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***  R135  ***

elNémo ID: 20072116435194248

Job options:

ID        	=	 20072116435194248
JOBID     	=	 R135
USERID    	=	 Chantal.abergel
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER R135

HEADER    OXIDOREDUCTASE                          28-MAR-15   4Z24              
TITLE     MIMIVIRUS R135 (RESIDUES 51-702)                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GMC-TYPE OXIDOREDUCTASE R135;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 51-702;                                       
COMPND   5 EC: 1.-.-.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: FAD COFACTOR BOUND TO THE ENZYME                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACANTHAMOEBA POLYPHAGA MIMIVIRUS;               
SOURCE   3 ORGANISM_COMMON: APMV;                                               
SOURCE   4 ORGANISM_TAXID: 212035;                                              
SOURCE   5 GENE: MIMI_R135;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GMC OXIDOREDUCTASE, FAD, FIBER, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KLOSE,M.G.ROSSMANN                                                  
REVDAT   6   11-DEC-19 4Z24    1       REMARK                                   
REVDAT   5 2 13-SEP-17 4Z24    1       SOURCE JRNL   REMARK                     
REVDAT   4 3 17-JUN-15 4Z24    1       JRNL                                     
REVDAT   3 4 10-JUN-15 4Z24    1       JRNL                                     
REVDAT   2 5 03-JUN-15 4Z24    1       TITLE  JRNL                              
REVDAT   1 6 15-APR-15 4Z24    0                                                
JRNL        AUTH   T.KLOSE,D.A.HERBST,H.ZHU,J.P.MAX,H.I.KENTTAMAA,M.G.ROSSMANN  
JRNL        TITL   A MIMIVIRUS ENZYME THAT PARTICIPATES IN VIRAL ENTRY.         
JRNL        REF    STRUCTURE                     V.  23  1058 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25982526                                                     
JRNL        DOI    10.1016/J.STR.2015.03.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 105097                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5247                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.7202 -  6.2100    0.99     3314   176  0.1423 0.1595        
REMARK   3     2  6.2100 -  4.9307    0.99     3311   169  0.1398 0.1742        
REMARK   3     3  4.9307 -  4.3079    0.98     3269   181  0.1198 0.1497        
REMARK   3     4  4.3079 -  3.9142    0.99     3337   168  0.1178 0.1409        
REMARK   3     5  3.9142 -  3.6337    0.99     3292   175  0.1369 0.1649        
REMARK   3     6  3.6337 -  3.4196    0.99     3357   160  0.1389 0.1737        
REMARK   3     7  3.4196 -  3.2484    0.99     3294   184  0.1430 0.1716        
REMARK   3     8  3.2484 -  3.1070    0.99     3378   153  0.1456 0.1819        
REMARK   3     9  3.1070 -  2.9874    0.99     3323   171  0.1563 0.1968        
REMARK   3    10  2.9874 -  2.8843    0.99     3331   192  0.1541 0.1963        
REMARK   3    11  2.8843 -  2.7941    0.99     3315   175  0.1630 0.2252        
REMARK   3    12  2.7941 -  2.7143    0.99     3359   174  0.1593 0.2003        
REMARK   3    13  2.7143 -  2.6428    1.00     3333   166  0.1616 0.2089        
REMARK   3    14  2.6428 -  2.5784    0.99     3321   154  0.1596 0.1921        
REMARK   3    15  2.5784 -  2.5197    0.99     3357   191  0.1629 0.2476        
REMARK   3    16  2.5197 -  2.4661    0.99     3381   149  0.1678 0.2246        
REMARK   3    17  2.4661 -  2.4168    0.99     3279   177  0.1775 0.2016        
REMARK   3    18  2.4168 -  2.3712    1.00     3344   194  0.1819 0.2356        
REMARK   3    19  2.3712 -  2.3288    0.99     3344   187  0.1818 0.2401        
REMARK   3    20  2.3288 -  2.2894    0.99     3321   172  0.1886 0.2323        
REMARK   3    21  2.2894 -  2.2524    0.99     3333   187  0.1920 0.2474        
REMARK   3    22  2.2524 -  2.2178    0.99     3294   179  0.1983 0.2339        
REMARK   3    23  2.2178 -  2.1852    0.99     3332   182  0.2000 0.2501        
REMARK   3    24  2.1852 -  2.1544    0.99     3265   186  0.2119 0.2824        
REMARK   3    25  2.1544 -  2.1253    0.99     3436   165  0.2199 0.2727        
REMARK   3    26  2.1253 -  2.0977    1.00     3253   176  0.2271 0.2852        
REMARK   3    27  2.0977 -  2.0715    1.00     3381   199  0.2290 0.2708        
REMARK   3    28  2.0715 -  2.0465    0.99     3277   173  0.2436 0.2714        
REMARK   3    29  2.0465 -  2.0227    0.99     3329   160  0.2486 0.3087        
REMARK   3    30  2.0227 -  2.0000    0.99     3390   172  0.2586 0.3165        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          10348                                  
REMARK   3   ANGLE     :  1.087          14140                                  
REMARK   3   CHIRALITY :  0.044           1570                                  
REMARK   3   PLANARITY :  0.006           1842                                  
REMARK   3   DIHEDRAL  : 11.865           3686                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 5:148)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9690  26.3735  40.3200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1163 T22:   0.1054                                     
REMARK   3      T33:   0.0819 T12:   0.0008                                     
REMARK   3      T13:  -0.0110 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9571 L22:   0.3679                                     
REMARK   3      L33:   1.0292 L12:   0.1497                                     
REMARK   3      L13:   0.0392 L23:  -0.3070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0326 S12:   0.1173 S13:   0.0168                       
