  
ATOM   4287  N   PHE H 173     105.580  -1.421 -10.171  1.00 16.75           N  
ANISOU 4287  N   PHE H 173     2385   2351   1628    128    224  -1103       N  
ATOM   4288  CA  PHE H 173     106.176  -0.254  -9.539  1.00 16.65           C  
ANISOU 4288  CA  PHE H 173     2494   2230   1603    165    250  -1063       C  
ATOM   4289  C   PHE H 173     105.507   1.029 -10.017  1.00 17.14           C  
ANISOU 4289  C   PHE H 173     2557   2347   1609    252    339  -1043       C  
ATOM   4290  O   PHE H 173     105.189   1.159 -11.205  1.00 17.40           O  
ANISOU 4290  O   PHE H 173     2489   2497   1626    292    362  -1048       O  
ATOM   4291  CB  PHE H 173     107.675  -0.192  -9.833  1.00 22.04           C  
ANISOU 4291  CB  PHE H 173     3185   2843   2346    140    206  -1069       C  
ATOM   4292  CG  PHE H 173     108.439  -1.370  -9.300  1.00 16.10           C  
ANISOU 4292  CG  PHE H 173     2445   2024   1648     71    125  -1076       C  
ATOM   4293  CD1 PHE H 173     108.992  -1.335  -8.030  1.00 16.12           C  
ANISOU 4293  CD1 PHE H 173     2574   1893   1655     39     68  -1055       C  
ATOM   4294  CD2 PHE H 173     108.595  -2.516 -10.062  1.00 16.07           C  
ANISOU 4294  CD2 PHE H 173     2351   2079   1674     50    100  -1101       C  
ATOM   4295  CE1 PHE H 173     109.688  -2.420  -7.531  1.00 16.06           C  
ANISOU 4295  CE1 PHE H 173     2593   1824   1683    -15     -3  -1050       C  
ATOM   4296  CE2 PHE H 173     109.292  -3.604  -9.569  1.00 32.44           C  
ANISOU 4296  CE2 PHE H 173     4456   4080   3790      4     36  -1102       C  
ATOM   4297  CZ  PHE H 173     109.840  -3.555  -8.302  1.00 17.12           C  
ANISOU 4297  CZ  PHE H 173     2631   2017   1855    -28    -13  -1072       C  
ATOM   4298  N   PRO H 174     105.283   1.972  -9.102  1.00 17.48           N  
ANISOU 4298  N   PRO H 174     2732   2298   1611    292    390  -1020       N  
ATOM   4299  CA  PRO H 174     104.601   3.216  -9.472  1.00 18.18           C  
ANISOU 4299  CA  PRO H 174     2829   2420   1659    371    499  -1002       C  
ATOM   4300  C   PRO H 174     105.384   4.007 -10.509  1.00 35.19           C  
ANISOU 4300  C   PRO H 174     4964   4574   3832    400    516  -1003       C  
ATOM   4301  O   PRO H 174     106.612   3.936 -10.586  1.00 47.31           O  
ANISOU 4301  O   PRO H 174     6530   6035   5410    365    463  -1023       O  
ATOM   4302  CB  PRO H 174     104.509   3.977  -8.144  1.00 25.74           C  
ANISOU 4302  CB  PRO H 174     3893   3261   2625    332    546  -1011       C  
ATOM   4303  CG  PRO H 174     104.590   2.916  -7.097  1.00 18.35           C  
ANISOU 4303  CG  PRO H 174     3038   2263   1671    295    477   -987       C  
ATOM   4304  CD  PRO H 174     105.522   1.882  -7.652  1.00 17.51           C  
ANISOU 4304  CD  PRO H 174     2884   2169   1601    268    354  -1010       C  
ATOM   4305  N   ALA H 175     104.648   4.776 -11.307  1.00 23.21           N  
ANISOU 4305  N   ALA H 175     3380   3159   2279    485    583   -984       N  
ATOM   4306  CA  ALA H 175     105.240   5.508 -12.415  1.00 25.94           C  
ANISOU 4306  CA  ALA H 175     3703   3535   2617    542    614   -972       C  
ATOM   4307  C   ALA H 175     105.828   6.830 -11.946  1.00 43.03           C  
ANISOU 4307  C   ALA H 175     5971   5576   4801    583    640   -995       C  
ATOM   4308  O   ALA H 175     105.212   7.561 -11.164  1.00 64.24           O  
ANISOU 4308  O   ALA H 175     8730   8211   7468    643    642   -984       O  
ATOM   4309  CB  ALA H 175     104.196   5.759 -13.503  1.00 28.93           C  
ANISOU 4309  CB  ALA H 175     3984   4084   2924    657    633   -922       C  
ATOM   4310  N   LEU H 176     107.027   7.133 -12.430  1.00 46.53           N  
ANISOU 4310  N   LEU H 176     6447   5957   5274    588    647  -1010       N  
ATOM   4311  CA  LEU H 176     107.683   8.406 -12.178  1.00 21.16           C  
ANISOU 4311  CA  LEU H 176     3424   2539   2077    650    676   -981       C  
ATOM   4312  C   LEU H 176     107.761   9.206 -13.470  1.00 35.84           C  
ANISOU 4312  C   LEU H 176     5288   4438   3892    760    790   -861       C  
ATOM   4313  O   LEU H 176     107.561   8.682 -14.569  1.00 39.00           O  
ANISOU 4313  O   LEU H 176     5556   5039   4222    815    833   -838       O  
ATOM   4314  CB  LEU H 176     109.083   8.197 -11.590  1.00 21.04           C  
ANISOU 4314  CB  LEU H 176     3451   2339   2205    491    600  -1027       C  
ATOM   4315  CG  LEU H 176     109.141   7.520 -10.222  1.00 41.46           C  
ANISOU 4315  CG  LEU H 176     6072   4859   4823    402    468  -1129       C  
ATOM   4316  CD1 LEU H 176     110.584   7.339  -9.781  1.00 47.42           C  
ANISOU 4316  CD1 LEU H 176     6849   5439   5731    245    370  -1168       C  
ATOM   4317  CD2 LEU H 176     108.354   8.322  -9.198  1.00 20.98           C  
ANISOU 4317  CD2 LEU H 176     3595   2185   2190    448    440  -1103       C  
ATOM   4318  N   LEU H 177     108.060  10.492 -13.326  1.00 37.85           N  
ANISOU 4318  N   LEU H 177     5693   4490   4199    773    817   -770       N  
ATOM   4319  CA  LEU H 177     108.106  11.418 -14.449  1.00 33.02           C  
ANISOU 4319  CA  LEU H 177     5103   3882   3562    864    922   -615       C  
ATOM   4320  C   LEU H 177     109.560  11.723 -14.785  1.00 52.69           C  
ANISOU 4320  C   LEU H 177     7564   6230   6225    706    939   -526       C  
ATOM   4321  O   LEU H 177     110.283  12.299 -13.964  1.00 79.71           O  
ANISOU 4321  O   LEU H 177    11087   9402   9796    575    870   -528       O  
ATOM   4322  CB  LEU H 177     107.344  12.701 -14.124  1.00 35.48           C  
ANISOU 4322  CB  LEU H 177     5614   4051   3815   1006    955   -555       C  
ATOM   4323  CG  LEU H 177     107.012  13.607 -15.310  1.00 62.08           C  
ANISOU 4323  CG  LEU H 177     9023   7459   7106   1162   1066   -390       C  
ATOM   4324  CD1 LEU H 177     106.056  12.908 -16.264  1.00 48.37           C  
ANISOU 4324  CD1 LEU H 177     7135   6046   5199   1318   1098   -394       C  
ATOM   4325  CD2 LEU H 177     106.428  14.926 -14.829  1.00 88.47           C  
ANISOU 4325  CD2 LEU H 177    12597  10597  10421   1295   1086   -335       C  
ATOM   4326  N   GLN H 178     109.985  11.332 -15.986  1.00 31.29           N  
ANISOU 4326  N   GLN H 178     4713   3680   3494    720   1029   -449       N  
ATOM   4327  CA  GLN H 178     111.310  11.659 -16.492  1.00 27.18           C  
ANISOU 4327  CA  GLN H 178     4130   3063   3134    595   1096   -325       C  
ATOM   4328  C   GLN H 178     111.189  12.115 -17.938  1.00 41.22           C  
ANISOU 4328  C   GLN H 178     5898   4964   4800    729   1261   -156       C  
ATOM   4329  O   GLN H 178     110.392  11.566 -18.705  1.00 46.27           O  
ANISOU 4329  O   GLN H 178     6497   5842   5242    888   1293   -184       O  
ATOM   4330  CB  GLN H 178     112.273  10.465 -16.394  1.00 35.99           C  
ANISOU 4330  CB  GLN H 178     5060   4257   4358    465   1053   -407       C  
ATOM   4331  CG  GLN H 178     111.901   9.274 -17.265  1.00 50.71           C  
ANISOU 4331  CG  GLN H 178     6799   6405   6063    574   1097   -471       C  
ATOM   4332  CD  GLN H 178     113.054   8.307 -17.455  1.00 57.52           C  
ANISOU 4332  CD  GLN H 178     7490   7324   7040    479   1105   -503       C  
ATOM   4333  OE1 GLN H 178     112.888   7.230 -18.028  1.00 49.83           O  
ANISOU 4333  OE1 GLN H 178     6434   6543   5954    553   1117   -583       O  
ATOM   4334  NE2 GLN H 178     114.233   8.691 -16.978  1.00 66.17           N  
ANISOU 4334  NE2 GLN H 178     8532   8245   8367    319   1087   -441       N  
ATOM   4335  N   SER H 179     111.978  13.131 -18.297  1.00 42.50           N  
ANISOU 4335  N   SER H 179     6105   4954   5087    660   1355     24       N  
ATOM   4336  CA  SER H 179     111.971  13.700 -19.647  1.00 43.45           C  
ANISOU 4336  CA  SER H 179     6248   5157   5103    784   1534    222       C  
ATOM   4337  C   SER H 179     110.564  14.108 -20.079  1.00 53.44           C  
ANISOU 4337  C   SER H 179     7651   6528   6127   1025   1543    236       C  
ATOM   4338  O   SER H 179     110.205  14.007 -21.255  1.00 45.61           O  
ANISOU 4338  O   SER H 179     6648   5733   4947   1190   1641    321       O  
ATOM   4339  CB  SER H 179     112.585  12.730 -20.660  1.00 33.86           C  
ANISOU 4339  CB  SER H 179     4854   4178   3832    805   1643    245       C  
ATOM   4340  OG  SER H 179     113.949  12.483 -20.368  1.00 49.85           O  
ANISOU 4340  OG  SER H 179     6729   6110   6100    604   1661    271       O  
ATOM   4341  N   GLY H 180     109.756  14.567 -19.126  1.00 31.46           N  
ANISOU 4341  N   GLY H 180     4997   3619   3336   1064   1437    153       N  
ATOM   4342  CA  GLY H 180     108.402  14.990 -19.412  1.00 50.71           C  
ANISOU 4342  CA  GLY H 180     7541   6154   5574   1303   1438    167       C  
ATOM   4343  C   GLY H 180     107.413  13.879 -19.683  1.00 47.75           C  
ANISOU 4343  C   GLY H 180     7036   6089   5018   1430   1375     28       C  
ATOM   4344  O   GLY H 180     106.255  14.173 -20.003  1.00 43.28           O  
ANISOU 4344  O   GLY H 180     6514   5639   4292   1635   1364     46       O  
ATOM   4345  N   LEU H 181     107.820  12.617 -19.565  1.00 60.99           N  
ANISOU 4345  N   LEU H 181     8551   7896   6725   1314   1322   -106       N  
ATOM   4346  CA  LEU H 181     106.943  11.486 -19.829  1.00 63.42           C  
ANISOU 4346  CA  LEU H 181     8736   8473   6887   1396   1243   -243       C  
ATOM   4347  C   LEU H 181     106.970  10.526 -18.648  1.00 68.62           C  
ANISOU 4347  C   LEU H 181     9308   9103   7660   1232   1116   -423       C  
ATOM   4348  O   LEU H 181     107.887  10.545 -17.824  1.00 58.16           O  
ANISOU 4348  O   LEU H 181     8010   7596   6491   1082   1109   -454       O  
ATOM   4349  CB  LEU H 181     107.348  10.749 -21.112  1.00 55.32           C  
ANISOU 4349  CB  LEU H 181     7597   7630   5792   1388   1251   -213       C  
ATOM   4350  CG  LEU H 181     107.221  11.537 -22.414  1.00 30.27           C  
ANISOU 4350  CG  LEU H 181     4507   4521   2471   1558   1353    -30       C  
ATOM   4351  CD1 LEU H 181     107.778  10.731 -23.573  1.00 30.84           C  
ANISOU 4351  CD1 LEU H 181     4494   4743   2480   1540   1364    -22       C  
ATOM   4352  CD2 LEU H 181     105.770  11.910 -22.664  1.00 30.86           C  
ANISOU 4352  CD2 LEU H 181     4609   4691   2424   1719   1244    -16       C  
ATOM   4353  N   TYR H 182     105.946   9.681 -18.576  1.00 25.16           N  
ANISOU 4353  N   TYR H 182     3679   3747   2134   1199    970   -513       N  
ATOM   4354  CA  TYR H 182     105.861   8.696 -17.511  1.00 23.64           C  
ANISOU 4354  CA  TYR H 182     3412   3530   2040   1044    871   -654       C  
ATOM   4355  C   TYR H 182     106.698   7.465 -17.841  1.00 43.86           C  
ANISOU 4355  C   TYR H 182     5876   6143   4648    919    844   -727       C  
ATOM   4356  O   TYR H 182     106.840   7.072 -19.003  1.00 57.87           O  
ANISOU 4356  O   TYR H 182     7599   8033   6356    954    855   -695       O  
ATOM   4357  CB  TYR H 182     104.408   8.287 -17.266  1.00 23.46           C  
ANISOU 4357  CB  TYR H 182     3314   3612   1988   1063    777   -684       C  
ATOM   4358  CG  TYR H 182     103.582   9.338 -16.560  1.00 51.55           C  
ANISOU 4358  CG  TYR H 182     6957   7102   5529   1174    800   -638       C  
ATOM   4359  CD1 TYR H 182     103.853   9.695 -15.245  1.00 23.71           C  
ANISOU 4359  CD1 TYR H 182     3532   3401   2076   1118    811   -681       C  
ATOM   4360  CD2 TYR H 182     102.522   9.965 -17.204  1.00 56.73           C  
ANISOU 4360  CD2 TYR H 182     7604   7867   6084   1354    802   -555       C  
ATOM   4361  CE1 TYR H 182     103.099  10.654 -14.593  1.00 24.59           C  
ANISOU 4361  CE1 TYR H 182     3745   3434   2163   1234    834   -639       C  
ATOM   4362  CE2 TYR H 182     101.761  10.924 -16.559  1.00 61.32           C  
ANISOU 4362  CE2 TYR H 182     8268   8381   6649   1480    832   -507       C  
ATOM   4363  CZ  TYR H 182     102.053  11.264 -15.255  1.00 51.33           C  
ANISOU 4363  CZ  TYR H 182     7113   6929   5460   1417    853   -550       C  
ATOM   4364  OH  TYR H 182     101.298  12.217 -14.611  1.00 44.47           O  
ANISOU 4364  OH  TYR H 182     6349   5982   4566   1554    885   -504       O  
ATOM   4365  N   THR H 183     107.257   6.859 -16.795  1.00 37.10           N  
ANISOU 4365  N   THR H 183     5015   5186   3896    791    805   -823       N  
ATOM   4366  CA  THR H 183     108.053   5.646 -16.930  1.00 41.79           C  
ANISOU 4366  CA  THR H 183     5538   5796   4545    692    773   -886       C  
ATOM   4367  C   THR H 183     107.903   4.822 -15.661  1.00 42.12           C  
ANISOU 4367  C   THR H 183     5593   5746   4663    580    670   -957       C  
ATOM   4368  O   THR H 183     107.977   5.364 -14.553  1.00 56.94           O  
ANISOU 4368  O   THR H 183     7554   7498   6583    553    662   -986       O  
ATOM   4369  CB  THR H 183     109.532   5.971 -17.185  1.00 30.39           C  
ANISOU 4369  CB  THR H 183     4086   4314   3146    710    878   -880       C  
ATOM   4370  OG1 THR H 183     109.658   6.721 -18.399  1.00 54.08           O  
ANISOU 4370  OG1 THR H 183     7099   7389   6059    828   1004   -747       O  
ATOM   4371  CG2 THR H 183     110.349   4.694 -17.303  1.00 21.19           C  
ANISOU 4371  CG2 THR H 183     2829   3176   2047    629    836   -946       C  
ATOM   4372  N   MET H 184     107.678   3.521 -15.830  1.00 30.08           N  
ANISOU 4372  N   MET H 184     4006   4280   3144    527    582   -983       N  
ATOM   4373  CA  MET H 184     107.578   2.593 -14.714  1.00 35.49           C  
ANISOU 4373  CA  MET H 184     4697   4897   3890    432    484  -1026       C  
ATOM   4374  C   MET H 184     108.043   1.223 -15.189  1.00 23.14           C  
ANISOU 4374  C   MET H 184     3064   3376   2351    387    418  -1067       C  
ATOM   4375  O   MET H 184     108.489   1.056 -16.327  1.00 28.04           O  
ANISOU 4375  O   MET H 184     3648   4070   2935    435    454  -1066       O  
ATOM   4376  CB  MET H 184     106.151   2.553 -14.155  1.00 32.53           C  
ANISOU 4376  CB  MET H 184     4323   4555   3482    436    458  -1014       C  
ATOM   4377  CG  MET H 184     105.115   1.978 -15.103  1.00 26.39           C  
ANISOU 4377  CG  MET H 184     3441   3943   2643    476    418  -1028       C  
ATOM   4378  SD  MET H 184     104.928   0.195 -14.922  1.00 39.78           S  
ANISOU 4378  SD  MET H 184     5063   5672   4381    376    306  -1107       S  
ATOM   4379  CE  MET H 184     103.806  -0.151 -16.266  1.00 27.17           C  
ANISOU 4379  CE  MET H 184     3349   4288   2688    449    251  -1158       C  
ATOM   4380  N   SER H 185     107.931   0.233 -14.308  1.00 22.50           N  
ANISOU 4380  N   SER H 185     2982   3243   2323    305    333  -1098       N  
ATOM   4381  CA  SER H 185     108.375  -1.116 -14.622  1.00 17.53           C  
ANISOU 4381  CA  SER H 185     2309   2628   1725    265    272  -1142       C  
ATOM   4382  C   SER H 185     107.520  -2.111 -13.851  1.00 20.54           C  
ANISOU 4382  C   SER H 185     2687   2991   2125    196    199  -1161       C  
ATOM   4383  O   SER H 185     106.747  -1.742 -12.964  1.00 17.01           O  
ANISOU 4383  O   SER H 185     2270   2522   1672    178    205  -1141       O  
ATOM   4384  CB  SER H 185     109.860  -1.302 -14.296  1.00 17.41           C  
ANISOU 4384  CB  SER H 185     2294   2532   1791    239    269  -1168       C  
ATOM   4385  OG  SER H 185     110.117  -1.017 -12.931  1.00 39.33           O  
ANISOU 4385  OG  SER H 185     5127   5188   4627    179    231  -1161       O  
ATOM   4386  N   SER H 186     107.667  -3.387 -14.205  1.00 17.42           N  
ANISOU 4386  N   SER H 186     2268   2604   1747    166    143  -1205       N  
ATOM   4387  CA  SER H 186     106.961  -4.456 -13.510  1.00 17.41           C  
ANISOU 4387  CA  SER H 186     2271   2573   1770     94     85  -1230       C  
ATOM   4388  C   SER H 186     107.816  -5.713 -13.535  1.00 19.07           C  
ANISOU 4388  C   SER H 186     2517   2707   2023     65     36  -1254       C  
ATOM   4389  O   SER H 186     108.262  -6.136 -14.603  1.00 23.17           O  
ANISOU 4389  O   SER H 186     3019   3265   2518    109     31  -1293       O  
ATOM   4390  CB  SER H 186     105.595  -4.726 -14.151  1.00 18.19           C  
ANISOU 4390  CB  SER H 186     2292   2802   1818     96     61  -1289       C  
ATOM   4391  OG  SER H 186     104.917  -5.780 -13.489  1.00 20.68           O  
ANISOU 4391  OG  SER H 186     2600   3092   2166     10     14  -1333       O  
ATOM   4392  N   SER H 187     108.039  -6.306 -12.367  1.00 17.25           N  
ANISOU 4392  N   SER H 187     2352   2365   1836      6      2  -1229       N  
ATOM   4393  CA  SER H 187     108.835  -7.518 -12.248  1.00 17.48           C  
ANISOU 4393  CA  SER H 187     2435   2309   1899    -14    -45  -1244       C  
ATOM   4394  C   SER H 187     107.947  -8.705 -11.900  1.00 21.97           C  
ANISOU 4394  C   SER H 187     3045   2840   2464    -84    -98  -1274       C  
ATOM   4395  O   SER H 187     106.820  -8.553 -11.420  1.00 18.14           O  
ANISOU 4395  O   SER H 187     2542   2384   1967   -128    -95  -1276       O  
ATOM   4396  CB  SER H 187     109.926  -7.364 -11.184  1.00 17.19           C  
ANISOU 4396  CB  SER H 187     2451   2171   1910    -25    -58  -1208       C  
ATOM   4397  OG  SER H 187     109.373  -7.430  -9.880  1.00 16.96           O  
ANISOU 4397  OG  SER H 187     2497   2074   1874    -79    -81  -1174       O  
ATOM   4398  N   VAL H 188     108.477  -9.899 -12.148  1.00 18.82           N  
ANISOU 4398  N   VAL H 188     2691   2380   2080    -93   -143  -1317       N  
ATOM   4399  CA  VAL H 188     107.796 -11.144 -11.810  1.00 19.68           C  
ANISOU 4399  CA  VAL H 188     2871   2417   2190   -172   -205  -1348       C  
ATOM   4400  C   VAL H 188     108.856 -12.210 -11.575  1.00 24.88           C  
ANISOU 4400  C   VAL H 188     3618   2964   2873   -171   -237  -1368       C  
ATOM   4401  O   VAL H 188     109.857 -12.275 -12.293  1.00 35.99           O  
ANISOU 4401  O   VAL H 188     5003   4387   4286    -95   -220  -1400       O  
ATOM   4402  CB  VAL H 188     106.800 -11.562 -12.915  1.00 24.02           C  
ANISOU 4402  CB  VAL H 188     3387   3035   2704   -194   -242  -1415       C  
ATOM   4403  CG1 VAL H 188     107.517 -11.746 -14.242  1.00 21.24           C  
ANISOU 4403  CG1 VAL H 188     3030   2724   2315   -110   -239  -1471       C  
ATOM   4404  CG2 VAL H 188     106.060 -12.830 -12.521  1.00 21.77           C  
ANISOU 4404  CG2 VAL H 188     3180   2656   2435   -305   -323  -1451       C  
ATOM   4405  N   THR H 189     108.647 -13.034 -10.553  1.00 20.71           N  
ANISOU 4405  N   THR H 189     3195   2320   2353   -248   -279  -1353       N  
ATOM   4406  CA  THR H 189     109.577 -14.102 -10.210  1.00 28.15           C  
ANISOU 4406  CA  THR H 189     4237   3148   3312   -258   -301  -1374       C  
ATOM   4407  C   THR H 189     108.896 -15.444 -10.436  1.00 22.88           C  
ANISOU 4407  C   THR H 189     3672   2394   2629   -347   -357  -1428       C  
ATOM   4408  O   THR H 189     107.814 -15.696  -9.890  1.00 23.20           O  
ANISOU 4408  O   THR H 189     3763   2389   2663   -441   -404  -1406       O  
ATOM   4409  CB  THR H 189     110.061 -13.977  -8.766  1.00 21.04           C  
ANISOU 4409  CB  THR H 189     3411   2164   2419   -290   -294  -1314       C  
ATOM   4410  OG1 THR H 189     110.633 -12.679  -8.564  1.00 48.79           O  
ANISOU 4410  OG1 THR H 189     6843   5746   5949   -227   -261  -1271       O  
ATOM   4411  CG2 THR H 189     111.112 -15.033  -8.468  1.00 21.90           C  
ANISOU 4411  CG2 THR H 189     3578   2180   2562   -291   -297  -1355       C  
ATOM   4412  N   VAL H 190     109.529 -16.289 -11.244  1.00 23.93           N  
ANISOU 4412  N   VAL H 190     3831   2497   2764   -310   -361  -1506       N  
ATOM   4413  CA  VAL H 190     109.019 -17.615 -11.584  1.00 28.77           C  
ANISOU 4413  CA  VAL H 190     4552   3015   3363   -401   -408  -1580       C  
ATOM   4414  C   VAL H 190     110.138 -18.624 -11.362  1.00 26.59           C  
ANISOU 4414  C   VAL H 190     4340   2637   3128   -365   -386  -1637       C  
ATOM   4415  O   VAL H 190     111.327 -18.270 -11.404  1.00 26.04           O  
ANISOU 4415  O   VAL H 190     4210   2595   3089   -233   -361  -1632       O  
ATOM   4416  CB  VAL H 190     108.500 -17.670 -13.041  1.00 26.53           C  
ANISOU 4416  CB  VAL H 190     4233   2807   3038   -373   -444  -1660       C  
ATOM   4417  CG1 VAL H 190     107.341 -16.707 -13.231  1.00 25.78           C  
ANISOU 4417  CG1 VAL H 190     4041   2826   2929   -402   -468  -1620       C  
ATOM   4418  CG2 VAL H 190     109.623 -17.363 -14.018  1.00 26.45           C  
ANISOU 4418  CG2 VAL H 190     4167   2869   3015   -208   -398  -1706       C  
ATOM   4419  N   PRO H 191     109.796 -19.889 -11.117  1.00 34.93           N  
ANISOU 4419  N   PRO H 191     5498   3571   4205   -474   -401  -1700       N  
ATOM   4420  CA  PRO H 191     110.836 -20.894 -10.873  1.00 51.12           C  
ANISOU 4420  CA  PRO H 191     7587   5512   6324   -402   -397  -1766       C  
ATOM   4421  C   PRO H 191     111.705 -21.118 -12.100  1.00 60.80           C  
ANISOU 4421  C   PRO H 191     8808   6759   7535   -234   -417  -1843       C  
ATOM   4422  O   PRO H 191     111.304 -20.876 -13.240  1.00 73.24           O  
ANISOU 4422  O   PRO H 191    10369   8410   9047   -211   -429  -1887       O  
ATOM   4423  CB  PRO H 191     110.039 -22.155 -10.520  1.00 31.07           C  
ANISOU 4423  CB  PRO H 191     5124   2846   3835   -555   -409  -1836       C  
ATOM   4424  CG  PRO H 191     108.704 -21.939 -11.136  1.00 31.36           C  
ANISOU 4424  CG  PRO H 191     5148   2953   3815   -680   -438  -1821       C  
ATOM   4425  CD  PRO H 191     108.446 -20.469 -11.011  1.00 29.25           C  
ANISOU 4425  CD  PRO H 191     4817   2815   3482   -642   -435  -1694       C  
ATOM   4426  N   SER H 192     112.924 -21.596 -11.843  1.00 30.50           N  
ANISOU 4426  N   SER H 192     4985   2851   3752   -105   -423  -1864       N  
ATOM   4427  CA  SER H 192     113.878 -21.855 -12.914  1.00 31.44           C  
ANISOU 4427  CA  SER H 192     5107   2981   3856     73   -421  -1942       C  
ATOM   4428  C   SER H 192     113.449 -22.997 -13.824  1.00 46.91           C  
ANISOU 4428  C   SER H 192     7182   4856   5784     64   -458  -2068       C  
ATOM   4429  O   SER H 192     114.088 -23.212 -14.860  1.00 34.79           O  
ANISOU 4429  O   SER H 192     5669   3339   4211    214   -446  -2148       O  
ATOM   4430  CB  SER H 192     115.256 -22.157 -12.325  1.00 31.65           C  
ANISOU 4430  CB  SER H 192     5130   2939   3956    215   -430  -1933       C  
ATOM   4431  OG  SER H 192     115.184 -23.216 -11.388  1.00 55.84           O  
ANISOU 4431  OG  SER H 192     8294   5842   7079    161   -480  -1940       O  
ATOM   4432  N   SER H 193     112.396 -23.732 -13.465  1.00 60.50           N  
ANISOU 4432  N   SER H 193     8978   6484   7524   -109   -498  -2097       N  
ATOM   4433  CA  SER H 193     111.892 -24.788 -14.333  1.00 59.33           C  
ANISOU 4433  CA  SER H 193     8939   6249   7355   -141   -553  -2230       C  
ATOM   4434  C   SER H 193     111.071 -24.229 -15.488  1.00 61.87           C  
ANISOU 4434  C   SER H 193     9233   6697   7577   -181   -568  -2270       C  
ATOM   4435  O   SER H 193     111.020 -24.842 -16.560  1.00 71.54           O  
ANISOU 4435  O   SER H 193    10540   7893   8751   -127   -613  -2394       O  
ATOM   4436  CB  SER H 193     111.051 -25.775 -13.523  1.00 55.70           C  
ANISOU 4436  CB  SER H 193     8550   5636   6978   -325   -595  -2255       C  
ATOM   4437  OG  SER H 193     111.739 -26.194 -12.357  1.00 58.07           O  
ANISOU 4437  OG  SER H 193     8876   5823   7367   -283   -589  -2200       O  
ATOM   4438  N   THR H 194     110.431 -23.076 -15.293  1.00 46.46           N  
ANISOU 4438  N   THR H 194     7180   4879   5592   -259   -542  -2170       N  
ATOM   4439  CA  THR H 194     109.561 -22.514 -16.326  1.00 46.23           C  
ANISOU 4439  CA  THR H 194     7123   4967   5474   -292   -577  -2198       C  
ATOM   4440  C   THR H 194     110.372 -21.783 -17.392  1.00 44.77           C  
ANISOU 4440  C   THR H 194     6888   4905   5216    -86   -532  -2214       C  
ATOM   4441  O   THR H 194     110.514 -22.263 -18.520  1.00 56.45           O  
ANISOU 4441  O   THR H 194     8438   6383   6626      0   -556  -2331       O  
ATOM   4442  CB  THR H 194     108.525 -21.581 -15.691  1.00 49.86           C  
ANISOU 4442  CB  THR H 194     7501   5509   5932   -433   -581  -2080       C  
ATOM   4443  OG1 THR H 194     109.192 -20.488 -15.047  1.00 56.23           O  
ANISOU 4443  OG1 THR H 194     8212   6394   6761   -338   -510  -1959       O  
ATOM   4444  CG2 THR H 194     107.690 -22.332 -14.665  1.00 34.44           C  
ANISOU 4444  CG2 THR H 194     5604   3440   4042   -650   -604  -2068       C  
ATOM   4445  N   TRP H 195     110.912 -20.619 -17.049  1.00 49.93           N  
ANISOU 4445  N   TRP H 195     7425   5664   5883     -7   -461  -2103       N  
ATOM   4446  CA  TRP H 195     111.634 -19.835 -18.042  1.00 58.00           C  
ANISOU 4446  CA  TRP H 195     8385   6811   6843    167   -395  -2112       C  
ATOM   4447  C   TRP H 195     113.015 -20.439 -18.292  1.00 54.70           C  
ANISOU 4447  C   TRP H 195     8009   6335   6439    335   -344  -2171       C  
ATOM   4448  O   TRP H 195     113.711 -20.813 -17.344  1.00 52.98           O  
ANISOU 4448  O   TRP H 195     7792   6028   6310    347   -337  -2138       O  
ATOM   4449  CB  TRP H 195     111.773 -18.385 -17.582  1.00 48.77           C  
ANISOU 4449  CB  TRP H 195     7070   5762   5699    183   -335  -1983       C  
ATOM   4450  CG  TRP H 195     112.043 -17.432 -18.703  1.00 29.93           C  
ANISOU 4450  CG  TRP H 195     4617   3521   3234    307   -268  -1986       C  
ATOM   4451  CD1 TRP H 195     111.157 -17.017 -19.654  1.00 30.42           C  
ANISOU 4451  CD1 TRP H 195     4677   3680   3202    298   -292  -2015       C  
ATOM   4452  CD2 TRP H 195     113.282 -16.773 -18.993  1.00 29.54           C  
ANISOU 4452  CD2 TRP H 195     4492   3540   3191    462   -165  -1962       C  
ATOM   4453  NE1 TRP H 195     111.767 -16.142 -20.520  1.00 41.73           N  
ANISOU 4453  NE1 TRP H 195     6055   5232   4570    437   -197  -2000       N  
ATOM   4454  CE2 TRP H 195     113.071 -15.974 -20.135  1.00 41.55           C  
ANISOU 4454  CE2 TRP H 195     5977   5199   4612    539   -116  -1974       C  
ATOM   4455  CE3 TRP H 195     114.547 -16.780 -18.399  1.00 29.30           C  
ANISOU 4455  CE3 TRP H 195     4407   3479   3247    554   -122  -1949       C  
ATOM   4456  CZ2 TRP H 195     114.079 -15.190 -20.694  1.00 34.47           C  
ANISOU 4456  CZ2 TRP H 195     4999   4404   3694    694      0  -1959       C  
ATOM   4457  CZ3 TRP H 195     115.546 -16.000 -18.955  1.00 29.48           C  
ANISOU 4457  CZ3 TRP H 195     4329   3608   3263    710    -22  -1947       C  
ATOM   4458  CH2 TRP H 195     115.306 -15.217 -20.091  1.00 35.99           C  
ANISOU 4458  CH2 TRP H 195     5127   4565   3982    772     52  -1945       C  
ATOM   4459  N   PRO H 196     113.443 -20.537 -19.561  1.00 52.80           N  
ANISOU 4459  N   PRO H 196     7808   6147   6107    481   -304  -2258       N  
ATOM   4460  CA  PRO H 196     112.688 -20.080 -20.729  1.00 35.73           C  
ANISOU 4460  CA  PRO H 196     5655   4097   3824    488   -318  -2301       C  
ATOM   4461  C   PRO H 196     111.907 -21.186 -21.432  1.00 45.09           C  
ANISOU 4461  C   PRO H 196     6988   5204   4941    435   -426  -2444       C  
ATOM   4462  O   PRO H 196     111.407 -20.958 -22.534  1.00 43.64           O  
ANISOU 4462  O   PRO H 196     6837   5107   4639    470   -452  -2506       O  
ATOM   4463  CB  PRO H 196     113.783 -19.532 -21.655  1.00 36.26           C  
ANISOU 4463  CB  PRO H 196     5683   4270   3823    705   -198  -2315       C  
ATOM   4464  CG  PRO H 196     115.120 -20.011 -21.056  1.00 36.55           C  
ANISOU 4464  CG  PRO H 196     5705   4229   3953    829   -146  -2318       C  
ATOM   4465  CD  PRO H 196     114.793 -20.967 -19.949  1.00 51.12           C  
ANISOU 4465  CD  PRO H 196     7618   5909   5897    688   -238  -2318       C  
ATOM   4466  N   SER H 197     111.810 -22.364 -20.808  1.00 46.99           N  
ANISOU 4466  N   SER H 197     7322   5279   5254    352   -494  -2498       N  
ATOM   4467  CA  SER H 197     111.089 -23.472 -21.430  1.00 42.17           C  
ANISOU 4467  CA  SER H 197     6856   4570   4595    286   -608  -2646       C  
ATOM   4468  C   SER H 197     109.626 -23.118 -21.662  1.00 51.29           C  
ANISOU 4468  C   SER H 197     7984   5791   5712    105   -704  -2647       C  
ATOM   4469  O   SER H 197     109.037 -23.511 -22.675  1.00 59.64           O  
ANISOU 4469  O   SER H 197     9128   6858   6676     97   -795  -2769       O  
ATOM   4470  CB  SER H 197     111.209 -24.728 -20.568  1.00 59.04           C  
ANISOU 4470  CB  SER H 197     9085   6505   6840    210   -658  -2687       C  
ATOM   4471  OG  SER H 197     112.558 -25.144 -20.462  1.00 88.80           O  
ANISOU 4471  OG  SER H 197    12892  10210  10639    402   -590  -2701       O  
ATOM   4472  N   GLN H 198     109.025 -22.379 -20.737  1.00 51.34           N  
ANISOU 4472  N   GLN H 198     7875   5846   5787    -33   -693  -2515       N  
ATOM   4473  CA  GLN H 198     107.671 -21.876 -20.896  1.00 43.82           C  
ANISOU 4473  CA  GLN H 198     6869   4977   4805   -186   -774  -2493       C  
ATOM   4474  C   GLN H 198     107.703 -20.414 -21.324  1.00 38.17           C  
ANISOU 4474  C   GLN H 198     6031   4445   4027    -78   -713  -2403       C  
ATOM   4475  O   GLN H 198     108.675 -19.693 -21.089  1.00 38.70           O  
ANISOU 4475  O   GLN H 198     6027   4564   4112     54   -596  -2321       O  
ATOM   4476  CB  GLN H 198     106.875 -22.028 -19.597  1.00 59.73           C  
ANISOU 4476  CB  GLN H 198     8846   6921   6928   -404   -803  -2406       C  
ATOM   4477  CG  GLN H 198     106.725 -23.463 -19.121  1.00 68.07           C  
ANISOU 4477  CG  GLN H 198    10012   7791   8059   -539   -853  -2494       C  
ATOM   4478  CD  GLN H 198     105.842 -23.577 -17.895  1.00 80.04           C  
ANISOU 4478  CD  GLN H 198    11490   9254   9668   -771   -864  -2408       C  
ATOM   4479  OE1 GLN H 198     105.239 -22.596 -17.458  1.00 84.71           O  
ANISOU 4479  OE1 GLN H 198    11988   9944  10255   -827   -860  -2283       O  
ATOM   4480  NE2 GLN H 198     105.760 -24.777 -17.331  1.00 89.80           N  
ANISOU 4480  NE2 GLN H 198    12798  10326  10995   -892   -879  -2478       N  
ATOM   4481  N   THR H 199     106.620 -19.984 -21.965  1.00 55.51           N  
ANISOU 4481  N   THR H 199     8195   6739   6156   -141   -798  -2424       N  
ATOM   4482  CA  THR H 199     106.503 -18.617 -22.453  1.00 41.07           C  
ANISOU 4482  CA  THR H 199     6254   5084   4265    -40   -749  -2351       C  
ATOM   4483  C   THR H 199     105.952 -17.722 -21.351  1.00 34.64           C  
ANISOU 4483  C   THR H 199     5300   4313   3549   -130   -725  -2208       C  
ATOM   4484  O   THR H 199     104.920 -18.030 -20.747  1.00 55.16           O  
ANISOU 4484  O   THR H 199     7882   6869   6207   -304   -817  -2193       O  
ATOM   4485  CB  THR H 199     105.600 -18.557 -23.687  1.00 39.09           C  
ANISOU 4485  CB  THR H 199     6036   4927   3888    -42   -863  -2447       C  
ATOM   4486  OG1 THR H 199     106.133 -19.403 -24.713  1.00 60.52           O  
ANISOU 4486  OG1 THR H 199     8900   7598   6498     61   -888  -2591       O  
ATOM   4487  CG2 THR H 199     105.514 -17.136 -24.214  1.00 37.92           C  
ANISOU 4487  CG2 THR H 199     5772   4964   3671     88   -810  -2381       C  
ATOM   4488  N   VAL H 200     106.648 -16.619 -21.089  1.00 32.53           N  
ANISOU 4488  N   VAL H 200     4933   4127   3299    -14   -603  -2107       N  
ATOM   4489  CA  VAL H 200     106.252 -15.642 -20.082  1.00 49.17           C  
ANISOU 4489  CA  VAL H 200     6909   6283   5489    -64   -564  -1982       C  
ATOM   4490  C   VAL H 200     106.078 -14.307 -20.792  1.00 45.75           C  
ANISOU 4490  C   VAL H 200     6362   6028   4992     50   -520  -1959       C  
ATOM   4491  O   VAL H 200     107.055 -13.728 -21.285  1.00 29.28           O  
ANISOU 4491  O   VAL H 200     4268   3996   2861    188   -418  -1937       O  
ATOM   4492  CB  VAL H 200     107.278 -15.537 -18.946  1.00 42.49           C  
ANISOU 4492  CB  VAL H 200     6042   5364   4739    -41   -472  -1898       C  
ATOM   4493  CG1 VAL H 200     106.896 -14.423 -17.985  1.00 26.62           C  
ANISOU 4493  CG1 VAL H 200     3909   3412   2794    -74   -427  -1783       C  
ATOM   4494  CG2 VAL H 200     107.394 -16.864 -18.212  1.00 29.57           C  
ANISOU 4494  CG2 VAL H 200     4516   3560   3160   -143   -521  -1932       C  
ATOM   4495  N   THR H 201     104.841 -13.819 -20.852  1.00 29.92           N  
ANISOU 4495  N   THR H 201     4263   4121   2983     -5   -594  -1967       N  
ATOM   4496  CA  THR H 201     104.526 -12.577 -21.541  1.00 29.66           C  
ANISOU 4496  CA  THR H 201     4128   4266   2877    102   -563  -1953       C  
ATOM   4497  C   THR H 201     104.022 -11.539 -20.549  1.00 27.88           C  
ANISOU 4497  C   THR H 201     3750   4109   2735     68   -509  -1868       C  
ATOM   4498  O   THR H 201     103.354 -11.869 -19.565  1.00 27.68           O  
ANISOU 4498  O   THR H 201     3679   4035   2804    -58   -548  -1857       O  
ATOM   4499  CB  THR H 201     103.464 -12.788 -22.628  1.00 48.92           C  
ANISOU 4499  CB  THR H 201     6575   6800   5214     99   -706  -2059       C  
ATOM   4500  OG1 THR H 201     102.163 -12.804 -22.027  1.00 65.30           O  
ANISOU 4500  OG1 THR H 201     8534   8911   7367    -36   -808  -2071       O  
ATOM   4501  CG2 THR H 201     103.692 -14.106 -23.347  1.00 35.86           C  
ANISOU 4501  CG2 THR H 201     5093   5039   3496     73   -794  -2168       C  
ATOM   4502  N   CYS H 202     104.348 -10.278 -20.815  1.00 52.65           N  
ANISOU 4502  N   CYS H 202     6819   7357   5827    182   -414  -1808       N  
ATOM   4503  CA  CYS H 202     103.812  -9.152 -20.064  1.00 39.06           C  
ANISOU 4503  CA  CYS H 202     4966   5722   4152    172   -360  -1743       C  
ATOM   4504  C   CYS H 202     102.918  -8.334 -20.985  1.00 40.05           C  
ANISOU 4504  C   CYS H 202     5011   6038   4170    258   -402  -1778       C  
ATOM   4505  O   CYS H 202     103.294  -8.041 -22.127  1.00 34.43           O  
ANISOU 4505  O   CYS H 202     4356   5388   3338    379   -393  -1785       O  
ATOM   4506  CB  CYS H 202     104.931  -8.287 -19.467  1.00 34.23           C  
ANISOU 4506  CB  CYS H 202     4359   5062   3583    220   -225  -1632       C  
ATOM   4507  SG  CYS H 202     105.897  -7.283 -20.628  1.00 44.03           S  
ANISOU 4507  SG  CYS H 202     5634   6381   4717    379   -127  -1586       S  
ATOM   4508  N   SER H 203     101.727  -7.998 -20.497  1.00 41.30           N  
ANISOU 4508  N   SER H 203     5035   6300   4357    205   -447  -1803       N  
ATOM   4509  CA  SER H 203     100.751  -7.219 -21.246  1.00 33.89           C  
ANISOU 4509  CA  SER H 203     3994   5568   3316    294   -505  -1838       C  
ATOM   4510  C   SER H 203     100.662  -5.821 -20.652  1.00 27.74           C  
ANISOU 4510  C   SER H 203     3128   4880   2532    365   -389  -1752       C  
ATOM   4511  O   SER H 203     100.420  -5.665 -19.451  1.00 26.63           O  
ANISOU 4511  O   SER H 203     2922   4711   2484    284   -333  -1731       O  
ATOM   4512  CB  SER H 203      99.377  -7.891 -21.224  1.00 29.75           C  
ANISOU 4512  CB  SER H 203     3357   5125   2821    182   -664  -1942       C  
ATOM   4513  OG  SER H 203      99.427  -9.166 -21.836  1.00 50.15           O  
ANISOU 4513  OG  SER H 203     6056   7597   5401    108   -790  -2014       O  
ATOM   4514  N   VAL H 204     100.859  -4.814 -21.493  1.00 26.95           N  
ANISOU 4514  N   VAL H 204     3051   4875   2313    521   -349  -1696       N  
ATOM   4515  CA  VAL H 204     100.794  -3.417 -21.089  1.00 35.89           C  
ANISOU 4515  CA  VAL H 204     4145   6069   3424    607   -243  -1594       C  
ATOM   4516  C   VAL H 204      99.589  -2.798 -21.783  1.00 27.72           C  
ANISOU 4516  C   VAL H 204     3002   5273   2258    734   -324  -1628       C  
ATOM   4517  O   VAL H 204      99.557  -2.680 -23.014  1.00 29.13           O  
ANISOU 4517  O   VAL H 204     3229   5535   2304    853   -384  -1634       O  
ATOM   4518  CB  VAL H 204     102.084  -2.664 -21.431  1.00 25.26           C  
ANISOU 4518  CB  VAL H 204     2930   4612   2055    679   -116  -1469       C  
ATOM   4519  CG1 VAL H 204     102.037  -1.253 -20.867  1.00 24.48           C  
ANISOU 4519  CG1 VAL H 204     2828   4510   1963    736     -8  -1351       C  
ATOM   4520  CG2 VAL H 204     103.283  -3.423 -20.895  1.00 24.11           C  
ANISOU 4520  CG2 VAL H 204     2869   4272   2020    572    -68  -1458       C  
ATOM   4521  N   ALA H 205      98.595  -2.413 -20.992  1.00 27.78           N  
ANISOU 4521  N   ALA H 205     2864   5406   2286    724   -327  -1650       N  
ATOM   4522  CA  ALA H 205      97.374  -1.796 -21.488  1.00 29.50           C  
ANISOU 4522  CA  ALA H 205     2942   5891   2376    860   -411  -1678       C  
ATOM   4523  C   ALA H 205      97.388  -0.320 -21.117  1.00 42.76           C  
ANISOU 4523  C   ALA H 205     4643   7592   4010   1015   -262  -1534       C  
ATOM   4524  O   ALA H 205      97.433   0.028 -19.929  1.00 27.65           O  
ANISOU 4524  O   ALA H 205     2723   5584   2197    961   -140  -1479       O  
ATOM   4525  CB  ALA H 205      96.137  -2.488 -20.916  1.00 70.19           C  
ANISOU 4525  CB  ALA H 205     7880  11204   7585    734   -538  -1802       C  
ATOM   4526  N   HIS H 206      97.367   0.538 -22.137  1.00 48.35           N  
ANISOU 4526  N   HIS H 206     5409   8382   4580   1205   -267  -1452       N  
ATOM   4527  CA  HIS H 206      97.258   1.987 -21.988  1.00 29.84           C  
ANISOU 4527  CA  HIS H 206     3107   6039   2192   1371   -145  -1292       C  
ATOM   4528  C   HIS H 206      95.956   2.398 -22.662  1.00 35.88           C  
ANISOU 4528  C   HIS H 206     3730   7120   2785   1580   -255  -1321       C  
ATOM   4529  O   HIS H 206      95.921   2.628 -23.883  1.00 33.59           O  
ANISOU 4529  O   HIS H 206     3498   6921   2343   1722   -341  -1298       O  
ATOM   4530  CB  HIS H 206      98.461   2.700 -22.603  1.00 29.32           C  
ANISOU 4530  CB  HIS H 206     3248   5787   2106   1417    -43  -1153       C  
ATOM   4531  CG  HIS H 206      98.495   4.174 -22.342  1.00 29.29           C  
ANISOU 4531  CG  HIS H 206     3326   5710   2094   1541     86   -987       C  
ATOM   4532  ND1 HIS H 206      98.762   5.098 -23.330  1.00 30.41           N  
ANISOU 4532  ND1 HIS H 206     3580   5864   2109   1709    128   -870       N  
ATOM   4533  CD2 HIS H 206      98.301   4.885 -21.206  1.00 28.83           C  
ANISOU 4533  CD2 HIS H 206     3275   5541   2136   1524    186   -917       C  
ATOM   4534  CE1 HIS H 206      98.729   6.313 -22.814  1.00 30.31           C  
ANISOU 4534  CE1 HIS H 206     3638   5753   2127   1786    242   -741       C  
ATOM   4535  NE2 HIS H 206      98.453   6.212 -21.526  1.00 29.19           N  
ANISOU 4535  NE2 HIS H 206     3439   5528   2124   1677    275   -772       N  
ATOM   4536  N   PRO H 207      94.852   2.473 -21.911  1.00 43.41           N  
ANISOU 4536  N   PRO H 207     4481   8205   3807   1586   -263  -1327       N  
ATOM   4537  CA  PRO H 207      93.570   2.842 -22.528  1.00 35.25           C  
ANISOU 4537  CA  PRO H 207     3264   7409   2723   1742   -403  -1280       C  
ATOM   4538  C   PRO H 207      93.499   4.297 -22.945  1.00 35.98           C  
ANISOU 4538  C   PRO H 207     3456   7528   2687   2024   -306  -1118       C  
ATOM   4539  O   PRO H 207      92.671   4.637 -23.799  1.00 54.77           O  
ANISOU 4539  O   PRO H 207     5744  10106   4961   2199   -447  -1079       O  
ATOM   4540  CB  PRO H 207      92.549   2.525 -21.429  1.00 35.69           C  
ANISOU 4540  CB  PRO H 207     3058   7516   2986   1629   -388  -1267       C  
ATOM   4541  CG  PRO H 207      93.320   2.678 -20.163  1.00 33.33           C  
ANISOU 4541  CG  PRO H 207     2889   6986   2789   1532   -163  -1238       C  
ATOM   4542  CD  PRO H 207      94.716   2.207 -20.468  1.00 31.54           C  
ANISOU 4542  CD  PRO H 207     2897   6589   2498   1429   -150  -1323       C  
ATOM   4543  N   ALA H 208      94.333   5.164 -22.369  1.00 34.38           N  
ANISOU 4543  N   ALA H 208     3444   7124   2494   2072    -85  -1023       N  
ATOM   4544  CA  ALA H 208      94.341   6.563 -22.779  1.00 35.24           C  
ANISOU 4544  CA  ALA H 208     3690   7186   2513   2303     -4   -844       C  
ATOM   4545  C   ALA H 208      94.728   6.703 -24.245  1.00 36.43           C  
ANISOU 4545  C   ALA H 208     3973   7414   2455   2434    -90   -822       C  
ATOM   4546  O   ALA H 208      94.181   7.548 -24.962  1.00 62.90           O  
ANISOU 4546  O   ALA H 208     7350  10908   5642   2700   -113   -727       O  
ATOM   4547  CB  ALA H 208      95.288   7.360 -21.887  1.00 33.44           C  
ANISOU 4547  CB  ALA H 208     3677   6594   2436   2189    169   -712       C  
ATOM   4548  N   SER H 209      95.669   5.884 -24.708  1.00 35.54           N  
ANISOU 4548  N   SER H 209     3954   7189   2361   2261   -129   -891       N  
ATOM   4549  CA  SER H 209      95.988   5.782 -26.124  1.00 37.03           C  
ANISOU 4549  CA  SER H 209     4252   7431   2388   2356   -212   -880       C  
ATOM   4550  C   SER H 209      95.328   4.577 -26.779  1.00 45.92           C  
ANISOU 4550  C   SER H 209     5250   8755   3444   2311   -445  -1062       C  
ATOM   4551  O   SER H 209      95.512   4.365 -27.982  1.00 50.41           O  
ANISOU 4551  O   SER H 209     5917   9342   3894   2378   -526  -1070       O  
ATOM   4552  CB  SER H 209      97.506   5.714 -26.328  1.00 35.60           C  
ANISOU 4552  CB  SER H 209     4263   6979   2286   2213    -79   -818       C  
ATOM   4553  OG  SER H 209      98.047   4.536 -25.757  1.00 33.95           O  
ANISOU 4553  OG  SER H 209     4012   6663   2225   1965    -98   -948       O  
ATOM   4554  N   SER H 210      94.565   3.795 -26.014  1.00 43.58           N  
ANISOU 4554  N   SER H 210     4746   8579   3235   2180   -557  -1200       N  
ATOM   4555  CA  SER H 210      93.875   2.603 -26.509  1.00 50.65           C  
ANISOU 4555  CA  SER H 210     5502   9588   4153   2059   -802  -1360       C  
ATOM   4556  C   SER H 210      94.847   1.654 -27.205  1.00 43.07           C  
ANISOU 4556  C   SER H 210     4717   8440   3207   1927   -810  -1440       C  
ATOM   4557  O   SER H 210      94.592   1.150 -28.301  1.00 49.94           O  
ANISOU 4557  O   SER H 210     5635   9352   3988   1955   -966  -1503       O  
ATOM   4558  CB  SER H 210      92.715   2.982 -27.433  1.00 59.23           C  
ANISOU 4558  CB  SER H 210     6485  10888   5130   2240   -989  -1326       C  
ATOM   4559  OG  SER H 210      93.183   3.566 -28.636  1.00 84.08           O  
ANISOU 4559  OG  SER H 210     9852  14001   8094   2430   -958  -1243       O  
ATOM   4560  N   THR H 211      95.981   1.409 -26.552  1.00 37.05           N  
ANISOU 4560  N   THR H 211     4058   7457   2561   1786   -644  -1427       N  
ATOM   4561  CA  THR H 211      97.018   0.545 -27.099  1.00 36.70           C  
ANISOU 4561  CA  THR H 211     4170   7233   2540   1679   -628  -1473       C  
ATOM   4562  C   THR H 211      97.344  -0.557 -26.103  1.00 35.02           C  
ANISOU 4562  C   THR H 211     3907   6876   2520   1429   -621  -1576       C  
ATOM   4563  O   THR H 211      97.385  -0.320 -24.893  1.00 33.26           O  
ANISOU 4563  O   THR H 211     3611   6602   2423   1344   -522  -1548       O  
ATOM   4564  CB  THR H 211      98.289   1.336 -27.437  1.00 65.44           C  
ANISOU 4564  CB  THR H 211     8002  10721   6143   1755   -429  -1314       C  
ATOM   4565  OG1 THR H 211      98.717   2.075 -26.287  1.00 72.27           O  
ANISOU 4565  OG1 THR H 211     8856  11462   7140   1695   -262  -1208       O  
ATOM   4566  CG2 THR H 211      98.029   2.298 -28.588  1.00 58.86           C  
ANISOU 4566  CG2 THR H 211     7255  10006   5102   2002   -435  -1207       C  
ATOM   4567  N   THR H 212      97.577  -1.762 -26.620  1.00 38.87           N  
ANISOU 4567  N   THR H 212     4461   7283   3024   1323   -724  -1687       N  
ATOM   4568  CA  THR H 212      97.902  -2.921 -25.797  1.00 39.58           C  
ANISOU 4568  CA  THR H 212     4537   7213   3289   1099   -728  -1773       C  
ATOM   4569  C   THR H 212      99.091  -3.639 -26.416  1.00 53.56           C  
ANISOU 4569  C   THR H 212     6500   8809   5039   1076   -682  -1781       C  
ATOM   4570  O   THR H 212      99.033  -4.052 -27.579  1.00 59.66           O  
ANISOU 4570  O   THR H 212     7374   9615   5680   1148   -784  -1836       O  
ATOM   4571  CB  THR H 212      96.707  -3.871 -25.676  1.00 36.20           C  
ANISOU 4571  CB  THR H 212     3969   6859   2928    962   -936  -1906       C  
ATOM   4572  OG1 THR H 212      95.539  -3.126 -25.312  1.00 36.90           O  
ANISOU 4572  OG1 THR H 212     3849   7163   3008   1017   -991  -1886       O  
ATOM   4573  CG2 THR H 212      96.975  -4.926 -24.614  1.00 34.90           C  
ANISOU 4573  CG2 THR H 212     3787   6517   2956    731   -912  -1959       C  
ATOM   4574  N   VAL H 213     100.162  -3.788 -25.641  1.00 32.42           N  
ANISOU 4574  N   VAL H 213     3877   5955   2485    984   -535  -1726       N  
ATOM   4575  CA  VAL H 213     101.383  -4.438 -26.100  1.00 32.34           C  
ANISOU 4575  CA  VAL H 213     4026   5797   2465    972   -471  -1724       C  
ATOM   4576  C   VAL H 213     101.568  -5.735 -25.325  1.00 31.66           C  
ANISOU 4576  C   VAL H 213     3944   5556   2529    790   -514  -1806       C  
ATOM   4577  O   VAL H 213     101.198  -5.837 -24.152  1.00 58.90           O  
ANISOU 4577  O   VAL H 213     7291   8966   6120    667   -509  -1805       O  
ATOM   4578  CB  VAL H 213     102.605  -3.511 -25.930  1.00 30.89           C  
ANISOU 4578  CB  VAL H 213     3905   5535   2297   1025   -267  -1577       C  
ATOM   4579  CG1 VAL H 213     103.810  -4.063 -26.677  1.00 56.37           C  
ANISOU 4579  CG1 VAL H 213     7273   8674   5469   1059   -196  -1578       C  
ATOM   4580  CG2 VAL H 213     102.272  -2.106 -26.403  1.00 31.43           C  
ANISOU 4580  CG2 VAL H 213     3962   5731   2249   1181   -213  -1467       C  
ATOM   4581  N   ASP H 214     102.138  -6.737 -25.992  1.00 33.09           N  
ANISOU 4581  N   ASP H 214     4260   5648   2666    784   -551  -1872       N  
ATOM   4582  CA  ASP H 214     102.425  -8.031 -25.378  1.00 38.18           C  
ANISOU 4582  CA  ASP H 214     4951   6125   3431    633   -589  -1935       C  
ATOM   4583  C   ASP H 214     103.871  -8.401 -25.679  1.00 49.33           C  
ANISOU 4583  C   ASP H 214     6499   7423   4823    684   -470  -1909       C  
ATOM   4584  O   ASP H 214     104.205  -8.723 -26.825  1.00 50.90           O  
ANISOU 4584  O   ASP H 214     6816   7645   4878    787   -486  -1960       O  
ATOM   4585  CB  ASP H 214     101.470  -9.112 -25.888  1.00 48.52           C  
ANISOU 4585  CB  ASP H 214     6294   7436   4707    555   -793  -2071       C  
ATOM   4586  CG  ASP H 214     100.032  -8.874 -25.464  1.00 58.92           C  
ANISOU 4586  CG  ASP H 214     7440   8868   6079    473   -920  -2102       C  
ATOM   4587  OD1 ASP H 214      99.818  -8.262 -24.396  1.00 55.68           O  
ANISOU 4587  OD1 ASP H 214     6893   8485   5778    428   -837  -2037       O  
ATOM   4588  OD2 ASP H 214      99.114  -9.303 -26.196  1.00 55.93           O  
ANISOU 4588  OD2 ASP H 214     7060   8558   5634    451  -1106  -2193       O  
ATOM   4589  N   LYS H 215     104.726  -8.360 -24.659  1.00 42.82           N  
ANISOU 4589  N   LYS H 215     5653   6483   4132    622   -355  -1835       N  
ATOM   4590  CA  LYS H 215     106.130  -8.721 -24.808  1.00 36.77           C  
ANISOU 4590  CA  LYS H 215     4980   5621   3369    667   -243  -1813       C  
ATOM   4591  C   LYS H 215     106.360 -10.146 -24.320  1.00 35.39           C  
ANISOU 4591  C   LYS H 215     4876   5295   3277    565   -306  -1887       C  
ATOM   4592  O   LYS H 215     105.789 -10.569 -23.311  1.00 38.54           O  
ANISOU 4592  O   LYS H 215     5229   5621   3793    429   -370  -1889       O  
ATOM   4593  CB  LYS H 215     107.032  -7.748 -24.048  1.00 28.15           C  
ANISOU 4593  CB  LYS H 215     3827   4501   2368    673    -90  -1686       C  
ATOM   4594  CG  LYS H 215     107.327  -6.469 -24.814  1.00 28.51           C  
ANISOU 4594  CG  LYS H 215     3866   4658   2308    799     20  -1601       C  
ATOM   4595  CD  LYS H 215     108.056  -6.774 -26.114  1.00 32.90           C  
ANISOU 4595  CD  LYS H 215     4529   5251   2719    932     80  -1631       C  
ATOM   4596  CE  LYS H 215     108.327  -5.510 -26.915  1.00 35.87           C  
ANISOU 4596  CE  LYS H 215     4911   5736   2983   1059    205  -1527       C  
ATOM   4597  NZ  LYS H 215     109.178  -5.782 -28.109  1.00 35.09           N  
ANISOU 4597  NZ  LYS H 215     4913   5674   2745   1196    300  -1539       N  
ATOM   4598  N   LYS H 216     107.210 -10.880 -25.039  1.00 33.55           N  
ANISOU 4598  N   LYS H 216     4762   5014   2972    640   -276  -1945       N  
ATOM   4599  CA  LYS H 216     107.353 -12.316 -24.842  1.00 38.80           C  
ANISOU 4599  CA  LYS H 216     5527   5539   3675    568   -349  -2036       C  
ATOM   4600  C   LYS H 216     108.578 -12.709 -24.025  1.00 57.71           C  
ANISOU 4600  C   LYS H 216     7931   7814   6181    562   -249  -1994       C  
ATOM   4601  O   LYS H 216     108.683 -13.877 -23.632  1.00 86.06           O  
ANISOU 4601  O   LYS H 216    11600  11275   9823    491   -306  -2053       O  
ATOM   4602  CB  LYS H 216     107.402 -13.027 -26.200  1.00 40.73           C  
ANISOU 4602  CB  LYS H 216     5916   5805   3756    666   -401  -2158       C  
ATOM   4603  CG  LYS H 216     106.271 -12.638 -27.142  1.00 46.10           C  
ANISOU 4603  CG  LYS H 216     6601   6616   4300    698   -519  -2209       C  
ATOM   4604  CD  LYS H 216     104.911 -12.926 -26.527  1.00 49.26           C  
ANISOU 4604  CD  LYS H 216     6933   6998   4784    525   -684  -2241       C  
ATOM   4605  CE  LYS H 216     103.781 -12.554 -27.476  1.00 53.87           C  
ANISOU 4605  CE  LYS H 216     7505   7726   5237    564   -825  -2302       C  
ATOM   4606  NZ  LYS H 216     102.448 -12.949 -26.940  1.00 43.27           N  
ANISOU 4606  NZ  LYS H 216     6082   6373   3987    384  -1000  -2346       N  
ATOM   4607  N   LEU H 217     109.502 -11.779 -23.770  1.00 38.73           N  
ANISOU 4607  N   LEU H 217     5451   5450   3814    632   -112  -1898       N  
ATOM   4608  CA  LEU H 217     110.692 -12.043 -22.964  1.00 38.82           C  
ANISOU 4608  CA  LEU H 217     5446   5368   3937    637    -33  -1862       C  
ATOM   4609  C   LEU H 217     111.541 -13.175 -23.530  1.00 51.49           C  
ANISOU 4609  C   LEU H 217     7160   6907   5497    726    -12  -1957       C  
ATOM   4610  O   LEU H 217     111.524 -14.292 -23.001  1.00 31.50           O  
ANISOU 4610  O   LEU H 217     4695   4250   3025    658    -85  -2012       O  
ATOM   4611  CB  LEU H 217     110.307 -12.373 -21.518  1.00 27.73           C  
ANISOU 4611  CB  LEU H 217     4007   3855   2675    484   -103  -1823       C  
ATOM   4612  CG  LEU H 217     109.673 -11.283 -20.657  1.00 25.85           C  
ANISOU 4612  CG  LEU H 217     3657   3660   2506    405   -101  -1725       C  
ATOM   4613  CD1 LEU H 217     109.211 -11.888 -19.351  1.00 85.91           C  
ANISOU 4613  CD1 LEU H 217    11271  11152  10220    266   -171  -1701       C  
ATOM   4614  CD2 LEU H 217     110.660 -10.167 -20.397  1.00 24.78           C  
ANISOU 4614  CD2 LEU H 217     3441   3566   2410    469     16  -1644       C  
ATOM   4615  N   GLU H 218     112.291 -12.901 -24.602  1.00 50.33           N  
ANISOU 4615  N   GLU H 218     7037   6843   5242    887    100  -1973       N  
ATOM   4616  CA  GLU H 218     113.191 -13.961 -25.026  1.00 37.10           C  
ANISOU 4616  CA  GLU H 218     5453   5105   3538    994    138  -2062       C  
ATOM   4617  C   GLU H 218     114.560 -13.792 -24.373  1.00 39.10           C  
ANISOU 4617  C   GLU H 218     5617   5330   3909   1061    263  -2006       C  
ATOM   4618  O   GLU H 218     114.979 -12.669 -24.074  1.00 37.73           O  
ANISOU 4618  O   GLU H 218     5321   5226   3789   1069    361  -1902       O  
ATOM   4619  CB  GLU H 218     113.344 -13.962 -26.545  1.00 51.77           C  
ANISOU 4619  CB  GLU H 218     7401   7062   5207   1157    198  -2122       C  
ATOM   4620  CG  GLU H 218     112.135 -14.503 -27.292  1.00 63.64           C  
ANISOU 4620  CG  GLU H 218     9027   8573   6583   1119     41  -2227       C  
ATOM   4621  CD  GLU H 218     111.362 -13.419 -28.015  1.00 78.03           C  
ANISOU 4621  CD  GLU H 218    10820  10543   8286   1145     32  -2178       C  
ATOM   4622  OE1 GLU H 218     111.930 -12.330 -28.240  1.00 85.71           O  
ANISOU 4622  OE1 GLU H 218    11714  11614   9236   1230    180  -2070       O  
ATOM   4623  OE2 GLU H 218     110.185 -13.658 -28.358  1.00 85.41           O  
ANISOU 4623  OE2 GLU H 218    11808  11493   9152   1081   -125  -2246       O  
ATOM   4624  N   PRO H 219     115.267 -14.895 -24.128  1.00 45.64           N  
ANISOU 4624  N   PRO H 219     6499   6055   4785   1111    255  -2078       N  
ATOM   4625  CA  PRO H 219     116.599 -14.792 -23.520  1.00 49.52           C  
ANISOU 4625  CA  PRO H 219     6890   6529   5397   1197    361  -2036       C  
ATOM   4626  C   PRO H 219     117.582 -14.081 -24.439  1.00 53.82           C  
ANISOU 4626  C   PRO H 219     7363   7200   5888   1372    564  -1991       C  
ATOM   4627  O   PRO H 219     117.506 -14.178 -25.665  1.00 47.69           O  
ANISOU 4627  O   PRO H 219     6668   6493   4957   1477    625  -2032       O  
ATOM   4628  CB  PRO H 219     117.003 -16.255 -23.297  1.00 42.98           C  
ANISOU 4628  CB  PRO H 219     6165   5565   4601   1242    299  -2141       C  
ATOM   4629  CG  PRO H 219     115.713 -17.008 -23.287  1.00 36.10           C  
ANISOU 4629  CG  PRO H 219     5425   4609   3681   1095    137  -2207       C  
ATOM   4630  CD  PRO H 219     114.823 -16.293 -24.252  1.00 49.03           C  
ANISOU 4630  CD  PRO H 219     7080   6367   5183   1079    134  -2200       C  
ATOM   4631  N   SER H 220     118.514 -13.361 -23.824  1.00 64.28           N  
ANISOU 4631  N   SER H 220     8526   8554   7344   1401    671  -1902       N  
ATOM   4632  CA  SER H 220     119.524 -12.615 -24.565  1.00 60.29           C  
ANISOU 4632  CA  SER H 220     7909   8164   6835   1545    897  -1826       C  
ATOM   4633  C   SER H 220     120.870 -13.330 -24.533  1.00 55.83           C  
ANISOU 4633  C   SER H 220     7276   7574   6364   1707   1006  -1851       C  
ATOM   4634  O   SER H 220     121.036 -14.389 -25.137  1.00 48.10           O  
ANISOU 4634  O   SER H 220     6418   6558   5299   1819   1001  -1951       O  
ATOM   4635  CB  SER H 220     119.665 -11.201 -23.998  1.00 54.43           C  
ANISOU 4635  CB  SER H 220     7000   7482   6200   1467    968  -1694       C  
ATOM   4636  OG  SER H 220     119.990 -11.236 -22.619  1.00 38.09           O  
ANISOU 4636  OG  SER H 220     4831   5337   4303   1394    873  -1689       O  
TER    4637      SER H 220                                                      
ATOM   4638  N   ASP L   1      88.886  26.556   5.864  1.00 50.12           N  
ANISOU 4638  N   ASP L   1     6874   6001   6167   1596   -425    -73       N  
ATOM   4639  CA  ASP L   1      90.196  27.190   5.961  1.00 51.49           C  
ANISOU 4639  CA  ASP L   1     7286   5958   6321   1487   -282    -99       C  
ATOM   4640  C   ASP L   1      90.995  26.623   7.129  1.00 48.24           C  
ANISOU 4640  C   ASP L   1     6781   5614   5936   1332   -130   -252       C  
ATOM   4641  O   ASP L   1      92.180  26.920   7.282  1.00 65.76           O  
ANISOU 4641  O   ASP L   1     9141   7694   8149   1204    -19   -302       O  
ATOM   4642  CB  ASP L   1      90.049  28.704   6.115  1.00 70.39           C  
ANISOU 4642  CB  ASP L   1     9826   8108   8812   1673   -258    -83       C  
ATOM   4643  CG  ASP L   1      89.263  29.330   4.983  1.00 85.69           C  
ANISOU 4643  CG  ASP L   1    11883   9950  10727   1855   -442     89       C  
ATOM   4644  OD1 ASP L   1      89.294  28.778   3.862  1.00 87.93           O  
ANISOU 4644  OD1 ASP L   1    12258  10288  10864   1767   -557    208       O  
ATOM   4645  OD2 ASP L   1      88.614  30.373   5.213  1.00 87.83           O  
ANISOU 4645  OD2 ASP L   1    12166  10082  11124   2088   -480    103       O  
ATOM   4646  N   ILE L   2      90.336  25.808   7.952  1.00 35.65           N  
ANISOU 4646  N   ILE L   2     4949   4229   4369   1338   -133   -326       N  
ATOM   4647  CA  ILE L   2      90.989  25.230   9.120  1.00 29.64           C  
ANISOU 4647  CA  ILE L   2     4120   3535   3608   1203    -22   -453       C  
ATOM   4648  C   ILE L   2      92.056  24.243   8.671  1.00 26.78           C  
ANISOU 4648  C   ILE L   2     3810   3198   3169    994    -16   -440       C  
ATOM   4649  O   ILE L   2      91.787  23.325   7.885  1.00 29.14           O  
ANISOU 4649  O   ILE L   2     4062   3607   3402    934    -89   -372       O  
ATOM   4650  CB  ILE L   2      89.957  24.557  10.037  1.00 20.79           C  
ANISOU 4650  CB  ILE L   2     2768   2622   2509   1242    -15   -520       C  
ATOM   4651  CG1 ILE L   2      89.036  25.605  10.661  1.00 22.77           C  
ANISOU 4651  CG1 ILE L   2     2952   2830   2869   1446     29   -581       C  
ATOM   4652  CG2 ILE L   2      90.653  23.742  11.117  1.00 63.08           C  
ANISOU 4652  CG2 ILE L   2     8097   8054   7816   1078     65   -615       C  
ATOM   4653  CD1 ILE L   2      88.082  25.038  11.687  1.00 42.39           C  
ANISOU 4653  CD1 ILE L   2     5217   5510   5380   1459     95   -680       C  
ATOM   4654  N   VAL L   3      93.273  24.426   9.170  1.00 18.25           N  
ANISOU 4654  N   VAL L   3     2813   2013   2108    882     71   -519       N  
ATOM   4655  CA  VAL L   3      94.398  23.567   8.822  1.00 30.41           C  
ANISOU 4655  CA  VAL L   3     4376   3554   3623    700     90   -534       C  
ATOM   4656  C   VAL L   3      94.430  22.384   9.778  1.00 21.74           C  
ANISOU 4656  C   VAL L   3     3130   2614   2514    628     72   -594       C  
ATOM   4657  O   VAL L   3      94.425  22.560  11.002  1.00 26.14           O  
ANISOU 4657  O   VAL L   3     3649   3195   3086    646     97   -676       O  
ATOM   4658  CB  VAL L   3      95.720  24.350   8.870  1.00 22.19           C  
ANISOU 4658  CB  VAL L   3     3468   2324   2640    613    182   -603       C  
ATOM   4659  CG1 VAL L   3      96.884  23.446   8.503  1.00 16.11           C  
ANISOU 4659  CG1 VAL L   3     2677   1559   1885    438    211   -640       C  
ATOM   4660  CG2 VAL L   3      95.654  25.553   7.943  1.00 35.46           C  
ANISOU 4660  CG2 VAL L   3     5340   3819   4316    673    216   -530       C  
ATOM   4661  N   LEU L   4      94.462  21.176   9.222  1.00 14.88           N  
ANISOU 4661  N   LEU L   4     2207   1842   1605    539     33   -553       N  
ATOM   4662  CA  LEU L   4      94.541  19.950  10.004  1.00 33.94           C  
ANISOU 4662  CA  LEU L   4     4517   4374   4005    461     10   -588       C  
ATOM   4663  C   LEU L   4      95.942  19.366   9.887  1.00 13.22           C  
ANISOU 4663  C   LEU L   4     1917   1674   1432    336     23   -634       C  
ATOM   4664  O   LEU L   4      96.489  19.266   8.784  1.00 13.86           O  
ANISOU 4664  O   LEU L   4     2052   1686   1529    274     55   -616       O  
ATOM   4665  CB  LEU L   4      93.495  18.932   9.543  1.00 29.00           C  
ANISOU 4665  CB  LEU L   4     3799   3901   3319    449    -42   -524       C  
ATOM   4666  CG  LEU L   4      92.033  19.332   9.764  1.00 14.89           C  
ANISOU 4666  CG  LEU L   4     1918   2222   1517    571    -63   -501       C  
ATOM   4667  CD1 LEU L   4      91.092  18.205   9.376  1.00 14.94           C  
ANISOU 4667  CD1 LEU L   4     1807   2390   1479    520   -113   -462       C  
ATOM   4668  CD2 LEU L   4      91.804  19.748  11.206  1.00 15.26           C  
ANISOU 4668  CD2 LEU L   4     1929   2292   1579    620     -4   -580       C  
ATOM   4669  N   THR L   5      96.516  18.987  11.025  1.00 35.49           N  
ANISOU 4669  N   THR L   5     4700   4505   4279    300     -1   -699       N  
ATOM   4670  CA  THR L   5      97.862  18.428  11.099  1.00 24.54           C  
ANISOU 4670  CA  THR L   5     3295   3049   2980    208    -19   -757       C  
ATOM   4671  C   THR L   5      97.777  17.071  11.784  1.00 26.50           C  
ANISOU 4671  C   THR L   5     3485   3383   3201    173    -97   -739       C  
ATOM   4672  O   THR L   5      97.455  16.990  12.975  1.00 39.52           O  
ANISOU 4672  O   THR L   5     5139   5089   4786    192   -144   -748       O  
ATOM   4673  CB  THR L   5      98.806  19.364  11.853  1.00 13.19           C  
ANISOU 4673  CB  THR L   5     1884   1515   1614    201    -16   -856       C  
ATOM   4674  OG1 THR L   5      98.842  20.638  11.199  1.00 49.31           O  
ANISOU 4674  OG1 THR L   5     6543   5982   6211    223     74   -865       O  
ATOM   4675  CG2 THR L   5     100.209  18.783  11.894  1.00 13.24           C  
ANISOU 4675  CG2 THR L   5     1824   1457   1749    116    -53   -930       C  
ATOM   4676  N   GLN L   6      98.059  16.012  11.034  1.00 11.86           N  
ANISOU 4676  N   GLN L   6     1598   1523   1384    114   -100   -717       N  
ATOM   4677  CA  GLN L   6      98.041  14.654  11.555  1.00 11.72           C  
ANISOU 4677  CA  GLN L   6     1550   1547   1357     78   -170   -691       C  
ATOM   4678  C   GLN L   6      99.452  14.230  11.939  1.00 40.54           C  
ANISOU 4678  C   GLN L   6     5162   5096   5144     55   -237   -756       C  
ATOM   4679  O   GLN L   6     100.416  14.520  11.224  1.00 31.81           O  
ANISOU 4679  O   GLN L   6     4018   3898   4170     30   -187   -825       O  
ATOM   4680  CB  GLN L   6      97.466  13.679  10.525  1.00 26.85           C  
ANISOU 4680  CB  GLN L   6     3454   3502   3244     27   -137   -640       C  
ATOM   4681  CG  GLN L   6      96.188  14.161   9.862  1.00 28.06           C  
ANISOU 4681  CG  GLN L   6     3616   3752   3293     51    -97   -587       C  
ATOM   4682  CD  GLN L   6      95.435  13.046   9.160  1.00 28.67           C  
ANISOU 4682  CD  GLN L   6     3675   3903   3317    -17    -98   -544       C  
ATOM   4683  OE1 GLN L   6      94.884  13.239   8.076  1.00 11.64           O  
ANISOU 4683  OE1 GLN L   6     1530   1782   1110    -29    -80   -519       O  
ATOM   4684  NE2 GLN L   6      95.398  11.874   9.784  1.00 23.98           N  
ANISOU 4684  NE2 GLN L   6     3068   3322   2721    -71   -128   -533       N  
ATOM   4685  N   SER L   7      99.568  13.544  13.077  1.00 39.07           N  
ANISOU 4685  N   SER L   7     4989   4926   4931     62   -352   -737       N  
ATOM   4686  CA  SER L   7     100.862  13.070  13.538  1.00 24.01           C  
ANISOU 4686  CA  SER L   7     3033   2926   3166     66   -467   -790       C  
ATOM   4687  C   SER L   7     100.687  11.761  14.291  1.00 23.32           C  
ANISOU 4687  C   SER L   7     2994   2841   3026     65   -586   -712       C  
ATOM   4688  O   SER L   7      99.749  11.639  15.092  1.00 46.97           O  
ANISOU 4688  O   SER L   7     6086   5918   5841     52   -602   -642       O  
ATOM   4689  CB  SER L   7     101.559  14.097  14.436  1.00 27.52           C  
ANISOU 4689  CB  SER L   7     3473   3349   3633     86   -543   -867       C  
ATOM   4690  OG  SER L   7     102.186  15.103  13.661  1.00 56.58           O  
ANISOU 4690  OG  SER L   7     7096   6967   7433     68   -441   -958       O  
ATOM   4691  N   PRO L   8     101.562  10.770  14.061  1.00 18.79           N  
ANISOU 4691  N   PRO L   8     2363   2165   2612     75   -657   -727       N  
ATOM   4692  CA  PRO L   8     102.671  10.861  13.104  1.00 14.43           C  
ANISOU 4692  CA  PRO L   8     1677   1517   2291     79   -602   -834       C  
ATOM   4693  C   PRO L   8     102.223  10.670  11.657  1.00 13.63           C  
ANISOU 4693  C   PRO L   8     1568   1416   2194     23   -414   -842       C  
ATOM   4694  O   PRO L   8     101.114  10.199  11.415  1.00 32.48           O  
ANISOU 4694  O   PRO L   8     4034   3871   4434    -10   -369   -760       O  
ATOM   4695  CB  PRO L   8     103.596   9.726  13.543  1.00 27.33           C  
ANISOU 4695  CB  PRO L   8     3254   3040   4089    130   -760   -841       C  
ATOM   4696  CG  PRO L   8     102.678   8.720  14.135  1.00 37.88           C  
ANISOU 4696  CG  PRO L   8     4736   4399   5258    123   -825   -705       C  
ATOM   4697  CD  PRO L   8     101.583   9.501  14.808  1.00 15.14           C  
ANISOU 4697  CD  PRO L   8     1972   1657   2125     88   -797   -645       C  
ATOM   4698  N   ALA L   9     103.080  11.047  10.707  1.00 13.86           N  
ANISOU 4698  N   ALA L   9     1510   1374   2383     -4   -303   -950       N  
ATOM   4699  CA  ALA L   9     102.726  10.920   9.298  1.00 13.43           C  
ANISOU 4699  CA  ALA L   9     1487   1322   2294    -74   -123   -950       C  
ATOM   4700  C   ALA L   9     102.889   9.488   8.808  1.00 13.90           C  
ANISOU 4700  C   ALA L   9     1528   1316   2436    -92   -102   -956       C  
ATOM   4701  O   ALA L   9     102.047   8.989   8.054  1.00 16.51           O  
ANISOU 4701  O   ALA L   9     1939   1678   2658   -155    -25   -928       O  
ATOM   4702  CB  ALA L   9     103.574  11.871   8.454  1.00 13.84           C  
ANISOU 4702  CB  ALA L   9     1493   1353   2414   -113     23   -988       C  
ATOM   4703  N   ILE L  10     103.965   8.821   9.217  1.00 52.39           N  
ANISOU 4703  N   ILE L  10     6295   6098   7515    -36   -177  -1001       N  
ATOM   4704  CA  ILE L  10     104.222   7.428   8.869  1.00 34.13           C  
ANISOU 4704  CA  ILE L  10     3962   3691   5316    -28   -167  -1014       C  
ATOM   4705  C   ILE L  10     104.523   6.680  10.158  1.00 16.74           C  
ANISOU 4705  C   ILE L  10     1748   1388   3225     70   -406  -1000       C  
ATOM   4706  O   ILE L  10     105.457   7.041  10.883  1.00 38.82           O  
ANISOU 4706  O   ILE L  10     4435   4148   6167    147   -541  -1046       O  
ATOM   4707  CB  ILE L  10     105.392   7.279   7.881  1.00 26.96           C  
ANISOU 4707  CB  ILE L  10     2919   2739   4586    -45    -14  -1099       C  
ATOM   4708  CG1 ILE L  10     105.267   8.285   6.734  1.00 40.64           C  
ANISOU 4708  CG1 ILE L  10     4692   4552   6197   -144    184  -1105       C  
ATOM   4709  CG2 ILE L  10     105.448   5.858   7.340  1.00 24.71           C  
ANISOU 4709  CG2 ILE L  10     2644   2367   4378    -51     36  -1112       C  
ATOM   4710  CD1 ILE L  10     106.474   8.324   5.823  1.00 17.83           C  
ANISOU 4710  CD1 ILE L  10     1670   1628   3476   -190    348  -1204       C  
ATOM   4711  N   MET L  11     103.737   5.645  10.445  1.00 23.41           N  
ANISOU 4711  N   MET L  11     2717   2219   3959     62   -459   -891       N  
ATOM   4712  CA  MET L  11     103.961   4.813  11.617  1.00 25.37           C  
ANISOU 4712  CA  MET L  11     3015   2383   4243    149   -676   -803       C  
ATOM   4713  C   MET L  11     103.696   3.358  11.263  1.00 19.57           C  
ANISOU 4713  C   MET L  11     2360   1521   3553    133   -645   -768       C  
ATOM   4714  O   MET L  11     102.950   3.057  10.328  1.00 18.83           O  
ANISOU 4714  O   MET L  11     2323   1460   3370     27   -472   -781       O  
ATOM   4715  CB  MET L  11     103.077   5.244  12.797  1.00 28.05           C  
ANISOU 4715  CB  MET L  11     3497   2845   4316    134   -793   -668       C  
ATOM   4716  CG  MET L  11     101.586   5.133  12.545  1.00 30.37           C  
ANISOU 4716  CG  MET L  11     3921   3258   4361     23   -668   -584       C  
ATOM   4717  SD  MET L  11     100.617   5.720  13.951  1.00 23.89           S  
ANISOU 4717  SD  MET L  11     3240   2580   3258      0   -756   -465       S  
ATOM   4718  CE  MET L  11     101.223   4.640  15.245  1.00 45.23           C  
ANISOU 4718  CE  MET L  11     6071   5133   5981     65   -996   -365       C  
ATOM   4719  N   SER L  12     104.327   2.459  12.015  1.00 33.86           N  
ANISOU 4719  N   SER L  12     4186   3175   5505    240   -830   -724       N  
ATOM   4720  CA  SER L  12     104.181   1.025  11.825  1.00 27.82           C  
ANISOU 4720  CA  SER L  12     3520   2242   4810    243   -824   -684       C  
ATOM   4721  C   SER L  12     103.602   0.391  13.084  1.00 25.87           C  
ANISOU 4721  C   SER L  12     3488   1957   4383    253  -1011   -495       C  
ATOM   4722  O   SER L  12     103.691   0.945  14.183  1.00 39.59           O  
ANISOU 4722  O   SER L  12     5271   3761   6010    298  -1189   -415       O  
ATOM   4723  CB  SER L  12     105.522   0.366  11.475  1.00 26.37           C  
ANISOU 4723  CB  SER L  12     3172   1856   4992    376   -860   -803       C  
ATOM   4724  OG  SER L  12     106.467   0.530  12.517  1.00 65.02           O  
ANISOU 4724  OG  SER L  12     7981   6700  10024    528  -1125   -776       O  
ATOM   4725  N   ALA L  13     103.008  -0.788  12.911  1.00 23.22           N  
ANISOU 4725  N   ALA L  13     3309   1507   4008    191   -956   -429       N  
ATOM   4726  CA  ALA L  13     102.382  -1.492  14.020  1.00 24.32           C  
ANISOU 4726  CA  ALA L  13     3695   1588   3957    162  -1089   -244       C  
ATOM   4727  C   ALA L  13     102.290  -2.973  13.688  1.00 30.53           C  
ANISOU 4727  C   ALA L  13     4612   2142   4846    144  -1050   -214       C  
ATOM   4728  O   ALA L  13     101.980  -3.341  12.553  1.00 29.22           O  
ANISOU 4728  O   ALA L  13     4402   1960   4740     53   -842   -318       O  
ATOM   4729  CB  ALA L  13     100.989  -0.929  14.323  1.00 22.77           C  
ANISOU 4729  CB  ALA L  13     3613   1616   3424     -7   -981   -169       C  
ATOM   4730  N   SER L  14     102.566  -3.813  14.684  1.00 28.18           N  
ANISOU 4730  N   SER L  14     4497   1652   4558    227  -1258    -70       N  
ATOM   4731  CA  SER L  14     102.428  -5.255  14.566  1.00 30.12           C  
ANISOU 4731  CA  SER L  14     4924   1638   4881    211  -1241     -9       C  
ATOM   4732  C   SER L  14     101.016  -5.682  14.935  1.00 29.91           C  
ANISOU 4732  C   SER L  14     5159   1672   4536    -11  -1128    120       C  
ATOM   4733  O   SER L  14     100.307  -4.967  15.649  1.00 51.17           O  
ANISOU 4733  O   SER L  14     7921   4567   6955   -105  -1135    200       O  
ATOM   4734  CB  SER L  14     103.437  -5.956  15.474  1.00 33.11           C  
ANISOU 4734  CB  SER L  14     5372   1800   5408    413  -1518     96       C  
ATOM   4735  OG  SER L  14     104.762  -5.758  15.018  1.00 57.32           O  
ANISOU 4735  OG  SER L  14     8129   4869   8782    592  -1557    -52       O  
ATOM   4736  N   PRO L  15     100.569  -6.843  14.454  1.00 48.61           N  
ANISOU 4736  N   PRO L  15     7666   3863   6939   -112  -1003    126       N  
ATOM   4737  CA  PRO L  15      99.245  -7.335  14.851  1.00 43.80           C  
ANISOU 4737  CA  PRO L  15     7302   3294   6047   -346   -888    241       C  
ATOM   4738  C   PRO L  15      99.156  -7.515  16.359  1.00 37.39           C  
ANISOU 4738  C   PRO L  15     6762   2411   5034   -333  -1081    458       C  
ATOM   4739  O   PRO L  15     100.079  -8.022  17.000  1.00 35.30           O  
ANISOU 4739  O   PRO L  15     6593   1934   4887   -151  -1308    552       O  
ATOM   4740  CB  PRO L  15      99.128  -8.674  14.114  1.00 32.85           C  
ANISOU 4740  CB  PRO L  15     6023   1653   4805   -417   -763    198       C  
ATOM   4741  CG  PRO L  15     100.049  -8.542  12.950  1.00 38.52           C  
ANISOU 4741  CG  PRO L  15     6470   2346   5820   -282   -696     -2       C  
ATOM   4742  CD  PRO L  15     101.197  -7.711  13.443  1.00 50.08           C  
ANISOU 4742  CD  PRO L  15     7768   3840   7421    -44   -910     -4       C  
ATOM   4743  N   GLY L  16      98.034  -7.079  16.923  1.00 32.35           N  
ANISOU 4743  N   GLY L  16     6226   1981   4083   -526   -978    524       N  
ATOM   4744  CA  GLY L  16      97.849  -7.152  18.358  1.00 34.11           C  
ANISOU 4744  CA  GLY L  16     6735   2168   4058   -556  -1118    718       C  
ATOM   4745  C   GLY L  16      98.461  -6.005  19.125  1.00 33.51           C  
ANISOU 4745  C   GLY L  16     6578   2243   3912   -413  -1313    734       C  
ATOM   4746  O   GLY L  16      98.899  -6.197  20.264  1.00 42.85           O  
ANISOU 4746  O   GLY L  16     7994   3307   4981   -341  -1541    889       O  
ATOM   4747  N   GLU L  17      98.514  -4.815  18.531  1.00 30.88           N  
ANISOU 4747  N   GLU L  17     5940   2158   3635   -375  -1237    578       N  
ATOM   4748  CA  GLU L  17      99.039  -3.630  19.190  1.00 30.23           C  
ANISOU 4748  CA  GLU L  17     5766   2229   3489   -264  -1390    565       C  
ATOM   4749  C   GLU L  17      98.003  -2.518  19.140  1.00 31.32           C  
ANISOU 4749  C   GLU L  17     5800   2676   3423   -406  -1186    490       C  
ATOM   4750  O   GLU L  17      97.131  -2.488  18.268  1.00 26.65           O  
ANISOU 4750  O   GLU L  17     5092   2202   2832   -533   -953    406       O  
ATOM   4751  CB  GLU L  17     100.345  -3.143  18.544  1.00 29.51           C  
ANISOU 4751  CB  GLU L  17     5387   2105   3720    -45  -1519    432       C  
ATOM   4752  CG  GLU L  17     101.544  -4.045  18.780  1.00 48.54           C  
ANISOU 4752  CG  GLU L  17     7849   4222   6371    150  -1777    491       C  
ATOM   4753  CD  GLU L  17     102.842  -3.422  18.299  1.00 45.85           C  
ANISOU 4753  CD  GLU L  17     7190   3883   6349    353  -1900    340       C  
ATOM   4754  OE1 GLU L  17     102.811  -2.260  17.840  1.00 35.44           O  
ANISOU 4754  OE1 GLU L  17     5651   2786   5030    326  -1784    206       O  
ATOM   4755  OE2 GLU L  17     103.894  -4.091  18.381  1.00 42.25           O  
ANISOU 4755  OE2 GLU L  17     6693   3209   6151    535  -2100    347       O  
ATOM   4756  N   LYS L  18      98.110  -1.599  20.094  1.00 28.49           N  
ANISOU 4756  N   LYS L  18     5485   2445   2896   -378  -1287    516       N  
ATOM   4757  CA  LYS L  18      97.243  -0.431  20.146  1.00 26.45           C  
ANISOU 4757  CA  LYS L  18     5119   2460   2471   -474  -1112    435       C  
ATOM   4758  C   LYS L  18      97.840   0.674  19.283  1.00 24.26           C  
ANISOU 4758  C   LYS L  18     4526   2296   2395   -346  -1109    277       C  
ATOM   4759  O   LYS L  18      99.034   0.972  19.384  1.00 37.24           O  
ANISOU 4759  O   LYS L  18     6089   3864   4195   -187  -1305    247       O  
ATOM   4760  CB  LYS L  18      97.070   0.045  21.589  1.00 27.85           C  
ANISOU 4760  CB  LYS L  18     5518   2704   2359   -519  -1196    519       C  
ATOM   4761  CG  LYS L  18      96.147   1.240  21.751  1.00 31.16           C  
ANISOU 4761  CG  LYS L  18     5839   3385   2615   -609   -999    424       C  
ATOM   4762  CD  LYS L  18      96.096   1.700  23.198  1.00 28.22           C  
ANISOU 4762  CD  LYS L  18     5707   3061   1954   -656  -1077    486       C  
ATOM   4763  CE  LYS L  18      95.218   2.930  23.357  1.00 44.66           C  
ANISOU 4763  CE  LYS L  18     7676   5385   3907   -726   -866    366       C  
ATOM   4764  NZ  LYS L  18      95.214   3.435  24.758  1.00 48.49           N  
ANISOU 4764  NZ  LYS L  18     8282   5907   4235   -745   -869    372       N  
ATOM   4765  N   VAL L  19      97.012   1.270  18.430  1.00 20.09           N  
ANISOU 4765  N   VAL L  19     3187   3328   1120    261    407   -166       N  
ATOM   4766  CA  VAL L  19      97.445   2.324  17.521  1.00 28.93           C  
ANISOU 4766  CA  VAL L  19     4082   4493   2418    327    393   -253       C  
ATOM   4767  C   VAL L  19      96.638   3.580  17.812  1.00 26.54           C  
ANISOU 4767  C   VAL L  19     3567   4340   2178    281    471   -290       C  
ATOM   4768  O   VAL L  19      95.421   3.514  18.011  1.00 21.10           O  
ANISOU 4768  O   VAL L  19     2855   3715   1446    139    555   -234       O  
ATOM   4769  CB  VAL L  19      97.290   1.901  16.045  1.00 25.47           C  
ANISOU 4769  CB  VAL L  19     3639   3975   2063    246    394   -224       C  
ATOM   4770  CG1 VAL L  19      97.807   2.991  15.119  1.00 27.70           C  
ANISOU 4770  CG1 VAL L  19     3718   4295   2514    314    381   -312       C  
ATOM   4771  CG2 VAL L  19      98.018   0.595  15.793  1.00 18.66           C  
ANISOU 4771  CG2 VAL L  19     3008   2952   1130    292    330   -189       C  
ATOM   4772  N   THR L  20      97.319   4.725  17.842  1.00 37.51           N  
ANISOU 4772  N   THR L  20     4799   5784   3668    401    449   -391       N  
ATOM   4773  CA  THR L  20      96.667   6.005  18.085  1.00 31.34           C  
ANISOU 4773  CA  THR L  20     3837   5060   3010    363    496   -416       C  
ATOM   4774  C   THR L  20      97.350   7.080  17.256  1.00 31.06           C  
ANISOU 4774  C   THR L  20     3664   4970   3168    418    446   -475       C  
ATOM   4775  O   THR L  20      98.571   7.243  17.331  1.00 31.14           O  
ANISOU 4775  O   THR L  20     3683   4932   3215    512    372   -531       O  
ATOM   4776  CB  THR L  20      96.710   6.383  19.570  1.00 25.11           C  
ANISOU 4776  CB  THR L  20     3073   4311   2156    401    502   -441       C  
ATOM   4777  OG1 THR L  20      96.074   5.359  20.346  1.00 23.91           O  
ANISOU 4777  OG1 THR L  20     3084   4186   1815    326    548   -371       O  
ATOM   4778  CG2 THR L  20      95.993   7.704  19.800  1.00 19.35           C  
ANISOU 4778  CG2 THR L  20     2185   3613   1554    368    547   -462       C  
ATOM   4779  N   MET L  21      96.560   7.809  16.472  1.00 15.29           N  
ANISOU 4779  N   MET L  21     1554   2969   1288    349    475   -451       N  
ATOM   4780  CA  MET L  21      97.054   8.898  15.642  1.00 14.34           C  
ANISOU 4780  CA  MET L  21     1356   2766   1328    368    428   -477       C  
ATOM   4781  C   MET L  21      96.294  10.174  15.974  1.00 32.77           C  
ANISOU 4781  C   MET L  21     3615   5095   3739    346    451   -468       C  
ATOM   4782  O   MET L  21      95.087  10.141  16.239  1.00 14.96           O  
ANISOU 4782  O   MET L  21     1323   2902   1459    298    506   -432       O  
ATOM   4783  CB  MET L  21      96.915   8.562  14.155  1.00 13.73           C  
ANISOU 4783  CB  MET L  21     1267   2653   1296    321    427   -449       C  
ATOM   4784  CG  MET L  21      95.537   8.073  13.755  1.00 14.11           C  
ANISOU 4784  CG  MET L  21     1286   2776   1301    220    485   -384       C  
ATOM   4785  SD  MET L  21      95.543   7.234  12.160  1.00 13.70           S  
ANISOU 4785  SD  MET L  21     1259   2708   1239    150    486   -356       S  
ATOM   4786  CE  MET L  21      96.473   5.753  12.552  1.00 14.15           C  
ANISOU 4786  CE  MET L  21     1499   2735   1143    185    476   -370       C  
ATOM   4787  N   THR L  22      97.005  11.298  15.960  1.00 43.55           N  
ANISOU 4787  N   THR L  22     4970   6386   5192    378    414   -500       N  
ATOM   4788  CA  THR L  22      96.451  12.577  16.374  1.00 14.16           C  
ANISOU 4788  CA  THR L  22     1211   2643   1528    376    440   -499       C  
ATOM   4789  C   THR L  22      96.170  13.466  15.170  1.00 13.60           C  
ANISOU 4789  C   THR L  22     1116   2492   1558    358    439   -466       C  
ATOM   4790  O   THR L  22      96.848  13.393  14.140  1.00 44.66           O  
ANISOU 4790  O   THR L  22     5068   6376   5524    349    404   -466       O  
ATOM   4791  CB  THR L  22      97.395  13.306  17.334  1.00 14.36           C  
ANISOU 4791  CB  THR L  22     1255   2651   1550    416    416   -556       C  
ATOM   4792  OG1 THR L  22      98.597  13.671  16.644  1.00 31.50           O  
ANISOU 4792  OG1 THR L  22     3437   4762   3770    423    360   -585       O  
ATOM   4793  CG2 THR L  22      97.744  12.413  18.512  1.00 24.70           C  
ANISOU 4793  CG2 THR L  22     2596   4046   2745    451    408   -591       C  
ATOM   4794  N   CYS L  23      95.157  14.314  15.327  1.00 17.93           N  
ANISOU 4794  N   CYS L  23     1614   3060   2137    361    476   -454       N  
ATOM   4795  CA  CYS L  23      94.742  15.275  14.311  1.00 28.16           C  
ANISOU 4795  CA  CYS L  23     2874   4321   3505    366    476   -439       C  
ATOM   4796  C   CYS L  23      94.447  16.581  15.035  1.00 19.83           C  
ANISOU 4796  C   CYS L  23     1792   3270   2474    408    507   -473       C  
ATOM   4797  O   CYS L  23      93.429  16.692  15.727  1.00 22.07           O  
ANISOU 4797  O   CYS L  23     2033   3603   2750    417    554   -463       O  
ATOM   4798  CB  CYS L  23      93.516  14.775  13.543  1.00 52.08           C  
ANISOU 4798  CB  CYS L  23     5856   7380   6554    333    496   -375       C  
ATOM   4799  SG  CYS L  23      92.834  15.904  12.298  1.00 60.38           S  
ANISOU 4799  SG  CYS L  23     6853   8399   7690    354    497   -348       S  
ATOM   4800  N   SER L  24      95.343  17.553  14.899  1.00 22.03           N  
ANISOU 4800  N   SER L  24     2094   3497   2778    429    489   -518       N  
ATOM   4801  CA  SER L  24      95.204  18.843  15.557  1.00 15.63           C  
ANISOU 4801  CA  SER L  24     1271   2678   1989    469    525   -557       C  