REMARK   3      S21:  -0.0499 S22:   0.0059 S23:   0.0140                       
REMARK   3      S31:   0.0655 S32:  -0.0980 S33:   0.0275                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 149:178)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5369  46.0518  26.1912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2823 T22:   0.3383                                     
REMARK   3      T33:   0.1117 T12:  -0.1830                                     
REMARK   3      T13:  -0.0178 T23:   0.2807                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7017 L22:   0.9250                                     
REMARK   3      L33:   0.4182 L12:  -0.2863                                     
REMARK   3      L13:  -0.0789 L23:  -0.1578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1458 S12:   0.2366 S13:   0.2459                       
REMARK   3      S21:  -0.1030 S22:  -0.1474 S23:  -0.0505                       
REMARK   3      S31:  -0.2907 S32:   0.3121 S33:  -0.3478                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 179:256)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8044  32.7087  28.7469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1500 T22:   0.1923                                     
REMARK   3      T33:   0.0974 T12:   0.0060                                     
REMARK   3      T13:  -0.0453 T23:   0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8218 L22:   0.8796                                     
REMARK   3      L33:   1.3894 L12:   0.6464                                     
REMARK   3      L13:  -0.3221 L23:  -0.3996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1133 S12:   0.2660 S13:   0.1297                       
REMARK   3      S21:  -0.1300 S22:   0.1034 S23:   0.0951                       
REMARK   3      S31:  -0.0423 S32:  -0.1611 S33:  -0.0152                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 257:413)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2458  25.6813  44.3070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0962 T22:   0.0991                                     
REMARK   3      T33:   0.1019 T12:   0.0252                                     
REMARK   3      T13:  -0.0067 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8192 L22:   0.3912                                     
REMARK   3      L33:   1.1611 L12:   0.1287                                     
REMARK   3      L13:   0.0120 L23:  -0.2533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0150 S12:   0.0578 S13:  -0.0040                       
REMARK   3      S21:  -0.0048 S22:  -0.0449 S23:  -0.0288                       
REMARK   3      S31:   0.0657 S32:   0.0980 S33:   0.0470                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 414:462)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1628  32.9107  50.9665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0921 T22:   0.1055                                     
REMARK   3      T33:   0.1037 T12:   0.0110                                     
REMARK   3      T13:  -0.0242 T23:   0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8636 L22:   0.4337                                     
REMARK   3      L33:   1.2477 L12:   0.5243                                     
REMARK   3      L13:  -0.2675 L23:  -0.3499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:   0.0020 S13:   0.0260                       
REMARK   3      S21:   0.0383 S22:  -0.0654 S23:  -0.0800                       
REMARK   3      S31:  -0.1076 S32:   0.1376 S33:   0.0894                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 463:515)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  38.9512  42.1548  40.8666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1787 T22:   0.2401                                     
REMARK   3      T33:   0.1872 T12:  -0.0950                                     
REMARK   3      T13:  -0.0408 T23:   0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5933 L22:   0.4049                                     
REMARK   3      L33:   0.7290 L12:  -0.5697                                     
REMARK   3      L13:   0.1606 L23:   0.0529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1214 S12:   0.0722 S13:   0.1664                       
REMARK   3      S21:   0.0038 S22:   0.0676 S23:  -0.0202                       
REMARK   3      S31:  -0.2784 S32:   0.2436 S33:   0.0370                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 516:573)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  43.8355  44.2782  47.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1871 T22:   0.2820                                     
REMARK   3      T33:   0.2195 T12:  -0.0915                                     
REMARK   3      T13:  -0.0444 T23:   0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3955 L22:   1.6787                                     
REMARK   3      L33:   0.6754 L12:  -0.0428                                     
REMARK   3      L13:  -0.7705 L23:   0.3270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0622 S12:  -0.0049 S13:   0.2818                       
REMARK   3      S21:   0.0250 S22:   0.0655 S23:  -0.2544                       
REMARK   3      S31:  -0.1710 S32:   0.3364 S33:  -0.0202                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 574:651)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2899  17.3819  34.4073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1762 T22:   0.1442                                     
REMARK   3      T33:   0.1011 T12:   0.0295                                     
REMARK   3      T13:   0.0099 T23:  -0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2160 L22:   1.0065                                     