ATOM   4802  C   SER L  24      94.732  19.887  14.556  1.00 27.64           C  
ANISOU 4802  C   SER L  24     2774   4147   3580    498    550   -533       C  
ATOM   4803  O   SER L  24      95.130  19.867  13.389  1.00 33.89           O  
ANISOU 4803  O   SER L  24     3585   4894   4398    482    524   -513       O  
ATOM   4804  CB  SER L  24      96.526  19.282  16.188  1.00 22.11           C  
ANISOU 4804  CB  SER L  24     2129   3483   2789    468    497   -632       C  
ATOM   4805  OG  SER L  24      96.389  20.533  16.838  1.00 37.65           O  
ANISOU 4805  OG  SER L  24     4091   5439   4774    504    541   -674       O  
ATOM   4806  N   ALA L  25      93.884  20.799  15.018  1.00 30.58           N  
ANISOU 4806  N   ALA L  25     3112   4526   3982    548    606   -536       N  
ATOM   4807  CA  ALA L  25      93.294  21.819  14.166  1.00 31.19           C  
ANISOU 4807  CA  ALA L  25     3168   4555   4129    599    639   -508       C  
ATOM   4808  C   ALA L  25      93.785  23.203  14.571  1.00 29.11           C  
ANISOU 4808  C   ALA L  25     2942   4237   3881    648    680   -560       C  
ATOM   4809  O   ALA L  25      94.090  23.456  15.740  1.00 38.23           O  
ANISOU 4809  O   ALA L  25     4111   5412   5002    652    698   -615       O  
ATOM   4810  CB  ALA L  25      91.766  21.774  14.234  1.00 35.92           C  
ANISOU 4810  CB  ALA L  25     3680   5204   4763    631    677   -468       C  
ATOM   4811  N   SER L  26      93.861  24.098  13.585  1.00 27.33           N  
ANISOU 4811  N   SER L  26     2741   3942   3703    687    698   -543       N  
ATOM   4812  CA  SER L  26      94.222  25.483  13.868  1.00 18.68           C  
ANISOU 4812  CA  SER L  26     1693   2785   2618    743    750   -588       C  
ATOM   4813  C   SER L  26      93.137  26.165  14.691  1.00 29.31           C  
ANISOU 4813  C   SER L  26     3000   4143   3994    821    822   -592       C  
ATOM   4814  O   SER L  26      93.381  26.613  15.818  1.00 38.68           O  
ANISOU 4814  O   SER L  26     4209   5340   5150    833    854   -652       O  
ATOM   4815  CB  SER L  26      94.474  26.238  12.561  1.00 18.55           C  
ANISOU 4815  CB  SER L  26     1725   2689   2632    779    761   -563       C  
ATOM   4816  OG  SER L  26      93.385  26.098  11.666  1.00 18.70           O  
ANISOU 4816  OG  SER L  26     1691   2704   2712    820    772   -486       O  
ATOM   4817  N   SER L  27      91.928  26.241  14.146  1.00 21.74           N  
ANISOU 4817  N   SER L  27     1972   3187   3101    872    848   -537       N  
ATOM   4818  CA  SER L  27      90.782  26.781  14.858  1.00 33.27           C  
ANISOU 4818  CA  SER L  27     3368   4668   4607    944    915   -547       C  
ATOM   4819  C   SER L  27      89.995  25.653  15.520  1.00 39.37           C  
ANISOU 4819  C   SER L  27     4052   5553   5352    898    897   -538       C  
ATOM   4820  O   SER L  27      90.247  24.467  15.294  1.00 21.10           O  
ANISOU 4820  O   SER L  27     1734   3288   2995    818    835   -515       O  
ATOM   4821  CB  SER L  27      89.884  27.570  13.905  1.00 40.39           C  
ANISOU 4821  CB  SER L  27     4222   5511   5613   1027    943   -513       C  
ATOM   4822  OG  SER L  27      90.648  28.442  13.091  1.00 48.06           O  
ANISOU 4822  OG  SER L  27     5298   6374   6588   1048    942   -509       O  
ATOM   4823  N   SER L  28      89.028  26.035  16.349  1.00 39.43           N  
ANISOU 4823  N   SER L  28     3998   5601   5384    952    962   -561       N  
ATOM   4824  CA  SER L  28      88.162  25.050  16.980  1.00 23.93           C  
ANISOU 4824  CA  SER L  28     1950   3751   3390    914    963   -553       C  
ATOM   4825  C   SER L  28      87.286  24.368  15.935  1.00 23.84           C  
ANISOU 4825  C   SER L  28     1845   3789   3422    895    915   -495       C  
ATOM   4826  O   SER L  28      86.898  24.965  14.928  1.00 31.73           O  
ANISOU 4826  O   SER L  28     2807   4746   4503    950    900   -470       O  
ATOM   4827  CB  SER L  28      87.295  25.706  18.053  1.00 31.40           C  
ANISOU 4827  CB  SER L  28     2844   4733   4354    982   1056   -595       C  
ATOM   4828  OG  SER L  28      88.092  26.209  19.112  1.00 46.24           O  
ANISOU 4828  OG  SER L  28     4813   6581   6176    988   1098   -654       O  
ATOM   4829  N   VAL L  29      86.978  23.098  16.185  1.00 26.78           N  
ANISOU 4829  N   VAL L  29     2182   4255   3737    816    889   -476       N  
ATOM   4830  CA  VAL L  29      86.238  22.262  15.249  1.00 23.32           C  
ANISOU 4830  CA  VAL L  29     1665   3877   3318    776    839   -423       C  
ATOM   4831  C   VAL L  29      85.003  21.713  15.948  1.00 54.49           C  
ANISOU 4831  C   VAL L  29     5503   7949   7251    759    883   -425       C  
ATOM   4832  O   VAL L  29      85.073  21.278  17.103  1.00 48.78           O  
ANISOU 4832  O   VAL L  29     4804   7272   6460    723    930   -453       O  
ATOM   4833  CB  VAL L  29      87.121  21.118  14.706  1.00 21.62           C  
ANISOU 4833  CB  VAL L  29     1524   3651   3041    681    770   -394       C  
ATOM   4834  CG1 VAL L  29      86.277  20.059  14.019  1.00 21.65           C  
ANISOU 4834  CG1 VAL L  29     1449   3738   3039    620    732   -346       C  
ATOM   4835  CG2 VAL L  29      88.159  21.669  13.748  1.00 20.67           C  
ANISOU 4835  CG2 VAL L  29     1483   3421   2948    697    729   -387       C  
ATOM   4836  N   THR L  30      83.869  21.743  15.248  1.00 25.62           N  
ANISOU 4836  N   THR L  30     1723   4354   3656    785    869   -397       N  
ATOM   4837  CA  THR L  30      82.637  21.178  15.784  1.00 27.02           C  
ANISOU 4837  CA  THR L  30     1779   4666   3823    758    911   -397       C  
ATOM   4838  C   THR L  30      82.685  19.655  15.751  1.00 26.18           C  
ANISOU 4838  C   THR L  30     1690   4628   3632    626    884   -365       C  
ATOM   4839  O   THR L  30      82.692  19.008  16.803  1.00 26.34           O  
ANISOU 4839  O   THR L  30     1734   4698   3577    567    937   -383       O  
ATOM   4840  CB  THR L  30      81.421  21.690  15.007  1.00 32.24           C  
ANISOU 4840  CB  THR L  30     2289   5383   4578    829    894   -380       C  
ATOM   4841  OG1 THR L  30      81.348  23.118  15.112  1.00 29.55           O  
ANISOU 4841  OG1 THR L  30     1938   4971   4319    963    929   -413       O  
ATOM   4842  CG2 THR L  30      80.142  21.082  15.560  1.00 30.22           C  
ANISOU 4842  CG2 THR L  30     1891   5281   4309    791    943   -385       C  
ATOM   4843  N   TYR L  31      82.727  19.073  14.554  1.00 28.83           N  
ANISOU 4843  N   TYR L  31     2019   4961   3973    579    805   -318       N  
ATOM   4844  CA  TYR L  31      82.718  17.626  14.380  1.00 40.97           C  
ANISOU 4844  CA  TYR L  31     3573   6556   5437    453    781   -285       C  
ATOM   4845  C   TYR L  31      83.937  17.180  13.586  1.00 40.30           C  
ANISOU 4845  C   TYR L  31     3612   6375   5324    416    713   -261       C  
ATOM   4846  O   TYR L  31      84.340  17.839  12.625  1.00 53.74           O  
ANISOU 4846  O   TYR L  31     5334   8003   7081    467    662   -250       O  
ATOM   4847  CB  TYR L  31      81.440  17.163  13.669  1.00 46.08           C  
ANISOU 4847  CB  TYR L  31     4075   7328   6105    412    756   -254       C  
ATOM   4848  CG  TYR L  31      80.233  17.095  14.575  1.00 56.67           C  
ANISOU 4848  CG  TYR L  31     5292   8797   7445    401    835   -278       C  
ATOM   4849  CD1 TYR L  31      80.350  16.650  15.885  1.00 52.89           C  
ANISOU 4849  CD1 TYR L  31     4858   8343   6893    352    919   -306       C  
ATOM   4850  CD2 TYR L  31      78.978  17.481  14.124  1.00 59.71           C  
ANISOU 4850  CD2 TYR L  31     5507   9284   7898    441    827   -276       C  
ATOM   4851  CE1 TYR L  31      79.252  16.587  16.719  1.00 42.48           C  
ANISOU 4851  CE1 TYR L  31     3426   7147   5568    334   1003   -331       C  
ATOM   4852  CE2 TYR L  31      77.873  17.422  14.952  1.00 42.19           C  
ANISOU 4852  CE2 TYR L  31     3160   7189   5681    429    907   -304       C  
ATOM   4853  CZ  TYR L  31      78.016  16.975  16.248  1.00 52.82           C  
ANISOU 4853  CZ  TYR L  31     4560   8556   6952    371   1001   -332       C  
ATOM   4854  OH  TYR L  31      76.917  16.915  17.074  1.00 76.13           O  
ANISOU 4854  OH  TYR L  31     7386  11638   9901    352   1092   -364       O  
ATOM   4855  N   MET L  32      84.519  16.055  13.991  1.00 27.00           N  
ANISOU 4855  N   MET L  32     2007   4704   3549    328    715   -257       N  
ATOM   4856  CA  MET L  32      85.654  15.460  13.303  1.00 27.49           C  
ANISOU 4856  CA  MET L  32     2173   4699   3573    290    657   -241       C  
ATOM   4857  C   MET L  32      85.243  14.121  12.704  1.00 20.44           C  
ANISOU 4857  C   MET L  32     1251   3908   2609    178    628   -204       C  
ATOM   4858  O   MET L  32      84.422  13.395  13.270  1.00 21.50           O  
ANISOU 4858  O   MET L  32     1328   4153   2687    104    669   -199       O  
ATOM   4859  CB  MET L  32      86.841  15.273  14.255  1.00 26.33           C  
ANISOU 4859  CB  MET L  32     2147   4486   3371    293    676   -272       C  
ATOM   4860  CG  MET L  32      88.114  14.782  13.588  1.00 17.95           C  
ANISOU 4860  CG  MET L  32     1186   3350   2284    273    620   -267       C  
ATOM   4861  SD  MET L  32      88.706  15.887  12.288  1.00 29.79           S  
ANISOU 4861  SD  MET L  32     2709   4731   3878    334    572   -259       S  
ATOM   4862  CE  MET L  32      89.259  17.295  13.243  1.00 17.55           C  
ANISOU 4862  CE  MET L  32     1190   3128   2350    424    606   -316       C  
ATOM   4863  N   TYR L  33      85.814  13.805  11.545  1.00 19.46           N  
ANISOU 4863  N   TYR L  33     1168   3744   2483    154    565   -179       N  
ATOM   4864  CA  TYR L  33      85.494  12.588  10.817  1.00 19.55           C  
ANISOU 4864  CA  TYR L  33     1162   3839   2427     38    535   -141       C  
ATOM   4865  C   TYR L  33      86.784  11.882  10.429  1.00 18.13           C  
ANISOU 4865  C   TYR L  33     1102   3589   2196      5    508   -139       C  
ATOM   4866  O   TYR L  33      87.813  12.521  10.199  1.00 17.09           O  
ANISOU 4866  O   TYR L  33     1039   3345   2108     79    490   -161       O  
ATOM   4867  CB  TYR L  33      84.654  12.895   9.570  1.00 20.20           C  
ANISOU 4867  CB  TYR L  33     1145   3975   2557     35    480   -107       C  
ATOM   4868  CG  TYR L  33      83.419  13.711   9.872  1.00 26.11           C  
ANISOU 4868  CG  TYR L  33     1758   4792   3370     94    500   -115       C  
ATOM   4869  CD1 TYR L  33      82.252  13.101  10.305  1.00 38.24           C  
ANISOU 4869  CD1 TYR L  33     3193   6466   4869     15    532   -110       C  
ATOM   4870  CD2 TYR L  33      83.424  15.093   9.736  1.00 31.93           C  
ANISOU 4870  CD2 TYR L  33     2470   5459   4204    225    494   -132       C  
ATOM   4871  CE1 TYR L  33      81.122  13.840  10.591  1.00 36.12           C  
ANISOU 4871  CE1 TYR L  33     2787   6270   4665     75    555   -125       C  
ATOM   4872  CE2 TYR L  33      82.295  15.843  10.019  1.00 42.03           C  
ANISOU 4872  CE2 TYR L  33     3620   6803   5547    290    515   -143       C  
ATOM   4873  CZ  TYR L  33      81.147  15.209  10.446  1.00 42.75           C  
ANISOU 4873  CZ  TYR L  33     3598   7038   5606    220    545   -141       C  
ATOM   4874  OH  TYR L  33      80.021  15.945  10.730  1.00 57.26           O  
ANISOU 4874  OH  TYR L  33     5294   8949   7513    291    570   -158       O  
ATOM   4875  N   TRP L  34      86.726  10.555  10.366  1.00 29.01           N  
ANISOU 4875  N   TRP L  34     2507   5033   3483   -117    513   -114       N  
ATOM   4876  CA  TRP L  34      87.901   9.743  10.088  1.00 17.16           C  
ANISOU 4876  CA  TRP L  34     1118   3478   1926   -154    501   -115       C  
ATOM   4877  C   TRP L  34      87.590   8.761   8.971  1.00 17.33           C  
ANISOU 4877  C   TRP L  34     1142   3546   1896   -287    469    -68       C  
ATOM   4878  O   TRP L  34      86.610   8.010   9.055  1.00 24.71           O  
ANISOU 4878  O   TRP L  34     2041   4572   2774   -409    483    -36       O  
ATOM   4879  CB  TRP L  34      88.362   8.995  11.341  1.00 22.18           C  
ANISOU 4879  CB  TRP L  34     1829   4124   2474   -180    555   -133       C  
ATOM   4880  CG  TRP L  34      88.932   9.899  12.383  1.00 16.98           C  
ANISOU 4880  CG  TRP L  34     1192   3406   1852    -58    574   -184       C  
ATOM   4881  CD1 TRP L  34      88.252  10.542  13.375  1.00 17.83           C  
ANISOU 4881  CD1 TRP L  34     1248   3546   1979    -21    617   -202       C  
ATOM   4882  CD2 TRP L  34      90.307  10.267  12.535  1.00 15.91           C  
ANISOU 4882  CD2 TRP L  34     1139   3170   1738     30    552   -226       C  
ATOM   4883  NE1 TRP L  34      89.118  11.285  14.138  1.00 19.07           N  
ANISOU 4883  NE1 TRP L  34     1458   3625   2162     76    621   -247       N  
ATOM   4884  CE2 TRP L  34      90.387  11.134  13.642  1.00 16.17           C  
ANISOU 4884  CE2 TRP L  34     1171   3176   1796    106    576   -263       C  
ATOM   4885  CE3 TRP L  34      91.478   9.946  11.843  1.00 14.91           C  
ANISOU 4885  CE3 TRP L  34     1083   2975   1609     47    516   -241       C  
ATOM   4886  CZ2 TRP L  34      91.591  11.683  14.073  1.00 15.47           C  
ANISOU 4886  CZ2 TRP L  34     1150   2998   1729    183    556   -308       C  
ATOM   4887  CZ3 TRP L  34      92.671  10.491  12.273  1.00 21.14           C  
ANISOU 4887  CZ3 TRP L  34     1931   3675   2427    135    496   -292       C  
ATOM   4888  CH2 TRP L  34      92.719  11.350  13.377  1.00 26.83           C  
ANISOU 4888  CH2 TRP L  34     2650   4374   3169    194    512   -321       C  
ATOM   4889  N   TYR L  35      88.434   8.768   7.938  1.00 35.18           N  
ANISOU 4889  N   TYR L  35     3453   5739   4174   -276    429    -67       N  
ATOM   4890  CA  TYR L  35      88.279   7.926   6.762  1.00 38.60           C  
ANISOU 4890  CA  TYR L  35     3909   6196   4560   -407    395    -24       C  
ATOM   4891  C   TYR L  35      89.509   7.048   6.578  1.00 34.04           C  
ANISOU 4891  C   TYR L  35     3465   5546   3923   -452    413    -36       C  
ATOM   4892  O   TYR L  35      90.638   7.463   6.861  1.00 33.72           O  
ANISOU 4892  O   TYR L  35     3468   5432   3912   -339    426    -88       O  
ATOM   4893  CB  TYR L  35      88.066   8.768   5.494  1.00 16.33           C  
ANISOU 4893  CB  TYR L  35     1028   3370   1809   -368    334     -8       C  
ATOM   4894  CG  TYR L  35      86.909   9.733   5.580  1.00 17.31           C  
ANISOU 4894  CG  TYR L  35     1024   3558   1996   -302    316      2       C  
ATOM   4895  CD1 TYR L  35      85.634   9.355   5.182  1.00 18.62           C  
ANISOU 4895  CD1 TYR L  35     1102   3838   2135   -397    287     42       C  
ATOM   4896  CD2 TYR L  35      87.091  11.024   6.056  1.00 17.10           C  
ANISOU 4896  CD2 TYR L  35      970   3471   2054   -149    331    -34       C  
ATOM   4897  CE1 TYR L  35      84.572  10.235   5.258  1.00 19.74           C  
ANISOU 4897  CE1 TYR L  35     1114   4047   2338   -324    273     44       C  
ATOM   4898  CE2 TYR L  35      86.036  11.910   6.137  1.00 37.06           C  
ANISOU 4898  CE2 TYR L  35     3387   6051   4642    -85    322    -28       C  
ATOM   4899  CZ  TYR L  35      84.778  11.511   5.737  1.00 36.84           C  
ANISOU 4899  CZ  TYR L  35     3256   6150   4592   -163    292      9       C  
ATOM   4900  OH  TYR L  35      83.723  12.390   5.816  1.00 31.08           O  
ANISOU 4900  OH  TYR L  35     2401   5480   3927    -87    283      9       O  
ATOM   4901  N   GLN L  36      89.281   5.832   6.090  1.00 16.08           N  
ANISOU 4901  N   GLN L  36     1269   3279   1562   -619    412      6       N  
ATOM   4902  CA  GLN L  36      90.341   4.887   5.772  1.00 15.56           C  
ANISOU 4902  CA  GLN L  36     1367   3122   1424   -678    435      1       C  
ATOM   4903  C   GLN L  36      90.394   4.669   4.266  1.00 15.42           C  
ANISOU 4903  C   GLN L  36     1397   3049   1414   -762    379     23       C  
ATOM   4904  O   GLN L  36      89.354   4.551   3.611  1.00 16.20           O  
ANISOU 4904  O   GLN L  36     1437   3215   1503   -872    338     67       O  
ATOM   4905  CB  GLN L  36      90.117   3.551   6.484  1.00 16.41           C  
ANISOU 4905  CB  GLN L  36     1620   3205   1411   -803    474     34       C  
ATOM   4906  CG  GLN L  36      91.191   2.513   6.222  1.00 31.43           C  
ANISOU 4906  CG  GLN L  36     3760   4926   3257   -804    459     25       C  
ATOM   4907  CD  GLN L  36      90.870   1.172   6.849  1.00 23.85           C  
ANISOU 4907  CD  GLN L  36     2975   3918   2167   -935    494     70       C  
ATOM   4908  OE1 GLN L  36      89.730   0.906   7.226  1.00 18.28           O  
ANISOU 4908  OE1 GLN L  36     2216   3301   1426  -1060    516    106       O  
ATOM   4909  NE2 GLN L  36      91.880   0.318   6.968  1.00 50.58           N  
ANISOU 4909  NE2 GLN L  36     6578   7139   5500   -884    486     58       N  
ATOM   4910  N   GLN L  37      91.607   4.621   3.717  1.00 14.57           N  
ANISOU 4910  N   GLN L  37     1409   2800   1326   -690    364    -19       N  
ATOM   4911  CA  GLN L  37      91.798   4.416   2.288  1.00 28.96           C  
ANISOU 4911  CA  GLN L  37     3304   4552   3148   -764    322     -9       C  
ATOM   4912  C   GLN L  37      93.008   3.527   2.055  1.00 27.99           C  
ANISOU 4912  C   GLN L  37     3384   4264   2989   -748    334    -50       C  
ATOM   4913  O   GLN L  37      94.089   3.790   2.591  1.00 13.45           O  
ANISOU 4913  O   GLN L  37     1567   2361   1185   -603    356   -113       O  
ATOM   4914  CB  GLN L  37      91.979   5.748   1.551  1.00 13.88           C  
ANISOU 4914  CB  GLN L  37     1285   2660   1329   -671    293    -29       C  
ATOM   4915  CG  GLN L  37      91.967   5.615   0.035  1.00 14.00           C  
ANISOU 4915  CG  GLN L  37     1369   2625   1326   -766    245     -8       C  
ATOM   4916  CD  GLN L  37      92.287   6.919  -0.668  1.00 40.22           C  
ANISOU 4916  CD  GLN L  37     4625   5935   4722   -671    224    -26       C  
ATOM   4917  OE1 GLN L  37      92.958   7.788  -0.113  1.00 47.91           O  
ANISOU 4917  OE1 GLN L  37     5552   6887   5765   -530    258    -80       O  
ATOM   4918  NE2 GLN L  37      91.805   7.063  -1.897  1.00 13.99           N  
ANISOU 4918  NE2 GLN L  37     1314   2624   1379   -756    166     17       N  
ATOM   4919  N   LYS L  38      92.821   2.482   1.257  1.00 28.76           N  
ANISOU 4919  N   LYS L  38     3620   4295   3012   -894    321    -21       N  
ATOM   4920  CA  LYS L  38      93.875   1.575   0.841  1.00 28.51           C  
ANISOU 4920  CA  LYS L  38     3789   4099   2944   -885    334    -61       C  
ATOM   4921  C   LYS L  38      94.318   1.897  -0.579  1.00 35.55           C  
ANISOU 4921  C   LYS L  38     4709   4935   3864   -907    315    -88       C  
ATOM   4922  O   LYS L  38      93.567   2.495  -1.355  1.00 14.38           O  
ANISOU 4922  O   LYS L  38     1935   2333   1194   -983    277    -51       O  
ATOM   4923  CB  LYS L  38      93.389   0.123   0.925  1.00 15.65           C  
ANISOU 4923  CB  LYS L  38     2335   2410   1202  -1041    345    -16       C  
ATOM   4924  CG  LYS L  38      93.095  -0.344   2.341  1.00 16.17           C  
ANISOU 4924  CG  LYS L  38     2427   2500   1216  -1028    375     11       C  
ATOM   4925  CD  LYS L  38      92.645  -1.795   2.370  1.00 25.81           C  
ANISOU 4925  CD  LYS L  38     3855   3637   2314  -1199    395     56       C  
ATOM   4926  CE  LYS L  38      92.387  -2.264   3.792  1.00 30.74           C  
ANISOU 4926  CE  LYS L  38     4535   4273   2873  -1192    432     86       C  
ATOM   4927  NZ  LYS L  38      91.899  -3.672   3.836  1.00 37.87           N  
ANISOU 4927  NZ  LYS L  38     5632   5065   3690  -1336    433    117       N  
ATOM   4928  N   PRO L  39      95.547   1.532  -0.949  1.00 33.33           N  
ANISOU 4928  N   PRO L  39     4553   4521   3590   -836    340   -156       N  
ATOM   4929  CA  PRO L  39      96.041   1.873  -2.289  1.00 16.87           C  
ANISOU 4929  CA  PRO L  39     2503   2382   1526   -862    339   -192       C  
ATOM   4930  C   PRO L  39      95.191   1.247  -3.385  1.00 14.50           C  
ANISOU 4930  C   PRO L  39     2290   2075   1143  -1062    308   -137       C  
ATOM   4931  O   PRO L  39      94.794   0.082  -3.304  1.00 33.14           O  
ANISOU 4931  O   PRO L  39     4780   4390   3421  -1175    311   -108       O  
ATOM   4932  CB  PRO L  39      97.467   1.310  -2.294  1.00 13.58           C  
ANISOU 4932  CB  PRO L  39     2210   1830   1119   -756    384   -283       C  
ATOM   4933  CG  PRO L  39      97.858   1.268  -0.860  1.00 13.90           C  
ANISOU 4933  CG  PRO L  39     2210   1888   1184   -613    392   -303       C  
ATOM   4934  CD  PRO L  39      96.601   0.933  -0.112  1.00 35.61           C  
ANISOU 4934  CD  PRO L  39     4938   4716   3877   -706    370   -212       C  
ATOM   4935  N   GLY L  40      94.911   2.042  -4.416  1.00 14.41           N  
ANISOU 4935  N   GLY L  40     2220   2108   1148  -1110    276   -123       N  
ATOM   4936  CA  GLY L  40      94.152   1.581  -5.559  1.00 15.24           C  
ANISOU 4936  CA  GLY L  40     2400   2220   1170  -1296    233    -76       C  
ATOM   4937  C   GLY L  40      92.656   1.510  -5.362  1.00 36.81           C  
ANISOU 4937  C   GLY L  40     5026   5094   3864  -1410    167      6       C  
ATOM   4938  O   GLY L  40      91.965   0.931  -6.207  1.00 59.57           O  
ANISOU 4938  O   GLY L  40     7973   7988   6673  -1520    108     26       O  
ATOM   4939  N   SER L  41      92.127   2.080  -4.281  1.00 15.84           N  
ANISOU 4939  N   SER L  41     2203   2554   1260  -1342    166     36       N  
ATOM   4940  CA  SER L  41      90.703   2.015  -3.998  1.00 16.76           C  
ANISOU 4940  CA  SER L  41     2196   2820   1352  -1423    110     97       C  
ATOM   4941  C   SER L  41      90.235   3.352  -3.439  1.00 16.44           C  
ANISOU 4941  C   SER L  41     1924   2925   1398  -1320     97    122       C  
ATOM   4942  O   SER L  41      91.030   4.260  -3.185  1.00 15.49           O  
ANISOU 4942  O   SER L  41     1766   2763   1358  -1151    122     83       O  
ATOM   4943  CB  SER L  41      90.377   0.878  -3.022  1.00 22.50           C  
ANISOU 4943  CB  SER L  41     2995   3529   2027  -1475    142     97       C  
ATOM   4944  OG  SER L  41      91.089   1.031  -1.806  1.00 36.11           O  
ANISOU 4944  OG  SER L  41     4708   5225   3788  -1365    217     78       O  
ATOM   4945  N   SER L  42      88.926   3.460  -3.249  1.00 17.41           N  
ANISOU 4945  N   SER L  42     1910   3194   1511  -1359     45    168       N  
ATOM   4946  CA  SER L  42      88.278   4.657  -2.742  1.00 19.02           C  
ANISOU 4946  CA  SER L  42     1891   3540   1795  -1245     25    188       C  
ATOM   4947  C   SER L  42      88.283   4.668  -1.219  1.00 17.22           C  
ANISOU 4947  C   SER L  42     1598   3344   1602  -1157     96    165       C  
ATOM   4948  O   SER L  42      88.466   3.628  -0.580  1.00 17.35           O  
ANISOU 4948  O   SER L  42     1727   3303   1561  -1221    143    152       O  
ATOM   4949  CB  SER L  42      86.846   4.731  -3.267  1.00 25.49           C  
ANISOU 4949  CB  SER L  42     2599   4502   2586  -1314    -58    240       C  
ATOM   4950  OG  SER L  42      86.833   4.815  -4.682  1.00 36.01           O  
ANISOU 4950  OG  SER L  42     3990   5814   3877  -1389   -133    266       O  
ATOM   4951  N   PRO L  43      88.105   5.834  -0.602  1.00 16.98           N  
ANISOU 4951  N   PRO L  43     1406   3388   1656  -1002    104    157       N  
ATOM   4952  CA  PRO L  43      88.049   5.888   0.862  1.00 32.52           C  
ANISOU 4952  CA  PRO L  43     3324   5384   3648   -915    169    130       C  
ATOM   4953  C   PRO L  43      86.746   5.311   1.393  1.00 18.24           C  
ANISOU 4953  C   PRO L  43     1458   3677   1794  -1002    164    155       C  
ATOM   4954  O   PRO L  43      85.743   5.200   0.684  1.00 19.33           O  
ANISOU 4954  O   PRO L  43     1539   3898   1907  -1085    105    189       O  
ATOM   4955  CB  PRO L  43      88.153   7.386   1.173  1.00 33.11           C  
ANISOU 4955  CB  PRO L  43     3269   5485   3827   -721    170    107       C  
ATOM   4956  CG  PRO L  43      88.649   8.023  -0.088  1.00 16.00           C  
ANISOU 4956  CG  PRO L  43     1113   3280   1687   -708    124    116       C  
ATOM   4957  CD  PRO L  43      88.121   7.180  -1.198  1.00 16.76           C  
ANISOU 4957  CD  PRO L  43     1269   3394   1705   -887     60    164       C  
ATOM   4958  N   ARG L  44      86.776   4.937   2.671  1.00 18.30           N  
ANISOU 4958  N   ARG L  44     1484   3686   1785   -987    230    134       N  
ATOM   4959  CA  ARG L  44      85.586   4.499   3.382  1.00 39.99           C  
ANISOU 4959  CA  ARG L  44     4168   6532   4493  -1062    247    145       C  
ATOM   4960  C   ARG L  44      85.513   5.214   4.723  1.00 44.12           C  
ANISOU 4960  C   ARG L  44     4605   7091   5068   -925    305    114       C  
ATOM   4961  O   ARG L  44      86.537   5.557   5.320  1.00 18.51           O  
ANISOU 4961  O   ARG L  44     1408   3773   1851   -815    343     83       O  
ATOM   4962  CB  ARG L  44      85.562   2.974   3.590  1.00 20.31           C  
ANISOU 4962  CB  ARG L  44     1841   3987   1891  -1243    275    156       C  
ATOM   4963  CG  ARG L  44      86.403   2.469   4.751  1.00 19.80           C  
ANISOU 4963  CG  ARG L  44     1900   3834   1791  -1217    352    138       C  
ATOM   4964  CD  ARG L  44      85.870   1.136   5.262  1.00 55.65           C  
ANISOU 4964  CD  ARG L  44     6568   8350   6228  -1385    384    153       C  
ATOM   4965  NE  ARG L  44      86.661   0.604   6.368  1.00 43.83           N  
ANISOU 4965  NE  ARG L  44     5219   6754   4680  -1354    452    149       N  
ATOM   4966  CZ  ARG L  44      86.320  -0.462   7.084  1.00 39.91           C  
ANISOU 4966  CZ  ARG L  44     4856   6214   4093  -1470    493    163       C  
ATOM   4967  NH1 ARG L  44      85.196  -1.112   6.817  1.00 39.98           N  
ANISOU 4967  NH1 ARG L  44     4855   6280   4057  -1635    480    170       N  
ATOM   4968  NH2 ARG L  44      87.102  -0.878   8.072  1.00 37.10           N  
ANISOU 4968  NH2 ARG L  44     4653   5761   3685  -1416    545    167       N  
ATOM   4969  N   LEU L  45      84.289   5.442   5.188  1.00 41.08           N  
ANISOU 4969  N   LEU L  45     4094   6821   4693   -934    313    115       N  
ATOM   4970  CA  LEU L  45      84.075   6.194   6.416  1.00 35.49           C  
ANISOU 4970  CA  LEU L  45     3305   6144   4036   -810    368     81       C  
ATOM   4971  C   LEU L  45      84.308   5.307   7.631  1.00 38.65           C  
ANISOU 4971  C   LEU L  45     3804   6525   4358   -883    444     71       C  
ATOM   4972  O   LEU L  45      83.716   4.229   7.748  1.00 42.97           O  
ANISOU 4972  O   LEU L  45     4402   7106   4820  -1051    463     90       O  
ATOM   4973  CB  LEU L  45      82.661   6.771   6.447  1.00 27.47           C  
ANISOU 4973  CB  LEU L  45     2118   5257   3064   -793    356     81       C  
ATOM   4974  CG  LEU L  45      82.235   7.446   7.752  1.00 23.21           C  
ANISOU 4974  CG  LEU L  45     1498   4753   2568   -693    423     43       C  
ATOM   4975  CD1 LEU L  45      83.129   8.635   8.067  1.00 21.93           C  
ANISOU 4975  CD1 LEU L  45     1354   4488   2491   -499    429     13       C  
ATOM   4976  CD2 LEU L  45      80.776   7.869   7.679  1.00 25.05           C  
ANISOU 4976  CD2 LEU L  45     1557   5121   2840   -695    415     40       C  
ATOM   4977  N   LEU L  46      85.175   5.764   8.535  1.00 41.30           N  
ANISOU 4977  N   LEU L  46     4178   6798   4714   -759    487     39       N  
ATOM   4978  CA  LEU L  46      85.411   5.081   9.802  1.00 20.72           C  
ANISOU 4978  CA  LEU L  46     1665   4178   2029   -802    561     32       C  
ATOM   4979  C   LEU L  46      84.612   5.710  10.937  1.00 29.40           C  
ANISOU 4979  C   LEU L  46     2659   5356   3155   -745    613      4       C  
ATOM   4980  O   LEU L  46      83.769   5.047  11.549  1.00 23.08           O  
ANISOU 4980  O   LEU L  46     1857   4625   2289   -867    663     13       O  
ATOM   4981  CB  LEU L  46      86.906   5.088  10.151  1.00 32.37           C  
ANISOU 4981  CB  LEU L  46     3262   5547   3491   -707    576     11       C  
ATOM   4982  CG  LEU L  46      87.863   4.269   9.289  1.00 36.72           C  
ANISOU 4982  CG  LEU L  46     3958   6002   3992   -767    552     31       C  
ATOM   4983  CD1 LEU L  46      89.261   4.336   9.879  1.00 17.56           C  
ANISOU 4983  CD1 LEU L  46     1635   3497   1542   -647    578     -4       C  
ATOM   4984  CD2 LEU L  46      87.392   2.828   9.173  1.00 19.63           C  
ANISOU 4984  CD2 LEU L  46     1930   3810   1717   -967    565     78       C  
ATOM   4985  N   ILE L  47      84.859   6.986  11.227  1.00 33.64           N  
ANISOU 4985  N   ILE L  47     3124   5872   3785   -570    609    -33       N  
ATOM   4986  CA  ILE L  47      84.255   7.660  12.371  1.00 21.98           C  
ANISOU 4986  CA  ILE L  47     1572   4444   2335   -503    666    -66       C  
ATOM   4987  C   ILE L  47      83.513   8.897  11.884  1.00 27.43           C  
ANISOU 4987  C   ILE L  47     2120   5162   3142   -397    634    -79       C  
ATOM   4988  O   ILE L  47      84.057   9.685  11.102  1.00 25.18           O  
ANISOU 4988  O   ILE L  47     1837   4800   2932   -294    578    -81       O  
ATOM   4989  CB  ILE L  47      85.308   8.041  13.428  1.00 21.15           C  
ANISOU 4989  CB  ILE L  47     1552   4262   2220   -395    701   -103       C  
ATOM   4990  CG1 ILE L  47      86.042   6.796  13.928  1.00 20.98           C  
ANISOU 4990  CG1 ILE L  47     1684   4214   2072   -489    734    -85       C  
ATOM   4991  CG2 ILE L  47      84.656   8.763  14.594  1.00 22.17           C  
ANISOU 4991  CG2 ILE L  47     1613   4436   2373   -337    764   -138       C  
ATOM   4992  CD1 ILE L  47      85.144   5.801  14.629  1.00 22.62           C  
ANISOU 4992  CD1 ILE L  47     1923   4495   2177   -649    801    -59       C  
ATOM   4993  N   TYR L  48      82.276   9.064  12.349  1.00 33.47           N  
ANISOU 4993  N   TYR L  48     2768   6032   3918   -424    675    -88       N  
ATOM   4994  CA  TYR L  48      81.491  10.261  12.089  1.00 37.33           C  
ANISOU 4994  CA  TYR L  48     3117   6551   4515   -313    660   -104       C  
ATOM   4995  C   TYR L  48      81.098  10.911  13.410  1.00 44.29           C  
ANISOU 4995  C   TYR L  48     3954   7452   5420   -243    743   -147       C  
ATOM   4996  O   TYR L  48      80.917  10.231  14.424  1.00 28.71           O  
ANISOU 4996  O   TYR L  48     2011   5530   3367   -328    816   -158       O  
ATOM   4997  CB  TYR L  48      80.235   9.948  11.256  1.00 28.33           C  
ANISOU 4997  CB  TYR L  48     1845   5540   3381   -401    625    -80       C  
ATOM   4998  CG  TYR L  48      79.169   9.155  11.982  1.00 33.81           C  
ANISOU 4998  CG  TYR L  48     2471   6367   4007   -540    694    -89       C  
ATOM   4999  CD1 TYR L  48      79.230   7.769  12.049  1.00 39.85           C  
ANISOU 4999  CD1 TYR L  48     3328   7158   4655   -726    712    -67       C  
ATOM   5000  CD2 TYR L  48      78.092   9.792  12.587  1.00 45.23           C  
ANISOU 5000  CD2 TYR L  48     3768   7908   5507   -493    746   -122       C  
ATOM   5001  CE1 TYR L  48      78.255   7.041  12.707  1.00 51.92           C  
ANISOU 5001  CE1 TYR L  48     4809   8801   6116   -872    781    -77       C  
ATOM   5002  CE2 TYR L  48      77.113   9.073  13.247  1.00 51.37           C  
ANISOU 5002  CE2 TYR L  48     4480   8815   6223   -630    818   -137       C  
ATOM   5003  CZ  TYR L  48      77.199   7.698  13.303  1.00 63.32           C  
ANISOU 5003  CZ  TYR L  48     6093  10350   7614   -825    836   -115       C  
ATOM   5004  OH  TYR L  48      76.225   6.980  13.959  1.00 83.09           O  
ANISOU 5004  OH  TYR L  48     8546  12975  10051   -978    913   -132       O  
ATOM   5005  N   ASP L  49      80.976  12.237  13.385  1.00 53.47           N  
ANISOU 5005  N   ASP L  49     5057   8569   6691    -95    736   -170       N  
ATOM   5006  CA  ASP L  49      80.655  13.041  14.566  1.00 40.84           C  
ANISOU 5006  CA  ASP L  49     3419   6970   5126    -14    816   -213       C  
ATOM   5007  C   ASP L  49      81.623  12.745  15.713  1.00 35.34           C  
ANISOU 5007  C   ASP L  49     2861   6211   4356    -21    868   -235       C  
ATOM   5008  O   ASP L  49      81.234  12.351  16.814  1.00 26.90           O  
ANISOU 5008  O   ASP L  49     1787   5211   3222    -76    950   -255       O  
ATOM   5009  CB  ASP L  49      79.202  12.829  15.000  1.00 43.45           C  
ANISOU 5009  CB  ASP L  49     3598   7459   5453    -74    877   -225       C  
ATOM   5010  CG  ASP L  49      78.213  13.528  14.087  1.00 45.13           C  
ANISOU 5010  CG  ASP L  49     3649   7734   5764    -12    830   -219       C  
ATOM   5011  OD1 ASP L  49      78.646  14.094  13.061  1.00 38.58           O  
ANISOU 5011  OD1 ASP L  49     2838   6826   4996     66    747   -198       O  
ATOM   5012  OD2 ASP L  49      77.004  13.515  14.399  1.00 54.14           O  
ANISOU 5012  OD2 ASP L  49     4641   9008   6920    -40    877   -237       O  
ATOM   5013  N   THR L  50      82.911  12.928  15.415  1.00 57.65           N  
ANISOU 5013  N   THR L  50     5807   8910   7186     31    818   -234       N  
ATOM   5014  CA  THR L  50      84.001  12.847  16.386  1.00 58.89           C  
ANISOU 5014  CA  THR L  50     6091   8996   7287     54    845   -260       C  
ATOM   5015  C   THR L  50      84.167  11.461  17.005  1.00 54.81           C  
ANISOU 5015  C   THR L  50     5646   8545   6636    -70    882   -248       C  
ATOM   5016  O   THR L  50      85.271  10.907  16.985  1.00 54.79           O  
ANISOU 5016  O   THR L  50     5759   8484   6576    -81    852   -243       O  
ATOM   5017  CB  THR L  50      83.812  13.893  17.492  1.00 24.01           C  
ANISOU 5017  CB  THR L  50     1656   4560   2907    142    913   -305       C  
ATOM   5018  OG1 THR L  50      83.943  15.207  16.936  1.00 23.68           O  
ANISOU 5018  OG1 THR L  50     1591   4425   2983    257    881   -314       O  
ATOM   5019  CG2 THR L  50      84.852  13.710  18.586  1.00 23.41           C  
ANISOU 5019  CG2 THR L  50     1704   4437   2753    151    939   -335       C  
ATOM   5020  N   SER L  51      83.092  10.884  17.558  1.00 35.86           N  
ANISOU 5020  N   SER L  51     3182   6263   4181   -169    950   -243       N  
ATOM   5021  CA  SER L  51      83.259   9.680  18.366  1.00 30.17           C  
ANISOU 5021  CA  SER L  51     2559   5586   3321   -291   1005   -230       C  
ATOM   5022  C   SER L  51      82.221   8.594  18.087  1.00 26.83           C  
ANISOU 5022  C   SER L  51     2092   5268   2833   -465   1032   -195       C  
ATOM   5023  O   SER L  51      82.019   7.721  18.938  1.00 40.31           O  
ANISOU 5023  O   SER L  51     3872   7017   4425   -583   1104   -186       O  
ATOM   5024  CB  SER L  51      83.224  10.036  19.857  1.00 34.59           C  
ANISOU 5024  CB  SER L  51     3148   6162   3834   -257   1094   -271       C  
ATOM   5025  OG  SER L  51      82.022  10.708  20.195  1.00 41.53           O  
ANISOU 5025  OG  SER L  51     3888   7119   4772   -239   1154   -296       O  
ATOM   5026  N   ASN L  52      81.567   8.606  16.929  1.00 27.01           N  
ANISOU 5026  N   ASN L  52     2013   5332   2919   -496    977   -174       N  
ATOM   5027  CA  ASN L  52      80.562   7.603  16.601  1.00 52.14           C  
ANISOU 5027  CA  ASN L  52     5151   8619   6043   -674    994   -148       C  
ATOM   5028  C   ASN L  52      81.100   6.661  15.533  1.00 41.49           C  
ANISOU 5028  C   ASN L  52     3896   7221   4648   -770    922   -101       C  
ATOM   5029  O   ASN L  52      81.662   7.108  14.527  1.00 51.57           O  
ANISOU 5029  O   ASN L  52     5166   8436   5993   -685    841    -91       O  
ATOM   5030  CB  ASN L  52      79.257   8.254  16.135  1.00 29.86           C  
ANISOU 5030  CB  ASN L  52     2129   5904   3312   -652    988   -164       C  
ATOM   5031  CG  ASN L  52      78.593   9.067  17.228  1.00 40.62           C  
ANISOU 5031  CG  ASN L  52     3397   7323   4712   -577   1076   -211       C  
ATOM   5032  OD1 ASN L  52      78.121   8.520  18.225  1.00 44.83           O  
ANISOU 5032  OD1 ASN L  52     3945   7925   5164   -679   1169   -226       O  
ATOM   5033  ND2 ASN L  52      78.549  10.381  17.045  1.00 30.97           N  
ANISOU 5033  ND2 ASN L  52     2092   6065   3612   -405   1053   -235       N  
ATOM   5034  N   LEU L  53      80.925   5.362  15.759  1.00 40.25           N  
ANISOU 5034  N   LEU L  53     3841   7079   4372   -954    959    -73       N  
ATOM   5035  CA  LEU L  53      81.423   4.346  14.843  1.00 37.87           C  
ANISOU 5035  CA  LEU L  53     3662   6713   4014  -1066    903    -28       C  
ATOM   5036  C   LEU L  53      80.459   4.176  13.675  1.00 36.73           C  
ANISOU 5036  C   LEU L  53     3402   6650   3903  -1157    847    -16       C  
ATOM   5037  O   LEU L  53      79.245   4.069  13.871  1.00 37.60           O  
ANISOU 5037  O   LEU L  53     3399   6881   4007  -1245    884    -31       O  
ATOM   5038  CB  LEU L  53      81.605   3.019  15.581  1.00 28.40           C  
ANISOU 5038  CB  LEU L  53     2658   5464   2670  -1227    964      0       C  
ATOM   5039  CG  LEU L  53      82.309   1.885  14.837  1.00 27.78           C  
ANISOU 5039  CG  LEU L  53     2769   5268   2520  -1332    918     48       C  
ATOM   5040  CD1 LEU L  53      83.744   2.270  14.522  1.00 30.94           C  
ANISOU 5040  CD1 LEU L  53     3249   5557   2951  -1179    869     52       C  
ATOM   5041  CD2 LEU L  53      82.261   0.605  15.656  1.00 39.77           C  
ANISOU 5041  CD2 LEU L  53     4495   6720   3895  -1491    982     78       C  
ATOM   5042  N   ALA L  54      81.001   4.154  12.461  1.00 41.81           N  
ANISOU 5042  N   ALA L  54     4073   7235   4577  -1137    760      8       N  
ATOM   5043  CA  ALA L  54      80.176   3.980  11.277  1.00 27.96           C  
ANISOU 5043  CA  ALA L  54     2227   5556   2842  -1222    697     23       C  
ATOM   5044  C   ALA L  54      79.746   2.523  11.131  1.00 29.19           C  
ANISOU 5044  C   ALA L  54     2494   5717   2879  -1460    712     45       C  
ATOM   5045  O   ALA L  54      80.359   1.606  11.684  1.00 45.91           O  
ANISOU 5045  O   ALA L  54     4802   7734   4906  -1545    753     61       O  
ATOM   5046  CB  ALA L  54      80.923   4.436  10.024  1.00 28.75           C  
ANISOU 5046  CB  ALA L  54     2338   5585   3003  -1130    603     43       C  
ATOM   5047  N   SER L  55      78.675   2.321  10.370  1.00 54.22           N  
ANISOU 5047  N   SER L  55     5554   8997   6048  -1564    676     45       N  
ATOM   5048  CA  SER L  55      78.120   0.986  10.191  1.00 51.43           C  
ANISOU 5048  CA  SER L  55     5300   8658   5583  -1802    690     54       C  
ATOM   5049  C   SER L  55      79.089   0.096   9.422  1.00 44.04           C  
ANISOU 5049  C   SER L  55     4582   7565   4586  -1876    639     89       C  
ATOM   5050  O   SER L  55      79.677   0.509   8.419  1.00 46.95           O  
ANISOU 5050  O   SER L  55     4946   7887   5006  -1790    563    105       O  
ATOM   5051  CB  SER L  55      76.782   1.064   9.458  1.00 66.29           C  
ANISOU 5051  CB  SER L  55     6999  10707   7480  -1886    654     40       C  
ATOM   5052  OG  SER L  55      76.220  -0.225   9.286  1.00 97.69           O  
ANISOU 5052  OG  SER L  55    11075  14700  11343  -2127    670     40       O  
ATOM   5053  N   GLY L  56      79.251  -1.138   9.901  1.00 38.91           N  
ANISOU 5053  N   GLY L  56     4136   6821   3826  -2034    686     98       N  
ATOM   5054  CA  GLY L  56      80.153  -2.089   9.289  1.00 51.33           C  
ANISOU 5054  CA  GLY L  56     5947   8218   5339  -2101    649    124       C  
ATOM   5055  C   GLY L  56      81.603  -1.956   9.696  1.00 62.97           C  
ANISOU 5055  C   GLY L  56     7568   9530   6828  -1958    659    143       C  
ATOM   5056  O   GLY L  56      82.422  -2.793   9.293  1.00 74.82           O  
ANISOU 5056  O   GLY L  56     9284  10864   8278  -1997    637    163       O  
ATOM   5057  N   VAL L  57      81.952  -0.938  10.475  1.00 44.55           N  
ANISOU 5057  N   VAL L  57     5132   7237   4560  -1787    691    133       N  
ATOM   5058  CA  VAL L  57      83.325  -0.737  10.928  1.00 42.79           C  
ANISOU 5058  CA  VAL L  57     5032   6884   4342  -1642    703    144       C  
ATOM   5059  C   VAL L  57      83.524  -1.523  12.218  1.00 44.20           C  
ANISOU 5059  C   VAL L  57     5393   6984   4418  -1692    780    159       C  
ATOM   5060  O   VAL L  57      82.646  -1.503  13.094  1.00 28.81           O  
ANISOU 5060  O   VAL L  57     3376   5130   2441  -1753    843    145       O  
ATOM   5061  CB  VAL L  57      83.630   0.757  11.124  1.00 25.27           C  
ANISOU 5061  CB  VAL L  57     2625   4742   2233  -1433    696    116       C  
ATOM   5062  CG1 VAL L  57      85.106   0.971  11.418  1.00 49.71           C  
ANISOU 5062  CG1 VAL L  57     5841   7719   5329  -1288    699    117       C  
ATOM   5063  CG2 VAL L  57      83.208   1.546   9.895  1.00 24.85           C  
ANISOU 5063  CG2 VAL L  57     2397   4769   2275  -1387    619    108       C  
ATOM   5064  N   PRO L  58      84.638  -2.240  12.373  1.00 32.00           N  
ANISOU 5064  N   PRO L  58     4089   5260   2808  -1662    777    187       N  
ATOM   5065  CA  PRO L  58      84.868  -2.993  13.611  1.00 27.85           C  
ANISOU 5065  CA  PRO L  58     3764   4645   2173  -1688    838    211       C  
ATOM   5066  C   PRO L  58      84.885  -2.089  14.836  1.00 34.15           C  
ANISOU 5066  C   PRO L  58     4458   5536   2979  -1567    895    193       C  
ATOM   5067  O   PRO L  58      85.130  -0.883  14.755  1.00 52.21           O  
ANISOU 5067  O   PRO L  58     6566   7912   5361  -1418    881    160       O  
ATOM   5068  CB  PRO L  58      86.239  -3.641  13.383  1.00 26.98           C  
ANISOU 5068  CB  PRO L  58     3903   4332   2016  -1604    799    241       C  
ATOM   5069  CG  PRO L  58      86.368  -3.728  11.901  1.00 42.73           C  
ANISOU 5069  CG  PRO L  58     5871   6294   4070  -1638    732    233       C  
ATOM   5070  CD  PRO L  58      85.667  -2.518  11.356  1.00 25.58           C  
ANISOU 5070  CD  PRO L  58     3398   4313   2010  -1613    714    200       C  
ATOM   5071  N   VAL L  59      84.623  -2.703  15.993  1.00 40.31           N  
ANISOU 5071  N   VAL L  59     5372   6287   3656  -1633    960    210       N  
ATOM   5072  CA  VAL L  59      84.584  -1.959  17.246  1.00 29.40           C  
ANISOU 5072  CA  VAL L  59     3922   4988   2263  -1537   1021    191       C  
ATOM   5073  C   VAL L  59      85.974  -1.512  17.681  1.00 41.58           C  
ANISOU 5073  C   VAL L  59     5557   6454   3787  -1331    993    193       C  
ATOM   5074  O   VAL L  59      86.097  -0.644  18.553  1.00 34.26           O  
ANISOU 5074  O   VAL L  59     4543   5604   2870  -1217   1027    160       O  
ATOM   5075  CB  VAL L  59      83.911  -2.809  18.340  1.00 31.59           C  
ANISOU 5075  CB  VAL L  59     4335   5250   2418  -1682   1100    211       C  
ATOM   5076  CG1 VAL L  59      83.419  -1.931  19.482  1.00 32.18           C  
ANISOU 5076  CG1 VAL L  59     4269   5459   2498  -1627   1176    174       C  
ATOM   5077  CG2 VAL L  59      82.767  -3.618  17.750  1.00 57.98           C  
ANISOU 5077  CG2 VAL L  59     7661   8623   5746  -1909   1112    208       C  
ATOM   5078  N   ARG L  60      87.030  -2.081  17.092  1.00 45.89           N  
ANISOU 5078  N   ARG L  60     6278   6854   4305  -1276    929    221       N  
ATOM   5079  CA  ARG L  60      88.385  -1.665  17.438  1.00 36.68           C  
ANISOU 5079  CA  ARG L  60     5192   5630   3114  -1073    889    209       C  
ATOM   5080  C   ARG L  60      88.599  -0.186  17.145  1.00 39.60           C  
ANISOU 5080  C   ARG L  60     5310   6127   3609   -935    878    143       C  
ATOM   5081  O   ARG L  60      89.295   0.510  17.894  1.00 35.69           O  
ANISOU 5081  O   ARG L  60     4802   5658   3101   -782    877    105       O  
ATOM   5082  CB  ARG L  60      89.406  -2.508  16.673  1.00 32.09           C  
ANISOU 5082  CB  ARG L  60     4819   4877   2499  -1035    816    238       C  
ATOM   5083  CG  ARG L  60      89.056  -3.982  16.570  1.00 49.77           C  
ANISOU 5083  CG  ARG L  60     7283   6969   4656  -1191    817    293       C  
ATOM   5084  CD  ARG L  60      90.104  -4.735  15.765  1.00 51.63           C  
ANISOU 5084  CD  ARG L  60     7718   7023   4876  -1127    744    309       C  
ATOM   5085  NE  ARG L  60      90.282  -4.171  14.429  1.00 43.14           N  
ANISOU 5085  NE  ARG L  60     6495   5984   3911  -1112    710    275       N  
ATOM   5086  CZ  ARG L  60      89.685  -4.633  13.335  1.00 35.46           C  
ANISOU 5086  CZ  ARG L  60     5504   4988   2983  -1261    701    279       C  
ATOM   5087  NH1 ARG L  60      88.868  -5.675  13.411  1.00 43.44           N  
ANISOU 5087  NH1 ARG L  60     6628   5938   3937  -1441    725    305       N  
ATOM   5088  NH2 ARG L  60      89.908  -4.057  12.162  1.00 36.25           N  
ANISOU 5088  NH2 ARG L  60     5475   5123   3174  -1235    665    250       N  
ATOM   5089  N   PHE L  61      88.004   0.310  16.064  1.00 30.65           N  
ANISOU 5089  N   PHE L  61     3981   5067   2596   -983    861    125       N  
ATOM   5090  CA  PHE L  61      88.164   1.703  15.675  1.00 35.28           C  
ANISOU 5090  CA  PHE L  61     4339   5749   3318   -846    839     66       C  
ATOM   5091  C   PHE L  61      87.339   2.602  16.586  1.00 38.12           C  
ANISOU 5091  C   PHE L  61     4531   6229   3724   -813    893     28       C  
ATOM   5092  O   PHE L  61      86.138   2.380  16.774  1.00 37.50           O  
ANISOU 5092  O   PHE L  61     4385   6221   3641   -938    935     40       O  
ATOM   5093  CB  PHE L  61      87.751   1.900  14.217  1.00 21.87           C  
ANISOU 5093  CB  PHE L  61     2511   4076   1723   -900    789     68       C  
ATOM   5094  CG  PHE L  61      88.575   1.108  13.243  1.00 33.74           C  
ANISOU 5094  CG  PHE L  61     4175   5455   3190   -930    740     96       C  
ATOM   5095  CD1 PHE L  61      89.711   1.657  12.670  1.00 25.35           C  
ANISOU 5095  CD1 PHE L  61     3103   4354   2175   -790    699     61       C  
ATOM   5096  CD2 PHE L  61      88.216  -0.186  12.902  1.00 29.52           C  
ANISOU 5096  CD2 PHE L  61     3808   4831   2578  -1095    737    146       C  
ATOM   5097  CE1 PHE L  61      90.472   0.930  11.773  1.00 19.29           C  
ANISOU 5097  CE1 PHE L  61     2492   3467   1372   -813    660     77       C  
ATOM   5098  CE2 PHE L  61      88.974  -0.917  12.006  1.00 23.49           C  
ANISOU 5098  CE2 PHE L  61     3210   3929   1788  -1111    691    164       C  
ATOM   5099  CZ  PHE L  61      90.103  -0.358  11.442  1.00 20.29           C  
ANISOU 5099  CZ  PHE L  61     2796   3489   1424   -969    655    131       C  
ATOM   5100  N   SER L  62      87.987   3.616  17.154  1.00 22.32           N  
ANISOU 5100  N   SER L  62     2469   4244   1767   -643    890    -26       N  
ATOM   5101  CA  SER L  62      87.319   4.583  18.008  1.00 22.91           C  
ANISOU 5101  CA  SER L  62     2404   4404   1896   -589    936    -70       C  
ATOM   5102  C   SER L  62      87.911   5.961  17.756  1.00 26.98           C  
ANISOU 5102  C   SER L  62     2797   4909   2547   -408    886   -133       C  
ATOM   5103  O   SER L  62      89.109   6.092  17.503  1.00 20.43           O  
ANISOU 5103  O   SER L  62     2029   4010   1724   -309    837   -155       O  
ATOM   5104  CB  SER L  62      87.453   4.214  19.491  1.00 36.47           C  
ANISOU 5104  CB  SER L  62     4261   6117   3481   -596   1000    -68       C  
ATOM   5105  OG  SER L  62      88.813   4.090  19.867  1.00 35.34           O  
ANISOU 5105  OG  SER L  62     4269   5895   3264   -482    962    -81       O  
ATOM   5106  N   GLY L  63      87.063   6.981  17.818  1.00 28.21           N  
ANISOU 5106  N   GLY L  63     2793   5117   2809   -365    898   -162       N  
ATOM   5107  CA  GLY L  63      87.491   8.352  17.635  1.00 21.03           C  
ANISOU 5107  CA  GLY L  63     1802   4160   2028   -208    852   -212       C  
ATOM   5108  C   GLY L  63      87.206   9.166  18.881  1.00 25.93           C  
ANISOU 5108  C   GLY L  63     2395   4801   2655   -144    908   -256       C  
ATOM   5109  O   GLY L  63      86.212   8.940  19.572  1.00 36.52           O  
ANISOU 5109  O   GLY L  63     3702   6223   3951   -217    982   -250       O  
ATOM   5110  N   SER L  64      88.092  10.115  19.167  1.00 40.48           N  
ANISOU 5110  N   SER L  64     4259   6567   4554    -18    876   -304       N  
ATOM   5111  CA  SER L  64      87.945  10.949  20.349  1.00 31.51           C  
ANISOU 5111  CA  SER L  64     3114   5437   3422     42    927   -349       C  
ATOM   5112  C   SER L  64      88.541  12.321  20.064  1.00 34.01           C  
ANISOU 5112  C   SER L  64     3409   5651   3861    160    876   -387       C  
ATOM   5113  O   SER L  64      89.070  12.580  18.979  1.00 26.59           O  
ANISOU 5113  O   SER L  64     2469   4638   2997    191    805   -376       O  
ATOM   5114  CB  SER L  64      88.601  10.291  21.567  1.00 49.54           C  
ANISOU 5114  CB  SER L  64     5524   7739   5559     26    963   -365       C  
ATOM   5115  OG  SER L  64      89.942   9.933  21.286  1.00 77.02           O  
ANISOU 5115  OG  SER L  64     9100  11157   9008     73    892   -375       O  
ATOM   5116  N   GLY L  65      88.447  13.201  21.050  1.00 37.89           N  
ANISOU 5116  N   GLY L  65     3896   6135   4365    214    921   -429       N  
ATOM   5117  CA  GLY L  65      88.981  14.543  20.952  1.00 29.01           C  
ANISOU 5117  CA  GLY L  65     2773   4908   3339    306    892   -461       C  
ATOM   5118  C   GLY L  65      87.890  15.598  21.009  1.00 29.03           C  
ANISOU 5118  C   GLY L  65     2685   4915   3429    345    949   -464       C  
ATOM   5119  O   GLY L  65      86.697  15.317  20.910  1.00 43.40           O  
ANISOU 5119  O   GLY L  65     4417   6819   5255    307    995   -442       O  
ATOM   5120  N   SER L  66      88.343  16.836  21.180  1.00 22.99           N  
ANISOU 5120  N   SER L  66     1930   4087   2717    421    942   -506       N  
ATOM   5121  CA  SER L  66      87.464  17.997  21.202  1.00 31.19           C  
ANISOU 5121  CA  SER L  66     2882   5139   3830    483    992   -526       C  
ATOM   5122  C   SER L  66      88.316  19.239  20.967  1.00 43.43           C  
ANISOU 5122  C   SER L  66     4472   6597   5432    555    958   -563       C  
ATOM   5123  O   SER L  66      89.546  19.166  20.875  1.00 55.69           O  
ANISOU 5123  O   SER L  66     6106   8093   6960    548    898   -578       O  
ATOM   5124  CB  SER L  66      86.684  18.084  22.518  1.00 27.02           C  
ANISOU 5124  CB  SER L  66     2326   4686   3254    482   1097   -558       C  
ATOM   5125  OG  SER L  66      87.560  18.185  23.628  1.00 38.08           O  
ANISOU 5125  OG  SER L  66     3824   6067   4579    490   1113   -604       O  
ATOM   5126  N   GLY L  67      87.644  20.385  20.866  1.00 25.10           N  
ANISOU 5126  N   GLY L  67     2089   4264   3185    626   1003   -579       N  
ATOM   5127  CA  GLY L  67      88.317  21.650  20.654  1.00 31.29           C  
ANISOU 5127  CA  GLY L  67     2914   4957   4017    693    994   -612       C  
ATOM   5128  C   GLY L  67      89.189  21.670  19.416  1.00 35.00           C  
ANISOU 5128  C   GLY L  67     3428   5349   4520    682    909   -585       C  
ATOM   5129  O   GLY L  67      88.687  21.797  18.295  1.00 31.64           O  
ANISOU 5129  O   GLY L  67     2954   4907   4160    698    887   -542       O  
ATOM   5130  N   THR L  68      90.505  21.539  19.610  1.00 33.45           N  
ANISOU 5130  N   THR L  68     3320   5112   4277    655    860   -613       N  
ATOM   5131  CA  THR L  68      91.458  21.543  18.506  1.00 34.21           C  
ANISOU 5131  CA  THR L  68     3462   5139   4397    637    788   -597       C  
ATOM   5132  C   THR L  68      92.362  20.315  18.524  1.00 37.88           C  
ANISOU 5132  C   THR L  68     3974   5621   4797    571    722   -593       C  
ATOM   5133  O   THR L  68      93.426  20.331  17.897  1.00 38.58           O  
ANISOU 5133  O   THR L  68     4109   5659   4892    555    665   -602       O  
ATOM   5134  CB  THR L  68      92.316  22.813  18.526  1.00 20.23           C  
ANISOU 5134  CB  THR L  68     1745   3292   2650    678    795   -646       C  
ATOM   5135  OG1 THR L  68      93.012  22.901  19.775  1.00 28.78           O  
ANISOU 5135  OG1 THR L  68     2869   4395   3671    667    803   -712       O  
ATOM   5136  CG2 THR L  68      91.453  24.051  18.346  1.00 21.38           C  
ANISOU 5136  CG2 THR L  68     1856   3403   2866    759    867   -643       C  
ATOM   5137  N   SER L  69      91.970  19.253  19.228  1.00 38.88           N  
ANISOU 5137  N   SER L  69     4093   5818   4863    536    736   -580       N  
ATOM   5138  CA  SER L  69      92.785  18.045  19.309  1.00 26.56           C  
ANISOU 5138  CA  SER L  69     2583   4269   3238    489    685   -574       C  
ATOM   5139  C   SER L  69      91.879  16.828  19.244  1.00 34.36           C  
ANISOU 5139  C   SER L  69     3545   5317   4193    443    709   -519       C  
ATOM   5140  O   SER L  69      91.028  16.639  20.117  1.00 31.04           O  
ANISOU 5140  O   SER L  69     3098   4960   3736    434    775   -519       O  
ATOM   5141  CB  SER L  69      93.623  18.021  20.591  1.00 36.18           C  
ANISOU 5141  CB  SER L  69     3854   5507   4387    496    684   -632       C  
ATOM   5142  OG  SER L  69      94.625  19.023  20.565  1.00 57.05           O  
ANISOU 5142  OG  SER L  69     6519   8100   7057    521    652   -687       O  
ATOM   5143  N   TYR L  70      92.067  16.005  18.216  1.00 43.43           N  
ANISOU 5143  N   TYR L  70     4705   6448   5350    407    663   -476       N  
ATOM   5144  CA  TYR L  70      91.291  14.790  18.023  1.00 44.60           C  
ANISOU 5144  CA  TYR L  70     4832   6654   5459    349    685   -427       C  
ATOM   5145  C   TYR L  70      92.247  13.631  17.778  1.00 16.74           C  
ANISOU 5145  C   TYR L  70     1365   3134   1861    321    636   -428       C  
ATOM   5146  O   TYR L  70      93.452  13.823  17.604  1.00 38.60           O  
ANISOU 5146  O   TYR L  70     4187   5835   4644    351    585   -455       O  
ATOM   5147  CB  TYR L  70      90.298  14.946  16.863  1.00 45.91           C  
ANISOU 5147  CB  TYR L  70     4923   6825   5697    333    682   -380       C  
ATOM   5148  CG  TYR L  70      89.351  16.113  17.041  1.00 18.69           C  
ANISOU 5148  CG  TYR L  70     1393   3399   2308    381    724   -393       C  
ATOM   5149  CD1 TYR L  70      88.082  15.927  17.571  1.00 19.92           C  
ANISOU 5149  CD1 TYR L  70     1470   3643   2455    361    787   -382       C  
ATOM   5150  CD2 TYR L  70      89.732  17.402  16.692  1.00 41.50           C  
ANISOU 5150  CD2 TYR L  70     4285   6224   5261    448    709   -419       C  
ATOM   5151  CE1 TYR L  70      87.216  16.990  17.739  1.00 21.11           C  
ANISOU 5151  CE1 TYR L  70     1538   3818   2667    419    829   -400       C  
ATOM   5152  CE2 TYR L  70      88.873  18.471  16.858  1.00 48.93           C  
ANISOU 5152  CE2 TYR L  70     5156   7177   6259    506    756   -431       C  
ATOM   5153  CZ  TYR L  70      87.616  18.258  17.382  1.00 21.05           C  
ANISOU 5153  CZ  TYR L  70     1538   3735   2724    498    814   -423       C  
ATOM   5154  OH  TYR L  70      86.757  19.319  17.549  1.00 71.17           O  
ANISOU 5154  OH  TYR L  70     7808  10098   9136    568    864   -441       O  
ATOM   5155  N   SER L  71      91.707  12.414  17.772  1.00 17.84           N  
ANISOU 5155  N   SER L  71     1496   3363   1918    260    658   -400       N  
ATOM   5156  CA  SER L  71      92.558  11.238  17.652  1.00 16.72           C  
ANISOU 5156  CA  SER L  71     1427   3236   1691    242    630   -399       C  
ATOM   5157  C   SER L  71      91.732  10.028  17.242  1.00 43.14           C  
ANISOU 5157  C   SER L  71     4765   6665   4962    145    665   -345       C  
ATOM   5158  O   SER L  71      90.570   9.883  17.636  1.00 18.21           O  
ANISOU 5158  O   SER L  71     1560   3583   1777     81    723   -318       O  
ATOM   5159  CB  SER L  71      93.293  10.951  18.966  1.00 17.18           C  
ANISOU 5159  CB  SER L  71     1559   3320   1648    277    638   -442       C  
ATOM   5160  OG  SER L  71      92.383  10.868  20.049  1.00 18.38           O  
ANISOU 5160  OG  SER L  71     1705   3551   1728    242    716   -437       O  
ATOM   5161  N   LEU L  72      92.357   9.161  16.449  1.00 45.15           N  
ANISOU 5161  N   LEU L  72     5073   6902   5182    124    633   -329       N  
ATOM   5162  CA  LEU L  72      91.804   7.870  16.067  1.00 36.52           C  
ANISOU 5162  CA  LEU L  72     4019   5868   3989      8    666   -271       C  
ATOM   5163  C   LEU L  72      92.618   6.766  16.727  1.00 17.42           C  
ANISOU 5163  C   LEU L  72     1762   3444   1414      9    677   -269       C  
ATOM   5164  O   LEU L  72      93.844   6.871  16.841  1.00 16.85           O  
ANISOU 5164  O   LEU L  72     1744   3316   1341    118    626   -319       O  
ATOM   5165  CB  LEU L  72      91.814   7.694  14.545  1.00 19.02           C  
ANISOU 5165  CB  LEU L  72     1771   3622   1833    -30    626   -245       C  
ATOM   5166  CG  LEU L  72      91.264   6.381  13.982  1.00 16.92           C  
ANISOU 5166  CG  LEU L  72     1564   3396   1469   -182    653   -178       C  
ATOM   5167  CD1 LEU L  72      89.769   6.265  14.243  1.00 18.11           C  
ANISOU 5167  CD1 LEU L  72     1640   3630   1610   -298    695   -135       C  
ATOM   5168  CD2 LEU L  72      91.565   6.267  12.498  1.00 16.12           C  
ANISOU 5168  CD2 LEU L  72     1451   3254   1421   -206    608   -167       C  
ATOM   5169  N   THR L  73      91.937   5.708  17.163  1.00 18.51           N  
ANISOU 5169  N   THR L  73     1996   3620   1417   -113    731   -208       N  
ATOM   5170  CA  THR L  73      92.580   4.635  17.914  1.00 28.04           C  
ANISOU 5170  CA  THR L  73     3417   4790   2446   -114    731   -186       C  
ATOM   5171  C   THR L  73      92.038   3.292  17.454  1.00 19.91           C  
ANISOU 5171  C   THR L  73     2532   3722   1312   -280    751    -97       C  
ATOM   5172  O   THR L  73      90.824   3.068  17.474  1.00 64.98           O  
ANISOU 5172  O   THR L  73     8193   9471   7026   -422    805    -52       O  
ATOM   5173  CB  THR L  73      92.360   4.806  19.422  1.00 20.21           C  
ANISOU 5173  CB  THR L  73     2474   3833   1373    -98    774   -198       C  
ATOM   5174  OG1 THR L  73      92.969   6.026  19.862  1.00 19.60           O  
ANISOU 5174  OG1 THR L  73     2291   3763   1393     43    742   -282       O  
ATOM   5175  CG2 THR L  73      92.971   3.641  20.185  1.00 21.13           C  
ANISOU 5175  CG2 THR L  73     2849   3889   1290    -98    754   -158       C  
ATOM   5176  N   ILE L  74      92.939   2.410  17.038  1.00 19.73           N  
ANISOU 5176  N   ILE L  74     2689   3586   1221   -253    692    -78       N  
ATOM   5177  CA  ILE L  74      92.638   1.002  16.819  1.00 20.70           C  
ANISOU 5177  CA  ILE L  74     3030   3604   1231   -396    697      9       C  
ATOM   5178  C   ILE L  74      93.096   0.257  18.067  1.00 33.38           C  
ANISOU 5178  C   ILE L  74     4876   5139   2669   -354    686     38       C  
ATOM   5179  O   ILE L  74      94.296   0.202  18.362  1.00 27.99           O  
ANISOU 5179  O   ILE L  74     4284   4373   1976   -175    599      5       O  
ATOM   5180  CB  ILE L  74      93.326   0.462  15.559  1.00 45.76           C  
ANISOU 5180  CB  ILE L  74     6279   6641   4467   -371    622     14       C  
ATOM   5181  CG1 ILE L  74      93.045   1.376  14.364  1.00 46.89           C  
ANISOU 5181  CG1 ILE L  74     6189   6854   4771   -381    618    -23       C  
ATOM   5182  CG2 ILE L  74      92.861  -0.955  15.267  1.00 48.92           C  
ANISOU 5182  CG2 ILE L  74     6906   6930   4751   -543    641    100       C  
ATOM   5183  CD1 ILE L  74      93.793   0.986  13.107  1.00 18.06           C  
ANISOU 5183  CD1 ILE L  74     2601   3077   1183   -350    553    -32       C  
ATOM   5184  N   SER L  75      92.139  -0.306  18.810  1.00 45.79           N  
ANISOU 5184  N   SER L  75     5591   7791   4018   -694   -590   1086       N  
ATOM   5185  CA  SER L  75      92.463  -0.934  20.088  1.00 31.62           C  
ANISOU 5185  CA  SER L  75     3991   6013   2009   -531   -542   1172       C  
ATOM   5186  C   SER L  75      93.378  -2.139  19.903  1.00 58.57           C  
ANISOU 5186  C   SER L  75     7733   9202   5320   -332   -646   1225       C  
ATOM   5187  O   SER L  75      94.351  -2.309  20.648  1.00 52.56           O  
ANISOU 5187  O   SER L  75     7077   8472   4423    -63   -688   1157       O  
ATOM   5188  CB  SER L  75      91.179  -1.341  20.812  1.00 33.60           C  
ANISOU 5188  CB  SER L  75     4303   6281   2183   -755   -391   1395       C  
ATOM   5189  OG  SER L  75      90.411  -2.238  20.027  1.00 34.29           O  
ANISOU 5189  OG  SER L  75     4543   6131   2357  -1009   -392   1572       O  
ATOM   5190  N   ARG L  76      93.084  -2.986  18.919  1.00 60.58           N  
ANISOU 5190  N   ARG L  76     8160   9223   5636   -460   -705   1335       N  
ATOM   5191  CA  ARG L  76      93.898  -4.161  18.622  1.00 34.76           C  
ANISOU 5191  CA  ARG L  76     5213   5727   2269   -262   -812   1383       C  
ATOM   5192  C   ARG L  76      94.206  -4.158  17.131  1.00 43.35           C  
ANISOU 5192  C   ARG L  76     6259   6702   3508   -287   -928   1268       C  
ATOM   5193  O   ARG L  76      93.296  -4.297  16.307  1.00 41.56           O  
ANISOU 5193  O   ARG L  76     6033   6351   3407   -567   -942   1338       O  
ATOM   5194  CB  ARG L  76      93.187  -5.449  19.037  1.00 37.27           C  
ANISOU 5194  CB  ARG L  76     5871   5796   2493   -393   -753   1661       C  
ATOM   5195  CG  ARG L  76      94.115  -6.640  19.190  1.00 52.79           C  
ANISOU 5195  CG  ARG L  76     8186   7567   4306    -98   -835   1729       C  
ATOM   5196  CD  ARG L  76      93.404  -7.822  19.826  1.00 57.83           C  
ANISOU 5196  CD  ARG L  76     9152   7945   4877   -222   -732   2010       C  
ATOM   5197  NE  ARG L  76      94.344  -8.859  20.243  1.00 63.26           N  
ANISOU 5197  NE  ARG L  76    10100   8517   5418     94   -793   2090       N  
ATOM   5198  CZ  ARG L  76      94.931  -8.897  21.434  1.00 73.41           C  
ANISOU 5198  CZ  ARG L  76    11363  10018   6513    314   -772   2155       C  
ATOM   5199  NH1 ARG L  76      95.776  -9.876  21.729  1.00 82.08           N  
ANISOU 5199  NH1 ARG L  76    12689  10967   7532    524   -868   2202       N  
ATOM   5200  NH2 ARG L  76      94.675  -7.956  22.333  1.00 75.21           N  
ANISOU 5200  NH2 ARG L  76    11361  10574   6642    304   -674   2136       N  
ATOM   5201  N   MET L  77      95.483  -3.998  16.791  1.00 58.06           N  
ANISOU 5201  N   MET L  77     8096   8607   5357      0  -1015   1081       N  
ATOM   5202  CA  MET L  77      95.892  -3.901  15.395  1.00 50.90           C  
ANISOU 5202  CA  MET L  77     7132   7633   4576     19  -1095    951       C  
ATOM   5203  C   MET L  77      95.607  -5.199  14.651  1.00 53.93           C  
ANISOU 5203  C   MET L  77     7822   7736   4932    -40  -1181   1081       C  
ATOM   5204  O   MET L  77      95.912  -6.292  15.138  1.00 67.89           O  
ANISOU 5204  O   MET L  77     9876   9349   6568     98  -1211   1197       O  
ATOM   5205  CB  MET L  77      97.381  -3.562  15.311  1.00 47.33           C  
ANISOU 5205  CB  MET L  77     6615   7240   4127    272  -1163    751       C  
ATOM   5206  CG  MET L  77      97.972  -3.636  13.912  1.00 45.84           C  
ANISOU 5206  CG  MET L  77     6409   6978   4031    300  -1234    649       C  
ATOM   5207  SD  MET L  77      97.438  -2.296  12.834  1.00 43.12           S  
ANISOU 5207  SD  MET L  77     5749   6721   3914    133  -1141    524       S  
ATOM   5208  CE  MET L  77      98.357  -2.681  11.346  1.00 43.76           C  
ANISOU 5208  CE  MET L  77     5903   6709   4014    236  -1224    435       C  
ATOM   5209  N   GLU L  78      95.018  -5.073  13.465  1.00 37.40           N  
ANISOU 5209  N   GLU L  78     5686   5541   2984   -245  -1226   1046       N  
ATOM   5210  CA  GLU L  78      94.784  -6.196  12.572  1.00 32.31           C  
ANISOU 5210  CA  GLU L  78     5348   4583   2346   -310  -1343   1097       C  
ATOM   5211  C   GLU L  78      95.515  -5.956  11.258  1.00 35.69           C  
ANISOU 5211  C   GLU L  78     5686   5043   2831   -158  -1408    899       C  
ATOM   5212  O   GLU L  78      95.793  -4.816  10.877  1.00 37.61           O  
ANISOU 5212  O   GLU L  78     5616   5517   3158   -130  -1344    767       O  
ATOM   5213  CB  GLU L  78      93.286  -6.403  12.314  1.00 40.49           C  
ANISOU 5213  CB  GLU L  78     6397   5447   3541   -690  -1307   1193       C  
ATOM   5214  CG  GLU L  78      92.478  -6.713  13.562  1.00 50.85           C  
ANISOU 5214  CG  GLU L  78     7777   6719   4823   -866  -1184   1394       C  
ATOM   5215  CD  GLU L  78      92.825  -8.062  14.160  1.00 62.90           C  
ANISOU 5215  CD  GLU L  78     9721   7971   6209   -749  -1206   1549       C  
ATOM   5216  OE1 GLU L  78      93.159  -8.986  13.389  1.00 67.38           O  
ANISOU 5216  OE1 GLU L  78    10557   8260   6784   -670  -1325   1512       O  
ATOM   5217  OE2 GLU L  78      92.767  -8.197  15.401  1.00 74.97           O  
ANISOU 5217  OE2 GLU L  78    11325   9556   7605   -720  -1103   1709       O  
ATOM   5218  N   ALA L  79      95.826  -7.053  10.561  1.00 42.30           N  
ANISOU 5218  N   ALA L  79     6821   5627   3623    -53  -1520    880       N  
ATOM   5219  CA  ALA L  79      96.550  -6.940   9.299  1.00 32.00           C  
ANISOU 5219  CA  ALA L  79     5450   4364   2345    109  -1562    697       C  
ATOM   5220  C   ALA L  79      95.726  -6.227   8.235  1.00 36.27           C  
ANISOU 5220  C   ALA L  79     5826   4942   3014   -122  -1573    638       C  
ATOM   5221  O   ALA L  79      96.293  -5.640   7.306  1.00 41.97           O  
ANISOU 5221  O   ALA L  79     6372   5811   3762     -8  -1536    501       O  
ATOM   5222  CB  ALA L  79      96.969  -8.324   8.807  1.00 34.45           C  
ANISOU 5222  CB  ALA L  79     6143   4374   2574    280  -1686    674       C  
ATOM   5223  N   GLU L  80      94.398  -6.262   8.349  1.00 37.65           N  
ANISOU 5223  N   GLU L  80     6024   5003   3277   -447  -1598    744       N  
ATOM   5224  CA  GLU L  80      93.531  -5.577   7.399  1.00 35.24           C  
ANISOU 5224  CA  GLU L  80     5529   4755   3104   -655  -1612    685       C  
ATOM   5225  C   GLU L  80      93.439  -4.078   7.651  1.00 35.40           C  
ANISOU 5225  C   GLU L  80     5166   5066   3218   -683  -1466    658       C  
ATOM   5226  O   GLU L  80      92.830  -3.368   6.845  1.00 26.33           O  
ANISOU 5226  O   GLU L  80     3845   3972   2188   -785  -1446    601       O  
ATOM   5227  CB  GLU L  80      92.126  -6.186   7.437  1.00 38.60           C  
ANISOU 5227  CB  GLU L  80     6042   4967   3656   -979  -1644    764       C  
ATOM   5228  CG  GLU L  80      92.079  -7.666   7.097  1.00 67.17           C  
ANISOU 5228  CG  GLU L  80    10041   8227   7254   -987  -1760    760       C  
ATOM   5229  CD  GLU L  80      90.666  -8.218   7.092  1.00 90.39           C  
ANISOU 5229  CD  GLU L  80    13028  10961  10355  -1356  -1786    820       C  
ATOM   5230  OE1 GLU L  80      89.737  -7.476   7.475  1.00 99.67           O  
ANISOU 5230  OE1 GLU L  80    13928  12300  11643  -1586  -1701    878       O  
ATOM   5231  OE2 GLU L  80      90.485  -9.392   6.704  1.00 93.73           O  
ANISOU 5231  OE2 GLU L  80    13754  11058  10801  -1419  -1891    795       O  
ATOM   5232  N   ASP L  81      94.027  -3.582   8.738  1.00 26.58           N  
ANISOU 5232  N   ASP L  81     3926   4108   2067   -566  -1355    677       N  
ATOM   5233  CA  ASP L  81      93.921  -2.172   9.083  1.00 24.73           C  
ANISOU 5233  CA  ASP L  81     3369   4082   1946   -591  -1214    628       C  
ATOM   5234  C   ASP L  81      94.987  -1.309   8.424  1.00 30.44           C  
ANISOU 5234  C   ASP L  81     3949   4909   2707   -383  -1146    476       C  
ATOM   5235  O   ASP L  81      94.797  -0.092   8.319  1.00 27.33           O  
ANISOU 5235  O   ASP L  81     3339   4604   2441   -439  -1045    436       O  
ATOM   5236  CB  ASP L  81      94.003  -1.995  10.602  1.00 24.95           C  
ANISOU 5236  CB  ASP L  81     3343   4222   1915   -580  -1141    698       C  
ATOM   5237  CG  ASP L  81      92.969  -2.818  11.342  1.00 34.35           C  
ANISOU 5237  CG  ASP L  81     4694   5321   3038   -807  -1184    892       C  
ATOM   5238  OD1 ASP L  81      91.928  -3.153  10.736  1.00 35.26           O  
ANISOU 5238  OD1 ASP L  81     4849   5299   3248  -1036  -1229    938       O  
ATOM   5239  OD2 ASP L  81      93.196  -3.129  12.530  1.00 37.06           O  
ANISOU 5239  OD2 ASP L  81     5118   5702   3260   -740  -1138    980       O  
ATOM   5240  N   ALA L  82      96.093  -1.904   7.979  1.00 44.04           N  
ANISOU 5240  N   ALA L  82     5804   6614   4317   -158  -1203    405       N  
ATOM   5241  CA  ALA L  82      97.198  -1.148   7.399  1.00 34.39           C  
ANISOU 5241  CA  ALA L  82     4470   5472   3124    -16  -1155    291       C  
ATOM   5242  C   ALA L  82      96.757  -0.385   6.156  1.00 39.64           C  
ANISOU 5242  C   ALA L  82     5035   6141   3884   -104  -1113    266       C  
ATOM   5243  O   ALA L  82      96.555  -0.980   5.092  1.00 42.86           O  
ANISOU 5243  O   ALA L  82     5580   6477   4228    -73  -1193    248       O  
ATOM   5244  CB  ALA L  82      98.365  -2.080   7.067  1.00 27.12           C  
ANISOU 5244  CB  ALA L  82     3732   4507   2067    155  -1248    265       C  
ATOM   5245  N   ALA L  83      96.609   0.929   6.283  1.00 33.45           N  
ANISOU 5245  N   ALA L  83     4028   5450   3232   -197   -991    265       N  
ATOM   5246  CA  ALA L  83      96.164   1.773   5.182  1.00 28.23           C  
ANISOU 5246  CA  ALA L  83     3285   4796   2643   -268   -946    271       C  
ATOM   5247  C   ALA L  83      96.549   3.216   5.502  1.00 19.60           C  
ANISOU 5247  C   ALA L  83     1967   3829   1650   -306   -805    261       C  
ATOM   5248  O   ALA L  83      97.418   3.463   6.346  1.00 19.56           O  
ANISOU 5248  O   ALA L  83     1870   3918   1644   -249   -750    214       O  
ATOM   5249  CB  ALA L  83      94.654   1.597   4.951  1.00 20.66           C  
ANISOU 5249  CB  ALA L  83     2361   3744   1744   -422   -995    328       C  
ATOM   5250  N   THR L  84      95.906   4.166   4.828  1.00 19.23           N  
ANISOU 5250  N   THR L  84     1844   3785   1679   -392   -757    298       N  
ATOM   5251  CA  THR L  84      96.106   5.589   5.068  1.00 28.10           C  
ANISOU 5251  CA  THR L  84     2793   4991   2893   -439   -636    298       C  
ATOM   5252  C   THR L  84      94.834   6.170   5.672  1.00 38.83           C  
ANISOU 5252  C   THR L  84     4122   6272   4361   -535   -608    330       C  
ATOM   5253  O   THR L  84      93.736   5.927   5.162  1.00 40.07           O  
ANISOU 5253  O   THR L  84     4336   6355   4534   -588   -666    377       O  
ATOM   5254  CB  THR L  84      96.464   6.324   3.774  1.00 18.82           C  
ANISOU 5254  CB  THR L  84     1566   3897   1688   -435   -605    334       C  
ATOM   5255  OG1 THR L  84      97.638   5.736   3.199  1.00 58.89           O  
ANISOU 5255  OG1 THR L  84     6663   9081   6632   -323   -617    296       O  
ATOM   5256  CG2 THR L  84      96.729   7.794   4.051  1.00 18.59           C  
ANISOU 5256  CG2 THR L  84     1375   3927   1763   -492   -490    334       C  
ATOM   5257  N   PHE L  85      94.983   6.932   6.752  1.00 17.65           N  
ANISOU 5257  N   PHE L  85     1353   3608   1744   -540   -528    287       N  
ATOM   5258  CA  PHE L  85      93.852   7.449   7.510  1.00 17.41           C  
ANISOU 5258  CA  PHE L  85     1302   3518   1794   -591   -501    294       C  
ATOM   5259  C   PHE L  85      93.831   8.969   7.442  1.00 25.43           C  
ANISOU 5259  C   PHE L  85     2238   4501   2922   -585   -433    259       C  
ATOM   5260  O   PHE L  85      94.853   9.620   7.683  1.00 17.34           O  
ANISOU 5260  O   PHE L  85     1154   3503   1933   -556   -383    195       O  
ATOM   5261  CB  PHE L  85      93.917   6.978   8.964  1.00 17.54           C  
ANISOU 5261  CB  PHE L  85     1311   3579   1774   -585   -490    265       C  
ATOM   5262  CG  PHE L  85      93.897   5.486   9.110  1.00 18.08           C  
ANISOU 5262  CG  PHE L  85     1465   3667   1737   -599   -575    315       C  
ATOM   5263  CD1 PHE L  85      92.698   4.808   9.241  1.00 21.18           C  
ANISOU 5263  CD1 PHE L  85     1903   4025   2120   -703   -621    394       C  
ATOM   5264  CD2 PHE L  85      95.075   4.759   9.102  1.00 32.86           C  
ANISOU 5264  CD2 PHE L  85     3381   5584   3521   -505   -621    281       C  
ATOM   5265  CE1 PHE L  85      92.673   3.434   9.368  1.00 19.42           C  
ANISOU 5265  CE1 PHE L  85     1789   3789   1800   -740   -721    451       C  
ATOM   5266  CE2 PHE L  85      95.056   3.383   9.229  1.00 34.25           C  
ANISOU 5266  CE2 PHE L  85     3692   5731   3592   -486   -726    324       C  
ATOM   5267  CZ  PHE L  85      93.853   2.721   9.362  1.00 32.36           C  
ANISOU 5267  CZ  PHE L  85     3520   5435   3341   -615   -779    416       C  
ATOM   5268  N   TYR L  86      92.666   9.527   7.119  1.00 27.77           N  
ANISOU 5268  N   TYR L  86     2527   4737   3289   -613   -444    293       N  
ATOM   5269  CA  TYR L  86      92.479  10.965   7.018  1.00 17.51           C  
ANISOU 5269  CA  TYR L  86     1151   3389   2112   -605   -402    266       C  
ATOM   5270  C   TYR L  86      91.476  11.440   8.059  1.00 17.62           C  
ANISOU 5270  C   TYR L  86     1126   3357   2212   -599   -386    215       C  
ATOM   5271  O   TYR L  86      90.544  10.717   8.425  1.00 38.45           O  
ANISOU 5271  O   TYR L  86     3789   6010   4811   -621   -415    239       O  
ATOM   5272  CB  TYR L  86      91.981  11.374   5.627  1.00 17.95           C  
ANISOU 5272  CB  TYR L  86     1199   3452   2171   -626   -442    360       C  
ATOM   5273  CG  TYR L  86      92.900  10.995   4.491  1.00 18.18           C  
ANISOU 5273  CG  TYR L  86     1247   3563   2097   -636   -459    433       C  
ATOM   5274  CD1 TYR L  86      94.003  11.775   4.175  1.00 43.10           C  
ANISOU 5274  CD1 TYR L  86     4327   6766   5284   -646   -387    437       C  
ATOM   5275  CD2 TYR L  86      92.654   9.868   3.721  1.00 18.32           C  
ANISOU 5275  CD2 TYR L  86     1348   3612   1999   -638   -546    486       C  
ATOM   5276  CE1 TYR L  86      94.843  11.436   3.132  1.00 19.07           C  
ANISOU 5276  CE1 TYR L  86     1269   3847   2132   -655   -387    513       C  
ATOM   5277  CE2 TYR L  86      93.486   9.521   2.677  1.00 35.34           C  
ANISOU 5277  CE2 TYR L  86     3523   5862   4041   -623   -572    538       C  
ATOM   5278  CZ  TYR L  86      94.579  10.309   2.386  1.00 19.13           C  
ANISOU 5278  CZ  TYR L  86     1367   3911   1990   -630   -490    565       C  
ATOM   5279  OH  TYR L  86      95.409   9.965   1.346  1.00 43.44           O  
ANISOU 5279  OH  TYR L  86     4440   7138   4926   -600   -507    625       O  
ATOM   5280  N   CYS L  87      91.676  12.668   8.530  1.00 17.91           N  
ANISOU 5280  N   CYS L  87     1083   3347   2376   -581   -340    146       N  
ATOM   5281  CA  CYS L  87      90.704  13.360   9.362  1.00 18.47           C  
ANISOU 5281  CA  CYS L  87     1082   3405   2531   -576   -330    104       C  
ATOM   5282  C   CYS L  87      90.150  14.554   8.598  1.00 19.04           C  
ANISOU 5282  C   CYS L  87     1076   3414   2744   -568   -333    109       C  
ATOM   5283  O   CYS L  87      90.895  15.280   7.934  1.00 26.73           O  
ANISOU 5283  O   CYS L  87     2014   4366   3775   -587   -305    122       O  
ATOM   5284  CB  CYS L  87      91.315  13.819  10.691  1.00 18.83           C  
ANISOU 5284  CB  CYS L  87     1075   3477   2602   -566   -289     17       C  
ATOM   5285  SG  CYS L  87      92.814  14.828  10.570  1.00 95.43           S  
ANISOU 5285  SG  CYS L  87    10719  13116  12425   -570   -250    -47       S  
ATOM   5286  N   GLN L  88      88.835  14.740   8.681  1.00 40.66           N  
ANISOU 5286  N   GLN L  88     3766   6163   5520   -555   -364    115       N  
ATOM   5287  CA  GLN L  88      88.140  15.827   8.007  1.00 20.56           C  
ANISOU 5287  CA  GLN L  88     1119   3617   3076   -539   -389    136       C  
ATOM   5288  C   GLN L  88      87.278  16.557   9.022  1.00 21.39           C  
ANISOU 5288  C   GLN L  88     1109   3713   3307   -504   -376     54       C  
ATOM   5289  O   GLN L  88      86.466  15.937   9.713  1.00 21.46           O  
ANISOU 5289  O   GLN L  88     1119   3757   3278   -500   -384     43       O  
ATOM   5290  CB  GLN L  88      87.276  15.308   6.855  1.00 36.22           C  
ANISOU 5290  CB  GLN L  88     3128   5659   4977   -536   -477    244       C  
ATOM   5291  CG  GLN L  88      86.337  16.348   6.269  1.00 44.69           C  
ANISOU 5291  CG  GLN L  88     4076   6766   6137   -487   -537    291       C  
ATOM   5292  CD  GLN L  88      84.882  15.942   6.386  1.00 61.80           C  
ANISOU 5292  CD  GLN L  88     6193   8979   8308   -456   -604    261       C  
ATOM   5293  OE1 GLN L  88      84.571  14.806   6.749  1.00 22.56           O  
ANISOU 5293  OE1 GLN L  88     1286   4013   3272   -499   -601    234       O  
ATOM   5294  NE2 GLN L  88      83.981  16.869   6.082  1.00 61.89           N  
ANISOU 5294  NE2 GLN L  88     6072   9036   8408   -377   -667    275       N  
ATOM   5295  N   GLN L  89      87.455  17.866   9.113  1.00 25.55           N  
ANISOU 5295  N   GLN L  89     1518   4207   3985   -489   -352     11       N  
ATOM   5296  CA  GLN L  89      86.756  18.660  10.108  1.00 23.36           C  
ANISOU 5296  CA  GLN L  89     1111   3924   3842   -449   -345    -41       C  
ATOM   5297  C   GLN L  89      85.528  19.318   9.496  1.00 24.74           C  
ANISOU 5297  C   GLN L  89     1154   4162   4083   -379   -403    -32       C  
ATOM   5298  O   GLN L  89      85.492  19.618   8.300  1.00 36.86           O  
ANISOU 5298  O   GLN L  89     2677   5750   5579   -361   -448     49       O  
ATOM   5299  CB  GLN L  89      87.682  19.728  10.698  1.00 29.89           C  
ANISOU 5299  CB  GLN L  89     1872   4701   4784   -476   -297    -44       C  
ATOM   5300  CG  GLN L  89      88.186  20.771   9.704  1.00 29.59           C  
ANISOU 5300  CG  GLN L  89     1774   4610   4861   -502   -269    -42       C  
ATOM   5301  CD  GLN L  89      87.245  21.954   9.552  1.00 38.20           C  
ANISOU 5301  CD  GLN L  89     2665   5911   5937   -457   -282    -38       C  
ATOM   5302  OE1 GLN L  89      86.478  22.275  10.461  1.00 42.14           O  
ANISOU 5302  OE1 GLN L  89     3091   6431   6491   -376   -294    -75       O  
ATOM   5303  NE2 GLN L  89      87.298  22.606   8.396  1.00 27.78           N  
ANISOU 5303  NE2 GLN L  89     1313   4372   4872   -424   -305     85       N  
ATOM   5304  N   TRP L  90      84.517  19.541  10.331  1.00 50.42           N  
ANISOU 5304  N   TRP L  90     4308   7450   7399   -329   -411    -41       N  
ATOM   5305  CA  TRP L  90      83.447  20.473   9.999  1.00 27.51           C  
ANISOU 5305  CA  TRP L  90     1244   4603   4604   -218   -464    -32       C  
ATOM   5306  C   TRP L  90      83.187  21.377  11.192  1.00 28.78           C  
ANISOU 5306  C   TRP L  90     1271   4859   4805   -170   -402    -27       C  
ATOM   5307  O   TRP L  90      82.870  20.889  12.280  1.00 28.70           O  
ANISOU 5307  O   TRP L  90     1283   4911   4709   -190   -348    -92       O  
ATOM   5308  CB  TRP L  90      82.155  19.762   9.590  1.00 46.27           C  
ANISOU 5308  CB  TRP L  90     3597   7060   6925   -185   -540    -20       C  
ATOM   5309  CG  TRP L  90      81.042  20.747   9.354  1.00 51.45           C  
ANISOU 5309  CG  TRP L  90     4066   7781   7703    -32   -608     -7       C  
ATOM   5310  CD1 TRP L  90      80.791  21.444   8.206  1.00 31.42           C  
ANISOU 5310  CD1 TRP L  90     1463   5298   5177    114   -713     17       C  
ATOM   5311  CD2 TRP L  90      80.053  21.170  10.301  1.00 52.64           C  
ANISOU 5311  CD2 TRP L  90     4069   8026   7908     34   -570     -1       C  
ATOM   5312  NE1 TRP L  90      79.700  22.262   8.376  1.00 33.65           N  
ANISOU 5312  NE1 TRP L  90     1591   5609   5588    283   -759     42       N  
ATOM   5313  CE2 TRP L  90      79.229  22.113   9.655  1.00 57.93           C  
ANISOU 5313  CE2 TRP L  90     4589   8754   8669    225   -656     37       C  
ATOM   5314  CE3 TRP L  90      79.781  20.837  11.631  1.00 36.85           C  
ANISOU 5314  CE3 TRP L  90     2056   6110   5836    -15   -463    -58       C  
ATOM   5315  CZ2 TRP L  90      78.153  22.725  10.294  1.00 63.99           C  
ANISOU 5315  CZ2 TRP L  90     5197   9652   9463    366   -627    -15       C  
ATOM   5316  CZ3 TRP L  90      78.714  21.445  12.262  1.00 34.04           C  