REMARK   3      L33:   1.1055 L12:  -0.1138                                     
REMARK   3      L13:  -0.0392 L23:  -0.0825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0491 S12:   0.2589 S13:  -0.1224                       
REMARK   3      S21:  -0.1666 S22:  -0.0939 S23:  -0.0454                       
REMARK   3      S31:   0.2297 S32:   0.0986 S33:   0.0289                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 5:178)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1562  26.1938  82.4195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1954 T22:   0.1942                                     
REMARK   3      T33:   0.0994 T12:  -0.0359                                     
REMARK   3      T13:  -0.0333 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3783 L22:   0.8568                                     
REMARK   3      L33:   1.0234 L12:   0.2612                                     
REMARK   3      L13:   0.0573 L23:  -0.3717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0351 S12:  -0.1694 S13:  -0.0061                       
REMARK   3      S21:   0.2370 S22:  -0.1112 S23:  -0.0652                       
REMARK   3      S31:  -0.1207 S32:   0.1500 S33:   0.0030                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 179:236)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6802  29.5710  94.2346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4012 T22:   0.3871                                     
REMARK   3      T33:   0.1342 T12:  -0.1483                                     
REMARK   3      T13:  -0.0794 T23:   0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5803 L22:   2.0679                                     
REMARK   3      L33:   1.2617 L12:   0.3781                                     
REMARK   3      L13:   0.0512 L23:   1.1688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0446 S12:  -0.2815 S13:  -0.0353                       
REMARK   3      S21:   0.4391 S22:  -0.0720 S23:  -0.1985                       
REMARK   3      S31:  -0.1705 S32:   0.4415 S33:  -0.1209                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 237:277)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5032   7.5286  77.8826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1865 T22:   0.1225                                     
REMARK   3      T33:   0.1396 T12:  -0.0276                                     
REMARK   3      T13:   0.0343 T23:   0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6483 L22:   0.9740                                     
REMARK   3      L33:   2.3542 L12:  -0.2599                                     
REMARK   3      L13:   1.1124 L23:  -0.5066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0231 S12:  -0.0185 S13:  -0.2940                       
REMARK   3      S21:  -0.1017 S22:   0.0687 S23:   0.0535                       
REMARK   3      S31:   0.3513 S32:  -0.0622 S33:  -0.0999                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 278:293)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9689   7.1442  70.0699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1833 T22:   0.1343                                     
REMARK   3      T33:   0.1720 T12:  -0.0021                                     
REMARK   3      T13:  -0.0233 T23:   0.0789                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5396 L22:   2.3289                                     
REMARK   3      L33:   8.0913 L12:  -1.7740                                     
REMARK   3      L13:  -6.4701 L23:   3.1247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2600 S12:   0.0455 S13:  -0.2148                       
REMARK   3      S21:   0.0682 S22:   0.0594 S23:   0.1067                       
REMARK   3      S31:   0.4551 S32:  -0.2236 S33:   0.1929                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 294:419)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1325  36.1823  77.1346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2269 T22:   0.1695                                     
REMARK   3      T33:   0.1329 T12:  -0.0417                                     
REMARK   3      T13:  -0.0126 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6516 L22:   0.8007                                     
REMARK   3      L33:   1.1747 L12:   0.3237                                     
REMARK   3      L13:  -0.0666 L23:  -0.2757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0403 S12:  -0.1586 S13:   0.1361                       
REMARK   3      S21:   0.2063 S22:  -0.0995 S23:  -0.0488                       
REMARK   3      S31:  -0.3159 S32:   0.1731 S33:   0.0539                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 420:573)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3462  50.3661  74.3819              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4454 T22:   0.1616                                     
REMARK   3      T33:   0.2152 T12:  -0.1052                                     
REMARK   3      T13:  -0.0263 T23:  -0.0506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2161 L22:   1.3173                                     
REMARK   3      L33:   1.2748 L12:   0.5684                                     
REMARK   3      L13:  -0.0822 L23:  -0.1008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1495 S12:  -0.1836 S13:   0.3705                       
REMARK   3      S21:   0.2388 S22:  -0.2002 S23:   0.0091                       
REMARK   3      S31:  -0.6186 S32:   0.1596 S33:   0.0901                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 574:587)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4823  32.6757  76.7857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2923 T22:   0.1839                                     