ANISOU 5316  CZ3 TRP L  90     1533   5894   5507    104   -432   -117       C  
ATOM   5317  CH2 TRP L  90      77.913  22.378  11.594  1.00 36.08           C  
ANISOU 5317  CH2 TRP L  90     1645   6197   5867    291   -509   -108       C  
ATOM   5318  N   SER L  91      83.335  22.690  10.976  1.00 31.68           N  
ANISOU 5318  N   SER L  91     3073   5324   3641    589    245   -613       N  
ATOM   5319  CA  SER L  91      82.777  23.736  11.829  1.00 48.03           C  
ANISOU 5319  CA  SER L  91     5073   7385   5790    620    267   -659       C  
ATOM   5320  C   SER L  91      82.061  24.830  11.049  1.00 45.04           C  
ANISOU 5320  C   SER L  91     4567   7031   5517    655    229   -638       C  
ATOM   5321  O   SER L  91      81.143  25.453  11.595  1.00 60.37           O  
ANISOU 5321  O   SER L  91     6434   8984   7521    660    257   -681       O  
ATOM   5322  CB  SER L  91      83.864  24.371  12.685  1.00 60.41           C  
ANISOU 5322  CB  SER L  91     6688   8894   7372    670    264   -670       C  
ATOM   5323  OG  SER L  91      84.887  24.871  11.844  1.00 66.23           O  
ANISOU 5323  OG  SER L  91     7425   9603   8136    719    203   -609       O  
ATOM   5324  N   SER L  92      82.469  25.095   9.810  1.00 27.57           N  
ANISOU 5324  N   SER L  92     2326   4823   3327    680    168   -572       N  
ATOM   5325  CA  SER L  92      81.851  26.009   8.862  1.00 32.42           C  
ANISOU 5325  CA  SER L  92     2824   5462   4031    710    123   -536       C  
ATOM   5326  C   SER L  92      82.499  25.744   7.514  1.00 24.64           C  
ANISOU 5326  C   SER L  92     1856   4486   3019    715     65   -462       C  
ATOM   5327  O   SER L  92      83.715  25.555   7.442  1.00 40.23           O  
ANISOU 5327  O   SER L  92     3908   6422   4954    734     48   -434       O  
ATOM   5328  CB  SER L  92      82.040  27.482   9.257  1.00 23.60           C  
ANISOU 5328  CB  SER L  92     1646   4298   3021    776    107   -539       C  
ATOM   5329  OG  SER L  92      83.407  27.798   9.479  1.00 52.72           O  
ANISOU 5329  OG  SER L  92     5403   7926   6702    816     85   -516       O  
ATOM   5330  N   TYR L  93      81.693  25.726   6.456  1.00 20.96           N  
ANISOU 5330  N   TYR L  93     1319   4072   2573    697     35   -430       N  
ATOM   5331  CA  TYR L  93      82.241  25.488   5.130  1.00 31.88           C  
ANISOU 5331  CA  TYR L  93     2715   5469   3928    699    -20   -360       C  
ATOM   5332  C   TYR L  93      83.260  26.576   4.784  1.00 40.20           C  
ANISOU 5332  C   TYR L  93     3768   6462   5043    764    -67   -307       C  
ATOM   5333  O   TYR L  93      83.114  27.728   5.205  1.00 25.05           O  
ANISOU 5333  O   TYR L  93     1830   4474   3216    785    -70   -306       O  
ATOM   5334  CB  TYR L  93      81.124  25.453   4.091  1.00 29.26           C  
ANISOU 5334  CB  TYR L  93     2296   5202   3618    673    -47   -337       C  
ATOM   5335  CG  TYR L  93      80.399  24.129   4.021  1.00 22.69           C  
ANISOU 5335  CG  TYR L  93     1500   4418   2702    593    -14   -366       C  
ATOM   5336  CD1 TYR L  93      79.475  23.764   4.992  1.00 28.14           C  
ANISOU 5336  CD1 TYR L  93     2180   5123   3388    554     45   -433       C  
ATOM   5337  CD2 TYR L  93      80.639  23.245   2.980  1.00 21.17           C  
ANISOU 5337  CD2 TYR L  93     1352   4255   2437    556    -40   -327       C  
ATOM   5338  CE1 TYR L  93      78.812  22.550   4.924  1.00 41.98           C  
ANISOU 5338  CE1 TYR L  93     3966   6918   5067    479     76   -459       C  
ATOM   5339  CE2 TYR L  93      79.983  22.037   2.903  1.00 21.36           C  
ANISOU 5339  CE2 TYR L  93     1410   4321   2387    481    -10   -355       C  
ATOM   5340  CZ  TYR L  93      79.073  21.691   3.875  1.00 30.54           C  
ANISOU 5340  CZ  TYR L  93     2561   5496   3548    443     48   -420       C  
ATOM   5341  OH  TYR L  93      78.426  20.480   3.785  1.00 27.96           O  
ANISOU 5341  OH  TYR L  93     2267   5207   3150    367     79   -447       O  
ATOM   5342  N   PRO L  94      84.308  26.242   4.007  1.00 43.15           N  
ANISOU 5342  N   PRO L  94     4196   6828   5371    775   -101   -255       N  
ATOM   5343  CA  PRO L  94      84.553  24.959   3.336  1.00 46.21           C  
ANISOU 5343  CA  PRO L  94     4649   7252   5655    728   -102   -237       C  
ATOM   5344  C   PRO L  94      85.075  23.853   4.252  1.00 55.20           C  
ANISOU 5344  C   PRO L  94     5903   8365   6704    691    -51   -280       C  
ATOM   5345  O   PRO L  94      85.400  24.101   5.413  1.00 56.80           O  
ANISOU 5345  O   PRO L  94     6136   8527   6919    709    -19   -321       O  
ATOM   5346  CB  PRO L  94      85.610  25.321   2.292  1.00 38.60           C  
ANISOU 5346  CB  PRO L  94     3698   6271   4697    767   -157   -164       C  
ATOM   5347  CG  PRO L  94      86.394  26.401   2.944  1.00 30.39           C  
ANISOU 5347  CG  PRO L  94     2685   5135   3727    809   -160   -158       C  
ATOM   5348  CD  PRO L  94      85.392  27.205   3.738  1.00 30.91           C  
ANISOU 5348  CD  PRO L  94     2690   5181   3873    809   -137   -201       C  
ATOM   5349  N   LEU L  95      85.147  22.640   3.713  1.00 19.10           N  
ANISOU 5349  N   LEU L  95     1396   3818   2043    638    -44   -271       N  
ATOM   5350  CA  LEU L  95      85.652  21.479   4.428  1.00 31.77           C  
ANISOU 5350  CA  LEU L  95     3113   5399   3557    599      1   -303       C  
ATOM   5351  C   LEU L  95      87.122  21.257   4.097  1.00 37.73           C  
ANISOU 5351  C   LEU L  95     3949   6111   4274    626    -22   -261       C  
ATOM   5352  O   LEU L  95      87.577  21.543   2.986  1.00 42.32           O  
ANISOU 5352  O   LEU L  95     4513   6700   4868    649    -69   -204       O  
ATOM   5353  CB  LEU L  95      84.842  20.231   4.072  1.00 34.84           C  
ANISOU 5353  CB  LEU L  95     3527   5837   3873    522     26   -322       C  
ATOM   5354  CG  LEU L  95      83.331  20.343   4.282  1.00 19.69           C  
ANISOU 5354  CG  LEU L  95     1525   3968   1989    488     48   -361       C  
ATOM   5355  CD1 LEU L  95      82.620  19.094   3.789  1.00 19.93           C  
ANISOU 5355  CD1 LEU L  95     1580   4046   1946    411     66   -374       C  
ATOM   5356  CD2 LEU L  95      83.025  20.594   5.747  1.00 31.49           C  
ANISOU 5356  CD2 LEU L  95     3022   5438   3506    493    100   -423       C  
ATOM   5357  N   THR L  96      87.865  20.742   5.074  1.00 28.80           N  
ANISOU 5357  N   THR L  96     2910   4936   3098    624     12   -288       N  
ATOM   5358  CA  THR L  96      89.295  20.514   4.917  1.00 24.44           C  
ANISOU 5358  CA  THR L  96     2437   4338   2512    651     -4   -253       C  
ATOM   5359  C   THR L  96      89.669  19.147   5.470  1.00 24.11           C  
ANISOU 5359  C   THR L  96     2506   4280   2374    605     38   -279       C  
ATOM   5360  O   THR L  96      89.108  18.697   6.473  1.00 17.29           O  
ANISOU 5360  O   THR L  96     1667   3419   1484    571     85   -331       O  
ATOM   5361  CB  THR L  96      90.121  21.594   5.628  1.00 17.06           C  
ANISOU 5361  CB  THR L  96     1493   3350   1641    717    -18   -252       C  
ATOM   5362  OG1 THR L  96      89.669  21.729   6.981  1.00 17.28           O  
ANISOU 5362  OG1 THR L  96     1523   3364   1677    711     25   -313       O  
ATOM   5363  CG2 THR L  96      89.990  22.930   4.913  1.00 17.21           C  
ANISOU 5363  CG2 THR L  96     1409   3374   1755    769    -67   -213       C  
ATOM   5364  N   PHE L  97      90.623  18.498   4.808  1.00 22.64           N  
ANISOU 5364  N   PHE L  97     2388   4078   2137    603     23   -240       N  
ATOM   5365  CA  PHE L  97      91.183  17.232   5.252  1.00 16.46           C  
ANISOU 5365  CA  PHE L  97     1716   3270   1268    568     58   -255       C  
ATOM   5366  C   PHE L  97      92.544  17.451   5.904  1.00 16.01           C  
ANISOU 5366  C   PHE L  97     1721   3150   1212    615     52   -244       C  
ATOM   5367  O   PHE L  97      93.095  18.554   5.911  1.00 15.86           O  
ANISOU 5367  O   PHE L  97     1660   3107   1259    674     19   -222       O  
ATOM   5368  CB  PHE L  97      91.332  16.257   4.079  1.00 16.38           C  
ANISOU 5368  CB  PHE L  97     1744   3282   1196    531     49   -224       C  
ATOM   5369  CG  PHE L  97      90.049  15.608   3.653  1.00 22.87           C  
ANISOU 5369  CG  PHE L  97     2537   4162   1989    466     67   -247       C  
ATOM   5370  CD1 PHE L  97      89.597  14.462   4.283  1.00 21.59           C  
ANISOU 5370  CD1 PHE L  97     2437   4004   1763    407    118   -290       C  
ATOM   5371  CD2 PHE L  97      89.308  16.130   2.606  1.00 31.04           C  
ANISOU 5371  CD2 PHE L  97     3484   5248   3062    464     32   -224       C  
ATOM   5372  CE1 PHE L  97      88.421  13.856   3.886  1.00 17.42           C  
ANISOU 5372  CE1 PHE L  97     1882   3528   1210    345    135   -312       C  
ATOM   5373  CE2 PHE L  97      88.132  15.528   2.206  1.00 17.57           C  
ANISOU 5373  CE2 PHE L  97     1749   3596   1329    403     46   -245       C  
ATOM   5374  CZ  PHE L  97      87.688  14.390   2.847  1.00 17.72           C  
ANISOU 5374  CZ  PHE L  97     1828   3617   1286    343     98   -291       C  
ATOM   5375  N   GLY L  98      93.085  16.367   6.459  1.00 15.82           N  
ANISOU 5375  N   GLY L  98     1797   3099   1115    589     84   -258       N  
ATOM   5376  CA  GLY L  98      94.473  16.328   6.860  1.00 15.38           C  
ANISOU 5376  CA  GLY L  98     1811   2986   1048    627     75   -239       C  
ATOM   5377  C   GLY L  98      95.343  15.759   5.754  1.00 21.16           C  
ANISOU 5377  C   GLY L  98     2585   3709   1747    630     52   -189       C  
ATOM   5378  O   GLY L  98      94.867  15.328   4.704  1.00 18.25           O  
ANISOU 5378  O   GLY L  98     2199   3378   1356    598     46   -173       O  
ATOM   5379  N   ALA L  99      96.653  15.767   6.001  1.00 14.68           N  
ANISOU 5379  N   ALA L  99     1819   2836    922    669     40   -167       N  
ATOM   5380  CA  ALA L  99      97.575  15.214   5.016  1.00 14.39           C  
ANISOU 5380  CA  ALA L  99     1826   2785    855    674     23   -121       C  
ATOM   5381  C   ALA L  99      97.483  13.696   4.953  1.00 14.43           C  
ANISOU 5381  C   ALA L  99     1912   2778    793    608     59   -132       C  
ATOM   5382  O   ALA L  99      97.783  13.101   3.912  1.00 36.04           O  
ANISOU 5382  O   ALA L  99     4667   5503   3524    583     50   -101       O  
ATOM   5383  CB  ALA L  99      99.006  15.648   5.328  1.00 21.97           C  
ANISOU 5383  CB  ALA L  99     2819   3688   1840    732      0    -94       C  
ATOM   5384  N   GLY L 100      97.069  13.061   6.037  1.00 14.59           N  
ANISOU 5384  N   GLY L 100     1974   2768    800    562     96   -170       N  
ATOM   5385  CA  GLY L 100      96.958  11.622   6.101  1.00 14.67           C  
ANISOU 5385  CA  GLY L 100     2055   2731    787    482    128   -176       C  
ATOM   5386  C   GLY L 100      98.027  11.009   6.994  1.00 14.42           C  
ANISOU 5386  C   GLY L 100     2103   2613    765    471    139   -170       C  
ATOM   5387  O   GLY L 100      99.035  11.633   7.339  1.00 14.14           O  
ANISOU 5387  O   GLY L 100     2069   2547    756    527    115   -152       O  
ATOM   5388  N   THR L 101      97.785   9.756   7.375  1.00 14.58           N  
ANISOU 5388  N   THR L 101     2184   2593    760    397    173   -184       N  
ATOM   5389  CA  THR L 101      98.713   8.978   8.188  1.00 14.42           C  
ANISOU 5389  CA  THR L 101     2235   2501    743    373    185   -179       C  
ATOM   5390  C   THR L 101      98.816   7.590   7.573  1.00 17.26           C  
ANISOU 5390  C   THR L 101     2645   2833   1081    305    204   -170       C  
ATOM   5391  O   THR L 101      97.840   6.833   7.575  1.00 40.08           O  
ANISOU 5391  O   THR L 101     5553   5734   3940    242    236   -194       O  
ATOM   5392  CB  THR L 101      98.251   8.899   9.645  1.00 14.85           C  
ANISOU 5392  CB  THR L 101     2311   2544    786    350    214   -214       C  
ATOM   5393  OG1 THR L 101      98.390  10.183  10.266  1.00 14.58           O  
ANISOU 5393  OG1 THR L 101     2236   2529    776    417    195   -223       O  
ATOM   5394  CG2 THR L 101      99.073   7.874  10.416  1.00 14.57           C  
ANISOU 5394  CG2 THR L 101     2343   2450    745    310    227   -208       C  
ATOM   5395  N   LYS L 102      99.988   7.262   7.039  1.00 30.11           N  
ANISOU 5395  N   LYS L 102     4293   4424   2726    319    185   -138       N  
ATOM   5396  CA  LYS L 102     100.220   5.970   6.403  1.00 35.31           C  
ANISOU 5396  CA  LYS L 102     4990   5060   3367    259    200   -131       C  
ATOM   5397  C   LYS L 102     100.616   4.967   7.480  1.00 35.39           C  
ANISOU 5397  C   LYS L 102     5044   5035   3369    219    222   -142       C  
ATOM   5398  O   LYS L 102     101.709   5.054   8.049  1.00 53.16           O  
ANISOU 5398  O   LYS L 102     7308   7249   5643    257    207   -124       O  
ATOM   5399  CB  LYS L 102     101.295   6.088   5.325  1.00 51.89           C  
ANISOU 5399  CB  LYS L 102     7083   7143   5491    297    172    -93       C  
ATOM   5400  CG  LYS L 102     101.470   4.846   4.468  1.00 67.07           C  
ANISOU 5400  CG  LYS L 102     9034   9053   7395    240    186    -89       C  
ATOM   5401  CD  LYS L 102     102.566   5.052   3.431  1.00 89.58           C  
ANISOU 5401  CD  LYS L 102    11878  11887  10273    282    161    -53       C  
ATOM   5402  CE  LYS L 102     102.804   3.796   2.608  1.00 97.44           C  
ANISOU 5402  CE  LYS L 102    12901  12873  11250    228    176    -52       C  
ATOM   5403  NZ  LYS L 102     103.934   3.962   1.651  1.00 83.84           N  
ANISOU 5403  NZ  LYS L 102    11174  11129   9552    268    156    -19       N  
ATOM   5404  N   LEU L 103      99.724   4.022   7.765  1.00 26.96           N  
ANISOU 5404  N   LEU L 103     3992   3984   2266    146    256   -171       N  
ATOM   5405  CA  LEU L 103      99.953   2.991   8.774  1.00 14.74           C  
ANISOU 5405  CA  LEU L 103     2465   2428    706    112    275   -183       C  
ATOM   5406  C   LEU L 103     100.395   1.718   8.063  1.00 14.76           C  
ANISOU 5406  C   LEU L 103     2475   2432    699     86    279   -172       C  
ATOM   5407  O   LEU L 103      99.580   1.017   7.461  1.00 38.28           O  
ANISOU 5407  O   LEU L 103     5439   5455   3650     39    296   -190       O  
ATOM   5408  CB  LEU L 103      98.693   2.755   9.601  1.00 15.14           C  
ANISOU 5408  CB  LEU L 103     2511   2517    725     61    309   -223       C  
ATOM   5409  CG  LEU L 103      98.729   1.578  10.578  1.00 50.47           C  
ANISOU 5409  CG  LEU L 103     6985   7010   5180     42    325   -235       C  
ATOM   5410  CD1 LEU L 103      99.777   1.803  11.657  1.00 53.95           C  
ANISOU 5410  CD1 LEU L 103     7455   7400   5643     84    310   -217       C  
ATOM   5411  CD2 LEU L 103      97.357   1.340  11.193  1.00 24.77           C  
ANISOU 5411  CD2 LEU L 103     3698   3801   1913     16    348   -268       C  
ATOM   5412  N   GLU L 104     101.688   1.423   8.128  1.00 18.92           N  
ANISOU 5412  N   GLU L 104     3026   2912   1252    124    262   -142       N  
ATOM   5413  CA  GLU L 104     102.209   0.192   7.556  1.00 22.12           C  
ANISOU 5413  CA  GLU L 104     3446   3306   1653    113    267   -131       C  
ATOM   5414  C   GLU L 104     102.237  -0.910   8.609  1.00 16.23           C  
ANISOU 5414  C   GLU L 104     2726   2547    893    103    285   -138       C  
ATOM   5415  O   GLU L 104     102.259  -0.654   9.815  1.00 15.46           O  
ANISOU 5415  O   GLU L 104     2640   2437    797    114    287   -142       O  
ATOM   5416  CB  GLU L 104     103.611   0.400   6.980  1.00 17.40           C  
ANISOU 5416  CB  GLU L 104     2867   2655   1090    162    243    -95       C  
ATOM   5417  CG  GLU L 104     104.666   0.743   8.018  1.00 35.25           C  
ANISOU 5417  CG  GLU L 104     5153   4862   3377    212    228    -76       C  
ATOM   5418  CD  GLU L 104     106.035   0.176   7.678  1.00 30.72           C  
ANISOU 5418  CD  GLU L 104     4612   4234   2827    246    218    -47       C  
ATOM   5419  OE1 GLU L 104     106.714  -0.329   8.597  1.00 20.96           O  
ANISOU 5419  OE1 GLU L 104     3412   2956   1596    263    220    -38       O  
ATOM   5420  OE2 GLU L 104     106.430   0.228   6.493  1.00 24.04           O  
ANISOU 5420  OE2 GLU L 104     3757   3386   1991    256    210    -33       O  
ATOM   5421  N   LEU L 105     102.233  -2.152   8.134  1.00 14.98           N  
ANISOU 5421  N   LEU L 105     2582   2390    721     88    299   -136       N  
ATOM   5422  CA  LEU L 105     102.257  -3.317   9.009  1.00 15.26           C  
ANISOU 5422  CA  LEU L 105     2655   2400    744     83    318   -137       C  
ATOM   5423  C   LEU L 105     103.701  -3.640   9.375  1.00 15.06           C  
ANISOU 5423  C   LEU L 105     2680   2298    744    116    307   -107       C  
ATOM   5424  O   LEU L 105     104.524  -3.912   8.494  1.00 14.90           O  
ANISOU 5424  O   LEU L 105     2676   2246    740    132    299    -88       O  
ATOM   5425  CB  LEU L 105     101.587  -4.514   8.334  1.00 15.60           C  
ANISOU 5425  CB  LEU L 105     2703   2463    762     59    339   -149       C  
ATOM   5426  CG  LEU L 105     101.534  -5.816   9.136  1.00 15.99           C  
ANISOU 5426  CG  LEU L 105     2809   2469    796     50    364   -147       C  
ATOM   5427  CD1 LEU L 105     100.922  -5.579  10.504  1.00 40.55           C  
ANISOU 5427  CD1 LEU L 105     5920   5593   3895     46    373   -160       C  
ATOM   5428  CD2 LEU L 105     100.748  -6.873   8.384  1.00 35.09           C  
ANISOU 5428  CD2 LEU L 105     5238   4902   3192     26    386   -160       C  
ATOM   5429  N   LYS L 106     104.006  -3.602  10.670  1.00 15.11           N  
ANISOU 5429  N   LYS L 106     2715   2275    753    130    307   -102       N  
ATOM   5430  CA  LYS L 106     105.345  -3.940  11.132  1.00 15.00           C  
ANISOU 5430  CA  LYS L 106     2754   2187    758    166    297    -74       C  
ATOM   5431  C   LYS L 106     105.651  -5.403  10.829  1.00 28.69           C  
ANISOU 5431  C   LYS L 106     4540   3880   2482    157    317    -64       C  
ATOM   5432  O   LYS L 106     104.768  -6.266  10.844  1.00 15.64           O  
ANISOU 5432  O   LYS L 106     2896   2244    803    122    342    -80       O  
ATOM   5433  CB  LYS L 106     105.477  -3.659  12.629  1.00 15.09           C  
ANISOU 5433  CB  LYS L 106     2784   2182    765    178    295    -73       C  
ATOM   5434  CG  LYS L 106     106.889  -3.763  13.175  1.00 14.93           C  
ANISOU 5434  CG  LYS L 106     2812   2095    768    222    278    -44       C  
ATOM   5435  CD  LYS L 106     106.923  -3.423  14.657  1.00 53.01           C  
ANISOU 5435  CD  LYS L 106     7650   6912   5581    231    274    -47       C  
ATOM   5436  CE  LYS L 106     108.281  -3.728  15.272  1.00 60.18           C  
ANISOU 5436  CE  LYS L 106     8609   7753   6503    272    260    -19       C  
ATOM   5437  NZ  LYS L 106     108.281  -3.544  16.753  1.00 47.23           N  
ANISOU 5437  NZ  LYS L 106     6990   6108   4847    276    258    -21       N  
ATOM   5438  N   ARG L 107     106.922  -5.679  10.551  1.00 18.05           N  
ANISOU 5438  N   ARG L 107     3227   2474   1157    191    307    -38       N  
ATOM   5439  CA  ARG L 107     107.323  -6.973  10.026  1.00 15.29           C  
ANISOU 5439  CA  ARG L 107     2924   2082    803    184    325    -30       C  
ATOM   5440  C   ARG L 107     108.779  -7.220  10.391  1.00 15.14           C  
ANISOU 5440  C   ARG L 107     2954   1992    807    228    313     -1       C  
ATOM   5441  O   ARG L 107     109.528  -6.288  10.693  1.00 14.82           O  
ANISOU 5441  O   ARG L 107     2900   1940    790    268    288     12       O  
ATOM   5442  CB  ARG L 107     107.123  -7.024   8.504  1.00 15.21           C  
ANISOU 5442  CB  ARG L 107     2886   2099    794    171    326    -36       C  
ATOM   5443  CG  ARG L 107     107.340  -8.379   7.865  1.00 15.48           C  
ANISOU 5443  CG  ARG L 107     2964   2097    819    157    349    -34       C  
ATOM   5444  CD  ARG L 107     107.904  -8.226   6.467  1.00 15.26           C  
ANISOU 5444  CD  ARG L 107     2921   2072    807    170    341    -27       C  
ATOM   5445  NE  ARG L 107     108.140  -9.517   5.831  1.00 15.54           N  
ANISOU 5445  NE  ARG L 107     3000   2071    832    156    364    -28       N  
ATOM   5446  CZ  ARG L 107     109.198 -10.284   6.071  1.00 15.58           C  
ANISOU 5446  CZ  ARG L 107     3063   2006    849    179    371     -9       C  
ATOM   5447  NH1 ARG L 107     110.119  -9.894   6.941  1.00 26.83           N  
ANISOU 5447  NH1 ARG L 107     4506   3391   2295    219    355     12       N  
ATOM   5448  NH2 ARG L 107     109.335 -11.444   5.444  1.00 32.21           N  
ANISOU 5448  NH2 ARG L 107     5208   4082   2946    163    395    -13       N  
ATOM   5449  N   ALA L 108     109.171  -8.492  10.374  1.00 15.40           N  
ANISOU 5449  N   ALA L 108     3043   1976    833    223    333      7       N  
ATOM   5450  CA  ALA L 108     110.574  -8.832  10.549  1.00 15.87           C  
ANISOU 5450  CA  ALA L 108     3147   1968    914    266    324     33       C  
ATOM   5451  C   ALA L 108     111.397  -8.266   9.398  1.00 14.92           C  
ANISOU 5451  C   ALA L 108     3003   1843    822    299    307     43       C  
ATOM   5452  O   ALA L 108     110.911  -8.112   8.274  1.00 36.30           O  
ANISOU 5452  O   ALA L 108     5676   4589   3528    279    311     32       O  
ATOM   5453  CB  ALA L 108     110.751 -10.349  10.633  1.00 15.68           C  
ANISOU 5453  CB  ALA L 108     3189   1893    874    250    353     37       C  
ATOM   5454  N   ASP L 109     112.654  -7.940   9.689  1.00 14.72           N  
ANISOU 5454  N   ASP L 109     3001   1771    821    353    290     65       N  
ATOM   5455  CA  ASP L 109     113.528  -7.379   8.669  1.00 14.40           C  
ANISOU 5455  CA  ASP L 109     2941   1720    809    392    275     77       C  
ATOM   5456  C   ASP L 109     113.847  -8.424   7.608  1.00 14.56           C  
ANISOU 5456  C   ASP L 109     2992   1713    826    384    297     79       C  
ATOM   5457  O   ASP L 109     114.115  -9.588   7.917  1.00 14.87           O  
ANISOU 5457  O   ASP L 109     3091   1705    854    379    318     83       O  
ATOM   5458  CB  ASP L 109     114.820  -6.856   9.295  1.00 34.73           C  
ANISOU 5458  CB  ASP L 109     5536   4249   3410    455    253     98       C  
ATOM   5459  CG  ASP L 109     114.576  -5.737  10.290  1.00 31.24           C  
ANISOU 5459  CG  ASP L 109     5064   3833   2972    467    229     95       C  
ATOM   5460  OD1 ASP L 109     113.508  -5.093  10.219  1.00 24.88           O  
ANISOU 5460  OD1 ASP L 109     4212   3085   2157    434    227     79       O  
ATOM   5461  OD2 ASP L 109     115.457  -5.499  11.143  1.00 34.86           O  
ANISOU 5461  OD2 ASP L 109     5547   4257   3444    509    214    107       O  
ATOM   5462  N   ALA L 110     113.810  -8.000   6.347  1.00 14.37           N  
ANISOU 5462  N   ALA L 110     2931   1720    811    382    294     76       N  
ATOM   5463  CA  ALA L 110     114.066  -8.876   5.212  1.00 14.53           C  
ANISOU 5463  CA  ALA L 110     2973   1722    826    372    314     75       C  
ATOM   5464  C   ALA L 110     115.109  -8.231   4.314  1.00 14.24           C  
ANISOU 5464  C   ALA L 110     2921   1672    816    419    301     91       C  
ATOM   5465  O   ALA L 110     115.026  -7.033   4.023  1.00 13.93           O  
ANISOU 5465  O   ALA L 110     2829   1671    792    433    278     93       O  
ATOM   5466  CB  ALA L 110     112.782  -9.154   4.424  1.00 14.71           C  
ANISOU 5466  CB  ALA L 110     2963   1805    822    312    329     50       C  
ATOM   5467  N   ALA L 111     116.086  -9.019   3.885  1.00 14.36           N  
ANISOU 5467  N   ALA L 111     2984   1633    839    446    316    102       N  
ATOM   5468  CA  ALA L 111     117.105  -8.495   2.987  1.00 14.13           C  
ANISOU 5468  CA  ALA L 111     2943   1591    834    492    308    116       C  
ATOM   5469  C   ALA L 111     116.589  -8.497   1.548  1.00 18.59           C  
ANISOU 5469  C   ALA L 111     3475   2201   1387    458    317    105       C  
ATOM   5470  O   ALA L 111     115.829  -9.388   1.160  1.00 25.95           O  
ANISOU 5470  O   ALA L 111     4420   3147   2292    408    339     87       O  
ATOM   5471  CB  ALA L 111     118.385  -9.321   3.084  1.00 14.28           C  
ANISOU 5471  CB  ALA L 111     3027   1535    865    537    324    130       C  
ATOM   5472  N   PRO L 112     116.977  -7.514   0.742  1.00 16.04           N  
ANISOU 5472  N   PRO L 112     3110   1902   1082    483    300    114       N  
ATOM   5473  CA  PRO L 112     116.462  -7.450  -0.628  1.00 14.88           C  
ANISOU 5473  CA  PRO L 112     2931   1804    920    449    307    104       C  
ATOM   5474  C   PRO L 112     117.084  -8.511  -1.517  1.00 14.22           C  
ANISOU 5474  C   PRO L 112     2890   1684    828    451    335    103       C  
ATOM   5475  O   PRO L 112     118.255  -8.872  -1.375  1.00 14.23           O  
ANISOU 5475  O   PRO L 112     2936   1624    848    499    344    119       O  
ATOM   5476  CB  PRO L 112     116.857  -6.041  -1.087  1.00 15.92           C  
ANISOU 5476  CB  PRO L 112     3011   1961   1076    486    280    118       C  
ATOM   5477  CG  PRO L 112     118.067  -5.721  -0.281  1.00 13.39           C  
ANISOU 5477  CG  PRO L 112     2714   1585    788    552    270    137       C  
ATOM   5478  CD  PRO L 112     117.848  -6.369   1.061  1.00 13.53           C  
ANISOU 5478  CD  PRO L 112     2771   1573    798    543    275    132       C  
ATOM   5479  N   THR L 113     116.273  -9.018  -2.443  1.00 33.29           N  
ANISOU 5479  N   THR L 113     5294   4140   3215    398    350     83       N  
ATOM   5480  CA  THR L 113     116.741  -9.915  -3.494  1.00 29.81           C  
ANISOU 5480  CA  THR L 113     4886   3677   2762    393    377     79       C  
ATOM   5481  C   THR L 113     117.015  -9.069  -4.732  1.00 32.75           C  
ANISOU 5481  C   THR L 113     5215   4090   3140    404    366     86       C  
ATOM   5482  O   THR L 113     116.081  -8.613  -5.400  1.00 30.23           O  
ANISOU 5482  O   THR L 113     4846   3840   2800    363    357     72       O  
ATOM   5483  CB  THR L 113     115.717 -11.009  -3.787  1.00 36.88           C  
ANISOU 5483  CB  THR L 113     5797   4594   3622    331    402     51       C  
ATOM   5484  OG1 THR L 113     115.392 -11.697  -2.573  1.00 46.05           O  
ANISOU 5484  OG1 THR L 113     6997   5721   4779    320    411     46       O  
ATOM   5485  CG2 THR L 113     116.279 -12.004  -4.791  1.00 24.83           C  
ANISOU 5485  CG2 THR L 113     4314   3036   2085    328    433     45       C  
ATOM   5486  N   VAL L 114     118.294  -8.856  -5.029  1.00 27.22           N  
ANISOU 5486  N   VAL L 114     4532   3346   2464    460    368    108       N  
ATOM   5487  CA  VAL L 114     118.723  -7.933  -6.073  1.00 24.58           C  
ANISOU 5487  CA  VAL L 114     4159   3043   2140    481    357    120       C  
ATOM   5488  C   VAL L 114     118.962  -8.710  -7.359  1.00 18.89           C  
ANISOU 5488  C   VAL L 114     3458   2322   1396    462    385    111       C  
ATOM   5489  O   VAL L 114     119.610  -9.764  -7.348  1.00 16.47           O  
ANISOU 5489  O   VAL L 114     3210   1959   1089    475    414    110       O  
ATOM   5490  CB  VAL L 114     119.989  -7.171  -5.648  1.00 13.99           C  
ANISOU 5490  CB  VAL L 114     2820   1658    838    557    344    148       C  
ATOM   5491  CG1 VAL L 114     120.312  -6.078  -6.651  1.00 13.80           C  
ANISOU 5491  CG1 VAL L 114     2748   1671    826    578    330    162       C  
ATOM   5492  CG2 VAL L 114     119.814  -6.593  -4.255  1.00 13.73           C  
ANISOU 5492  CG2 VAL L 114     2776   1616    824    575    320    152       C  
ATOM   5493  N   SER L 115     118.441  -8.191  -8.469  1.00 14.68           N  
ANISOU 5493  N   SER L 115     2879   1853    845    431    378    104       N  
ATOM   5494  CA  SER L 115     118.679  -8.776  -9.781  1.00 15.01           C  
ANISOU 5494  CA  SER L 115     2934   1906    864    414    402     94       C  
ATOM   5495  C   SER L 115     118.818  -7.654 -10.797  1.00 14.87           C  
ANISOU 5495  C   SER L 115     2865   1936    847    422    385    108       C  
ATOM   5496  O   SER L 115     117.950  -6.780 -10.881  1.00 14.71           O  
ANISOU 5496  O   SER L 115     2794   1977    819    397    359    107       O  
ATOM   5497  CB  SER L 115     117.548  -9.732 -10.182  1.00 16.90           C  
ANISOU 5497  CB  SER L 115     3177   2183   1061    345    419     60       C  
ATOM   5498  OG  SER L 115     116.294  -9.077 -10.185  1.00 19.70           O  
ANISOU 5498  OG  SER L 115     3476   2613   1397    302    395     48       O  
ATOM   5499  N   ILE L 116     119.909  -7.677 -11.560  1.00 14.94           N  
ANISOU 5499  N   ILE L 116     2892   1918    865    459    401    123       N  
ATOM   5500  CA  ILE L 116     120.223  -6.616 -12.509  1.00 14.82           C  
ANISOU 5500  CA  ILE L 116     2835   1941    854    476    387    141       C  
ATOM   5501  C   ILE L 116     119.916  -7.101 -13.918  1.00 15.24           C  
ANISOU 5501  C   ILE L 116     2885   2038    866    429    406    123       C  
ATOM   5502  O   ILE L 116     119.946  -8.303 -14.212  1.00 22.46           O  
ANISOU 5502  O   ILE L 116     3841   2933   1759    406    437    101       O  
ATOM   5503  CB  ILE L 116     121.694  -6.162 -12.373  1.00 18.09           C  
ANISOU 5503  CB  ILE L 116     3263   2300   1309    555    391    172       C  
ATOM   5504  CG1 ILE L 116     121.893  -4.783 -13.006  1.00 15.17           C  
ANISOU 5504  CG1 ILE L 116     2840   1970    953    579    368    196       C  
ATOM   5505  CG2 ILE L 116     122.636  -7.183 -12.994  1.00 19.50           C  
ANISOU 5505  CG2 ILE L 116     3495   2432   1481    571    431    170       C  
ATOM   5506  CD1 ILE L 116     123.277  -4.211 -12.806  1.00 14.17           C  
ANISOU 5506  CD1 ILE L 116     2716   1797    869    659    371    225       C  
ATOM   5507  N   PHE L 117     119.604  -6.151 -14.800  1.00 15.20           N  
ANISOU 5507  N   PHE L 117     2833   2093    849    415    388    132       N  
ATOM   5508  CA  PHE L 117     119.194  -6.424 -16.170  1.00 15.61           C  
ANISOU 5508  CA  PHE L 117     2874   2201    856    367    400    116       C  
ATOM   5509  C   PHE L 117     119.814  -5.412 -17.126  1.00 23.57           C  
ANISOU 5509  C   PHE L 117     3855   3230   1870    393    392    144       C  
ATOM   5510  O   PHE L 117     119.621  -4.197 -16.965  1.00 25.49           O  
ANISOU 5510  O   PHE L 117     4057   3495   2131    410    361    167       O  
ATOM   5511  CB  PHE L 117     117.669  -6.393 -16.294  1.00 15.74           C  
ANISOU 5511  CB  PHE L 117     2856   2291    834    299    384     92       C  
ATOM   5512  CG  PHE L 117     116.969  -7.378 -15.405  1.00 26.53           C  
ANISOU 5512  CG  PHE L 117     4244   3645   2193    271    393     64       C  
ATOM   5513  CD1 PHE L 117     116.696  -8.661 -15.850  1.00 16.31           C  
ANISOU 5513  CD1 PHE L 117     2979   2353    865    237    422     32       C  
ATOM   5514  CD2 PHE L 117     116.583  -7.022 -14.123  1.00 25.37           C  
ANISOU 5514  CD2 PHE L 117     4089   3481   2070    282    374     70       C  
ATOM   5515  CE1 PHE L 117     116.053  -9.568 -15.034  1.00 31.37           C  
ANISOU 5515  CE1 PHE L 117     4909   4244   2766    215    432      8       C  
ATOM   5516  CE2 PHE L 117     115.942  -7.927 -13.301  1.00 25.93           C  
ANISOU 5516  CE2 PHE L 117     4181   3538   2132    257    384     46       C  
ATOM   5517  CZ  PHE L 117     115.675  -9.200 -13.757  1.00 35.83           C  
ANISOU 5517  CZ  PHE L 117     5466   4793   3355    224    413     16       C  
ATOM   5518  N   PRO L 118     120.560  -5.872 -18.126  1.00 28.11           N  
ANISOU 5518  N   PRO L 118     4453   3797   2431    400    420    143       N  
ATOM   5519  CA  PRO L 118     121.113  -4.961 -19.131  1.00 34.49           C  
ANISOU 5519  CA  PRO L 118     5235   4630   3239    420    415    169       C  
ATOM   5520  C   PRO L 118     120.040  -4.536 -20.117  1.00 16.13           C  
ANISOU 5520  C   PRO L 118     2872   2389    867    357    398    160       C  
ATOM   5521  O   PRO L 118     118.972  -5.163 -20.187  1.00 16.37           O  
ANISOU 5521  O   PRO L 118     2900   2461    859    296    399    128       O  
ATOM   5522  CB  PRO L 118     122.196  -5.812 -19.810  1.00 16.23           C  
ANISOU 5522  CB  PRO L 118     2967   2279    921    441    457    164       C  
ATOM   5523  CG  PRO L 118     121.693  -7.204 -19.678  1.00 16.57           C  
ANISOU 5523  CG  PRO L 118     3047   2314    936    398    482    124       C  
ATOM   5524  CD  PRO L 118     120.977  -7.267 -18.353  1.00 20.60           C  
ANISOU 5524  CD  PRO L 118     3554   2809   1464    391    461    118       C  
ATOM   5525  N   PRO L 119     120.280  -3.478 -20.894  1.00 23.49           N  
ANISOU 5525  N   PRO L 119     3775   3351   1800    370    384    188       N  
ATOM   5526  CA  PRO L 119     119.261  -3.026 -21.850  1.00 35.32           C  
ANISOU 5526  CA  PRO L 119     5243   4926   3252    310    366    184       C  
ATOM   5527  C   PRO L 119     118.980  -4.075 -22.916  1.00 27.23           C  
ANISOU 5527  C   PRO L 119     4236   3941   2168    252    394    150       C  
ATOM   5528  O   PRO L 119     119.884  -4.763 -23.395  1.00 29.54           O  
ANISOU 5528  O   PRO L 119     4559   4207   2458    271    428    143       O  
ATOM   5529  CB  PRO L 119     119.878  -1.758 -22.453  1.00 16.24           C  
ANISOU 5529  CB  PRO L 119     2800   2515    856    351    351    226       C  
ATOM   5530  CG  PRO L 119     121.343  -1.899 -22.223  1.00 16.10           C  
ANISOU 5530  CG  PRO L 119     2805   2434    879    422    375    243       C  
ATOM   5531  CD  PRO L 119     121.470  -2.612 -20.913  1.00 15.85           C  
ANISOU 5531  CD  PRO L 119     2799   2346    876    443    382    227       C  
ATOM   5532  N   SER L 120     117.707  -4.188 -23.285  1.00 19.38           N  
ANISOU 5532  N   SER L 120     3223   3014   1127    184    380    128       N  
ATOM   5533  CA  SER L 120     117.277  -5.181 -24.255  1.00 35.81           C  
ANISOU 5533  CA  SER L 120     5311   5148   3147    129    403     91       C  
ATOM   5534  C   SER L 120     117.791  -4.832 -25.650  1.00 44.66           C  
ANISOU 5534  C   SER L 120     6431   6299   4238    121    412    105       C  
ATOM   5535  O   SER L 120     118.348  -3.758 -25.893  1.00 53.94           O  
ANISOU 5535  O   SER L 120     7599   7459   5438    154    398    144       O  
ATOM   5536  CB  SER L 120     115.752  -5.287 -24.267  1.00 44.46           C  
ANISOU 5536  CB  SER L 120     6377   6315   4200     63    383     67       C  
ATOM   5537  OG  SER L 120     115.157  -4.034 -24.567  1.00 27.29           O  
ANISOU 5537  OG  SER L 120     4182   4169   2019     40    348     94       O  
ATOM   5538  N   SER L 121     117.592  -5.768 -26.582  1.00 46.07           N  
ANISOU 5538  N   SER L 121     6616   6525   4363     82    437     71       N  
ATOM   5539  CA  SER L 121     117.967  -5.515 -27.968  1.00 44.00           C  
ANISOU 5539  CA  SER L 121     6354   6303   4061     64    447     80       C  
ATOM   5540  C   SER L 121     117.045  -4.494 -28.621  1.00 37.54           C  
ANISOU 5540  C   SER L 121     5512   5544   3208     11    412     98       C  
ATOM   5541  O   SER L 121     117.485  -3.734 -29.492  1.00 35.65           O  
ANISOU 5541  O   SER L 121     5278   5308   2958     13    408    126       O  
ATOM   5542  CB  SER L 121     117.960  -6.821 -28.765  1.00 45.40           C  
ANISOU 5542  CB  SER L 121     6543   6518   4188     44    482     36       C  
ATOM   5543  OG  SER L 121     118.956  -7.713 -28.298  1.00 40.12           O  
ANISOU 5543  OG  SER L 121     5919   5770   3555     91    519     24       O  
ATOM   5544  N   GLU L 122     115.772  -4.460 -28.216  1.00 34.83           N  
ANISOU 5544  N   GLU L 122     5149   5230   2855    -31    385     83       N  
ATOM   5545  CA  GLU L 122     114.840  -3.488 -28.779  1.00 35.46           C  
ANISOU 5545  CA  GLU L 122     5229   5319   2925    -75    349    100       C  
ATOM   5546  C   GLU L 122     115.279  -2.064 -28.463  1.00 42.11           C  
ANISOU 5546  C   GLU L 122     6084   6121   3793    -27    326    154       C  
ATOM   5547  O   GLU L 122     115.309  -1.199 -29.347  1.00 56.05           O  
ANISOU 5547  O   GLU L 122     7864   7891   5542    -24    312    184       O  
ATOM   5548  CB  GLU L 122     113.426  -3.740 -28.250  1.00 45.78           C  
ANISOU 5548  CB  GLU L 122     6523   6640   4232   -118    327     74       C  
ATOM   5549  CG  GLU L 122     112.782  -5.033 -28.728  1.00 59.71           C  
ANISOU 5549  CG  GLU L 122     8238   8489   5959   -140    340     28       C  
ATOM   5550  CD  GLU L 122     113.086  -6.213 -27.825  1.00 68.36           C  
ANISOU 5550  CD  GLU L 122     9322   9588   7062    -73    366      2       C  
ATOM   5551  OE1 GLU L 122     114.122  -6.185 -27.126  1.00 66.90           O  
ANISOU 5551  OE1 GLU L 122     9175   9339   6906    -43    386     14       O  
ATOM   5552  OE2 GLU L 122     112.281  -7.169 -27.810  1.00 68.52           O  
ANISOU 5552  OE2 GLU L 122     9321   9656   7057    -37    370    -29       O  
ATOM   5553  N   GLN L 123     115.625  -1.801 -27.201  1.00 33.04           N  
ANISOU 5553  N   GLN L 123     4918   4930   2707     31    318    168       N  
ATOM   5554  CA  GLN L 123     116.017  -0.450 -26.815  1.00 17.87           C  
ANISOU 5554  CA  GLN L 123     2975   2975    840     99    289    216       C  
ATOM   5555  C   GLN L 123     117.348  -0.059 -27.445  1.00 26.15           C  
ANISOU 5555  C   GLN L 123     4021   4006   1909    153    305    247       C  
ATOM   5556  O   GLN L 123     117.540   1.100 -27.831  1.00 32.85           O  
ANISOU 5556  O   GLN L 123     4848   4858   2776    189    282    288       O  
ATOM   5557  CB  GLN L 123     116.089  -0.334 -25.294  1.00 17.28           C  
ANISOU 5557  CB  GLN L 123     2883   2858    824    146    279    219       C  
ATOM   5558  CG  GLN L 123     116.200   1.097 -24.799  1.00 28.60           C  
ANISOU 5558  CG  GLN L 123     4282   4275   2312    210    244    263       C  
ATOM   5559  CD  GLN L 123     116.296   1.189 -23.291  1.00 28.39           C  
ANISOU 5559  CD  GLN L 123     4241   4207   2339    252    236    262       C  
ATOM   5560  OE1 GLN L 123     116.761   0.262 -22.628  1.00 25.31           O  
ANISOU 5560  OE1 GLN L 123     3872   3784   1961    259    261    240       O  
ATOM   5561  NE2 GLN L 123     115.851   2.312 -22.739  1.00 44.34           N  
ANISOU 5561  NE2 GLN L 123     6226   6230   4393    285    202    287       N  
ATOM   5562  N   LEU L 124     118.277  -1.010 -27.556  1.00 43.60           N  
ANISOU 5562  N   LEU L 124     6250   6198   4118    163    344    228       N  
ATOM   5563  CA  LEU L 124     119.564  -0.715 -28.177  1.00 40.00           C  
ANISOU 5563  CA  LEU L 124     5798   5723   3679    213    364    255       C  
ATOM   5564  C   LEU L 124     119.395  -0.385 -29.654  1.00 44.89           C  
ANISOU 5564  C   LEU L 124     6422   6391   4244    172    365    265       C  
ATOM   5565  O   LEU L 124     119.901   0.637 -30.134  1.00 43.67           O  
ANISOU 5565  O   LEU L 124     6250   6235   4106    212    353    307       O  
ATOM   5566  CB  LEU L 124     120.522  -1.892 -27.989  1.00 24.05           C  
ANISOU 5566  CB  LEU L 124     3806   3664   1667    234    409    230       C  
ATOM   5567  CG  LEU L 124     121.029  -2.086 -26.560  1.00 17.64           C  
ANISOU 5567  CG  LEU L 124     3001   2785    918    293    411    232       C  
ATOM   5568  CD1 LEU L 124     122.010  -3.244 -26.488  1.00 17.81           C  
ANISOU 5568  CD1 LEU L 124     3062   2758    946    318    456    211       C  
ATOM   5569  CD2 LEU L 124     121.660  -0.801 -26.048  1.00 22.33           C  
ANISOU 5569  CD2 LEU L 124     3566   3345   1571    366    387    280       C  
ATOM   5570  N   THR L 125     118.677  -1.235 -30.393  1.00 36.28           N  
ANISOU 5570  N   THR L 125     5353   5347   3085     94    378    226       N  
ATOM   5571  CA  THR L 125     118.389  -0.927 -31.789  1.00 43.50           C  
ANISOU 5571  CA  THR L 125     6283   6305   3940     48    376    233       C  
ATOM   5572  C   THR L 125     117.540   0.329 -31.931  1.00 43.37           C  
ANISOU 5572  C   THR L 125     6259   6294   3926     52    329    268       C  
ATOM   5573  O   THR L 125     117.520   0.933 -33.009  1.00 40.72           O  
ANISOU 5573  O   THR L 125     5934   5978   3559     46    322    292       O  
ATOM   5574  CB  THR L 125     117.692  -2.112 -32.461  1.00 35.89           C  
ANISOU 5574  CB  THR L 125     5339   5392   2905    -37    396    180       C  
ATOM   5575  OG1 THR L 125     116.580  -2.532 -31.661  1.00 53.58           O  
ANISOU 5575  OG1 THR L 125     7568   7631   5157    -67    377    151       O  
ATOM   5576  CG2 THR L 125     118.660  -3.273 -32.629  1.00 20.58           C  
ANISOU 5576  CG2 THR L 125     3397   3463    957    -22    444    151       C  
ATOM   5577  N   SER L 126     116.846   0.739 -30.867  1.00 34.53           N  
ANISOU 5577  N   SER L 126     5119   5158   2843     69    299    273       N  
ATOM   5578  CA  SER L 126     116.098   1.989 -30.902  1.00 25.24           C  
ANISOU 5578  CA  SER L 126     3919   3990   1679     94    253    310       C  
ATOM   5579  C   SER L 126     117.018   3.194 -30.742  1.00 18.73           C  
ANISOU 5579  C   SER L 126     3045   3154    917    176    238    363       C  
ATOM   5580  O   SER L 126     116.853   4.198 -31.443  1.00 36.50           O  
ANISOU 5580  O   SER L 126     5274   5431   3166    196    213    400       O  
ATOM   5581  CB  SER L 126     115.022   1.989 -29.816  1.00 44.94           C  
ANISOU 5581  CB  SER L 126     6407   6477   4192     86    228    294       C  
ATOM   5582  OG  SER L 126     114.090   0.942 -30.024  1.00 58.24           O  
ANISOU 5582  OG  SER L 126     8143   8170   5818     10    242    247       O  
ATOM   5583  N   GLY L 127     117.985   3.118 -29.830  1.00 29.27           N  
ANISOU 5583  N   GLY L 127     4362   4450   2310    228    253    368       N  
ATOM   5584  CA  GLY L 127     118.931   4.204 -29.655  1.00 29.82           C  
ANISOU 5584  CA  GLY L 127     4389   4502   2439    306    244    415       C  
ATOM   5585  C   GLY L 127     119.251   4.552 -28.215  1.00 30.80           C  
ANISOU 5585  C   GLY L 127     4484   4584   2635    365    233    422       C  
ATOM   5586  O   GLY L 127     120.224   5.266 -27.950  1.00 42.51           O  
ANISOU 5586  O   GLY L 127     5938   6042   4172    431    235    455       O  
ATOM   5587  N   GLY L 128     118.443   4.063 -27.272  1.00 19.34           N  
ANISOU 5587  N   GLY L 128     3040   3123   1185    341    224    392       N  
ATOM   5588  CA  GLY L 128     118.643   4.321 -25.865  1.00 33.30           C  
ANISOU 5588  CA  GLY L 128     4787   4853   3014    389    214    395       C  
ATOM   5589  C   GLY L 128     119.199   3.104 -25.139  1.00 42.30           C  
ANISOU 5589  C   GLY L 128     5964   5950   4160    389    247    361       C  
ATOM   5590  O   GLY L 128     119.225   1.989 -25.659  1.00 16.69           O  
ANISOU 5590  O   GLY L 128     2758   2712    871    343    276    331       O  
ATOM   5591  N   ALA L 129     119.654   3.339 -23.908  1.00 15.83           N  
ANISOU 5591  N   ALA L 129     2597   2553    865    444    243    367       N  
ATOM   5592  CA  ALA L 129     120.220   2.266 -23.095  1.00 15.68           C  
ANISOU 5592  CA  ALA L 129     2614   2486    860    455    270    341       C  
ATOM   5593  C   ALA L 129     119.808   2.474 -21.646  1.00 32.40           C  
ANISOU 5593  C   ALA L 129     4719   4577   3016    476    250    335       C  
ATOM   5594  O   ALA L 129     120.305   3.388 -20.984  1.00 25.02           O  
ANISOU 5594  O   ALA L 129     3754   3620   2135    536    235    360       O  
ATOM   5595  CB  ALA L 129     121.741   2.216 -23.228  1.00 39.77           C  
ANISOU 5595  CB  ALA L 129     5675   5493   3942    517    298    360       C  
ATOM   5596  N   SER L 130     118.914   1.623 -21.153  1.00 15.29           N  
ANISOU 5596  N   SER L 130     2572   2415    821    425    252    300       N  
ATOM   5597  CA  SER L 130     118.496   1.640 -19.759  1.00 14.91           C  
ANISOU 5597  CA  SER L 130     2519   2343    803    438    239    289       C  
ATOM   5598  C   SER L 130     118.944   0.352 -19.086  1.00 14.91           C  
ANISOU 5598  C   SER L 130     2563   2298    804    437    268    261       C  
ATOM   5599  O   SER L 130     118.651  -0.744 -19.574  1.00 40.90           O  
ANISOU 5599  O   SER L 130     5885   5604   4053    385    291    232       O  
ATOM   5600  CB  SER L 130     116.979   1.801 -19.639  1.00 14.99           C  
ANISOU 5600  CB  SER L 130     2515   2399    783    381    215    273       C  
ATOM   5601  OG  SER L 130     116.556   3.043 -20.170  1.00 15.00           O  
ANISOU 5601  OG  SER L 130     2476   2435    787    391    185    302       O  
ATOM   5602  N   VAL L 131     119.661   0.488 -17.975  1.00 14.53           N  
ANISOU 5602  N   VAL L 131     2520   2196    805    495    267    270       N  
ATOM   5603  CA  VAL L 131     120.082  -0.644 -17.159  1.00 48.78           C  
ANISOU 5603  CA  VAL L 131     6901   6482   5151    503    291    249       C  
ATOM   5604  C   VAL L 131     119.193  -0.672 -15.926  1.00 14.28           C  
ANISOU 5604  C   VAL L 131     2526   2110    789    486    273    233       C  
ATOM   5605  O   VAL L 131     119.145   0.302 -15.167  1.00 13.92           O  
ANISOU 5605  O   VAL L 131     2452   2060    779    522    248    250       O  
ATOM   5606  CB  VAL L 131     121.565  -0.541 -16.773  1.00 21.79           C  
ANISOU 5606  CB  VAL L 131     3498   3002   1779    580    305    270       C  
ATOM   5607  CG1 VAL L 131     122.056  -1.861 -16.194  1.00 14.41           C  
ANISOU 5607  CG1 VAL L 131     2619   2012    843    586    335    250       C  
ATOM   5608  CG2 VAL L 131     122.399  -0.128 -17.977  1.00 15.04           C  
ANISOU 5608  CG2 VAL L 131     2633   2158    922    604    318    294       C  
ATOM   5609  N   VAL L 132     118.489  -1.779 -15.719  1.00 14.50           N  
ANISOU 5609  N   VAL L 132     2581   2145    784    433    288    201       N  
ATOM   5610  CA  VAL L 132     117.494  -1.869 -14.659  1.00 14.36           C  
ANISOU 5610  CA  VAL L 132     2557   2135    766    406    274    183       C  
ATOM   5611  C   VAL L 132     118.049  -2.717 -13.524  1.00 14.25           C  
ANISOU 5611  C   VAL L 132     2584   2057    775    433    290    174       C  
ATOM   5612  O   VAL L 132     118.905  -3.583 -13.727  1.00 14.42           O  
ANISOU 5612  O   VAL L 132     2645   2037    797    450    317    171       O  
ATOM   5613  CB  VAL L 132     116.162  -2.439 -15.194  1.00 14.73           C  
ANISOU 5613  CB  VAL L 132     2597   2241    757    325    277    153       C  
ATOM   5614  CG1 VAL L 132     115.042  -2.253 -14.180  1.00 14.58           C  
ANISOU 5614  CG1 VAL L 132     2562   2240    738    299    259    140       C  
ATOM   5615  CG2 VAL L 132     115.800  -1.764 -16.504  1.00 19.12           C  
ANISOU 5615  CG2 VAL L 132     3125   2853   1285    298    265    164       C  
ATOM   5616  N   CYS L 133     117.571  -2.445 -12.312  1.00 14.00           N  
ANISOU 5616  N   CYS L 133     2544   2015    760    439    273    171       N  
ATOM   5617  CA  CYS L 133     117.972  -3.187 -11.124  1.00 13.91           C  
ANISOU 5617  CA  CYS L 133     2572   1946    768    460    284    164       C  
ATOM   5618  C   CYS L 133     116.760  -3.310 -10.215  1.00 22.28           C  
ANISOU 5618  C   CYS L 133     3622   3029   1815    419    274    143       C  
ATOM   5619  O   CYS L 133     116.148  -2.298  -9.855  1.00 31.42           O  
ANISOU 5619  O   CYS L 133     4742   4216   2981    419    248    150       O  
ATOM   5620  CB  CYS L 133     119.132  -2.491 -10.402  1.00 13.56           C  
ANISOU 5620  CB  CYS L 133     2528   1849    773    538    275    190       C  
ATOM   5621  SG  CYS L 133     120.004  -3.522  -9.204  1.00 42.30           S  
ANISOU 5621  SG  CYS L 133     6230   5408   4434    575    294    186       S  
ATOM   5622  N   PHE L 134     116.407  -4.543  -9.859  1.00 16.72           N  
ANISOU 5622  N   PHE L 134     2952   2311   1089    384    296    119       N  
ATOM   5623  CA  PHE L 134     115.239  -4.835  -9.037  1.00 16.33           C  
ANISOU 5623  CA  PHE L 134     2897   2286   1023    341    292     97       C  
ATOM   5624  C   PHE L 134     115.678  -5.298  -7.655  1.00 18.78           C  
ANISOU 5624  C   PHE L 134     3245   2534   1358    371    297     99       C  
ATOM   5625  O   PHE L 134     116.509  -6.206  -7.535  1.00 37.70           O  
ANISOU 5625  O   PHE L 134     5691   4874   3761    392    318    101       O  
ATOM   5626  CB  PHE L 134     114.360  -5.906  -9.688  1.00 14.80           C  
ANISOU 5626  CB  PHE L 134     2709   2131    783    277    313     66       C  
ATOM   5627  CG  PHE L 134     113.501  -5.393 -10.808  1.00 17.98           C  
ANISOU 5627  CG  PHE L 134     3067   2612   1152    233    303     58       C  
ATOM   5628  CD1 PHE L 134     112.809  -4.200 -10.679  1.00 24.35           C  
ANISOU 5628  CD1 PHE L 134     3831   3460   1962    226    275     67       C  
ATOM   5629  CD2 PHE L 134     113.386  -6.103 -11.991  1.00 16.82           C  
ANISOU 5629  CD2 PHE L 134     2927   2494    968    202    322     42       C  
ATOM   5630  CE1 PHE L 134     112.016  -3.727 -11.710  1.00 14.77           C  
ANISOU 5630  CE1 PHE L 134     2584   2313    716    185    265     63       C  
ATOM   5631  CE2 PHE L 134     112.598  -5.635 -13.026  1.00 29.69           C  
ANISOU 5631  CE2 PHE L 134     4520   4199   2564    163    311     36       C  
ATOM   5632  CZ  PHE L 134     111.912  -4.445 -12.885  1.00 23.46           C  
ANISOU 5632  CZ  PHE L 134     3690   3447   1777    152    282     48       C  
ATOM   5633  N   LEU L 135     115.118  -4.673  -6.620  1.00 13.85           N  
ANISOU 5633  N   LEU L 135     2600   1918    744    372    277    100       N  
ATOM   5634  CA  LEU L 135     115.323  -5.078  -5.231  1.00 13.77           C  
ANISOU 5634  CA  LEU L 135     2623   1860    750    391    280     99       C  
ATOM   5635  C   LEU L 135     113.981  -5.590  -4.723  1.00 26.18           C  
ANISOU 5635  C   LEU L 135     4187   3468   2291    332    286     73       C  
ATOM   5636  O   LEU L 135     113.089  -4.800  -4.401  1.00 50.20           O  
ANISOU 5636  O   LEU L 135     7189   6555   5328    314    268     67       O  
ATOM   5637  CB  LEU L 135     115.825  -3.918  -4.381  1.00 32.85           C  
ANISOU 5637  CB  LEU L 135     5021   4258   3203    445    254    120       C  
ATOM   5638  CG  LEU L 135     116.761  -2.898  -5.023  1.00 28.76           C  
ANISOU 5638  CG  LEU L 135     4479   3734   2714    499    239    145       C  
ATOM   5639  CD1 LEU L 135     116.938  -1.739  -4.072  1.00 27.36           C  
ANISOU 5639  CD1 LEU L 135     4276   3550   2568    542    213    157       C  
ATOM   5640  CD2 LEU L 135     118.102  -3.517  -5.367  1.00 15.85           C  
ANISOU 5640  CD2 LEU L 135     2884   2043   1094    541    258    157       C  
ATOM   5641  N   ASN L 136     113.836  -6.908  -4.649  1.00 24.73           N  
ANISOU 5641  N   ASN L 136     4045   3265   2088    306    312     56       N  
ATOM   5642  CA  ASN L 136     112.547  -7.520  -4.370  1.00 14.61           C  
ANISOU 5642  CA  ASN L 136     2758   2020    772    252    323     28       C  
ATOM   5643  C   ASN L 136     112.448  -7.955  -2.915  1.00 14.61           C  
ANISOU 5643  C   ASN L 136     2790   1981    781    257    328     27       C  
ATOM   5644  O   ASN L 136     113.395  -8.519  -2.358  1.00 19.65           O  
ANISOU 5644  O   ASN L 136     3477   2552   1438    289    337     40       O  
ATOM   5645  CB  ASN L 136     112.308  -8.720  -5.286  1.00 47.31           C  
ANISOU 5645  CB  ASN L 136     6925   6168   4884    218    351      8       C  
ATOM   5646  CG  ASN L 136     112.181  -8.321  -6.737  1.00 34.95           C  
ANISOU 5646  CG  ASN L 136     5325   4654   3300    203    347      5       C  
ATOM   5647  OD1 ASN L 136     111.630  -7.267  -7.056  1.00 14.97           O  
ANISOU 5647  OD1 ASN L 136     2744   2181    765    193    325      8       O  
ATOM   5648  ND2 ASN L 136     112.699  -9.157  -7.628  1.00 51.39           N  
ANISOU 5648  ND2 ASN L 136     7437   6719   5372    200    369     -1       N  
ATOM   5649  N   ASN L 137     111.293  -7.672  -2.308  1.00 14.67           N  
ANISOU 5649  N   ASN L 137     2771   2031    771    226    322     12       N  
ATOM   5650  CA  ASN L 137     110.907  -8.220  -1.013  1.00 14.79           C  
ANISOU 5650  CA  ASN L 137     2815   2023    783    217    331      4       C  
ATOM   5651  C   ASN L 137     111.929  -7.949   0.083  1.00 14.52           C  
ANISOU 5651  C   ASN L 137     2808   1928    782    266    320     28       C  
ATOM   5652  O   ASN L 137     112.668  -8.853   0.489  1.00 32.92           O  
ANISOU 5652  O   ASN L 137     5193   4196   3119    282    335     35       O  
ATOM   5653  CB  ASN L 137     110.660  -9.724  -1.140  1.00 15.24           C  
ANISOU 5653  CB  ASN L 137     2920   2054    816    188    363    -12       C  
ATOM   5654  CG  ASN L 137     109.620 -10.053  -2.189  1.00 20.92           C  
ANISOU 5654  CG  ASN L 137     3613   2834   1501    142    374    -38       C  
ATOM   5655  OD1 ASN L 137     109.918 -10.098  -3.381  1.00 26.38           O  
ANISOU 5655  OD1 ASN L 137     4296   3539   2186    141    376    -39       O  
ATOM   5656  ND2 ASN L 137     108.390 -10.289  -1.751  1.00 44.58           N  
ANISOU 5656  ND2 ASN L 137     6597   5869   4474    107    381    -60       N  
ATOM   5657  N   PHE L 138     111.969  -6.714   0.575  1.00 14.18           N  
ANISOU 5657  N   PHE L 138     2729   1902    758    289    294     38       N  
ATOM   5658  CA  PHE L 138     112.833  -6.343   1.684  1.00 13.96           C  
ANISOU 5658  CA  PHE L 138     2723   1823    758    337    281     57       C  
ATOM   5659  C   PHE L 138     112.043  -5.530   2.700  1.00 13.86           C  
ANISOU 5659  C   PHE L 138     2680   1843    743    328    266     50       C  
ATOM   5660  O   PHE L 138     110.978  -4.986   2.403  1.00 13.87           O  
ANISOU 5660  O   PHE L 138     2636   1905    728    294    261     34       O  
ATOM   5661  CB  PHE L 138     114.066  -5.550   1.215  1.00 13.64           C  
ANISOU 5661  CB  PHE L 138     2677   1756    751    397    263     82       C  
ATOM   5662  CG  PHE L 138     113.739  -4.282   0.472  1.00 13.40           C  
ANISOU 5662  CG  PHE L 138     2588   1777    728    400    242     84       C  
ATOM   5663  CD1 PHE L 138     113.585  -3.082   1.149  1.00 13.85           C  
ANISOU 5663  CD1 PHE L 138     2613   1848    801    423    218     90       C  
ATOM   5664  CD2 PHE L 138     113.604  -4.288  -0.906  1.00 13.47           C  
ANISOU 5664  CD2 PHE L 138     2575   1816    725    381    247     82       C  
ATOM   5665  CE1 PHE L 138     113.289  -1.916   0.467  1.00 12.96           C  
ANISOU 5665  CE1 PHE L 138     2451   1776    696    430    200     95       C  
ATOM   5666  CE2 PHE L 138     113.308  -3.126  -1.594  1.00 13.28           C  
ANISOU 5666  CE2 PHE L 138     2502   1837    707    385    228     88       C  
ATOM   5667  CZ  PHE L 138     113.151  -1.939  -0.906  1.00 34.04           C  
ANISOU 5667  CZ  PHE L 138     5103   4477   3355    411    204     95       C  
ATOM   5668  N   TYR L 139     112.590  -5.454   3.913  1.00 13.79           N  
ANISOU 5668  N   TYR L 139     2699   1792    748    359    259     61       N  
ATOM   5669  CA  TYR L 139     111.998  -4.695   5.000  1.00 13.71           C  
ANISOU 5669  CA  TYR L 139     2667   1805    737    356    245     54       C  
ATOM   5670  C   TYR L 139     113.135  -4.304   5.930  1.00 13.53           C  
ANISOU 5670  C   TYR L 139     2671   1729    741    414    229     74       C  
ATOM   5671  O   TYR L 139     114.012  -5.137   6.198  1.00 13.64           O  
ANISOU 5671  O   TYR L 139     2735   1688    760    436    238     86       O  
ATOM   5672  CB  TYR L 139     110.935  -5.493   5.763  1.00 14.06           C  
ANISOU 5672  CB  TYR L 139     2725   1867    749    307    266     34       C  
ATOM   5673  CG  TYR L 139     110.150  -4.667   6.759  1.00 14.02           C  
ANISOU 5673  CG  TYR L 139     2692   1898    738    297    256     22       C  
ATOM   5674  CD1 TYR L 139     108.993  -4.000   6.379  1.00 18.19           C  
ANISOU 5674  CD1 TYR L 139     3169   2492   1252    264    254      3       C  
ATOM   5675  CD2 TYR L 139     110.571  -4.550   8.075  1.00 14.02           C  
ANISOU 5675  CD2 TYR L 139     2718   1864    744    320    248     30       C  
ATOM   5676  CE1 TYR L 139     108.277  -3.240   7.285  1.00 21.97           C  
ANISOU 5676  CE1 TYR L 139     3623   3002   1724    255    248    -10       C  
ATOM   5677  CE2 TYR L 139     109.864  -3.793   8.985  1.00 14.02           C  
ANISOU 5677  CE2 TYR L 139     2693   1897    736    311    241     18       C  
ATOM   5678  CZ  TYR L 139     108.718  -3.141   8.589  1.00 15.95           C  
ANISOU 5678  CZ  TYR L 139     2888   2205    968    279    242     -3       C  
ATOM   5679  OH  TYR L 139     108.015  -2.389   9.503  1.00 20.80           O  
ANISOU 5679  OH  TYR L 139     3481   2850   1574    271    238    -17       O  
ATOM   5680  N   PRO L 140     113.162  -3.061   6.438  1.00 13.28           N  
ANISOU 5680  N   PRO L 140     2608   1713    726    442    205     78       N  
ATOM   5681  CA  PRO L 140     112.194  -1.977   6.231  1.00 13.16           C  
ANISOU 5681  CA  PRO L 140     2539   1757    707    424    193     66       C  
ATOM   5682  C   PRO L 140     112.229  -1.356   4.836  1.00 12.99           C  
ANISOU 5682  C   PRO L 140     2478   1761    695    432    185     72       C  
ATOM   5683  O   PRO L 140     113.007  -1.773   3.980  1.00 12.95           O  
ANISOU 5683  O   PRO L 140     2488   1732    701    448    190     84       O  
ATOM   5684  CB  PRO L 140     112.606  -0.935   7.281  1.00 28.71           C  
ANISOU 5684  CB  PRO L 140     4500   3712   2695    469    170     72       C  
ATOM   5685  CG  PRO L 140     113.468  -1.673   8.256  1.00 13.09           C  
ANISOU 5685  CG  PRO L 140     2575   1678    720    491    173     82       C  
ATOM   5686  CD  PRO L 140     114.174  -2.697   7.441  1.00 13.16           C  
ANISOU 5686  CD  PRO L 140     2616   1653    732    495    188     92       C  
ATOM   5687  N   LYS L 141     111.374  -0.351   4.627  1.00 43.41           N  
ANISOU 5687  N   LYS L 141     6286   5663   4544    421    174     63       N  
ATOM   5688  CA  LYS L 141     111.271   0.289   3.321  1.00 45.10           C  
ANISOU 5688  CA  LYS L 141     6463   5908   4764    425    165     70       C  
ATOM   5689  C   LYS L 141     112.508   1.115   2.995  1.00 12.48           C  
ANISOU 5689  C   LYS L 141     2324   1746    671    494    145     95       C  
ATOM   5690  O   LYS L 141     112.863   1.259   1.819  1.00 12.41           O  
ANISOU 5690  O   LYS L 141     2301   1744    670    504    143    106       O  
ATOM   5691  CB  LYS L 141     110.017   1.164   3.273  1.00 12.81           C  
ANISOU 5691  CB  LYS L 141     2332   1876    660    400    159     55       C  
ATOM   5692  CG  LYS L 141     109.747   1.821   1.933  1.00 12.75           C  
ANISOU 5692  CG  LYS L 141     2287   1904    652    400    149     62       C  
ATOM   5693  CD  LYS L 141     108.474   2.652   1.989  1.00 46.83           C  
ANISOU 5693  CD  LYS L 141     6567   6273   4952    380    143     47       C  
ATOM   5694  CE  LYS L 141     108.176   3.315   0.655  1.00 32.25           C  
ANISOU 5694  CE  LYS L 141     4687   4463   3104    383    131     58       C  
ATOM   5695  NZ  LYS L 141     106.884   4.057   0.691  1.00 36.28           N  
ANISOU 5695  NZ  LYS L 141     5164   5023   3596    367    126     44       N  
ATOM   5696  N   ASP L 142     113.177   1.653   4.011  1.00 12.32           N  
ANISOU 5696  N   ASP L 142     2312   1695    674    541    130    102       N  
ATOM   5697  CA  ASP L 142     114.336   2.504   3.781  1.00 12.05           C  
ANISOU 5697  CA  ASP L 142     2265   1637    678    608    112    122       C  
ATOM   5698  C   ASP L 142     115.491   1.693   3.206  1.00 12.06           C  
ANISOU 5698  C   ASP L 142     2296   1594    690    627    123    134       C  
ATOM   5699  O   ASP L 142     115.899   0.680   3.782  1.00 32.12           O  
ANISOU 5699  O   ASP L 142     4882   4097   3224    621    137    132       O  
ATOM   5700  CB  ASP L 142     114.759   3.176   5.085  1.00 11.94           C  
ANISOU 5700  CB  ASP L 142     2254   1601    682    649     96    120       C  
ATOM   5701  CG  ASP L 142     115.832   4.223   4.876  1.00 11.68           C  
ANISOU 5701  CG  ASP L 142     2196   1554    688    714     78    133       C  
ATOM   5702  OD1 ASP L 142     115.998   4.684   3.727  1.00 11.57           O  
ANISOU 5702  OD1 ASP L 142     2151   1558    687    726     76    143       O  
ATOM   5703  OD2 ASP L 142     116.514   4.579   5.859  1.00 19.11           O  
ANISOU 5703  OD2 ASP L 142     3148   2469   1645    750     67    130       O  
ATOM   5704  N   ILE L 143     116.023   2.147   2.071  1.00 11.52           N  
ANISOU 5704  N   ILE L 143     1874   1855    647    -23   -308   -325       N  
ATOM   5705  CA  ILE L 143     117.139   1.473   1.418  1.00 11.01           C  
ANISOU 5705  CA  ILE L 143     1774   1812    597    -19   -318   -242       C  
ATOM   5706  C   ILE L 143     117.816   2.476   0.496  1.00 10.89           C  
ANISOU 5706  C   ILE L 143     1763   1770    604    -60   -288   -304       C  
ATOM   5707  O   ILE L 143     117.162   3.352  -0.076  1.00 50.21           O  
ANISOU 5707  O   ILE L 143     6778   6679   5621    -85   -242   -370       O  
ATOM   5708  CB  ILE L 143     116.661   0.209   0.658  1.00 30.87           C  
ANISOU 5708  CB  ILE L 143     4213   4353   3162      3   -289   -151       C  
ATOM   5709  CG1 ILE L 143     117.848  -0.607   0.148  1.00 13.60           C  
ANISOU 5709  CG1 ILE L 143     2029   2170    967     24   -278    -49       C  
ATOM   5710  CG2 ILE L 143     115.737   0.582  -0.488  1.00 14.07           C  
ANISOU 5710  CG2 ILE L 143     2141   2128   1079    -45   -277   -174       C  
ATOM   5711  CD1 ILE L 143     117.451  -1.927  -0.462  1.00  9.66           C  
ANISOU 5711  CD1 ILE L 143     1587   1612    470      4   -260     36       C  
ATOM   5712  N   ASN L 144     119.134   2.355   0.363  1.00 16.56           N  
ANISOU 5712  N   ASN L 144     2494   2507   1291    -84   -308   -255       N  
ATOM   5713  CA  ASN L 144     119.917   3.235  -0.492  1.00 17.63           C  
ANISOU 5713  CA  ASN L 144     2671   2584   1443   -147   -282   -290       C  
ATOM   5714  C   ASN L 144     120.498   2.447  -1.661  1.00 34.90           C  
ANISOU 5714  C   ASN L 144     4858   4747   3657   -104   -274   -171       C  
ATOM   5715  O   ASN L 144     120.848   1.271  -1.526  1.00 27.95           O  
ANISOU 5715  O   ASN L 144     3931   3939   2750    -44   -281    -65       O  
ATOM   5716  CB  ASN L 144     121.041   3.912   0.299  1.00 40.96           C  
ANISOU 5716  CB  ASN L 144     5622   5623   4316   -320   -283   -333       C  
ATOM   5717  CG  ASN L 144     121.926   4.785  -0.569  1.00 60.20           C  
ANISOU 5717  CG  ASN L 144     8125   7995   6755   -426   -245   -370       C  
ATOM   5718  OD1 ASN L 144     121.477   5.350  -1.566  1.00 89.29           O  
ANISOU 5718  OD1 ASN L 144    11931  11493  10503   -382   -200   -399       O  
ATOM   5719  ND2 ASN L 144     123.196   4.896  -0.195  1.00 53.05           N  
ANISOU 5719  ND2 ASN L 144     7131   7262   5763   -592   -251   -345       N  
ATOM   5720  N   VAL L 145     120.596   3.108  -2.815  1.00 14.99           N  
ANISOU 5720  N   VAL L 145     2443   2078   1174   -120   -252   -174       N  
ATOM   5721  CA  VAL L 145     121.060   2.478  -4.047  1.00  9.67           C  
ANISOU 5721  CA  VAL L 145     1820   1330    525    -66   -243    -83       C  
ATOM   5722  C   VAL L 145     122.040   3.410  -4.745  1.00 20.92           C  
ANISOU 5722  C   VAL L 145     3346   2690   1913   -104   -232    -78       C  
ATOM   5723  O   VAL L 145     121.762   4.604  -4.906  1.00 42.21           O  
ANISOU 5723  O   VAL L 145     6162   5274   4602   -145   -210   -141       O  
ATOM   5724  CB  VAL L 145     119.888   2.128  -4.985  1.00  9.06           C  
ANISOU 5724  CB  VAL L 145     1783   1153    508     -3   -237    -79       C  
ATOM   5725  CG1 VAL L 145     120.387   1.847  -6.394  1.00 26.82           C  
ANISOU 5725  CG1 VAL L 145     4103   3337   2750     35   -217    -41       C  
ATOM   5726  CG2 VAL L 145     119.149   0.930  -4.453  1.00  8.78           C  
ANISOU 5726  CG2 VAL L 145     1683   1166    485      1   -238    -75       C  
ATOM   5727  N   LYS L 146     123.182   2.865  -5.160  1.00 10.43           N  
ANISOU 5727  N   LYS L 146     2000   1417    545    -90   -223     13       N  
ATOM   5728  CA  LYS L 146     124.181   3.598  -5.926  1.00 22.09           C  
ANISOU 5728  CA  LYS L 146     3564   2853   1976   -129   -199     53       C  
ATOM   5729  C   LYS L 146     124.516   2.815  -7.185  1.00 10.81           C  
ANISOU 5729  C   LYS L 146     2156   1372    580     -9   -149    142       C  
ATOM   5730  O   LYS L 146     124.832   1.624  -7.112  1.00 13.54           O  
ANISOU 5730  O   LYS L 146     2448   1767    930     51   -116    213       O  
ATOM   5731  CB  LYS L 146     125.457   3.836  -5.108  1.00 26.35           C  
ANISOU 5731  CB  LYS L 146     4008   3593   2411   -279   -217     96       C  
ATOM   5732  CG  LYS L 146     125.318   4.853  -3.990  1.00 38.50           C  
ANISOU 5732  CG  LYS L 146     5520   5200   3908   -498   -229    -71       C  
ATOM   5733  CD  LYS L 146     126.615   4.975  -3.203  1.00 34.35           C  
ANISOU 5733  CD  LYS L 146     4794   4981   3278   -704   -251    -32       C  
ATOM   5734  CE  LYS L 146     126.482   5.978  -2.067  1.00 39.76           C  
ANISOU 5734  CE  LYS L 146     5431   5733   3941   -955   -215   -248       C  
ATOM   5735  NZ  LYS L 146     127.715   6.041  -1.238  1.00 46.88           N  
ANISOU 5735  NZ  LYS L 146     6083   7011   4720  -1186   -233   -204       N  
ATOM   5736  N   TRP L 147     124.443   3.481  -8.332  1.00 33.84           N  
ANISOU 5736  N   TRP L 147     5166   4186   3504     23   -118    146       N  
ATOM   5737  CA  TRP L 147     124.923   2.916  -9.584  1.00 14.83           C  
ANISOU 5737  CA  TRP L 147     2770   1769   1095     99    -55    203       C  
ATOM   5738  C   TRP L 147     126.387   3.281  -9.778  1.00 12.11           C  
ANISOU 5738  C   TRP L 147     2405   1474    724     81      1    324       C  
ATOM   5739  O   TRP L 147     126.810   4.390  -9.441  1.00 12.69           O  
ANISOU 5739  O   TRP L 147     2517   1537    766    -18     -3    352       O  
ATOM   5740  CB  TRP L 147     124.101   3.426 -10.767  1.00 17.83           C  
ANISOU 5740  CB  TRP L 147     3199   2111   1463    138    -53    186       C  
ATOM   5741  CG  TRP L 147     122.767   2.774 -10.905  1.00 11.13           C  
ANISOU 5741  CG  TRP L 147     2326   1292    612    141    -92    111       C  
ATOM   5742  CD1 TRP L 147     121.583   3.210 -10.390  1.00 10.86           C  
ANISOU 5742  CD1 TRP L 147     2264   1263    599    135   -145     84       C  
ATOM   5743  CD2 TRP L 147     122.477   1.565 -11.614  1.00 11.52           C  
ANISOU 5743  CD2 TRP L 147     2391   1378    610    132    -62     58       C  
ATOM   5744  NE1 TRP L 147     120.571   2.346 -10.733  1.00 16.85           N  
ANISOU 5744  NE1 TRP L 147     2968   2106   1330    112   -165     37       N  
ATOM   5745  CE2 TRP L 147     121.095   1.327 -11.484  1.00 11.45           C  
ANISOU 5745  CE2 TRP L 147     2323   1436    593     93   -115      3       C  
ATOM   5746  CE3 TRP L 147     123.252   0.659 -12.344  1.00 12.33           C  
ANISOU 5746  CE3 TRP L 147     2577   1456    652    147     34     44       C  
ATOM   5747  CZ2 TRP L 147     120.472   0.225 -12.059  1.00 12.26           C  
ANISOU 5747  CZ2 TRP L 147     2429   1608    621     34    -92    -85       C  
ATOM   5748  CZ3 TRP L 147     122.632  -0.436 -12.912  1.00 13.22           C  
ANISOU 5748  CZ3 TRP L 147     2741   1585    696     94     82    -62       C  
ATOM   5749  CH2 TRP L 147     121.257  -0.645 -12.766  1.00 17.01           C  
ANISOU 5749  CH2 TRP L 147     3142   2158   1164     21      8   -135       C  
ATOM   5750  N   LYS L 148     127.161   2.343 -10.318  1.00 18.49           N  
ANISOU 5750  N   LYS L 148     3180   2312   1535    156     83    401       N  
ATOM   5751  CA  LYS L 148     128.583   2.570 -10.550  1.00 18.61           C  
ANISOU 5751  CA  LYS L 148     3123   2403   1543    155    153    555       C  
ATOM   5752  C   LYS L 148     128.963   2.013 -11.912  1.00 16.18           C  
ANISOU 5752  C   LYS L 148     2866   2041   1241    260    273    570       C  
ATOM   5753  O   LYS L 148     128.857   0.806 -12.144  1.00 29.47           O  
ANISOU 5753  O   LYS L 148     4604   3665   2927    358    374    543       O  
ATOM   5754  CB  LYS L 148     129.436   1.936  -9.446  1.00 21.56           C  
ANISOU 5754  CB  LYS L 148     3344   2932   1915    149    163    694       C  
ATOM   5755  CG  LYS L 148     129.495   2.768  -8.172  1.00 17.82           C  
ANISOU 5755  CG  LYS L 148     2780   2633   1358    -21     56    694       C  
ATOM   5756  CD  LYS L 148     130.303   2.083  -7.083  1.00 17.71           C  
ANISOU 5756  CD  LYS L 148     2509   2870   1351    -27     43    831       C  
ATOM   5757  CE  LYS L 148     130.402   2.965  -5.847  1.00 18.55           C  
ANISOU 5757  CE  LYS L 148     2467   3239   1342   -294    -80    765       C  
ATOM   5758  NZ  LYS L 148     131.040   2.262  -4.700  1.00 20.56           N  
ANISOU 5758  NZ  LYS L 148     2424   3805   1584   -296   -112    907       N  
ATOM   5759  N   ILE L 149     129.403   2.896 -12.802  1.00 19.86           N  
ANISOU 5759  N   ILE L 149     3341   2513   1693    241    297    616       N  
ATOM   5760  CA  ILE L 149     129.865   2.526 -14.134  1.00 15.94           C  
ANISOU 5760  CA  ILE L 149     2885   2010   1160    325    416    637       C  
ATOM   5761  C   ILE L 149     131.387   2.487 -14.106  1.00 31.93           C  
ANISOU 5761  C   ILE L 149     4787   4110   3236    356    513    803       C  
ATOM   5762  O   ILE L 149     132.037   3.520 -13.901  1.00 17.60           O  
ANISOU 5762  O   ILE L 149     2891   2357   1440    260    480    903       O  
ATOM   5763  CB  ILE L 149     129.356   3.511 -15.197  1.00 16.23           C  
ANISOU 5763  CB  ILE L 149     2967   2055   1143    296    382    627       C  
ATOM   5764  CG1 ILE L 149     127.837   3.666 -15.095  1.00 25.85           C  
ANISOU 5764  CG1 ILE L 149     4234   3259   2329    270    276    517       C  
ATOM   5765  CG2 ILE L 149     129.747   3.040 -16.580  1.00 17.57           C  
ANISOU 5765  CG2 ILE L 149     3182   2273   1219    361    499    634       C  
ATOM   5766  CD1 ILE L 149     127.270   4.731 -16.009  1.00 16.18           C  
ANISOU 5766  CD1 ILE L 149     3001   2084   1065    268    249    589       C  
ATOM   5767  N   ASP L 150     131.950   1.293 -14.303  1.00 52.64           N  
ANISOU 5767  N   ASP L 150     7396   6717   5888    495    670    846       N  
ATOM   5768  CA  ASP L 150     133.398   1.076 -14.247  1.00 19.72           C  
ANISOU 5768  CA  ASP L 150     3053   2646   1795    574    784   1036       C  
ATOM   5769  C   ASP L 150     133.991   1.618 -12.949  1.00 19.85           C  
ANISOU 5769  C   ASP L 150     2855   2839   1846    462    663   1166       C  
ATOM   5770  O   ASP L 150     135.075   2.202 -12.930  1.00 33.01           O  
ANISOU 5770  O   ASP L 150     4355   4659   3527    409    671   1309       O  
ATOM   5771  CB  ASP L 150     134.097   1.686 -15.463  1.00 20.79           C  
ANISOU 5771  CB  ASP L 150     3192   2810   1898    581    856   1084       C  
ATOM   5772  CG  ASP L 150     133.904   0.860 -16.722  1.00 38.66           C  
ANISOU 5772  CG  ASP L 150     5623   4972   4095    708   1041    995       C  
ATOM   5773  OD1 ASP L 150     133.740  -0.374 -16.607  1.00 38.37           O  
ANISOU 5773  OD1 ASP L 150     5670   4818   4093    829   1202    953       O  
ATOM   5774  OD2 ASP L 150     133.921   1.442 -17.826  1.00 35.93           O  
ANISOU 5774  OD2 ASP L 150     5332   4661   3658    674   1049    970       O  
ATOM   5775  N   GLY L 151     133.264   1.426 -11.849  1.00 18.86           N  
ANISOU 5775  N   GLY L 151     2726   2729   1710    405    556   1114       N  
ATOM   5776  CA  GLY L 151     133.707   1.876 -10.549  1.00 19.37           C  
ANISOU 5776  CA  GLY L 151     2585   3024   1751    272    444   1213       C  
ATOM   5777  C   GLY L 151     133.406   3.321 -10.220  1.00 44.80           C  
ANISOU 5777  C   GLY L 151     5847   6294   4880     29    330   1140       C  
ATOM   5778  O   GLY L 151     133.603   3.729  -9.068  1.00 49.65           O  
ANISOU 5778  O   GLY L 151     6294   7143   5428   -160    232   1163       O  
ATOM   5779  N   SER L 152     132.934   4.112 -11.181  1.00 27.50           N  
ANISOU 5779  N   SER L 152     3851   3915   2682      7    357   1060       N  
ATOM   5780  CA  SER L 152     132.646   5.520 -10.944  1.00 35.20           C  
ANISOU 5780  CA  SER L 152     4875   4834   3667   -216    306    960       C  
ATOM   5781  C   SER L 152     131.176   5.695 -10.582  1.00 28.87           C  
ANISOU 5781  C   SER L 152     4249   3851   2867   -217    227    763       C  
ATOM   5782  O   SER L 152     130.295   5.175 -11.274  1.00 22.07           O  
ANISOU 5782  O   SER L 152     3541   2863   1981    -46    235    732       O  
ATOM   5783  CB  SER L 152     132.996   6.354 -12.177  1.00 44.69           C  
ANISOU 5783  CB  SER L 152     6153   5908   4918   -207    411   1026       C  
ATOM   5784  OG  SER L 152     134.362   6.198 -12.519  1.00 56.66           O  
ANISOU 5784  OG  SER L 152     7491   7606   6433   -205    494   1218       O  
ATOM   5785  N   GLU L 153     130.917   6.427  -9.501  1.00 36.93           N  
ANISOU 5785  N   GLU L 153     5238   4892   3902   -432    165    619       N  
ATOM   5786  CA  GLU L 153     129.549   6.608  -9.033  1.00 16.22           C  
ANISOU 5786  CA  GLU L 153     2757   2115   1291   -423    113    448       C  
ATOM   5787  C   GLU L 153     128.762   7.473 -10.009  1.00 16.16           C  
ANISOU 5787  C   GLU L 153     2928   1838   1374   -338    192    437       C  
ATOM   5788  O   GLU L 153     129.235   8.526 -10.447  1.00 33.43           O  
ANISOU 5788  O   GLU L 153     5134   3909   3660   -427    302    474       O  
ATOM   5789  CB  GLU L 153     129.539   7.235  -7.640  1.00 20.71           C  
ANISOU 5789  CB  GLU L 153     3251   2777   1840   -693     76    273       C  
ATOM   5790  CG  GLU L 153     128.145   7.386  -7.050  1.00 18.82           C  
ANISOU 5790  CG  GLU L 153     3142   2392   1615   -671     48    102       C  
ATOM   5791  CD  GLU L 153     128.165   7.649  -5.558  1.00 47.86           C  
ANISOU 5791  CD  GLU L 153     6727   6250   5209   -930      8    -82       C  
ATOM   5792  OE1 GLU L 153     129.269   7.791  -4.990  1.00 59.13           O  
ANISOU 5792  OE1 GLU L 153     7972   7951   6544  -1165    -10    -82       O  
ATOM   5793  OE2 GLU L 153     127.074   7.710  -4.952  1.00 57.31           O  
ANISOU 5793  OE2 GLU L 153     8011   7360   6403   -914     -4   -222       O  
ATOM   5794  N   ARG L 154     127.554   7.025 -10.343  1.00 28.81           N  
ANISOU 5794  N   ARG L 154     4638   3367   2941   -170    149    418       N  
ATOM   5795  CA  ARG L 154     126.703   7.685 -11.325  1.00 15.21           C  
ANISOU 5795  CA  ARG L 154     3026   1495   1258    -45    208    488       C  
ATOM   5796  C   ARG L 154     125.293   7.778 -10.766  1.00 20.34           C  
ANISOU 5796  C   ARG L 154     3733   2076   1919      1    162    396       C  
ATOM   5797  O   ARG L 154     124.680   6.753 -10.448  1.00 28.21           O  
ANISOU 5797  O   ARG L 154     4724   3179   2814     47     55    331       O  
ATOM   5798  CB  ARG L 154     126.708   6.919 -12.651  1.00 14.95           C  
ANISOU 5798  CB  ARG L 154     2947   1589   1144    109    189    573       C  
ATOM   5799  CG  ARG L 154     125.760   7.464 -13.701  1.00 15.68           C  
ANISOU 5799  CG  ARG L 154     3025   1688   1246    214    202    652       C  
ATOM   5800  CD  ARG L 154     126.155   8.862 -14.129  1.00 17.44           C  
ANISOU 5800  CD  ARG L 154     3268   1767   1592    216    336    812       C  
ATOM   5801  NE  ARG L 154     125.538   9.232 -15.398  1.00 65.35           N  
ANISOU 5801  NE  ARG L 154     9260   7937   7633    329    341    955       N  
ATOM   5802  CZ  ARG L 154     126.110   9.053 -16.585  1.00 59.85           C  
ANISOU 5802  CZ  ARG L 154     8507   7382   6852    347    346   1037       C  
ATOM   5803  NH1 ARG L 154     125.477   9.419 -17.690  1.00 88.55           N  
ANISOU 5803  NH1 ARG L 154    12084  11141  10420    426    344   1171       N  
ATOM   5804  NH2 ARG L 154     127.317   8.511 -16.665  1.00 19.15           N  
ANISOU 5804  NH2 ARG L 154     3350   2262   1665    290    364    998       N  
ATOM   5805  N   GLN L 155     124.782   9.004 -10.642  1.00 22.63           N  
ANISOU 5805  N   GLN L 155     4075   2167   2356     -8    280    403       N  
ATOM   5806  CA  GLN L 155     123.423   9.228 -10.175  1.00 23.72           C  
ANISOU 5806  CA  GLN L 155     4250   2229   2532     73    283    359       C  
ATOM   5807  C   GLN L 155     122.597  10.085 -11.124  1.00 32.00           C  
ANISOU 5807  C   GLN L 155     5321   3168   3669    269    405    584       C  
ATOM   5808  O   GLN L 155     121.413  10.313 -10.854  1.00 36.10           O  
ANISOU 5808  O   GLN L 155     5837   3652   4228    380    429    613       O  
ATOM   5809  CB  GLN L 155     123.432   9.870  -8.779  1.00 19.89           C  
ANISOU 5809  CB  GLN L 155     3793   1605   2159   -114    366    139       C  
ATOM   5810  CG  GLN L 155     123.947   8.942  -7.691  1.00 41.17           C  
ANISOU 5810  CG  GLN L 155     6411   4517   4714   -281    219    -31       C  
ATOM   5811  CD  GLN L 155     123.958   9.592  -6.323  1.00 57.21           C  
ANISOU 5811  CD  GLN L 155     8452   6500   6785   -514    298   -272       C  
ATOM   5812  OE1 GLN L 155     123.770  10.800  -6.198  1.00 55.45           O  
ANISOU 5812  OE1 GLN L 155     8325   6013   6730   -587    508   -358       O  
ATOM   5813  NE2 GLN L 155     124.179   8.789  -5.288  1.00 57.55           N  
ANISOU 5813  NE2 GLN L 155     8394   6801   6670   -636    162   -377       N  
ATOM   5814  N   ASN L 156     123.180  10.561 -12.221  1.00 41.73           N  
ANISOU 5814  N   ASN L 156     6489   4422   4943    319    472    750       N  
ATOM   5815  CA  ASN L 156     122.435  11.313 -13.221  1.00 20.43           C  
ANISOU 5815  CA  ASN L 156     3677   1768   2319    490    541    965       C  
ATOM   5816  C   ASN L 156     121.705  10.341 -14.140  1.00 32.16           C  
ANISOU 5816  C   ASN L 156     5038   3605   3577    564    350   1024       C  
ATOM   5817  O   ASN L 156     122.339   9.544 -14.841  1.00 26.28           O  
ANISOU 5817  O   ASN L 156     4261   3040   2685    502    255    988       O  
ATOM   5818  CB  ASN L 156     123.377  12.210 -14.021  1.00 47.70           C  
ANISOU 5818  CB  ASN L 156     7103   5127   5893    480    680   1100       C  
ATOM   5819  CG  ASN L 156     122.647  13.066 -15.035  1.00 24.92           C  
ANISOU 5819  CG  ASN L 156     4100   2292   3075    664    774   1348       C  
ATOM   5820  OD1 ASN L 156     121.554  13.564 -14.771  1.00 26.16           O  
ANISOU 5820  OD1 ASN L 156     4219   2395   3324    785    855   1418       O  
ATOM   5821  ND2 ASN L 156     123.248  13.235 -16.207  1.00 68.36           N  
ANISOU 5821  ND2 ASN L 156     9532   7917   8523    696    780   1499       N  
ATOM   5822  N   GLY L 157     120.376  10.403 -14.135  1.00 30.11           N  
ANISOU 5822  N   GLY L 157     4702   3442   3297    665    320   1095       N  
ATOM   5823  CA  GLY L 157     119.578   9.514 -14.953  1.00 20.37           C  
ANISOU 5823  CA  GLY L 157     3348   2545   1845    655    151   1113       C  
ATOM   5824  C   GLY L 157     119.094   8.267 -14.252  1.00 38.28           C  
ANISOU 5824  C   GLY L 157     5631   4919   3996    545      4    903       C  
ATOM   5825  O   GLY L 157     118.834   7.257 -14.917  1.00 27.79           O  
ANISOU 5825  O   GLY L 157     4245   3817   2497    431   -113    827       O  
ATOM   5826  N   VAL L 158     118.963   8.301 -12.928  1.00 59.04           N  
ANISOU 5826  N   VAL L 158     8351   7367   6715    553     34    789       N  
ATOM   5827  CA  VAL L 158     118.510   7.161 -12.142  1.00 15.40           C  
ANISOU 5827  CA  VAL L 158     2823   1920   1109    459    -84    589       C  
ATOM   5828  C   VAL L 158     117.109   7.453 -11.627  1.00 16.08           C  
ANISOU 5828  C   VAL L 158     2857   2042   1210    547    -90    656       C  
ATOM   5829  O   VAL L 158     116.810   8.581 -11.219  1.00 17.34           O  
ANISOU 5829  O   VAL L 158     3063   2015   1509    693     55    781       O  
ATOM   5830  CB  VAL L 158     119.469   6.862 -10.974  1.00 13.82           C  
ANISOU 5830  CB  VAL L 158     2766   1531    954    376    -74    403       C  
ATOM   5831  CG1 VAL L 158     119.057   5.585 -10.255  1.00 12.38           C  