REMARK   3      T33:   0.0905 T12:  -0.0220                                     
REMARK   3      T13:  -0.0104 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2434 L22:   2.0838                                     
REMARK   3      L33:   4.0745 L12:   2.1816                                     
REMARK   3      L13:  -3.0042 L23:  -0.9101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1280 S12:   0.2356 S13:   0.3100                       
REMARK   3      S21:   0.1101 S22:   0.1405 S23:  -0.0213                       
REMARK   3      S31:  -0.5386 S32:   0.0195 S33:  -0.2343                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 588:651)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5007  21.4488  88.0795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2041 T22:   0.2119                                     
REMARK   3      T33:   0.1067 T12:   0.0137                                     
REMARK   3      T13:   0.0282 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4358 L22:   1.1740                                     
REMARK   3      L33:   1.5294 L12:  -0.0573                                     
REMARK   3      L13:   0.0770 L23:  -0.6060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0187 S12:  -0.3126 S13:  -0.0660                       
REMARK   3      S21:   0.2934 S22:   0.0429 S23:   0.0892                       
REMARK   3      S31:  -0.1567 S32:  -0.0580 S33:  -0.0145                       
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 4Z24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208468.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03320                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105150                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.20900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3Q9T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, PEG 8000, CALCIUM CHLORIDE,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     THR B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 289    CG   CD   CE   NZ                                   
REMARK 470     LYS A 324    CG   CD   CE   NZ                                   
REMARK 470     LYS A 480    CG   CD   CE   NZ                                   
REMARK 470     LYS B 269    CG   CD   CE   NZ                                   
REMARK 470     GLU B 282    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1537     O    HOH B  1599              1.81            
REMARK 500   OD2  ASP B   128     O    HOH B  1001              1.83            
REMARK 500   O    HOH A  1166     O    HOH A  1794              1.84            
REMARK 500   O    HOH A  1050     O    HOH A  1691              1.85            
REMARK 500   O    HOH A  1348     O    HOH A  1352              1.86            
REMARK 500   NE   ARG B   587     O    HOH B  1002              1.88            
REMARK 500   O    HOH B  1584     O    HOH B  1606              1.88            
REMARK 500   O    HOH A  1452     O    HOH A  1574              1.90            
REMARK 500   O    HOH B  1594     O    HOH B  1654              1.93            
REMARK 500   O    HOH A  1856     O    HOH A  1872              1.93            
REMARK 500   O    HOH A  1661     O    HOH A  1812              1.93            
REMARK 500   O    THR A   192     O    HOH A  1001              1.94            
REMARK 500   O    HOH B  1539     O    HOH B  1671              1.94            
REMARK 500   O    HOH A  1099     O    HOH A  1490              1.96            
REMARK 500   O    HOH B  1492     O    HOH B  1576              1.97            
REMARK 500   O    HOH A  1508     O    HOH A  1554              1.97            
REMARK 500   O    VAL A   349     O    HOH A  1002              1.98            
REMARK 500   O    HOH B  1179     O    HOH B  1549              2.00            
REMARK 500   O    HOH B  1468     O    HOH B  1672              2.00            
REMARK 500   O    HOH B  1478     O    HOH B  1577              2.00            
REMARK 500   O    HOH A  1073     O    HOH A  1161              2.00            
REMARK 500   O    HOH A  1690     O    HOH A  1795              2.01            
REMARK 500   O    HOH A  1745     O    HOH A  1796              2.01            
REMARK 500   OD1  ASN B     4     O    HOH B  1003              2.02            
REMARK 500   O    HOH B  1094     O    HOH B  1623              2.02            
REMARK 500   O    HOH B  1060     O    HOH B  1549              2.02            
REMARK 500   O    HOH A  1507     O    HOH A  1660              2.02            
REMARK 500   O    VAL B   462     O    HOH B  1004              2.03            
REMARK 500   O    HOH B  1522     O    HOH B  1652              2.03            
REMARK 500   O    HOH A  1230     O    HOH A  1768              2.04            
REMARK 500   O    HOH B  1210     O    HOH B  1595              2.04            
REMARK 500   O    HOH A  1005     O    HOH A  1073              2.04            
REMARK 500   O    HOH B  1463     O    HOH B  1616              2.04            
REMARK 500   O    HOH A  1004     O    HOH A  1664              2.04            
REMARK 500   O    HOH B  1242     O    HOH B  1467              2.04            
REMARK 500   O    HOH A  1454     O    HOH A  1645              2.05            
REMARK 500   O    HOH B  1020     O    HOH B  1659              2.06            
REMARK 500   O    HOH A  1447     O    HOH B  1545              2.06            
REMARK 500   O    HOH A  1212     O    HOH A  1307              2.06            
REMARK 500   O    HOH A  1043     O    HOH B  1228              2.07            
REMARK 500   O    HOH B  1113     O    HOH B  1578              2.07            
REMARK 500   O    HOH A  1020     O    HOH A  1578              2.08            
REMARK 500   O    HOH B  1154     O    HOH B  1507              2.08            
REMARK 500   NH2  ARG B   239     O    HOH B  1005              2.08            
REMARK 500   O    HOH B  1109     O    HOH B  1246              2.09            
REMARK 500   O    HOH A  1322     O    HOH A  1409              2.09            
REMARK 500   O    HOH A  1597     O    HOH A  1750              2.09            
REMARK 500   O    HOH B  1387     O    HOH B  1593              2.09            
REMARK 500   O    HOH A  1538     O    HOH A  1848              2.09            
REMARK 500   O    HOH B  1463     O    HOH B  1677              2.10            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      95 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1503     O    HOH A  1605     1455     1.88            
REMARK 500   O    HOH A  1609     O    HOH B  1525     1444     2.08            
REMARK 500   O    HOH A  1298     O    HOH A  1592     1655     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  14       53.57    -91.56                                   
REMARK 500    ALA A  85       57.38   -148.05                                   
REMARK 500    ASN A 142       67.62     63.12                                   
REMARK 500    ASP A 264      -69.84    -93.58                                   
REMARK 500    LYS A 292      -60.64   -123.76                                   
REMARK 500    LEU A 375      -36.24   -142.46                                   
REMARK 500    ASN A 386       51.06   -107.02                                   
REMARK 500    ARG A 435       52.22   -119.14                                   
REMARK 500    PHE A 458       89.84   -151.51                                   
REMARK 500    THR A 460      -94.77   -102.31                                   
REMARK 500    THR A 467     -165.15   -101.98                                   
REMARK 500    ASP A 551       38.95    -91.26                                   
REMARK 500    SER A 577       46.06    -94.70                                   
REMARK 500    CYS A 583       49.64   -141.44                                   
REMARK 500    ARG A 587      -60.08   -125.16                                   
REMARK 500    ASN A 600       32.01   -157.60                                   
REMARK 500    ASP A 605     -168.93   -111.00                                   
REMARK 500    ALA B  85       56.11   -147.47                                   
REMARK 500    ASN B 142       66.18     63.07                                   
REMARK 500    ASP B 264      -70.14    -94.92                                   
REMARK 500    LYS B 292      -61.18   -123.98                                   
REMARK 500    LEU B 375      -36.35   -141.58                                   
REMARK 500    ASN B 386       50.97   -108.72                                   
REMARK 500    ARG B 435       52.33   -119.09                                   
REMARK 500    PHE B 458       89.66   -151.15                                   
REMARK 500    THR B 460      -93.84   -101.07                                   
REMARK 500    THR B 467     -165.86   -105.74                                   
REMARK 500    ASP B 551       39.24    -91.60                                   
REMARK 500    SER B 577       46.16    -94.93                                   
REMARK 500    CYS B 583       50.19   -141.07                                   
REMARK 500    ARG B 587      -59.82   -127.87                                   
REMARK 500    ASN B 600       31.33   -157.58                                   
REMARK 500    ASP B 605     -168.67   -111.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1873        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A1874        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A1875        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A1876        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A1877        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A1878        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A1879        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A1880        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A1881        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A1882        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH A1883        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A1884        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A1885        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH A1886        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH A1887        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH A1888        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH A1889        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH A1890        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH B1751        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B1752        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B1753        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B1754        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B1755        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH B1756        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH B1757        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH B1758        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH B1759        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH B1760        DISTANCE =  8.74 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Z25   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Z26   RELATED DB: PDB                                   
DBREF  4Z24 A    1   652  UNP    Q5UPL2   YR135_MIMIV     51    702             
DBREF  4Z24 B    1   652  UNP    Q5UPL2   YR135_MIMIV     51    702             