ANISOU 5831  CG1 VAL L 158     2513   1441    748    279   -172    228       C  
ATOM   5832  CG2 VAL L 158     120.902   6.767 -11.473  1.00 13.67           C  
ANISOU 5832  CG2 VAL L 158     2774   1481    940    318    -40    398       C  
ATOM   5833  N   LEU L 159     116.250   6.436 -11.652  1.00 29.21           N  
ANISOU 5833  N   LEU L 159     4412   3917   2769    444   -214    575       N  
ATOM   5834  CA  LEU L 159     114.900   6.531 -11.112  1.00 32.40           C  
ANISOU 5834  CA  LEU L 159     4746   4393   3171    505   -239    627       C  
ATOM   5835  C   LEU L 159     114.683   5.403 -10.117  1.00 33.96           C  
ANISOU 5835  C   LEU L 159     4943   4602   3356    364   -308    410       C  
ATOM   5836  O   LEU L 159     114.886   4.231 -10.449  1.00 44.09           O  
ANISOU 5836  O   LEU L 159     6161   5997   4594    188   -351    293       O  
ATOM   5837  CB  LEU L 159     113.844   6.466 -12.220  1.00 29.86           C  
ANISOU 5837  CB  LEU L 159     4277   4331   2737    498   -309    769       C  
ATOM   5838  CG  LEU L 159     113.693   7.694 -13.116  1.00 32.61           C  
ANISOU 5838  CG  LEU L 159     4524   4733   3131    697   -197   1044       C  
ATOM   5839  CD1 LEU L 159     112.566   7.479 -14.109  1.00 36.96           C  
ANISOU 5839  CD1 LEU L 159     4872   5638   3533    695   -263   1167       C  
ATOM   5840  CD2 LEU L 159     113.442   8.938 -12.280  1.00 53.42           C  
ANISOU 5840  CD2 LEU L 159     7169   7140   5987    928      2   1201       C  
ATOM   5841  N   ASN L 160     114.272   5.758  -8.902  1.00 14.28           N  
ANISOU 5841  N   ASN L 160     2523   1986    916    456   -274    372       N  
ATOM   5842  CA  ASN L 160     113.974   4.792  -7.852  1.00 12.83           C  
ANISOU 5842  CA  ASN L 160     2310   1817    749    333   -324    198       C  
ATOM   5843  C   ASN L 160     112.492   4.880  -7.521  1.00 19.01           C  
ANISOU 5843  C   ASN L 160     3002   2731   1490    397   -352    285       C  
ATOM   5844  O   ASN L 160     111.991   5.961  -7.194  1.00 24.54           O  
ANISOU 5844  O   ASN L 160     3750   3366   2208    626   -264    422       O  
ATOM   5845  CB  ASN L 160     114.823   5.051  -6.607  1.00 11.88           C  
ANISOU 5845  CB  ASN L 160     2345   1485    684    325   -282     59       C  
ATOM   5846  CG  ASN L 160     116.301   5.133  -6.919  1.00 29.02           C  
ANISOU 5846  CG  ASN L 160     4588   3549   2890    265   -254     21       C  
ATOM   5847  OD1 ASN L 160     116.750   4.681  -7.973  1.00 11.28           O  
ANISOU 5847  OD1 ASN L 160     2267   1372    645    235   -264     63       O  
ATOM   5848  ND2 ASN L 160     117.070   5.710  -6.002  1.00 55.11           N  
ANISOU 5848  ND2 ASN L 160     8023   6718   6199    215   -204    -75       N  
ATOM   5849  N   SER L 161     111.797   3.748  -7.602  1.00 13.68           N  
ANISOU 5849  N   SER L 161     2207   2213    777    209   -427    237       N  
ATOM   5850  CA  SER L 161     110.364   3.690  -7.345  1.00 14.85           C  
ANISOU 5850  CA  SER L 161     2284   2475    883    242   -481    308       C  
ATOM   5851  C   SER L 161     110.081   2.562  -6.366  1.00 23.70           C  
ANISOU 5851  C   SER L 161     3410   3564   2029     71   -504    173       C  
ATOM   5852  O   SER L 161     110.401   1.401  -6.645  1.00 21.18           O  
ANISOU 5852  O   SER L 161     3119   3170   1758   -106   -492     79       O  
ATOM   5853  CB  SER L 161     109.581   3.487  -8.644  1.00 16.83           C  
ANISOU 5853  CB  SER L 161     2455   2905   1034    229   -549    392       C  
ATOM   5854  OG  SER L 161     108.186   3.567  -8.414  1.00 33.22           O  
ANISOU 5854  OG  SER L 161     4348   5195   3080    300   -556    494       O  
ATOM   5855  N   TRP L 162     109.489   2.904  -5.224  1.00 27.15           N  
ANISOU 5855  N   TRP L 162     3819   4010   2487    188   -475    168       N  
ATOM   5856  CA  TRP L 162     109.076   1.920  -4.234  1.00 20.43           C  
ANISOU 5856  CA  TRP L 162     2961   3141   1659     56   -492     83       C  
ATOM   5857  C   TRP L 162     107.622   1.524  -4.453  1.00 14.58           C  
ANISOU 5857  C   TRP L 162     2133   2542    866     94   -560    131       C  
ATOM   5858  O   TRP L 162     106.776   2.367  -4.760  1.00 20.59           O  
ANISOU 5858  O   TRP L 162     2737   3504   1581    241   -543    283       O  
ATOM   5859  CB  TRP L 162     109.231   2.470  -2.815  1.00 18.30           C  
ANISOU 5859  CB  TRP L 162     2713   2826   1414    174   -420     12       C  
ATOM   5860  CG  TRP L 162     110.629   2.533  -2.306  1.00 15.48           C  
ANISOU 5860  CG  TRP L 162     2422   2333   1128    126   -359    -97       C  
ATOM   5861  CD1 TRP L 162     111.248   1.622  -1.502  1.00 16.69           C  
ANISOU 5861  CD1 TRP L 162     2505   2497   1338      1   -327   -147       C  
ATOM   5862  CD2 TRP L 162     111.582   3.574  -2.543  1.00 33.16           C  
ANISOU 5862  CD2 TRP L 162     4799   4432   3371    220   -318   -136       C  
ATOM   5863  NE1 TRP L 162     112.531   2.027  -1.230  1.00 28.82           N  
ANISOU 5863  NE1 TRP L 162     4073   3961   2916      1   -287   -199       N  
ATOM   5864  CE2 TRP L 162     112.761   3.223  -1.858  1.00 35.58           C  
ANISOU 5864  CE2 TRP L 162     5067   4702   3751     94   -282   -214       C  
ATOM   5865  CE3 TRP L 162     111.555   4.766  -3.273  1.00 31.98           C  
ANISOU 5865  CE3 TRP L 162     4804   4203   3144    419   -280    -66       C  
ATOM   5866  CZ2 TRP L 162     113.903   4.020  -1.880  1.00 38.18           C  
ANISOU 5866  CZ2 TRP L 162     5488   4922   4095     86   -240   -272       C  
ATOM   5867  CZ3 TRP L 162     112.689   5.556  -3.294  1.00 38.71           C  
ANISOU 5867  CZ3 TRP L 162     5770   4856   4081    394   -179   -137       C  
ATOM   5868  CH2 TRP L 162     113.847   5.180  -2.603  1.00 48.21           C  
ANISOU 5868  CH2 TRP L 162     6964   6039   5314    211   -195   -271       C  
ATOM   5869  N   THR L 163     107.335   0.239  -4.277  1.00 14.44           N  
ANISOU 5869  N   THR L 163     2136   2495    855      3   -591     29       N  
ATOM   5870  CA  THR L 163     105.954  -0.209  -4.270  1.00 16.05           C  
ANISOU 5870  CA  THR L 163     2157   2937   1003    -49   -613     72       C  
ATOM   5871  C   THR L 163     105.301   0.115  -2.929  1.00 40.57           C  
ANISOU 5871  C   THR L 163     5185   6103   4127     17   -582    120       C  
ATOM   5872  O   THR L 163     105.960   0.500  -1.958  1.00 14.74           O  
ANISOU 5872  O   THR L 163     2008   2695    898     72   -537     81       O  
ATOM   5873  CB  THR L 163     105.865  -1.713  -4.531  1.00 16.45           C  
ANISOU 5873  CB  THR L 163     2211   3000   1039   -222   -616    -50       C  
ATOM   5874  OG1 THR L 163     106.645  -2.417  -3.555  1.00 14.91           O  
ANISOU 5874  OG1 THR L 163     2122   2616    926   -217   -570   -135       O  
ATOM   5875  CG2 THR L 163     106.368  -2.049  -5.919  1.00 31.89           C  
ANISOU 5875  CG2 THR L 163     4204   4975   2940   -302   -621   -108       C  
ATOM   5876  N   ASP L 164     103.981  -0.037  -2.886  1.00 25.65           N  
ANISOU 5876  N   ASP L 164     3095   4469   2183     -3   -593    209       N  
ATOM   5877  CA  ASP L 164     103.293  -0.078  -1.609  1.00 17.83           C  
ANISOU 5877  CA  ASP L 164     2019   3558   1197     39   -557    238       C  
ATOM   5878  C   ASP L 164     103.620  -1.389  -0.901  1.00 16.81           C  
ANISOU 5878  C   ASP L 164     1984   3298   1104   -118   -561    109       C  
ATOM   5879  O   ASP L 164     104.137  -2.336  -1.501  1.00 16.54           O  
ANISOU 5879  O   ASP L 164     2037   3167   1082   -251   -577     18       O  
ATOM   5880  CB  ASP L 164     101.785   0.071  -1.803  1.00 49.86           C  
ANISOU 5880  CB  ASP L 164     5807   7953   5186     60   -556    405       C  
ATOM   5881  CG  ASP L 164     101.378   1.492  -2.131  1.00 36.07           C  
ANISOU 5881  CG  ASP L 164     3920   6357   3428    325   -489    625       C  
ATOM   5882  OD1 ASP L 164     101.740   2.407  -1.362  1.00 33.89           O  
ANISOU 5882  OD1 ASP L 164     3707   5982   3186    559   -395    664       O  
ATOM   5883  OD2 ASP L 164     100.700   1.696  -3.161  1.00 41.58           O  
ANISOU 5883  OD2 ASP L 164     4439   7286   4073    322   -499    781       O  
ATOM   5884  N   GLN L 165     103.321  -1.439   0.394  1.00 16.62           N  
ANISOU 5884  N   GLN L 165     1923   3310   1083    -82   -521    120       N  
ATOM   5885  CA  GLN L 165     103.612  -2.637   1.170  1.00 16.08           C  
ANISOU 5885  CA  GLN L 165     1904   3170   1036   -204   -506     62       C  
ATOM   5886  C   GLN L 165     102.827  -3.820   0.619  1.00 17.54           C  
ANISOU 5886  C   GLN L 165     1993   3493   1177   -425   -534     60       C  
ATOM   5887  O   GLN L 165     101.592  -3.809   0.613  1.00 40.26           O  
ANISOU 5887  O   GLN L 165     4687   6612   3997   -476   -549    139       O  
ATOM   5888  CB  GLN L 165     103.279  -2.409   2.641  1.00 16.17           C  
ANISOU 5888  CB  GLN L 165     1851   3271   1023   -130   -452    100       C  
ATOM   5889  CG  GLN L 165     103.825  -3.484   3.560  1.00 15.75           C  
ANISOU 5889  CG  GLN L 165     1841   3165    976   -218   -424     94       C  
ATOM   5890  CD  GLN L 165     103.577  -3.178   5.018  1.00 16.12           C  
ANISOU 5890  CD  GLN L 165     1817   3333    976   -143   -361    131       C  
ATOM   5891  OE1 GLN L 165     102.643  -2.455   5.361  1.00 17.06           O  
ANISOU 5891  OE1 GLN L 165     1822   3624   1038    -56   -333    159       O  
ATOM   5892  NE2 GLN L 165     104.419  -3.721   5.888  1.00 15.97           N  
ANISOU 5892  NE2 GLN L 165     1840   3274    955   -163   -326    150       N  
ATOM   5893  N   ASP L 166     103.550  -4.833   0.145  1.00 17.36           N  
ANISOU 5893  N   ASP L 166     2089   3343   1164   -584   -523    -31       N  
ATOM   5894  CA  ASP L 166     102.919  -5.991  -0.474  1.00 19.31           C  
ANISOU 5894  CA  ASP L 166     2293   3696   1348   -885   -517    -95       C  
ATOM   5895  C   ASP L 166     101.981  -6.676   0.511  1.00 20.51           C  
ANISOU 5895  C   ASP L 166     2320   4013   1460  -1037   -506    -37       C  
ATOM   5896  O   ASP L 166     102.383  -7.045   1.617  1.00 19.80           O  
ANISOU 5896  O   ASP L 166     2271   3871   1380  -1025   -480     13       O  
ATOM   5897  CB  ASP L 166     103.986  -6.972  -0.963  1.00 48.26           C  
ANISOU 5897  CB  ASP L 166     6161   7140   5036  -1056   -448   -231       C  
ATOM   5898  CG  ASP L 166     103.405  -8.118  -1.773  1.00 64.69           C  
ANISOU 5898  CG  ASP L 166     8254   9256   7070  -1412   -378   -375       C  
ATOM   5899  OD1 ASP L 166     102.221  -8.042  -2.163  1.00 78.24           O  
ANISOU 5899  OD1 ASP L 166     9795  11230   8702  -1510   -420   -351       O  
ATOM   5900  OD2 ASP L 166     104.137  -9.100  -2.020  1.00 77.76           O  
ANISOU 5900  OD2 ASP L 166    10103  10657   8784  -1595   -240   -519       O  
ATOM   5901  N   SER L 167     100.723  -6.844   0.103  1.00 28.98           N  
ANISOU 5901  N   SER L 167     3217   5333   2463  -1187   -527    -13       N  
ATOM   5902  CA  SER L 167      99.723  -7.453   0.971  1.00 30.38           C  
ANISOU 5902  CA  SER L 167     3238   5696   2608  -1341   -518     58       C  
ATOM   5903  C   SER L 167      99.975  -8.935   1.223  1.00 36.31           C  
ANISOU 5903  C   SER L 167     4085   6296   3416  -1703   -437    -61       C  
ATOM   5904  O   SER L 167      99.380  -9.494   2.150  1.00 26.28           O  
ANISOU 5904  O   SER L 167     2715   5045   2224  -1767   -360     39       O  
ATOM   5905  CB  SER L 167      98.330  -7.258   0.371  1.00 45.47           C  
ANISOU 5905  CB  SER L 167     4927   7930   4419  -1424   -546    126       C  
ATOM   5906  OG  SER L 167      98.283  -7.733  -0.963  1.00 60.69           O  
ANISOU 5906  OG  SER L 167     6901   9889   6268  -1654   -537     -8       O  
ATOM   5907  N   LYS L 168     100.839  -9.579   0.437  1.00 57.54           N  
ANISOU 5907  N   LYS L 168     6993   8708   6162  -1865   -347   -242       N  
ATOM   5908  CA  LYS L 168     101.071 -11.009   0.610  1.00 67.18           C  
ANISOU 5908  CA  LYS L 168     8363   9581   7582  -2118   -104   -331       C  
ATOM   5909  C   LYS L 168     102.033 -11.297   1.758  1.00 58.07           C  
ANISOU 5909  C   LYS L 168     7325   8099   6641  -1834     54   -136       C  
ATOM   5910  O   LYS L 168     101.812 -12.236   2.531  1.00 59.27           O  
ANISOU 5910  O   LYS L 168     7469   8081   6969  -1907    245    -24       O  
ATOM   5911  CB  LYS L 168     101.594 -11.618  -0.692  1.00 88.93           C  
ANISOU 5911  CB  LYS L 168    11327  12126  10336  -2317     14   -588       C  
ATOM   5912  CG  LYS L 168     100.565 -11.655  -1.815  1.00110.49           C  
ANISOU 5912  CG  LYS L 168    13951  15164  12868  -2475    -42   -699       C  
ATOM   5913  CD  LYS L 168     101.096 -12.385  -3.042  1.00116.83           C  
ANISOU 5913  CD  LYS L 168    14952  15773  13666  -2643    127   -938       C  
ATOM   5914  CE  LYS L 168     100.033 -12.507  -4.125  1.00114.62           C  
ANISOU 5914  CE  LYS L 168    14536  15861  13155  -2882     90  -1038       C  
ATOM   5915  NZ  LYS L 168     100.539 -13.246  -5.316  1.00113.31           N  
ANISOU 5915  NZ  LYS L 168    14547  15551  12954  -3082    274  -1287       N  
ATOM   5916  N   ASP L 169     103.106 -10.509   1.890  1.00 54.07           N  
ANISOU 5916  N   ASP L 169     6899   7536   6111  -1524    -14    -66       N  
ATOM   5917  CA  ASP L 169     104.110 -10.763   2.919  1.00 22.45           C  
ANISOU 5917  CA  ASP L 169     2955   3325   2250  -1278    116    142       C  
ATOM   5918  C   ASP L 169     104.550  -9.488   3.632  1.00 25.91           C  
ANISOU 5918  C   ASP L 169     3315   3982   2547   -971    -51    253       C  
ATOM   5919  O   ASP L 169     105.570  -9.503   4.331  1.00 19.34           O  
ANISOU 5919  O   ASP L 169     2515   3076   1759   -785     10    404       O  
ATOM   5920  CB  ASP L 169     105.324 -11.481   2.322  1.00 32.59           C  
ANISOU 5920  CB  ASP L 169     4457   4226   3700  -1283    313     97       C  
ATOM   5921  CG  ASP L 169     105.932 -10.730   1.155  1.00 36.91           C  
ANISOU 5921  CG  ASP L 169     5110   4794   4121  -1265    185    -94       C  
ATOM   5922  OD1 ASP L 169     105.203  -9.961   0.493  1.00 42.95           O  
ANISOU 5922  OD1 ASP L 169     5796   5832   4692  -1354    -14   -229       O  
ATOM   5923  OD2 ASP L 169     107.141 -10.914   0.896  1.00 37.93           O  
ANISOU 5923  OD2 ASP L 169     5380   4686   4346  -1146    299    -69       O  
ATOM   5924  N   SER L 170     103.801  -8.393   3.472  1.00 19.26           N  
ANISOU 5924  N   SER L 170     2360   3422   1537   -926   -232    191       N  
ATOM   5925  CA  SER L 170     104.051  -7.142   4.192  1.00 17.70           C  
ANISOU 5925  CA  SER L 170     2106   3393   1225   -676   -326    246       C  
ATOM   5926  C   SER L 170     105.460  -6.617   3.923  1.00 16.90           C  
ANISOU 5926  C   SER L 170     2149   3155   1118   -544   -342    205       C  
ATOM   5927  O   SER L 170     106.135  -6.103   4.816  1.00 25.72           O  
ANISOU 5927  O   SER L 170     3252   4314   2207   -392   -332    263       O  
ATOM   5928  CB  SER L 170     103.809  -7.311   5.693  1.00 29.10           C  
ANISOU 5928  CB  SER L 170     3433   4967   2656   -588   -260    413       C  
ATOM   5929  OG  SER L 170     102.561  -7.936   5.936  1.00 32.49           O  
ANISOU 5929  OG  SER L 170     3727   5501   3115   -725   -223    472       O  
ATOM   5930  N   THR L 171     105.905  -6.744   2.679  1.00 24.83           N  
ANISOU 5930  N   THR L 171     3274   4008   2152   -625   -356     88       N  
ATOM   5931  CA  THR L 171     107.268  -6.414   2.297  1.00 29.96           C  
ANISOU 5931  CA  THR L 171     4055   4511   2816   -523   -351     61       C  
ATOM   5932  C   THR L 171     107.267  -5.254   1.308  1.00 30.30           C  
ANISOU 5932  C   THR L 171     4097   4511   2906   -397   -413    -52       C  
ATOM   5933  O   THR L 171     106.221  -4.819   0.819  1.00 29.35           O  
ANISOU 5933  O   THR L 171     3892   4479   2781   -402   -455    -76       O  
ATOM   5934  CB  THR L 171     107.970  -7.634   1.688  1.00 15.56           C  
ANISOU 5934  CB  THR L 171     2366   2410   1137   -627   -197     52       C  
ATOM   5935  OG1 THR L 171     109.390  -7.458   1.762  1.00 23.45           O  
ANISOU 5935  OG1 THR L 171     3436   3304   2170   -478   -158    125       O  
ATOM   5936  CG2 THR L 171     107.556  -7.805   0.236  1.00 16.30           C  
ANISOU 5936  CG2 THR L 171     2541   2460   1194   -823   -216   -152       C  
ATOM   5937  N   TYR L 172     108.464  -4.749   1.017  1.00 12.71           N  
ANISOU 5937  N   TYR L 172     1942   2161    725   -274   -400    -75       N  
ATOM   5938  CA  TYR L 172     108.647  -3.672   0.057  1.00 20.46           C  
ANISOU 5938  CA  TYR L 172     2929   3091   1754   -146   -429   -139       C  
ATOM   5939  C   TYR L 172     109.608  -4.108  -1.041  1.00 17.27           C  
ANISOU 5939  C   TYR L 172     2589   2605   1368   -204   -394   -183       C  
ATOM   5940  O   TYR L 172     110.514  -4.915  -0.814  1.00 11.96           O  
ANISOU 5940  O   TYR L 172     2023   1837    683   -282   -342   -154       O  
ATOM   5941  CB  TYR L 172     109.177  -2.397   0.734  1.00 11.27           C  
ANISOU 5941  CB  TYR L 172     1785   1863    635      2   -420   -131       C  
ATOM   5942  CG  TYR L 172     108.168  -1.719   1.634  1.00 11.85           C  
ANISOU 5942  CG  TYR L 172     1852   1998    652    -32   -440    -95       C  
ATOM   5943  CD1 TYR L 172     107.191  -0.886   1.109  1.00 12.55           C  
ANISOU 5943  CD1 TYR L 172     1880   2183    705    -20   -454    -71       C  
ATOM   5944  CD2 TYR L 172     108.193  -1.914   3.009  1.00 26.47           C  
ANISOU 5944  CD2 TYR L 172     3649   3933   2477    -43   -399    -76       C  
ATOM   5945  CE1 TYR L 172     106.265  -0.267   1.926  1.00 13.46           C  
ANISOU 5945  CE1 TYR L 172     1882   2475    758     43   -414    -53       C  
ATOM   5946  CE2 TYR L 172     107.272  -1.299   3.834  1.00 12.93           C  
ANISOU 5946  CE2 TYR L 172     1846   2364    703    -25   -365    -79       C  
ATOM   5947  CZ  TYR L 172     106.311  -0.477   3.287  1.00 13.59           C  
ANISOU 5947  CZ  TYR L 172     1874   2540    748     35   -366    -78       C  
ATOM   5948  OH  TYR L 172     105.391   0.138   4.105  1.00 28.10           O  
ANISOU 5948  OH  TYR L 172     3610   4574   2494    122   -304    -83       O  
ATOM   5949  N   SER L 173     109.391  -3.570  -2.239  1.00 18.72           N  
ANISOU 5949  N   SER L 173     2753   2810   1550   -171   -422   -227       N  
ATOM   5950  CA  SER L 173     110.284  -3.779  -3.367  1.00 12.16           C  
ANISOU 5950  CA  SER L 173     1978   1915    728   -212   -386   -271       C  
ATOM   5951  C   SER L 173     110.497  -2.447  -4.068  1.00 20.49           C  
ANISOU 5951  C   SER L 173     2968   3043   1775    -82   -409   -252       C  
ATOM   5952  O   SER L 173     109.606  -1.593  -4.090  1.00 19.58           O  
ANISOU 5952  O   SER L 173     2829   2970   1640      0   -459   -203       O  
ATOM   5953  CB  SER L 173     109.730  -4.818  -4.351  1.00 13.93           C  
ANISOU 5953  CB  SER L 173     2266   2136    891   -419   -372   -353       C  
ATOM   5954  OG  SER L 173     109.537  -6.070  -3.717  1.00 44.33           O  
ANISOU 5954  OG  SER L 173     6212   5901   4730   -618   -296   -392       O  
ATOM   5955  N   MET L 174     111.686  -2.272  -4.639  1.00 29.01           N  
ANISOU 5955  N   MET L 174     4291   4058   2674     26    220    384       N  
ATOM   5956  CA  MET L 174     112.040  -1.013  -5.276  1.00 17.19           C  
ANISOU 5956  CA  MET L 174     2818   2535   1177     45    237    373       C  
ATOM   5957  C   MET L 174     112.743  -1.277  -6.599  1.00 14.87           C  
ANISOU 5957  C   MET L 174     2526   2221    902     70    220    384       C  
ATOM   5958  O   MET L 174     113.550  -2.206  -6.714  1.00 14.52           O  
ANISOU 5958  O   MET L 174     2461   2191    864     57    204    400       O  
ATOM   5959  CB  MET L 174     112.927  -0.161  -4.360  1.00 16.17           C  
ANISOU 5959  CB  MET L 174     2682   2442   1019      2    258    371       C  
ATOM   5960  CG  MET L 174     113.115   1.262  -4.844  1.00 15.89           C  
ANISOU 5960  CG  MET L 174     2703   2356    979     20    301    357       C  
ATOM   5961  SD  MET L 174     114.770   1.544  -5.482  1.00 14.37           S  
ANISOU 5961  SD  MET L 174     2496   2184    781     -3    297    381       S  
ATOM   5962  CE  MET L 174     115.676   1.703  -3.950  1.00 27.83           C  
ANISOU 5962  CE  MET L 174     4167   3981   2428    -59    307    379       C  
ATOM   5963  N   SER L 175     112.424  -0.454  -7.594  1.00 13.69           N  
ANISOU 5963  N   SER L 175     2409   2038    753    113    232    382       N  
ATOM   5964  CA  SER L 175     112.999  -0.547  -8.930  1.00 13.73           C  
ANISOU 5964  CA  SER L 175     2421   2033    762    137    223    392       C  
ATOM   5965  C   SER L 175     113.879   0.667  -9.188  1.00 13.99           C  
ANISOU 5965  C   SER L 175     2475   2048    791    133    254    407       C  
ATOM   5966  O   SER L 175     113.456   1.804  -8.958  1.00 14.30           O  
ANISOU 5966  O   SER L 175     2556   2054    825    150    289    410       O  
ATOM   5967  CB  SER L 175     111.902  -0.635  -9.991  1.00 13.95           C  
ANISOU 5967  CB  SER L 175     2468   2057    775    189    210    391       C  
ATOM   5968  OG  SER L 175     112.434  -0.438 -11.287  1.00 14.19           O  
ANISOU 5968  OG  SER L 175     2512   2087    794    211    208    403       O  
ATOM   5969  N   SER L 176     115.096   0.424  -9.671  1.00 21.24           N  
ANISOU 5969  N   SER L 176     3379   2982   1710    115    254    419       N  
ATOM   5970  CA  SER L 176     116.050   1.485  -9.971  1.00 14.38           C  
ANISOU 5970  CA  SER L 176     2532   2103    830    101    290    438       C  
ATOM   5971  C   SER L 176     116.493   1.351 -11.420  1.00 21.46           C  
ANISOU 5971  C   SER L 176     3439   2994   1723    132    293    454       C  
ATOM   5972  O   SER L 176     117.131   0.358 -11.785  1.00 14.49           O  
ANISOU 5972  O   SER L 176     2533   2136    838    129    282    452       O  
ATOM   5973  CB  SER L 176     117.254   1.424  -9.028  1.00 14.48           C  
ANISOU 5973  CB  SER L 176     2510   2166    825     38    296    446       C  
ATOM   5974  OG  SER L 176     118.165   2.477  -9.291  1.00 25.05           O  
ANISOU 5974  OG  SER L 176     3873   3499   2144     16    341    465       O  
ATOM   5975  N   THR L 177     116.163   2.347 -12.238  1.00 21.44           N  
ANISOU 5975  N   THR L 177     3480   2956   1711    168    318    474       N  
ATOM   5976  CA  THR L 177     116.476   2.336 -13.662  1.00 15.42           C  
ANISOU 5976  CA  THR L 177     2731   2199    929    197    324    495       C  
ATOM   5977  C   THR L 177     117.474   3.444 -13.972  1.00 23.83           C  
ANISOU 5977  C   THR L 177     3827   3240   1986    180    379    530       C  
ATOM   5978  O   THR L 177     117.203   4.622 -13.713  1.00 18.09           O  
ANISOU 5978  O   THR L 177     3148   2460   1264    190    421    553       O  
ATOM   5979  CB  THR L 177     115.213   2.506 -14.505  1.00 15.75           C  
ANISOU 5979  CB  THR L 177     2796   2237    950    255    304    508       C  
ATOM   5980  OG1 THR L 177     114.267   1.485 -14.165  1.00 15.35           O  
ANISOU 5980  OG1 THR L 177     2719   2214    899    258    260    475       O  
ATOM   5981  CG2 THR L 177     115.548   2.406 -15.987  1.00 16.31           C  
ANISOU 5981  CG2 THR L 177     2881   2337    980    275    306    529       C  
ATOM   5982  N   LEU L 178     118.620   3.060 -14.531  1.00 32.36           N  
ANISOU 5982  N   LEU L 178     4891   4352   3054    159    394    538       N  
ATOM   5983  CA  LEU L 178     119.669   3.987 -14.949  1.00 24.42           C  
ANISOU 5983  CA  LEU L 178     3909   3334   2035    135    454    576       C  
ATOM   5984  C   LEU L 178     119.579   4.143 -16.465  1.00 19.39           C  
ANISOU 5984  C   LEU L 178     3302   2697   1369    179    466    605       C  
ATOM   5985  O   LEU L 178     120.013   3.267 -17.217  1.00 42.28           O  
ANISOU 5985  O   LEU L 178     6183   5638   4243    186    459    593       O  
ATOM   5986  CB  LEU L 178     121.041   3.475 -14.519  1.00 27.72           C  
ANISOU 5986  CB  LEU L 178     4284   3803   2446     81    469    575       C  
ATOM   5987  CG  LEU L 178     122.280   4.158 -15.108  1.00 35.40           C  
ANISOU 5987  CG  LEU L 178     5267   4785   3398     48    537    616       C  
ATOM   5988  CD1 LEU L 178     122.481   5.543 -14.512  1.00 48.38           C  
ANISOU 5988  CD1 LEU L 178     6949   6385   5047      0    596    638       C  
ATOM   5989  CD2 LEU L 178     123.520   3.298 -14.914  1.00 17.75           C  
ANISOU 5989  CD2 LEU L 178     2979   2616   1148     17    549    618       C  
ATOM   5990  N   THR L 179     119.008   5.258 -16.912  1.00 29.12           N  
ANISOU 5990  N   THR L 179     4587   3881   2596    212    494    648       N  
ATOM   5991  CA  THR L 179     118.883   5.542 -18.335  1.00 30.54           C  
ANISOU 5991  CA  THR L 179     4797   4073   2735    253    505    692       C  
ATOM   5992  C   THR L 179     120.068   6.376 -18.804  1.00 24.63           C  
ANISOU 5992  C   THR L 179     4077   3303   1979    222    582    739       C  
ATOM   5993  O   THR L 179     120.544   7.258 -18.085  1.00 28.42           O  
ANISOU 5993  O   THR L 179     4582   3726   2490    185    639    755       O  
ATOM   5994  CB  THR L 179     117.577   6.282 -18.635  1.00 21.10           C  
ANISOU 5994  CB  THR L 179     3641   2845   1533    320    496    735       C  
ATOM   5995  OG1 THR L 179     117.632   7.599 -18.077  1.00 45.54           O  
ANISOU 5995  OG1 THR L 179     6791   5847   4664    326    567    776       O  
ATOM   5996  CG2 THR L 179     116.391   5.540 -18.035  1.00 31.67           C  
ANISOU 5996  CG2 THR L 179     4948   4206   2880    342    430    691       C  
ATOM   5997  N   LEU L 180     120.540   6.088 -20.014  1.00 31.94           N  
ANISOU 5997  N   LEU L 180     5005   4274   2856    230    593    759       N  
ATOM   5998  CA  LEU L 180     121.657   6.820 -20.599  1.00 21.24           C  
ANISOU 5998  CA  LEU L 180     3674   2908   1487    201    673    809       C  
ATOM   5999  C   LEU L 180     121.724   6.509 -22.089  1.00 28.83           C  
ANISOU 5999  C   LEU L 180     4652   3927   2377    229    675    834       C  
ATOM   6000  O   LEU L 180     121.016   5.633 -22.602  1.00 40.59           O  
ANISOU 6000  O   LEU L 180     6131   5470   3822    260    616    802       O  
ATOM   6001  CB  LEU L 180     122.981   6.490 -19.896  1.00 20.97           C  
ANISOU 6001  CB  LEU L 180     3596   2896   1475    131    709    783       C  
ATOM   6002  CG  LEU L 180     123.396   5.029 -19.705  1.00 27.55           C  
ANISOU 6002  CG  LEU L 180     4370   3797   2299    127    671    726       C  
ATOM   6003  CD1 LEU L 180     124.173   4.530 -20.898  1.00 48.21           C  
ANISOU 6003  CD1 LEU L 180     6988   6463   4868    138    713    734       C  
ATOM   6004  CD2 LEU L 180     124.221   4.868 -18.442  1.00 20.58           C  
ANISOU 6004  CD2 LEU L 180     3440   2931   1450     68    683    709       C  
ATOM   6005  N   THR L 181     122.592   7.248 -22.775  1.00 23.10           N  
ANISOU 6005  N   THR L 181     3955   3192   1631    209    751    892       N  
ATOM   6006  CA  THR L 181     122.725   7.137 -24.219  1.00 33.79           C  
ANISOU 6006  CA  THR L 181     5335   4602   2902    230    768    928       C  
ATOM   6007  C   THR L 181     123.407   5.830 -24.601  1.00 38.66           C  
ANISOU 6007  C   THR L 181     5914   5296   3479    214    767    864       C  
ATOM   6008  O   THR L 181     124.281   5.327 -23.889  1.00 38.34           O  
ANISOU 6008  O   THR L 181     5830   5257   3481    181    790    825       O  
ATOM   6009  CB  THR L 181     123.532   8.312 -24.770  1.00 25.48           C  
ANISOU 6009  CB  THR L 181     4324   3511   1845    206    863   1012       C  
ATOM   6010  OG1 THR L 181     124.889   8.207 -24.322  1.00 25.42           O  
ANISOU 6010  OG1 THR L 181     4280   3508   1870    139    928    993       O  
ATOM   6011  CG2 THR L 181     122.954   9.630 -24.282  1.00 25.90           C  
ANISOU 6011  CG2 THR L 181     4427   3459   1954    226    891   1075       C  
ATOM   6012  N   LYS L 182     123.002   5.282 -25.750  1.00 41.01           N  
ANISOU 6012  N   LYS L 182     6234   5661   3688    240    746    858       N  
ATOM   6013  CA  LYS L 182     123.632   4.064 -26.246  1.00 24.61           C  
ANISOU 6013  CA  LYS L 182     4140   3648   1564    233    769    796       C  
ATOM   6014  C   LYS L 182     125.126   4.259 -26.469  1.00 25.28           C  
ANISOU 6014  C   LYS L 182     4213   3738   1653    203    869    818       C  
ATOM   6015  O   LYS L 182     125.912   3.327 -26.260  1.00 25.04           O  
ANISOU 6015  O   LYS L 182     4148   3730   1637    201    905    767       O  
ATOM   6016  CB  LYS L 182     122.954   3.612 -27.540  1.00 25.55           C  
ANISOU 6016  CB  LYS L 182     4299   3847   1564    250    744    787       C  
ATOM   6017  CG  LYS L 182     123.439   2.271 -28.062  1.00 41.83           C  
ANISOU 6017  CG  LYS L 182     6356   5970   3568    247    776    707       C  
ATOM   6018  CD  LYS L 182     122.785   1.934 -29.389  1.00 42.31           C  
ANISOU 6018  CD  LYS L 182     6464   6125   3486    242    758    695       C  
ATOM   6019  CE  LYS L 182     123.135   0.525 -29.827  1.00 49.69           C  
ANISOU 6019  CE  LYS L 182     7403   7114   4362    238    797    594       C  
ATOM   6020  NZ  LYS L 182     122.465   0.151 -31.101  1.00 56.31           N  
ANISOU 6020  NZ  LYS L 182     8291   8064   5041    212    779    564       N  
ATOM   6021  N   ASP L 183     125.539   5.463 -26.874  1.00 26.25           N  
ANISOU 6021  N   ASP L 183     4364   3840   1770    182    925    899       N  
ATOM   6022  CA  ASP L 183     126.958   5.727 -27.090  1.00 34.51           C  
ANISOU 6022  CA  ASP L 183     5393   4898   2822    141   1029    926       C  
ATOM   6023  C   ASP L 183     127.744   5.584 -25.792  1.00 40.49           C  
ANISOU 6023  C   ASP L 183     6087   5628   3671    103   1048    899       C  
ATOM   6024  O   ASP L 183     128.765   4.889 -25.745  1.00 46.28           O  
ANISOU 6024  O   ASP L 183     6773   6402   4409     91   1104    872       O  
ATOM   6025  CB  ASP L 183     127.151   7.121 -27.686  1.00 49.72           C  
ANISOU 6025  CB  ASP L 183     7367   6793   4732    120   1089   1026       C  
ATOM   6026  CG  ASP L 183     128.558   7.338 -28.214  1.00 68.94           C  
ANISOU 6026  CG  ASP L 183     9786   9257   7150     72   1205   1058       C  
ATOM   6027  OD1 ASP L 183     129.259   6.336 -28.472  1.00 71.52           O  
ANISOU 6027  OD1 ASP L 183    10075   9648   7451     75   1240   1004       O  
ATOM   6028  OD2 ASP L 183     128.965   8.508 -28.364  1.00 76.66           O  
ANISOU 6028  OD2 ASP L 183    10789  10191   8147     34   1273   1138       O  
ATOM   6029  N   GLU L 184     127.279   6.236 -24.723  1.00 33.06           N  
ANISOU 6029  N   GLU L 184     5141   4623   2796     83   1009    910       N  
ATOM   6030  CA  GLU L 184     127.957   6.112 -23.437  1.00 30.43           C  
ANISOU 6030  CA  GLU L 184     4748   4284   2529     33   1019    886       C  
ATOM   6031  C   GLU L 184     127.891   4.686 -22.905  1.00 31.99           C  
ANISOU 6031  C   GLU L 184     4900   4519   2737     67    969    816       C  
ATOM   6032  O   GLU L 184     128.825   4.230 -22.236  1.00 30.89           O  
ANISOU 6032  O   GLU L 184     4699   4411   2625     40   1003    805       O  
ATOM   6033  CB  GLU L 184     127.354   7.083 -22.422  1.00 28.22           C  
ANISOU 6033  CB  GLU L 184     4486   3930   2304      4    992    904       C  
ATOM   6034  CG  GLU L 184     128.105   7.138 -21.101  1.00 32.75           C  
ANISOU 6034  CG  GLU L 184     5001   4515   2926    -71   1011    888       C  
ATOM   6035  CD  GLU L 184     127.428   8.029 -20.081  1.00 61.07           C  
ANISOU 6035  CD  GLU L 184     8620   8025   6559    -98    994    891       C  
ATOM   6036  OE1 GLU L 184     126.215   8.290 -20.230  1.00 74.69           O  
ANISOU 6036  OE1 GLU L 184    10400   9691   8287    -37    946    890       O  
ATOM   6037  OE2 GLU L 184     128.109   8.472 -19.133  1.00 70.03           O  
ANISOU 6037  OE2 GLU L 184     9724   9163   7723   -183   1038    893       O  
ATOM   6038  N   TYR L 185     126.802   3.968 -23.192  1.00 23.24           N  
ANISOU 6038  N   TYR L 185     3816   3408   1604    126    895    773       N  
ATOM   6039  CA  TYR L 185     126.708   2.577 -22.765  1.00 22.49           C  
ANISOU 6039  CA  TYR L 185     3691   3333   1522    163    863    711       C  
ATOM   6040  C   TYR L 185     127.769   1.722 -23.444  1.00 32.96           C  
ANISOU 6040  C   TYR L 185     4999   4706   2819    189    947    699       C  
ATOM   6041  O   TYR L 185     128.412   0.885 -22.798  1.00 27.31           O  
ANISOU 6041  O   TYR L 185     4234   4002   2140    209    974    683       O  
ATOM   6042  CB  TYR L 185     125.314   2.024 -23.058  1.00 21.97           C  
ANISOU 6042  CB  TYR L 185     3659   3260   1429    207    783    669       C  
ATOM   6043  CG  TYR L 185     125.138   0.579 -22.651  1.00 36.89           C  
ANISOU 6043  CG  TYR L 185     5529   5155   3331    244    761    607       C  
ATOM   6044  CD1 TYR L 185     124.940   0.232 -21.320  1.00 35.09           C  
ANISOU 6044  CD1 TYR L 185     5265   4899   3168    240    717    592       C  
ATOM   6045  CD2 TYR L 185     125.169  -0.439 -23.595  1.00 36.98           C  
ANISOU 6045  CD2 TYR L 185     5568   5199   3285    283    795    565       C  
ATOM   6046  CE1 TYR L 185     124.780  -1.088 -20.942  1.00 20.01           C  
ANISOU 6046  CE1 TYR L 185     3346   2985   1272    282    708    550       C  
ATOM   6047  CE2 TYR L 185     125.010  -1.761 -23.226  1.00 21.62           C  
ANISOU 6047  CE2 TYR L 185     3619   3243   1354    324    794    512       C  
ATOM   6048  CZ  TYR L 185     124.816  -2.079 -21.898  1.00 20.64           C  
ANISOU 6048  CZ  TYR L 185     3459   3081   1301    328    752    511       C  
ATOM   6049  OH  TYR L 185     124.657  -3.391 -21.525  1.00 20.46           O  
ANISOU 6049  OH  TYR L 185     3443   3038   1293    376    763    472       O  
ATOM   6050  N   GLU L 186     127.972   1.923 -24.747  1.00 25.42           N  
ANISOU 6050  N   GLU L 186     4081   3781   1795    195    999    713       N  
ATOM   6051  CA  GLU L 186     128.927   1.105 -25.483  1.00 25.28           C  
ANISOU 6051  CA  GLU L 186     4052   3810   1745    225   1093    694       C  
ATOM   6052  C   GLU L 186     130.374   1.429 -25.131  1.00 25.91           C  
ANISOU 6052  C   GLU L 186     4065   3911   1869    193   1188    738       C  
ATOM   6053  O   GLU L 186     131.263   0.628 -25.436  1.00 51.42           O  
ANISOU 6053  O   GLU L 186     7259   7177   5100    232   1276    724       O  
ATOM   6054  CB  GLU L 186     128.705   1.274 -26.985  1.00 38.57           C  
ANISOU 6054  CB  GLU L 186     5796   5534   3327    229   1123    695       C  
ATOM   6055  CG  GLU L 186     127.365   0.748 -27.470  1.00 36.68           C  
ANISOU 6055  CG  GLU L 186     5609   5306   3023    254   1042    646       C  
ATOM   6056  CD  GLU L 186     127.119   1.044 -28.934  1.00 64.05           C  
ANISOU 6056  CD  GLU L 186     9132   8837   6367    243   1064    660       C  
ATOM   6057  OE1 GLU L 186     127.762   1.971 -29.471  1.00 76.86           O  
ANISOU 6057  OE1 GLU L 186    10764  10474   7967    216   1123    727       O  
ATOM   6058  OE2 GLU L 186     126.286   0.347 -29.550  1.00 73.82           O  
ANISOU 6058  OE2 GLU L 186    10406  10119   7523    254   1026    604       O  
ATOM   6059  N   ARG L 187     130.632   2.571 -24.496  1.00 30.88           N  
ANISOU 6059  N   ARG L 187     4814   3858   3060   1224    844    749       N  
ATOM   6060  CA  ARG L 187     131.995   2.972 -24.173  1.00 29.98           C  
ANISOU 6060  CA  ARG L 187     4670   3677   3044   1054    950    736       C  
ATOM   6061  C   ARG L 187     132.470   2.463 -22.818  1.00 27.30           C  
ANISOU 6061  C   ARG L 187     4233   3241   2899    961    858    614       C  
ATOM   6062  O   ARG L 187     133.641   2.660 -22.479  1.00 36.89           O  
ANISOU 6062  O   ARG L 187     5387   4424   4205    823    924    568       O  
ATOM   6063  CB  ARG L 187     132.124   4.499 -24.215  1.00 38.35           C  
ANISOU 6063  CB  ARG L 187     5906   4592   4072    988   1102    910       C  
ATOM   6064  CG  ARG L 187     131.939   5.096 -25.602  1.00 46.94           C  
ANISOU 6064  CG  ARG L 187     7103   5771   4959   1063   1225   1051       C  
ATOM   6065  CD  ARG L 187     132.182   6.596 -25.602  1.00 54.84           C  
ANISOU 6065  CD  ARG L 187     8265   6600   5973    970   1365   1197       C  
ATOM   6066  NE  ARG L 187     131.905   7.189 -26.908  1.00 71.26           N  
ANISOU 6066  NE  ARG L 187    10401   8755   7918   1029   1412   1279       N  
ATOM   6067  CZ  ARG L 187     132.787   7.257 -27.901  1.00 69.11           C  
ANISOU 6067  CZ  ARG L 187    10117   8590   7552    965   1547   1313       C  
ATOM   6068  NH1 ARG L 187     132.446   7.814 -29.056  1.00 72.10           N  
ANISOU 6068  NH1 ARG L 187    10562   9028   7804   1029   1575   1398       N  
ATOM   6069  NH2 ARG L 187     134.009   6.767 -27.740  1.00 57.69           N  
ANISOU 6069  NH2 ARG L 187     8578   7201   6139    836   1659   1250       N  
ATOM   6070  N   HIS L 188     131.603   1.816 -22.043  1.00 20.45           N  
ANISOU 6070  N   HIS L 188     3346   2334   2089   1032    710    558       N  
ATOM   6071  CA  HIS L 188     131.970   1.274 -20.743  1.00 19.25           C  
ANISOU 6071  CA  HIS L 188     3115   2097   2101    964    614    455       C  
ATOM   6072  C   HIS L 188     131.608  -0.204 -20.690  1.00 19.47           C  
ANISOU 6072  C   HIS L 188     3027   2214   2158   1046    475    324       C  
ATOM   6073  O   HIS L 188     130.931  -0.734 -21.575  1.00 32.67           O  
ANISOU 6073  O   HIS L 188     4682   4001   3730   1151    448    307       O  
ATOM   6074  CB  HIS L 188     131.289   2.043 -19.606  1.00 18.53           C  
ANISOU 6074  CB  HIS L 188     3139   1831   2068    948    584    526       C  
ATOM   6075  CG  HIS L 188     131.727   3.471 -19.501  1.00 31.98           C  
ANISOU 6075  CG  HIS L 188     4960   3414   3777    851    720    635       C  
ATOM   6076  ND1 HIS L 188     131.223   4.466 -20.310  1.00 36.27           N  
ANISOU 6076  ND1 HIS L 188     5648   3932   4202    900    824    782       N  
ATOM   6077  CD2 HIS L 188     132.631   4.068 -18.689  1.00 19.89           C  
ANISOU 6077  CD2 HIS L 188     3425   1776   2356    706    770    614       C  
ATOM   6078  CE1 HIS L 188     131.792   5.616 -19.996  1.00 21.64           C  
ANISOU 6078  CE1 HIS L 188     3886   1940   2396    784    942    851       C  
ATOM   6079  NE2 HIS L 188     132.651   5.402 -19.016  1.00 34.37           N  
ANISOU 6079  NE2 HIS L 188     5403   3506   4149    657    912    742       N  
ATOM   6080  N   ASN L 189     132.067  -0.873 -19.633  1.00 17.41           N  
ANISOU 6080  N   ASN L 189     2688   1895   2032    999    388    228       N  
ATOM   6081  CA  ASN L 189     131.969  -2.326 -19.574  1.00 16.77           C  
ANISOU 6081  CA  ASN L 189     2497   1876   1998   1061    272     98       C  
ATOM   6082  C   ASN L 189     131.303  -2.812 -18.292  1.00 31.76           C  
ANISOU 6082  C   ASN L 189     4418   3659   3989   1074    153     77       C  
ATOM   6083  O   ASN L 189     130.372  -3.623 -18.343  1.00 28.12           O  
ANISOU 6083  O   ASN L 189     3933   3235   3518   1092     71     37       O  
ATOM   6084  CB  ASN L 189     133.362  -2.945 -19.716  1.00 25.34           C  
ANISOU 6084  CB  ASN L 189     3444   3033   3149   1012    282    -16       C  
ATOM   6085  CG  ASN L 189     133.323  -4.457 -19.814  1.00 17.02           C  
ANISOU 6085  CG  ASN L 189     2287   2039   2142   1090    175   -152       C  
ATOM   6086  OD1 ASN L 189     133.780  -5.161 -18.915  1.00 26.60           O  
ANISOU 6086  OD1 ASN L 189     3443   3193   3470   1082     89   -227       O  
ATOM   6087  ND2 ASN L 189     132.773  -4.963 -20.910  1.00 31.46           N  
ANISOU 6087  ND2 ASN L 189     4095   3980   3878   1172    178   -186       N  
ATOM   6088  N   SER L 190     131.768  -2.330 -17.141  1.00 15.19           N  