SEQRES   1 A  652  THR LYS ASP ASN LEU THR GLY ASP ILE VAL ILE ILE GLY          
SEQRES   2 A  652  ALA GLY ALA ALA GLY SER LEU LEU ALA HIS TYR LEU ALA          
SEQRES   3 A  652  ARG PHE SER ASN MET LYS ILE ILE LEU LEU GLU ALA GLY          
SEQRES   4 A  652  HIS SER HIS PHE ASN ASP PRO VAL VAL THR ASP PRO MET          
SEQRES   5 A  652  GLY PHE PHE GLY LYS TYR ASN PRO PRO ASN GLU ASN ILE          
SEQRES   6 A  652  SER MET SER GLN ASN PRO SER TYR SER TRP GLN GLY ALA          
SEQRES   7 A  652  GLN GLU PRO ASN THR GLY ALA TYR GLY ASN ARG PRO ILE          
SEQRES   8 A  652  ILE ALA HIS GLY MET GLY PHE GLY GLY SER THR MET ILE          
SEQRES   9 A  652  ASN ARG LEU ASN LEU VAL VAL GLY GLY ARG THR VAL PHE          
SEQRES  10 A  652  ASP ASN ASP TRP PRO VAL GLY TRP LYS TYR ASP ASP VAL          
SEQRES  11 A  652  LYS ASN TYR PHE ARG ARG VAL LEU VAL ASP ILE ASN PRO          
SEQRES  12 A  652  VAL ARG ASP ASN THR LYS ALA SER ILE THR SER VAL ALA          
SEQRES  13 A  652  LEU ASP ALA LEU ARG ILE ILE ALA GLU GLN GLN ILE ALA          
SEQRES  14 A  652  SER GLY GLU PRO VAL ASP PHE LEU LEU ASN LYS ALA THR          
SEQRES  15 A  652  GLY ASN VAL PRO ASN VAL GLU LYS THR THR PRO ASP ALA          
SEQRES  16 A  652  VAL PRO LEU ASN LEU ASN ASP TYR GLU GLY VAL ASN SER          
SEQRES  17 A  652  VAL VAL ALA PHE SER SER PHE TYR MET GLY VAL ASN GLN          
SEQRES  18 A  652  LEU SER ASP GLY ASN TYR ILE ARG LYS TYR ALA GLY ASN          
SEQRES  19 A  652  THR TYR LEU ASN ARG ASN TYR VAL ASP GLU ASN GLY ARG          
SEQRES  20 A  652  GLY ILE GLY LYS PHE SER GLY LEU ARG VAL VAL SER ASP          
SEQRES  21 A  652  ALA VAL VAL ASP ARG ILE ILE PHE LYS GLY ASN ARG ALA          
SEQRES  22 A  652  VAL GLY VAL ASN TYR ILE ASP ARG GLU GLY ILE MET HIS          
SEQRES  23 A  652  TYR VAL LYS VAL ASN LYS GLU VAL VAL VAL THR SER GLY          
SEQRES  24 A  652  ALA PHE TYR THR PRO THR ILE LEU GLN ARG SER GLY ILE          
SEQRES  25 A  652  GLY ASP PHE THR TYR LEU SER SER ILE GLY VAL LYS ASN          
SEQRES  26 A  652  LEU VAL TYR ASN ASN PRO LEU VAL GLY THR GLY LEU LYS          
SEQRES  27 A  652  ASN HIS TYR SER PRO VAL THR ILE THR ARG VAL HIS GLY          
SEQRES  28 A  652  GLU PRO SER GLU VAL SER ARG PHE LEU SER ASN MET ALA          
SEQRES  29 A  652  ALA ASN PRO THR ASN MET GLY PHE LYS GLY LEU ALA GLU          
SEQRES  30 A  652  LEU GLY PHE HIS ARG LEU ASP PRO ASN LYS PRO ALA ASN          
SEQRES  31 A  652  ALA ASN THR VAL THR TYR ARG LYS TYR GLN LEU MET MET          
SEQRES  32 A  652  THR ALA GLY VAL GLY ILE PRO ALA GLU GLN GLN TYR LEU          
SEQRES  33 A  652  SER GLY LEU SER PRO SER SER ASN ASN LEU PHE THR LEU          
SEQRES  34 A  652  ILE ALA ASP ASP ILE ARG PHE ALA PRO GLU GLY TYR ILE          
SEQRES  35 A  652  LYS ILE GLY THR PRO ASN ILE PRO ARG ASP VAL PRO LYS          
SEQRES  36 A  652  ILE PHE PHE ASN THR PHE VAL THR TYR THR PRO THR SER          
SEQRES  37 A  652  ALA PRO ALA ASP GLN GLN TRP PRO ILE ALA GLN LYS THR          
SEQRES  38 A  652  LEU ALA PRO LEU ILE SER ALA LEU LEU GLY TYR ASP ILE          
SEQRES  39 A  652  ILE TYR GLN THR LEU MET SER MET ASN GLN THR ALA ARG          
SEQRES  40 A  652  ASP SER GLY PHE GLN VAL SER LEU GLU MET VAL TYR PRO          
SEQRES  41 A  652  LEU ASN ASP LEU ILE TYR LYS LEU HIS ASN GLY LEU ALA          
SEQRES  42 A  652  THR TYR GLY ALA ASN TRP TRP HIS TYR PHE VAL PRO THR          
SEQRES  43 A  652  LEU VAL GLY ASP ASP THR PRO ALA GLY ARG GLU PHE ALA          
SEQRES  44 A  652  ASP THR LEU SER LYS LEU SER TYR TYR PRO ARG VAL GLY          
SEQRES  45 A  652  ALA HIS LEU ASP SER HIS GLN GLY CYS SER CYS SER ILE          
SEQRES  46 A  652  GLY ARG THR VAL ASP SER ASN LEU LYS VAL ILE GLY THR          
SEQRES  47 A  652  GLN ASN VAL ARG VAL ALA ASP LEU SER ALA ALA ALA PHE          
SEQRES  48 A  652  PRO PRO GLY GLY ASN THR TRP ALA THR ALA SER MET ILE          
SEQRES  49 A  652  GLY ALA ARG ALA VAL ASP LEU ILE LEU GLY PHE PRO TYR          
SEQRES  50 A  652  LEU ARG ASP LEU PRO VAL ASN ASP VAL PRO ILE LEU ASN          
SEQRES  51 A  652  VAL ASN                                                      
SEQRES   1 B  652  THR LYS ASP ASN LEU THR GLY ASP ILE VAL ILE ILE GLY          
SEQRES   2 B  652  ALA GLY ALA ALA GLY SER LEU LEU ALA HIS TYR LEU ALA          
SEQRES   3 B  652  ARG PHE SER ASN MET LYS ILE ILE LEU LEU GLU ALA GLY          
SEQRES   4 B  652  HIS SER HIS PHE ASN ASP PRO VAL VAL THR ASP PRO MET          
SEQRES   5 B  652  GLY PHE PHE GLY LYS TYR ASN PRO PRO ASN GLU ASN ILE          
SEQRES   6 B  652  SER MET SER GLN ASN PRO SER TYR SER TRP GLN GLY ALA          
SEQRES   7 B  652  GLN GLU PRO ASN THR GLY ALA TYR GLY ASN ARG PRO ILE          
SEQRES   8 B  652  ILE ALA HIS GLY MET GLY PHE GLY GLY SER THR MET ILE          
SEQRES   9 B  652  ASN ARG LEU ASN LEU VAL VAL GLY GLY ARG THR VAL PHE          
SEQRES  10 B  652  ASP ASN ASP TRP PRO VAL GLY TRP LYS TYR ASP ASP VAL          
SEQRES  11 B  652  LYS ASN TYR PHE ARG ARG VAL LEU VAL ASP ILE ASN PRO          
SEQRES  12 B  652  VAL ARG ASP ASN THR LYS ALA SER ILE THR SER VAL ALA          
SEQRES  13 B  652  LEU ASP ALA LEU ARG ILE ILE ALA GLU GLN GLN ILE ALA          
SEQRES  14 B  652  SER GLY GLU PRO VAL ASP PHE LEU LEU ASN LYS ALA THR          
SEQRES  15 B  652  GLY ASN VAL PRO ASN VAL GLU LYS THR THR PRO ASP ALA          
SEQRES  16 B  652  VAL PRO LEU ASN LEU ASN ASP TYR GLU GLY VAL ASN SER          
SEQRES  17 B  652  VAL VAL ALA PHE SER SER PHE TYR MET GLY VAL ASN GLN          
SEQRES  18 B  652  LEU SER ASP GLY ASN TYR ILE ARG LYS TYR ALA GLY ASN          
SEQRES  19 B  652  THR TYR LEU ASN ARG ASN TYR VAL ASP GLU ASN GLY ARG          
SEQRES  20 B  652  GLY ILE GLY LYS PHE SER GLY LEU ARG VAL VAL SER ASP          
SEQRES  21 B  652  ALA VAL VAL ASP ARG ILE ILE PHE LYS GLY ASN ARG ALA          
SEQRES  22 B  652  VAL GLY VAL ASN TYR ILE ASP ARG GLU GLY ILE MET HIS          
SEQRES  23 B  652  TYR VAL LYS VAL ASN LYS GLU VAL VAL VAL THR SER GLY          
SEQRES  24 B  652  ALA PHE TYR THR PRO THR ILE LEU GLN ARG SER GLY ILE          
SEQRES  25 B  652  GLY ASP PHE THR TYR LEU SER SER ILE GLY VAL LYS ASN          
SEQRES  26 B  652  LEU VAL TYR ASN ASN PRO LEU VAL GLY THR GLY LEU LYS          
SEQRES  27 B  652  ASN HIS TYR SER PRO VAL THR ILE THR ARG VAL HIS GLY          
SEQRES  28 B  652  GLU PRO SER GLU VAL SER ARG PHE LEU SER ASN MET ALA          
SEQRES  29 B  652  ALA ASN PRO THR ASN MET GLY PHE LYS GLY LEU ALA GLU          
SEQRES  30 B  652  LEU GLY PHE HIS ARG LEU ASP PRO ASN LYS PRO ALA ASN          
SEQRES  31 B  652  ALA ASN THR VAL THR TYR ARG LYS TYR GLN LEU MET MET          
SEQRES  32 B  652  THR ALA GLY VAL GLY ILE PRO ALA GLU GLN GLN TYR LEU          
SEQRES  33 B  652  SER GLY LEU SER PRO SER SER ASN ASN LEU PHE THR LEU          
SEQRES  34 B  652  ILE ALA ASP ASP ILE ARG PHE ALA PRO GLU GLY TYR ILE          
SEQRES  35 B  652  LYS ILE GLY THR PRO ASN ILE PRO ARG ASP VAL PRO LYS          
SEQRES  36 B  652  ILE PHE PHE ASN THR PHE VAL THR TYR THR PRO THR SER          
SEQRES  37 B  652  ALA PRO ALA ASP GLN GLN TRP PRO ILE ALA GLN LYS THR          
SEQRES  38 B  652  LEU ALA PRO LEU ILE SER ALA LEU LEU GLY TYR ASP ILE          
SEQRES  39 B  652  ILE TYR GLN THR LEU MET SER MET ASN GLN THR ALA ARG          
SEQRES  40 B  652  ASP SER GLY PHE GLN VAL SER LEU GLU MET VAL TYR PRO          
SEQRES  41 B  652  LEU ASN ASP LEU ILE TYR LYS LEU HIS ASN GLY LEU ALA          
SEQRES  42 B  652  THR TYR GLY ALA ASN TRP TRP HIS TYR PHE VAL PRO THR          
SEQRES  43 B  652  LEU VAL GLY ASP ASP THR PRO ALA GLY ARG GLU PHE ALA          
SEQRES  44 B  652  ASP THR LEU SER LYS LEU SER TYR TYR PRO ARG VAL GLY          
SEQRES  45 B  652  ALA HIS LEU ASP SER HIS GLN GLY CYS SER CYS SER ILE          
SEQRES  46 B  652  GLY ARG THR VAL ASP SER ASN LEU LYS VAL ILE GLY THR          
SEQRES  47 B  652  GLN ASN VAL ARG VAL ALA ASP LEU SER ALA ALA ALA PHE          
SEQRES  48 B  652  PRO PRO GLY GLY ASN THR TRP ALA THR ALA SER MET ILE          
SEQRES  49 B  652  GLY ALA ARG ALA VAL ASP LEU ILE LEU GLY PHE PRO TYR          
SEQRES  50 B  652  LEU ARG ASP LEU PRO VAL ASN ASP VAL PRO ILE LEU ASN          
SEQRES  51 B  652  VAL ASN                                                      
HET    FAD  A 901      53                                                       
HET    FAD  B 901      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   5  HOH   *1650(H2 O)                                                   
HELIX    1 AA1 GLY A   15  SER A   29  1                                  15    
HELIX    2 AA2 ASP A   45  ASP A   50  1                                   6    
HELIX    3 AA3 PRO A   51  GLY A   56  5                                   6    
HELIX    4 AA4 PRO A   60  ASN A   64  5                                   5    
HELIX    5 AA5 SER A   66  ASN A   70  5                                   5    
HELIX    6 AA6 GLY A   99  ILE A  104  5                                   6    
HELIX    7 AA7 GLY A  113  TRP A  121  1                                   9    
HELIX    8 AA8 LYS A  126  ASN A  142  1                                  17    
HELIX    9 AA9 ALA A  150  GLY A  171  1                                  22    
HELIX   10 AB1 ASN A  179  GLY A  183  5                                   5    
HELIX   11 AB2 TYR A  231  LEU A  237  1                                   7    
HELIX   12 AB3 ILE A  249  SER A  253  5                                   5    
HELIX   13 AB4 TYR A  302  SER A  310  1                                   9    
HELIX   14 AB5 ASP A  314  ILE A  321  1                                   8    
HELIX   15 AB6 GLU A  352  LEU A  360  1                                   9    
HELIX   16 AB7 PRO A  410  GLY A  418  1                                   9    
HELIX   17 AB8 PRO A  470  LEU A  482  1                                  13    
HELIX   18 AB9 LEU A  482  SER A  509  1                                  28    
HELIX   19 AC1 LEU A  521  GLY A  536  1                                  16    
HELIX   20 AC2 ALA A  537  PHE A  543  5                                   7    
HELIX   21 AC3 VAL A  544  GLY A  549  1                                   6    
HELIX   22 AC4 THR A  552  SER A  566  1                                  15    
HELIX   23 AC5 SER A  566  GLY A  572  1                                   7    
HELIX   24 AC6 ASP A  605  ALA A  609  5                                   5    
HELIX   25 AC7 THR A  617  GLY A  634  1                                  18    
HELIX   26 AC8 PRO A  636  LEU A  641  1                                   6    
HELIX   27 AC9 GLY B   15  SER B   29  1                                  15    
HELIX   28 AD1 ASP B   45  ASP B   50  1                                   6    
HELIX   29 AD2 PRO B   51  GLY B   56  5                                   6    
HELIX   30 AD3 SER B   66  ASN B   70  5                                   5    
HELIX   31 AD4 GLY B   99  ILE B  104  5                                   6    
HELIX   32 AD5 GLY B  113  TRP B  121  1                                   9    
HELIX   33 AD6 LYS B  126  ASN B  142  1                                  17    
HELIX   34 AD7 ALA B  150  GLY B  171  1                                  22    
HELIX   35 AD8 ASN B  179  GLY B  183  5                                   5    
HELIX   36 AD9 TYR B  231  ASN B  238  1                                   8    
HELIX   37 AE1 ILE B  249  SER B  253  5                                   5    
HELIX   38 AE2 TYR B  302  SER B  310  1                                   9    