ANISOU 6088  N   SER L 190     2345   1449   1977    994    144     96       N  
ATOM   6089  CA  SER L 190     131.286  -2.807 -15.849  1.00 14.16           C  
ANISOU 6089  CA  SER L 190     2195   1257   1928    921     32     70       C  
ATOM   6090  C   SER L 190     130.126  -1.941 -15.371  1.00 21.58           C  
ANISOU 6090  C   SER L 190     3206   2166   2829    851     35    150       C  
ATOM   6091  O   SER L 190     130.262  -0.718 -15.255  1.00 14.06           O  
ANISOU 6091  O   SER L 190     2338   1150   1854    832    107    223       O  
ATOM   6092  CB  SER L 190     132.414  -2.804 -14.819  1.00 14.24           C  
ANISOU 6092  CB  SER L 190     2174   1197   2040    885      7     26       C  
ATOM   6093  OG  SER L 190     133.388  -3.782 -15.133  1.00 14.70           O  
ANISOU 6093  OG  SER L 190     2124   1316   2143    938    -27    -82       O  
ATOM   6094  N   TYR L 191     128.993  -2.579 -15.084  1.00 12.92           N  
ANISOU 6094  N   TYR L 191     2068   1111   1730    811    -26    129       N  
ATOM   6095  CA  TYR L 191     127.808  -1.902 -14.566  1.00 12.47           C  
ANISOU 6095  CA  TYR L 191     2043   1050   1646    758    -28    172       C  
ATOM   6096  C   TYR L 191     127.436  -2.549 -13.240  1.00 24.14           C  
ANISOU 6096  C   TYR L 191     3455   2512   3204    671    -82    143       C  
ATOM   6097  O   TYR L 191     127.068  -3.729 -13.199  1.00 11.34           O  
ANISOU 6097  O   TYR L 191     1785    921   1602    667   -113    103       O  
ATOM   6098  CB  TYR L 191     126.658  -1.962 -15.569  1.00 12.64           C  
ANISOU 6098  CB  TYR L 191     2087   1149   1568    822    -17    180       C  
ATOM   6099  CG  TYR L 191     126.939  -1.149 -16.808  1.00 21.35           C  
ANISOU 6099  CG  TYR L 191     3268   2280   2566    921     64    241       C  
ATOM   6100  CD1 TYR L 191     126.513   0.169 -16.908  1.00 18.35           C  
ANISOU 6100  CD1 TYR L 191     2971   1874   2126    925    126    319       C  
ATOM   6101  CD2 TYR L 191     127.658  -1.688 -17.866  1.00 16.40           C  
ANISOU 6101  CD2 TYR L 191     2627   1706   1898   1016     90    222       C  
ATOM   6102  CE1 TYR L 191     126.780   0.921 -18.035  1.00 24.17           C  
ANISOU 6102  CE1 TYR L 191     3791   2628   2763   1014    221    399       C  
ATOM   6103  CE2 TYR L 191     127.931  -0.945 -18.995  1.00 31.21           C  
ANISOU 6103  CE2 TYR L 191     4577   3616   3664   1120    188    302       C  
ATOM   6104  CZ  TYR L 191     127.490   0.357 -19.075  1.00 32.58           C  
ANISOU 6104  CZ  TYR L 191     4850   3752   3776   1113    258    404       C  
ATOM   6105  OH  TYR L 191     127.763   1.096 -20.200  1.00 38.48           O  
ANISOU 6105  OH  TYR L 191     5684   4526   4410   1206    369    508       O  
ATOM   6106  N   THR L 192     127.538  -1.774 -12.163  1.00 22.67           N  
ANISOU 6106  N   THR L 192     3282   2278   3052    613    -79    169       N  
ATOM   6107  CA  THR L 192     127.382  -2.269 -10.803  1.00 11.18           C  
ANISOU 6107  CA  THR L 192     1818    811   1619    574   -110    150       C  
ATOM   6108  C   THR L 192     126.193  -1.588 -10.144  1.00 37.99           C  
ANISOU 6108  C   THR L 192     5265   4210   4959    560   -104    168       C  
ATOM   6109  O   THR L 192     126.073  -0.358 -10.185  1.00 35.58           O  
ANISOU 6109  O   THR L 192     5004   3882   4633    557    -72    199       O  
ATOM   6110  CB  THR L 192     128.653  -2.024  -9.982  1.00 27.02           C  
ANISOU 6110  CB  THR L 192     3804   2765   3698    544   -110    148       C  
ATOM   6111  OG1 THR L 192     129.735  -2.789 -10.528  1.00 32.70           O  
ANISOU 6111  OG1 THR L 192     4482   3485   4459    579   -115    117       O  
ATOM   6112  CG2 THR L 192     128.441  -2.421  -8.535  1.00 11.11           C  
ANISOU 6112  CG2 THR L 192     1801    747   1673    518   -140    136       C  
ATOM   6113  N   CYS L 193     125.326  -2.392  -9.537  1.00 47.91           N  
ANISOU 6113  N   CYS L 193     6520   5491   6195    554   -131    145       N  
ATOM   6114  CA  CYS L 193     124.154  -1.922  -8.806  1.00 14.68           C  
ANISOU 6114  CA  CYS L 193     2349   1288   1943    546   -128    150       C  
ATOM   6115  C   CYS L 193     124.379  -2.237  -7.330  1.00 15.10           C  
ANISOU 6115  C   CYS L 193     2405   1317   2017    508   -152    141       C  
ATOM   6116  O   CYS L 193     124.206  -3.380  -6.896  1.00 13.99           O  
ANISOU 6116  O   CYS L 193     2250   1182   1885    501   -181    121       O  
ATOM   6117  CB  CYS L 193     122.886  -2.581  -9.345  1.00 20.75           C  
ANISOU 6117  CB  CYS L 193     3112   2100   2672    577   -136    131       C  
ATOM   6118  SG  CYS L 193     121.394  -2.290  -8.374  1.00 55.91           S  
ANISOU 6118  SG  CYS L 193     7596   6561   7088    572   -135    127       S  
ATOM   6119  N   GLU L 194     124.787  -1.225  -6.569  1.00 11.12           N  
ANISOU 6119  N   GLU L 194     1924    779   1521    487   -140    155       N  
ATOM   6120  CA  GLU L 194     125.004  -1.347  -5.134  1.00 11.62           C  
ANISOU 6120  CA  GLU L 194     2000    824   1589    460   -164    147       C  
ATOM   6121  C   GLU L 194     123.776  -0.863  -4.375  1.00 10.72           C  
ANISOU 6121  C   GLU L 194     1926    717   1431    457   -157    147       C  
ATOM   6122  O   GLU L 194     123.024  -0.009  -4.851  1.00 33.23           O  
ANISOU 6122  O   GLU L 194     4798   3573   4254    476   -127    158       O  
ATOM   6123  CB  GLU L 194     126.228  -0.546  -4.684  1.00 18.93           C  
ANISOU 6123  CB  GLU L 194     2928   1706   2559    441   -158    152       C  
ATOM   6124  CG  GLU L 194     127.554  -1.053  -5.216  1.00 28.12           C  
ANISOU 6124  CG  GLU L 194     4049   2858   3776    448   -165    145       C  
ATOM   6125  CD  GLU L 194     128.739  -0.361  -4.570  1.00 39.59           C  
ANISOU 6125  CD  GLU L 194     5501   4260   5280    429   -159    139       C  
ATOM   6126  OE1 GLU L 194     128.522   0.470  -3.663  1.00 37.66           O  
ANISOU 6126  OE1 GLU L 194     5293   3989   5028    408   -155    138       O  
ATOM   6127  OE2 GLU L 194     129.888  -0.650  -4.968  1.00 48.81           O  
ANISOU 6127  OE2 GLU L 194     6636   5412   6500    440   -155    126       O  
ATOM   6128  N   ALA L 195     123.585  -1.412  -3.177  1.00 10.67           N  
ANISOU 6128  N   ALA L 195     1932    708   1414    442   -184    137       N  
ATOM   6129  CA  ALA L 195     122.417  -1.068  -2.371  1.00 38.74           C  
ANISOU 6129  CA  ALA L 195     5522   4268   4930    442   -175    136       C  
ATOM   6130  C   ALA L 195     122.748  -1.336  -0.911  1.00 23.71           C  
ANISOU 6130  C   ALA L 195     3643   2346   3019    423   -204    131       C  
ATOM   6131  O   ALA L 195     122.907  -2.496  -0.517  1.00 33.30           O  
ANISOU 6131  O   ALA L 195     4853   3561   4238    418   -233    130       O  
ATOM   6132  CB  ALA L 195     121.198  -1.869  -2.814  1.00 53.35           C  
ANISOU 6132  CB  ALA L 195     7361   6146   6765    457   -171    130       C  
ATOM   6133  N   THR L 196     122.856  -0.272  -0.119  1.00 19.52           N  
ANISOU 6133  N   THR L 196     3146   1794   2477    416   -197    129       N  
ATOM   6134  CA  THR L 196     123.039  -0.400   1.319  1.00 19.91           C  
ANISOU 6134  CA  THR L 196     3230   1829   2506    406   -226    123       C  
ATOM   6135  C   THR L 196     121.674  -0.479   1.988  1.00 16.19           C  
ANISOU 6135  C   THR L 196     2790   1367   1993    412   -211    125       C  
ATOM   6136  O   THR L 196     120.786   0.333   1.704  1.00 17.93           O  
ANISOU 6136  O   THR L 196     3020   1593   2200    426   -176    123       O  
ATOM   6137  CB  THR L 196     123.841   0.771   1.888  1.00 11.39           C  
ANISOU 6137  CB  THR L 196     2173    713   1441    397   -228    114       C  
ATOM   6138  OG1 THR L 196     123.184   2.003   1.573  1.00 21.76           O  
ANISOU 6138  OG1 THR L 196     3505   2011   2753    402   -182    115       O  
ATOM   6139  CG2 THR L 196     125.250   0.789   1.313  1.00 11.47           C  
ANISOU 6139  CG2 THR L 196     2149    704   1505    390   -239    111       C  
ATOM   6140  N   HIS L 197     121.512  -1.466   2.867  1.00 11.60           N  
ANISOU 6140  N   HIS L 197     2228    784   1394    406   -234    132       N  
ATOM   6141  CA  HIS L 197     120.263  -1.684   3.577  1.00 12.61           C  
ANISOU 6141  CA  HIS L 197     2386    914   1491    408   -214    139       C  
ATOM   6142  C   HIS L 197     120.573  -2.049   5.023  1.00 11.63           C  
ANISOU 6142  C   HIS L 197     2313    770   1335    403   -242    149       C  
ATOM   6143  O   HIS L 197     121.696  -2.432   5.361  1.00 29.94           O  
ANISOU 6143  O   HIS L 197     4638   3079   3660    403   -285    152       O  
ATOM   6144  CB  HIS L 197     119.420  -2.778   2.903  1.00 17.97           C  
ANISOU 6144  CB  HIS L 197     3037   1602   2190    408   -199    150       C  
ATOM   6145  CG  HIS L 197     118.071  -2.969   3.521  1.00 27.90           C  
ANISOU 6145  CG  HIS L 197     4318   2854   3430    408   -170    160       C  
ATOM   6146  ND1 HIS L 197     117.745  -4.080   4.269  1.00 20.75           N  
ANISOU 6146  ND1 HIS L 197     3437   1922   2525    392   -171    186       N  
ATOM   6147  CD2 HIS L 197     116.967  -2.183   3.514  1.00 17.81           C  
ANISOU 6147  CD2 HIS L 197     3044   1587   2135    427   -137    149       C  
ATOM   6148  CE1 HIS L 197     116.497  -3.975   4.689  1.00 16.03           C  
ANISOU 6148  CE1 HIS L 197     2856   1319   1916    392   -136    193       C  
ATOM   6149  NE2 HIS L 197     116.003  -2.833   4.245  1.00 20.74           N  
ANISOU 6149  NE2 HIS L 197     3437   1941   2503    418   -117    166       N  
ATOM   6150  N   LYS L 198     119.552  -1.919   5.875  1.00 21.50           N  
ANISOU 6150  N   LYS L 198     3604   2015   2551    405   -218    157       N  
ATOM   6151  CA  LYS L 198     119.715  -2.163   7.305  1.00 12.22           C  
ANISOU 6151  CA  LYS L 198     2489    821   1332    404   -239    174       C  
ATOM   6152  C   LYS L 198     120.134  -3.599   7.601  1.00 19.68           C  
ANISOU 6152  C   LYS L 198     3445   1752   2281    399   -266    210       C  
ATOM   6153  O   LYS L 198     120.803  -3.854   8.609  1.00 13.14           O  
ANISOU 6153  O   LYS L 198     2661    912   1419    409   -303    229       O  
ATOM   6154  CB  LYS L 198     118.407  -1.828   8.025  1.00 12.32           C  
ANISOU 6154  CB  LYS L 198     2540    831   1309    408   -196    181       C  
ATOM   6155  CG  LYS L 198     118.392  -2.103   9.520  1.00 13.19           C  
ANISOU 6155  CG  LYS L 198     2775    909   1328    421   -215    200       C  
ATOM   6156  CD  LYS L 198     117.006  -1.851  10.093  1.00 30.08           C  
ANISOU 6156  CD  LYS L 198     5003   3029   3398    437   -164    202       C  
ATOM   6157  CE  LYS L 198     116.957  -2.109  11.589  1.00 40.87           C  
ANISOU 6157  CE  LYS L 198     6511   4366   4652    448   -172    232       C  
ATOM   6158  NZ  LYS L 198     115.594  -1.865  12.141  1.00 51.99           N  
ANISOU 6158  NZ  LYS L 198     8020   5754   5981    463   -104    239       N  
ATOM   6159  N   THR L 199     119.768  -4.544   6.734  1.00 15.21           N  
ANISOU 6159  N   THR L 199     2841   1182   1756    390   -250    223       N  
ATOM   6160  CA  THR L 199     119.963  -5.960   7.018  1.00 13.10           C  
ANISOU 6160  CA  THR L 199     2592    884   1501    386   -264    265       C  
ATOM   6161  C   THR L 199     121.403  -6.431   6.852  1.00 13.36           C  
ANISOU 6161  C   THR L 199     2614    911   1550    406   -320    263       C  
ATOM   6162  O   THR L 199     121.706  -7.566   7.235  1.00 29.32           O  
ANISOU 6162  O   THR L 199     4663   2900   3576    416   -339    302       O  
ATOM   6163  CB  THR L 199     119.052  -6.804   6.122  1.00 19.86           C  
ANISOU 6163  CB  THR L 199     3413   1725   2407    368   -228    275       C  
ATOM   6164  OG1 THR L 199     119.138  -6.334   4.771  1.00 18.44           O  
ANISOU 6164  OG1 THR L 199     3168   1576   2264    375   -224    234       O  
ATOM   6165  CG2 THR L 199     117.610  -6.719   6.597  1.00 29.66           C  
ANISOU 6165  CG2 THR L 199     4678   2957   3635    349   -177    293       C  
ATOM   6166  N   SER L 200     122.293  -5.609   6.298  1.00 12.95           N  
ANISOU 6166  N   SER L 200     2525    883   1511    415   -344    224       N  
ATOM   6167  CA  SER L 200     123.674  -6.016   6.077  1.00 13.20           C  
ANISOU 6167  CA  SER L 200     2538    911   1565    437   -396    217       C  
ATOM   6168  C   SER L 200     124.613  -4.863   6.393  1.00 24.12           C  
ANISOU 6168  C   SER L 200     3921   2309   2936    447   -429    187       C  
ATOM   6169  O   SER L 200     124.337  -3.711   6.046  1.00 34.06           O  
ANISOU 6169  O   SER L 200     5164   3579   4198    430   -400    162       O  
ATOM   6170  CB  SER L 200     123.894  -6.487   4.634  1.00 12.86           C  
ANISOU 6170  CB  SER L 200     2433    875   1578    435   -386    201       C  
ATOM   6171  OG  SER L 200     123.539  -5.475   3.708  1.00 80.51           O  
ANISOU 6171  OG  SER L 200    10960   9470  10158    420   -352    174       O  
ATOM   6172  N   THR L 201     125.731  -5.184   7.052  1.00 40.00           N  
ANISOU 6172  N   THR L 201     5948   4314   4938    478   -490    191       N  
ATOM   6173  CA  THR L 201     126.709  -4.162   7.405  1.00 36.55           C  
ANISOU 6173  CA  THR L 201     5504   3884   4498    491   -531    160       C  
ATOM   6174  C   THR L 201     127.513  -3.689   6.200  1.00 13.20           C  
ANISOU 6174  C   THR L 201     2480    932   1604    483   -527    127       C  
ATOM   6175  O   THR L 201     128.024  -2.565   6.214  1.00 22.18           O  
ANISOU 6175  O   THR L 201     3627   2054   2748    481   -545     92       O  
ATOM   6176  CB  THR L 201     127.653  -4.685   8.492  1.00 38.91           C  
ANISOU 6176  CB  THR L 201     5862   4174   4749    549   -626    166       C  
ATOM   6177  OG1 THR L 201     128.641  -3.690   8.790  1.00 36.75           O  
ANISOU 6177  OG1 THR L 201     5628   3884   4453    581   -715    105       O  
ATOM   6178  CG2 THR L 201     128.346  -5.966   8.041  1.00 15.02           C  
ANISOU 6178  CG2 THR L 201     2786   1153   1767    577   -642    191       C  
ATOM   6179  N   SER L 202     127.635  -4.517   5.164  1.00 25.21           N  
ANISOU 6179  N   SER L 202     3959   2457   3163    485   -516    131       N  
ATOM   6180  CA  SER L 202     128.292  -4.153   3.921  1.00 38.00           C  
ANISOU 6180  CA  SER L 202     5517   4084   4839    479   -501    108       C  
ATOM   6181  C   SER L 202     127.266  -4.071   2.793  1.00 30.73           C  
ANISOU 6181  C   SER L 202     4573   3174   3929    451   -434    115       C  
ATOM   6182  O   SER L 202     126.216  -4.717   2.859  1.00 50.15           O  
ANISOU 6182  O   SER L 202     7051   5635   6368    444   -413    133       O  
ATOM   6183  CB  SER L 202     129.388  -5.164   3.555  1.00 35.92           C  
ANISOU 6183  CB  SER L 202     5218   3822   4608    519   -550    101       C  
ATOM   6184  OG  SER L 202     128.884  -6.487   3.518  1.00 40.06           O  
ANISOU 6184  OG  SER L 202     5760   4337   5124    531   -551    126       O  
ATOM   6185  N   PRO L 203     127.527  -3.275   1.755  1.00 14.92           N  
ANISOU 6185  N   PRO L 203     2532   1175   1963    440   -399    104       N  
ATOM   6186  CA  PRO L 203     126.529  -3.104   0.693  1.00 19.83           C  
ANISOU 6186  CA  PRO L 203     3136   1812   2587    426   -342    113       C  
ATOM   6187  C   PRO L 203     126.230  -4.409  -0.031  1.00 20.14           C  
ANISOU 6187  C   PRO L 203     3152   1863   2637    437   -345    117       C  
ATOM   6188  O   PRO L 203     127.075  -5.301  -0.133  1.00 30.81           O  
ANISOU 6188  O   PRO L 203     4487   3208   4011    457   -381    110       O  
ATOM   6189  CB  PRO L 203     127.180  -2.083  -0.249  1.00 22.71           C  
ANISOU 6189  CB  PRO L 203     3469   2166   2992    421   -308    109       C  
ATOM   6190  CG  PRO L 203     128.166  -1.359   0.602  1.00 21.47           C  
ANISOU 6190  CG  PRO L 203     3326   1979   2853    417   -332     94       C  
ATOM   6191  CD  PRO L 203     128.682  -2.379   1.572  1.00 25.37           C  
ANISOU 6191  CD  PRO L 203     3831   2480   3327    440   -403     86       C  
ATOM   6192  N   ILE L 204     125.002  -4.509  -0.531  1.00 27.08           N  
ANISOU 6192  N   ILE L 204     4031   2755   3503    430   -309    123       N  
ATOM   6193  CA  ILE L 204     124.558  -5.636  -1.343  1.00 11.15           C  
ANISOU 6193  CA  ILE L 204     1991    741   1504    438   -305    122       C  
ATOM   6194  C   ILE L 204     124.726  -5.243  -2.802  1.00 23.69           C  
ANISOU 6194  C   ILE L 204     3538   2350   3114    448   -279    113       C  
ATOM   6195  O   ILE L 204     124.148  -4.248  -3.256  1.00 24.01           O  
ANISOU 6195  O   ILE L 204     3580   2405   3138    446   -245    118       O  
ATOM   6196  CB  ILE L 204     123.102  -6.011  -1.032  1.00 11.10           C  
ANISOU 6196  CB  ILE L 204     2004    732   1480    428   -283    132       C  
ATOM   6197  CG1 ILE L 204     122.934  -6.265   0.467  1.00 18.08           C  
ANISOU 6197  CG1 ILE L 204     2938   1592   2338    420   -300    150       C  
ATOM   6198  CG2 ILE L 204     122.680  -7.222  -1.849  1.00 11.17           C  
ANISOU 6198  CG2 ILE L 204     1990    732   1522    435   -279    127       C  
ATOM   6199  CD1 ILE L 204     121.503  -6.468   0.899  1.00 23.71           C  
ANISOU 6199  CD1 ILE L 204     3674   2298   3038    407   -269    163       C  
ATOM   6200  N   VAL L 205     125.513  -6.019  -3.541  1.00 21.90           N  
ANISOU 6200  N   VAL L 205     3280   2122   2920    465   -294    100       N  
ATOM   6201  CA  VAL L 205     125.975  -5.631  -4.866  1.00 10.89           C  
ANISOU 6201  CA  VAL L 205     1848    743   1545    480   -271     94       C  
ATOM   6202  C   VAL L 205     125.526  -6.664  -5.889  1.00 10.89           C  
ANISOU 6202  C   VAL L 205     1826    754   1560    499   -270     76       C  
ATOM   6203  O   VAL L 205     125.616  -7.873  -5.648  1.00 18.79           O  
ANISOU 6203  O   VAL L 205     2826   1734   2579    506   -298     64       O  
ATOM   6204  CB  VAL L 205     127.508  -5.472  -4.892  1.00 11.11           C  
ANISOU 6204  CB  VAL L 205     1854    759   1607    492   -287     86       C  
ATOM   6205  CG1 VAL L 205     127.983  -5.125  -6.286  1.00 23.28           C  
ANISOU 6205  CG1 VAL L 205     3359   2311   3175    511   -253     84       C  
ATOM   6206  CG2 VAL L 205     127.945  -4.412  -3.894  1.00 11.16           C  
ANISOU 6206  CG2 VAL L 205     1883    747   1608    474   -289     96       C  
ATOM   6207  N   LYS L 206     125.042  -6.180  -7.032  1.00 10.70           N  
ANISOU 6207  N   LYS L 206     1785    755   1526    513   -240     75       N  
ATOM   6208  CA  LYS L 206     124.758  -7.012  -8.198  1.00 17.40           C  
ANISOU 6208  CA  LYS L 206     2605   1619   2386    539   -240     50       C  
ATOM   6209  C   LYS L 206     125.302  -6.290  -9.422  1.00 31.34           C  
ANISOU 6209  C   LYS L 206     4348   3409   4150    566   -215     53       C  
ATOM   6210  O   LYS L 206     124.799  -5.225  -9.792  1.00 48.47           O  
ANISOU 6210  O   LYS L 206     6534   5595   6286    572   -189     75       O  
ATOM   6211  CB  LYS L 206     123.262  -7.286  -8.344  1.00 10.64           C  
ANISOU 6211  CB  LYS L 206     1758    775   1511    541   -233     42       C  
ATOM   6212  CG  LYS L 206     122.797  -8.584  -7.710  1.00 14.96           C  
ANISOU 6212  CG  LYS L 206     2312   1286   2088    528   -252     29       C  
ATOM   6213  CD  LYS L 206     123.239  -9.787  -8.525  1.00 26.16           C  
ANISOU 6213  CD  LYS L 206     3702   2690   3547    551   -267     -9       C  
ATOM   6214  CE  LYS L 206     122.627 -11.071  -7.987  1.00 31.97           C  
ANISOU 6214  CE  LYS L 206     4453   3371   4323    539   -273    -20       C  
ATOM   6215  NZ  LYS L 206     122.998 -12.251  -8.813  1.00 41.17           N  
ANISOU 6215  NZ  LYS L 206     5596   4512   5533    565   -285    -67       N  
ATOM   6216  N   SER L 207     126.324  -6.864 -10.049  1.00 34.73           N  
ANISOU 6216  N   SER L 207     4744   3837   4613    589   -222     31       N  
ATOM   6217  CA  SER L 207     127.021  -6.223 -11.152  1.00 11.07           C  
ANISOU 6217  CA  SER L 207     1724    859   1625    617   -193     36       C  
ATOM   6218  C   SER L 207     127.076  -7.162 -12.348  1.00 11.30           C  
ANISOU 6218  C   SER L 207     1716    919   1661    661   -198     -9       C  
ATOM   6219  O   SER L 207     126.794  -8.359 -12.245  1.00 20.06           O  
ANISOU 6219  O   SER L 207     2817   2022   2782    664   -228    -48       O  
ATOM   6220  CB  SER L 207     128.439  -5.805 -10.739  1.00 11.23           C  
ANISOU 6220  CB  SER L 207     1727    850   1690    610   -186     45       C  
ATOM   6221  OG  SER L 207     129.152  -5.268 -11.837  1.00 62.41           O  
ANISOU 6221  OG  SER L 207     8178   7338   8196    639   -150     48       O  
ATOM   6222  N   PHE L 208     127.441  -6.600 -13.498  1.00 11.45           N  
ANISOU 6222  N   PHE L 208     1714    966   1671    696   -168     -7       N  
ATOM   6223  CA  PHE L 208     127.699  -7.398 -14.686  1.00 39.83           C  
ANISOU 6223  CA  PHE L 208     5277   4603   5254    760   -178    -67       C  
ATOM   6224  C   PHE L 208     128.673  -6.650 -15.584  1.00 32.10           C  
ANISOU 6224  C   PHE L 208     4303   3648   4245    829   -155    -73       C  
ATOM   6225  O   PHE L 208     128.688  -5.417 -15.619  1.00 12.62           O  
ANISOU 6225  O   PHE L 208     1886   1168   1741    837   -120    -16       O  
ATOM   6226  CB  PHE L 208     126.409  -7.731 -15.453  1.00 11.99           C  
ANISOU 6226  CB  PHE L 208     1758   1127   1671    792   -188    -95       C  
ATOM   6227  CG  PHE L 208     125.831  -6.570 -16.218  1.00 12.19           C  
ANISOU 6227  CG  PHE L 208     1827   1202   1602    844   -164    -59       C  
ATOM   6228  CD1 PHE L 208     124.963  -5.682 -15.605  1.00 40.37           C  
ANISOU 6228  CD1 PHE L 208     5435   4755   5149    806   -150     -1       C  
ATOM   6229  CD2 PHE L 208     126.140  -6.379 -17.556  1.00 12.94           C  
ANISOU 6229  CD2 PHE L 208     1925   1373   1616    944   -147    -82       C  
ATOM   6230  CE1 PHE L 208     124.426  -4.619 -16.308  1.00 43.50           C  
ANISOU 6230  CE1 PHE L 208     5886   5197   5447    866   -120     39       C  
ATOM   6231  CE2 PHE L 208     125.607  -5.316 -18.261  1.00 13.32           C  
ANISOU 6231  CE2 PHE L 208     2033   1478   1552   1012   -109    -27       C  
ATOM   6232  CZ  PHE L 208     124.749  -4.437 -17.637  1.00 12.95           C  
ANISOU 6232  CZ  PHE L 208     2036   1399   1486    972    -96     36       C  
ATOM   6233  N   ASN L 209     129.494  -7.414 -16.298  1.00 13.17           N  
ANISOU 6233  N   ASN L 209     1855   1287   1861    885   -165   -145       N  
ATOM   6234  CA  ASN L 209     130.385  -6.887 -17.319  1.00 13.98           C  
ANISOU 6234  CA  ASN L 209     1943   1445   1922    973   -126   -172       C  
ATOM   6235  C   ASN L 209     129.923  -7.376 -18.683  1.00 20.48           C  
ANISOU 6235  C   ASN L 209     2739   2377   2665   1050   -119   -230       C  
ATOM   6236  O   ASN L 209     129.531  -8.537 -18.835  1.00 15.96           O  
ANISOU 6236  O   ASN L 209     2127   1822   2117   1035   -163   -297       O  
ATOM   6237  CB  ASN L 209     131.833  -7.325 -17.081  1.00 27.17           C  
ANISOU 6237  CB  ASN L 209     3545   3110   3668    985   -137   -236       C  
ATOM   6238  CG  ASN L 209     132.332  -6.962 -15.703  1.00 30.91           C  
ANISOU 6238  CG  ASN L 209     4038   3497   4210    921   -157   -195       C  
ATOM   6239  OD1 ASN L 209     131.783  -6.079 -15.044  1.00 30.40           O  
ANISOU 6239  OD1 ASN L 209     4038   3378   4136    873   -141   -117       O  
ATOM   6240  ND2 ASN L 209     133.383  -7.641 -15.258  1.00 14.47           N  
ANISOU 6240  ND2 ASN L 209     1895   1416   2189    926   -196   -255       N  
ATOM   6241  N   ARG L 210     129.977  -6.489 -19.678  1.00 15.18           N  
ANISOU 6241  N   ARG L 210     2097   1785   1886   1139    -52   -199       N  
ATOM   6242  CA  ARG L 210     129.558  -6.862 -21.023  1.00 15.90           C  
ANISOU 6242  CA  ARG L 210     2155   2014   1871   1224    -38   -253       C  
ATOM   6243  C   ARG L 210     130.464  -7.913 -21.654  1.00 26.03           C  
ANISOU 6243  C   ARG L 210     3328   3373   3189   1241    -49   -382       C  
ATOM   6244  O   ARG L 210     130.094  -8.481 -22.687  1.00 34.24           O  
ANISOU 6244  O   ARG L 210     4325   4528   4158   1287    -56   -453       O  
ATOM   6245  CB  ARG L 210     129.494  -5.621 -21.914  1.00 16.65           C  
ANISOU 6245  CB  ARG L 210     2315   2191   1818   1327     64   -162       C  
ATOM   6246  CG  ARG L 210     128.593  -4.519 -21.374  1.00 16.80           C  
ANISOU 6246  CG  ARG L 210     2457   2128   1798   1312     79    -25       C  
ATOM   6247  CD  ARG L 210     128.111  -3.606 -22.489  1.00 17.12           C  
ANISOU 6247  CD  ARG L 210     2571   2269   1666   1438    162     69       C  
ATOM   6248  NE  ARG L 210     129.222  -3.019 -23.230  1.00 18.23           N  
ANISOU 6248  NE  ARG L 210     2709   2470   1746   1400    278    112       N  
ATOM   6249  CZ  ARG L 210     129.115  -2.503 -24.450  1.00 50.56           C  
ANISOU 6249  CZ  ARG L 210     6838   6696   5677   1459    358    174       C  
ATOM   6250  NH1 ARG L 210     127.945  -2.509 -25.074  1.00 53.26           N  
ANISOU 6250  NH1 ARG L 210     7212   7131   5895   1576    320    192       N  
ATOM   6251  NH2 ARG L 210     130.180  -1.991 -25.051  1.00 44.93           N  
ANISOU 6251  NH2 ARG L 210     6124   6031   4918   1401    477    215       N  
ATOM   6252  N   ASN L 211     131.628  -8.190 -21.060  1.00 27.24           N  
ANISOU 6252  N   ASN L 211     3430   3474   3446   1206    -55   -420       N  
ATOM   6253  CA  ASN L 211     132.518  -9.232 -21.559  1.00 25.12           C  
ANISOU 6253  CA  ASN L 211     3056   3270   3220   1214    -71   -543       C  
ATOM   6254  C   ASN L 211     132.012 -10.637 -21.260  1.00 40.61           C  
ANISOU 6254  C   ASN L 211     5007   5173   5250   1167   -156   -598       C  
ATOM   6255  O   ASN L 211     132.598 -11.604 -21.759  1.00 46.11           O  
ANISOU 6255  O   ASN L 211     5633   5915   5974   1181   -176   -699       O  
ATOM   6256  CB  ASN L 211     133.916  -9.060 -20.964  1.00 26.76           C  
ANISOU 6256  CB  ASN L 211     3205   3451   3512   1200    -55   -569       C  
ATOM   6257  CG  ASN L 211     134.555  -7.745 -21.350  1.00 42.96           C  
ANISOU 6257  CG  ASN L 211     5249   5578   5496   1250     61   -539       C  
ATOM   6258  OD1 ASN L 211     133.884  -6.838 -21.843  1.00 54.33           O  
ANISOU 6258  OD1 ASN L 211     6776   7045   6823   1240    131   -430       O  
ATOM   6259  ND2 ASN L 211     135.859  -7.633 -21.126  1.00 39.15           N  
ANISOU 6259  ND2 ASN L 211     4679   5122   5073   1201     92   -586       N  
ATOM   6260  N   GLU L 212     130.961 -10.774 -20.458  1.00 32.61           N  
ANISOU 6260  N   GLU L 212     4064   4066   4262   1112   -196   -537       N  
ATOM   6261  CA  GLU L 212     130.397 -12.081 -20.140  1.00 41.66           C  
ANISOU 6261  CA  GLU L 212     5208   5156   5464   1073   -254   -583       C  
ATOM   6262  C   GLU L 212     129.810 -12.749 -21.382  1.00 37.62           C  
ANISOU 6262  C   GLU L 212     4653   4744   4895   1120   -266   -684       C  
ATOM   6263  O   GLU L 212     129.455 -13.927 -21.357  1.00 17.22           O  
ANISOU 6263  O   GLU L 212     2054   2125   2362   1101   -309   -752       O  
ATOM   6264  CB  GLU L 212     129.323 -11.948 -19.059  1.00 45.45           C  
ANISOU 6264  CB  GLU L 212     5761   5541   5965   1005   -270   -497       C  
ATOM   6265  CG  GLU L 212     129.853 -11.532 -17.696  1.00 42.73           C  
ANISOU 6265  CG  GLU L 212     5453   5106   5678    947   -266   -411       C  
ATOM   6266  CD  GLU L 212     128.742 -11.185 -16.724  1.00 47.65           C  
ANISOU 6266  CD  GLU L 212     6138   5669   6299    881   -262   -328       C  
ATOM   6267  OE1 GLU L 212     127.944 -10.276 -17.031  1.00 57.31           O  
ANISOU 6267  OE1 GLU L 212     7389   6924   7462    890   -240   -289       O  
ATOM   6268  OE2 GLU L 212     128.659 -11.827 -15.656  1.00 53.43           O  
ANISOU 6268  OE2 GLU L 212     6889   6332   7079    829   -278   -303       O  
TER    6269      GLU L 212                                                      
HETATM 6270  N   SAR B   1      72.554  21.047  18.169  1.00 83.48           N  
HETATM 6271  CA  SAR B   1      71.510  22.059  18.206  1.00 82.58           C  
HETATM 6272  C   SAR B   1      70.073  21.589  17.856  1.00 73.81           C  
HETATM 6273  O   SAR B   1      69.872  20.392  17.493  1.00 73.27           O  
HETATM 6274  CN  SAR B   1      72.708  20.325  19.409  1.00 72.40           C  
ATOM   6275  N   ARG B   2      69.106  22.495  17.956  1.00131.16           N  
ANISOU 6275  N   ARG B   2     9348  20288  20197  -1060   -434   -208       N  
ATOM   6276  CA  ARG B   2      67.719  22.171  17.639  1.00105.44           C  
ANISOU 6276  CA  ARG B   2     6213  16950  16898  -1025   -332   -194       C  
ATOM   6277  C   ARG B   2      66.958  23.387  17.126  1.00 90.38           C  
ANISOU 6277  C   ARG B   2     4480  14989  14872  -1106   -270   -375       C  
ATOM   6278  O   ARG B   2      67.023  24.467  17.712  1.00 85.40           O  
ANISOU 6278  O   ARG B   2     3865  14475  14110  -1179   -313   -508       O  
ATOM   6279  CB  ARG B   2      67.008  21.594  18.866  1.00102.12           C  
ANISOU 6279  CB  ARG B   2     5727  16693  16382   -960   -398   -104       C  
ATOM   6280  CG  ARG B   2      66.985  20.077  18.907  1.00 95.68           C  
ANISOU 6280  CG  ARG B   2     4819  15834  15703   -843   -350     63       C  
ATOM   6281  CD  ARG B   2      66.303  19.557  20.163  1.00 92.68           C  
ANISOU 6281  CD  ARG B   2     4417  15641  15155   -799   -410    251       C  
ATOM   6282  NE  ARG B   2      64.971  20.126  20.354  1.00 98.56           N  
ANISOU 6282  NE  ARG B   2     5328  16386  15733   -852   -341    148       N  
ATOM   6283  CZ  ARG B   2      63.877  19.702  19.729  1.00 96.18           C  
ANISOU 6283  CZ  ARG B   2     5098  15949  15496   -843   -197    131       C  
ATOM   6284  NH1 ARG B   2      62.707  20.277  19.973  1.00 85.66           N  
ANISOU 6284  NH1 ARG B   2     3868  14637  14043   -877   -145     47       N  
ATOM   6285  NH2 ARG B   2      63.950  18.709  18.853  1.00 93.41           N  
ANISOU 6285  NH2 ARG B   2     4707  15443  15340   -812    -91    191       N  
ATOM   6286  N   VAL B   3      66.237  23.202  16.021  1.00 83.58           N  
ANISOU 6286  N   VAL B   3     3732  13971  14055  -1106   -163   -384       N  
ATOM   6287  CA  VAL B   3      65.382  24.236  15.457  1.00 82.64           C  
ANISOU 6287  CA  VAL B   3     3732  13795  13871  -1151   -118   -515       C  
ATOM   6288  C   VAL B   3      64.041  23.611  15.101  1.00 93.60           C  
ANISOU 6288  C   VAL B   3     5157  15140  15267  -1105    -76   -433       C  
ATOM   6289  O   VAL B   3      63.915  22.394  14.952  1.00 92.64           O  
ANISOU 6289  O   VAL B   3     5007  14989  15204  -1081    -41   -318       O  
ATOM   6290  CB  VAL B   3      66.007  24.910  14.217  1.00 82.27           C  
ANISOU 6290  CB  VAL B   3     3772  13609  13876  -1246    -54   -646       C  
ATOM   6291  CG1 VAL B   3      67.223  25.728  14.612  1.00 83.22           C  
ANISOU 6291  CG1 VAL B   3     3855  13785  13980  -1319    -79   -766       C  
ATOM   6292  CG2 VAL B   3      66.372  23.866  13.172  1.00 82.02           C  
ANISOU 6292  CG2 VAL B   3     3763  13442  13958  -1273     24   -587       C  
ATOM   6293  N   TYR B   4      63.031  24.465  14.957  1.00 84.23           N  
ANISOU 6293  N   TYR B   4     4012  13958  14034  -1100    -66   -503       N  
ATOM   6294  CA  TYR B   4      61.683  24.023  14.614  1.00 81.25           C  
ANISOU 6294  CA  TYR B   4     3638  13564  13667  -1065    -46   -431       C  
ATOM   6295  C   TYR B   4      61.517  24.073  13.098  1.00 80.81           C  
ANISOU 6295  C   TYR B   4     3646  13398  13660  -1143    -35   -458       C  
ATOM   6296  O   TYR B   4      61.439  25.156  12.508  1.00 92.36           O  
ANISOU 6296  O   TYR B   4     5131  14828  15133  -1168    -47   -554       O  
ATOM   6297  CB  TYR B   4      60.639  24.886  15.317  1.00 81.69           C  
ANISOU 6297  CB  TYR B   4     3654  13701  13683  -1003    -36   -476       C  
ATOM   6298  CG  TYR B   4      59.283  24.228  15.444  1.00 81.85           C  
ANISOU 6298  CG  TYR B   4     3630  13747  13722   -954    -14   -381       C  
ATOM   6299  CD1 TYR B   4      58.310  24.404  14.470  1.00 81.90           C  
ANISOU 6299  CD1 TYR B   4     3625  13716  13777   -952    -34   -354       C  
ATOM   6300  CD2 TYR B   4      58.977  23.430  16.540  1.00 82.28           C  
ANISOU 6300  CD2 TYR B   4     3633  13884  13748   -927     24   -323       C  
ATOM   6301  CE1 TYR B   4      57.068  23.806  14.582  1.00 82.37           C  
ANISOU 6301  CE1 TYR B   4     3621  13816  13861   -926    -18   -273       C  
ATOM   6302  CE2 TYR B   4      57.736  22.827  16.661  1.00 82.63           C  
ANISOU 6302  CE2 TYR B   4     3631  13943  13820   -906     74   -261       C  
ATOM   6303  CZ  TYR B   4      56.786  23.018  15.679  1.00 87.65           C  
ANISOU 6303  CZ  TYR B   4     4255  14537  14510   -906     52   -236       C  
ATOM   6304  OH  TYR B   4      55.551  22.422  15.792  1.00 92.99           O  
ANISOU 6304  OH  TYR B   4     4864  15244  15224   -903     97   -179       O  
ATOM   6305  N   ILE B   5      61.452  22.899  12.473  1.00 80.66           N  
ANISOU 6305  N   ILE B   5     3641  13328  13677  -1202      3   -391       N  
ATOM   6306  CA  ILE B   5      61.373  22.797  11.025  1.00 80.59           C  
ANISOU 6306  CA  ILE B   5     3689  13230  13702  -1336     25   -440       C  
ATOM   6307  C   ILE B   5      59.963  22.475  10.537  1.00101.45           C  
ANISOU 6307  C   ILE B   5     6298  15927  16323  -1374    -16   -387       C  
ATOM   6308  O   ILE B   5      59.618  22.834   9.405  1.00104.19           O  
ANISOU 6308  O   ILE B   5     6665  16258  16665  -1486    -60   -430       O  
ATOM   6309  CB  ILE B   5      62.382  21.749  10.506  1.00 80.66           C  
ANISOU 6309  CB  ILE B   5     3733  13127  13785  -1431    139   -450       C  
ATOM   6310  CG1 ILE B   5      63.770  22.025  11.091  1.00 90.36           C  
ANISOU 6310  CG1 ILE B   5     4946  14336  15052  -1374    155   -478       C  
ATOM   6311  CG2 ILE B   5      62.450  21.737   8.987  1.00 81.08           C  
ANISOU 6311  CG2 ILE B   5     3863  13071  13874  -1628    199   -548       C  
ATOM   6312  CD1 ILE B   5      64.836  21.073  10.616  1.00 91.15           C  
ANISOU 6312  CD1 ILE B   5     5046  14314  15273  -1433    288   -484       C  
ATOM   6313  N   HIS B   6      59.129  21.843  11.361  1.00 81.10           N  
ANISOU 6313  N   HIS B   6     3661  13428  13728  -1301     -9   -295       N  
ATOM   6314  CA  HIS B   6      57.820  21.397  10.904  1.00 81.73           C  
ANISOU 6314  CA  HIS B   6     3689  13567  13798  -1361    -39   -247       C  
ATOM   6315  C   HIS B   6      56.947  22.587  10.500  1.00 92.99           C  
ANISOU 6315  C   HIS B   6     5046  15062  15222  -1314   -165   -249       C  
ATOM   6316  O   HIS B   6      57.103  23.691  11.033  1.00 82.30           O  
ANISOU 6316  O   HIS B   6     3674  13712  13884  -1186   -186   -279       O  
ATOM   6317  CB  HIS B   6      57.135  20.583  11.999  1.00 95.07           C  
ANISOU 6317  CB  HIS B   6     5320  15312  15492  -1290     24   -170       C  
ATOM   6318  CG  HIS B   6      57.961  19.438  12.495  1.00 92.59           C  
ANISOU 6318  CG  HIS B   6     5028  14950  15200  -1306    147   -150       C  
ATOM   6319  ND1 HIS B   6      58.223  18.322  11.729  1.00 88.61           N  
ANISOU 6319  ND1 HIS B   6     4559  14370  14740  -1451    258   -169       N  
ATOM   6320  CD2 HIS B   6      58.603  19.247  13.671  1.00 81.76           C  
ANISOU 6320  CD2 HIS B   6     3628  13603  13836  -1197    181   -116       C  
ATOM   6321  CE1 HIS B   6      58.985  17.489  12.416  1.00 82.19           C  
ANISOU 6321  CE1 HIS B   6     3729  13515  13984  -1398    369   -135       C  
ATOM   6322  NE2 HIS B   6      59.230  18.026  13.597  1.00 82.05           N  
ANISOU 6322  NE2 HIS B   6     3663  13579  13935  -1244    301    -94       N  
ATOM   6323  N   PRO B   7      56.017  22.389   9.556  1.00 94.47           N  
ANISOU 6323  N   PRO B   7     5176  15319  15401  -1423   -248   -221       N  
ATOM   6324  CA  PRO B   7      55.186  23.520   9.104  1.00 90.61           C  
ANISOU 6324  CA  PRO B   7     4616  14899  14912  -1347   -397   -167       C  
ATOM   6325  C   PRO B   7      54.303  24.106  10.193  1.00 90.13           C  
ANISOU 6325  C   PRO B   7     4393  14908  14945  -1140   -389   -125       C  
ATOM   6326  O   PRO B   7      54.089  25.325  10.223  1.00 95.04           O  
ANISOU 6326  O   PRO B   7     5023  15490  15599   -993   -434    -87       O  
ATOM   6327  CB  PRO B   7      54.350  22.910   7.966  1.00 85.79           C  
ANISOU 6327  CB  PRO B   7     3971  14385  14238  -1537   -507   -115       C  
ATOM   6328  CG  PRO B   7      55.121  21.717   7.512  1.00 85.11           C  
ANISOU 6328  CG  PRO B   7     4006  14230  14104  -1761   -381   -202       C  
ATOM   6329  CD  PRO B   7      55.773  21.175   8.755  1.00 90.49           C  
ANISOU 6329  CD  PRO B   7     4698  14819  14864  -1639   -213   -228       C  
ATOM   6330  N   ILE B   8      53.776  23.274  11.085  1.00 85.02           N  
ANISOU 6330  N   ILE B   8     3727  14260  14317  -1111   -300    -84       N  
ATOM   6331  CA  ILE B   8      52.947  23.761  12.180  1.00 85.78           C  
ANISOU 6331  CA  ILE B   8     3715  14403  14473   -943   -241    -48       C  
ATOM   6332  C   ILE B   8      53.592  23.408  13.516  1.00107.09           C  
ANISOU 6332  C   ILE B   8     6500  17063  17127   -903    -92    -99       C  
ATOM   6333  O   ILE B   8      53.485  24.150  14.493  1.00107.01           O  
ANISOU 6333  O   ILE B   8     6452  17063  17143   -787    -14   -144       O  
ATOM   6334  CB  ILE B   8      51.522  23.195  12.093  1.00 87.32           C  
ANISOU 6334  CB  ILE B   8     3785  14631  14761   -958   -266      5       C  
ATOM   6335  CG1 ILE B   8      50.952  23.398  10.689  1.00 88.67           C  
ANISOU 6335  CG1 ILE B   8     3859  14878  14954  -1036   -454    -42       C  
ATOM   6336  CG2 ILE B   8      50.622  23.863  13.116  1.00 88.51           C  
ANISOU 6336  CG2 ILE B   8     3807  14907  14917   -788   -178     36       C  
ATOM   6337  CD1 ILE B   8      49.550  22.862  10.518  1.00 90.65           C  
ANISOU 6337  CD1 ILE B   8     3955  15219  15267  -1075   -504    -35       C  
ATOM   6338  OXT ILE B   8      54.243  22.371  13.649  1.00103.12           O  
ANISOU 6338  OXT ILE B   8     6085  16520  16575   -993    -42   -103       O  
TER    6339      ILE B   8                                                      
CONECT    6 2760                                                                
CONECT  670 1311                                                                
CONECT 1311  670                                                                
CONECT 2760    6                                                                
CONECT 3144 3731                                                                
CONECT 3731 3144                                                                
CONECT 4097 4507                                                                
CONECT 4507 4097                                                                
CONECT 4799 5285                                                                
CONECT 5285 4799                                                                
CONECT 5621 6118                                                                
CONECT 6118 5621                                                                
CONECT 6270 6271 6274                                                           
CONECT 6271 6270 6272                                                           
CONECT 6272 6271 6273 6275                                                      
CONECT 6273 6272                                                                
CONECT 6274 6270                                                                
CONECT 6275 6272                                                                
MASTER      518    0    1   17   45    0    0    6 6335    4   18   68          
END