HELIX   39 AE3 ASP B  314  ILE B  321  1                                   8    
HELIX   40 AE4 GLU B  352  LEU B  360  1                                   9    
HELIX   41 AE5 PRO B  410  GLY B  418  1                                   9    
HELIX   42 AE6 PRO B  470  LEU B  482  1                                  13    
HELIX   43 AE7 LEU B  482  SER B  509  1                                  28    
HELIX   44 AE8 LEU B  521  GLY B  536  1                                  16    
HELIX   45 AE9 ALA B  537  PHE B  543  5                                   7    
HELIX   46 AF1 VAL B  544  GLY B  549  1                                   6    
HELIX   47 AF2 THR B  552  SER B  566  1                                  15    
HELIX   48 AF3 SER B  566  GLY B  572  1                                   7    
HELIX   49 AF4 ASP B  605  ALA B  609  5                                   5    
HELIX   50 AF5 THR B  617  GLY B  634  1                                  18    
SHEET    1 AA1 6 LEU A 255  VAL A 258  0                                        
SHEET    2 AA1 6 ILE A  33  LEU A  36  1  N  LEU A  35   O  VAL A 258           
SHEET    3 AA1 6 LEU A   5  ILE A  12  1  N  ILE A  11   O  ILE A  34           
SHEET    4 AA1 6 MET A 285  VAL A 296  1  O  ASN A 291   N  GLY A   7           
SHEET    5 AA1 6 ARG A 272  ILE A 279 -1  N  VAL A 276   O  VAL A 288           
SHEET    6 AA1 6 VAL A 262  LYS A 269 -1  N  ILE A 267   O  VAL A 274           
SHEET    1 AA2 5 LEU A 255  VAL A 258  0                                        
SHEET    2 AA2 5 ILE A  33  LEU A  36  1  N  LEU A  35   O  VAL A 258           
SHEET    3 AA2 5 LEU A   5  ILE A  12  1  N  ILE A  11   O  ILE A  34           
SHEET    4 AA2 5 MET A 285  VAL A 296  1  O  ASN A 291   N  GLY A   7           
SHEET    5 AA2 5 VAL A 601  VAL A 603  1  O  ARG A 602   N  VAL A 296           
SHEET    1 AA3 2 SER A  74  ALA A  78  0                                        
SHEET    2 AA3 2 ILE A  91  GLY A  95 -1  O  HIS A  94   N  TRP A  75           
SHEET    1 AA4 2 VAL A 144  ARG A 145  0                                        
SHEET    2 AA4 2 TYR A 216  MET A 217 -1  O  MET A 217   N  VAL A 144           
SHEET    1 AA5 6 VAL A 210  PHE A 212  0                                        
SHEET    2 AA5 6 LEU A 375  LEU A 378 -1  O  LEU A 375   N  PHE A 212           
SHEET    3 AA5 6 TYR A 399  ALA A 405 -1  O  TYR A 399   N  LEU A 378           
SHEET    4 AA5 6 LEU A 426  ASP A 433 -1  O  ILE A 430   N  MET A 402           
SHEET    5 AA5 6 TYR A 341  GLY A 351 -1  N  TYR A 341   O  ASP A 433           
SHEET    6 AA5 6 VAL A 513  TYR A 519 -1  O  SER A 514   N  HIS A 350           
SHEET    1 AA6 6 VAL A 210  PHE A 212  0                                        
SHEET    2 AA6 6 LEU A 375  LEU A 378 -1  O  LEU A 375   N  PHE A 212           
SHEET    3 AA6 6 TYR A 399  ALA A 405 -1  O  TYR A 399   N  LEU A 378           
SHEET    4 AA6 6 LEU A 426  ASP A 433 -1  O  ILE A 430   N  MET A 402           
SHEET    5 AA6 6 TYR A 341  GLY A 351 -1  N  TYR A 341   O  ASP A 433           
SHEET    6 AA6 6 ALA A 573  LEU A 575 -1  O  HIS A 574   N  SER A 342           
SHEET    1 AA7 2 VAL A 219  GLN A 221  0                                        
SHEET    2 AA7 2 TYR A 227  ARG A 229 -1  O  ILE A 228   N  ASN A 220           
SHEET    1 AA8 2 ILE A 312  GLY A 313  0                                        
SHEET    2 AA8 2 TYR A 328  ASN A 329  1  O  TYR A 328   N  GLY A 313           
SHEET    1 AA9 3 THR A 335  LEU A 337  0                                        
SHEET    2 AA9 3 GLY A 440  LYS A 443 -1  O  GLY A 440   N  LEU A 337           
SHEET    3 AA9 3 LYS A 455  PHE A 457 -1  O  LYS A 455   N  LYS A 443           
SHEET    1 AB1 6 LEU B 255  VAL B 258  0                                        
SHEET    2 AB1 6 ILE B  33  LEU B  36  1  N  LEU B  35   O  VAL B 258           
SHEET    3 AB1 6 THR B   6  ILE B  12  1  N  ILE B  11   O  ILE B  34           
SHEET    4 AB1 6 MET B 285  VAL B 296  1  O  ASN B 291   N  GLY B   7           
SHEET    5 AB1 6 ARG B 272  ILE B 279 -1  N  TYR B 278   O  HIS B 286           
SHEET    6 AB1 6 VAL B 262  LYS B 269 -1  N  ILE B 267   O  GLY B 275           
SHEET    1 AB2 5 LEU B 255  VAL B 258  0                                        
SHEET    2 AB2 5 ILE B  33  LEU B  36  1  N  LEU B  35   O  VAL B 258           
SHEET    3 AB2 5 THR B   6  ILE B  12  1  N  ILE B  11   O  ILE B  34           
SHEET    4 AB2 5 MET B 285  VAL B 296  1  O  ASN B 291   N  GLY B   7           
SHEET    5 AB2 5 VAL B 601  VAL B 603  1  O  ARG B 602   N  VAL B 296           
SHEET    1 AB3 2 SER B  74  ALA B  78  0                                        
SHEET    2 AB3 2 ILE B  91  GLY B  95 -1  O  HIS B  94   N  TRP B  75           
SHEET    1 AB4 6 VAL B 210  PHE B 212  0                                        
SHEET    2 AB4 6 LEU B 375  LEU B 378 -1  O  LEU B 375   N  PHE B 212           
SHEET    3 AB4 6 TYR B 399  ALA B 405 -1  O  TYR B 399   N  LEU B 378           
SHEET    4 AB4 6 LEU B 426  ASP B 433 -1  O  ILE B 430   N  MET B 402           
SHEET    5 AB4 6 TYR B 341  GLY B 351 -1  N  TYR B 341   O  ASP B 433           
SHEET    6 AB4 6 VAL B 513  TYR B 519 -1  O  GLU B 516   N  ARG B 348           
SHEET    1 AB5 6 VAL B 210  PHE B 212  0                                        
SHEET    2 AB5 6 LEU B 375  LEU B 378 -1  O  LEU B 375   N  PHE B 212           
SHEET    3 AB5 6 TYR B 399  ALA B 405 -1  O  TYR B 399   N  LEU B 378           
SHEET    4 AB5 6 LEU B 426  ASP B 433 -1  O  ILE B 430   N  MET B 402           
SHEET    5 AB5 6 TYR B 341  GLY B 351 -1  N  TYR B 341   O  ASP B 433           
SHEET    6 AB5 6 ALA B 573  LEU B 575 -1  O  HIS B 574   N  SER B 342           
SHEET    1 AB6 2 VAL B 219  GLN B 221  0                                        
SHEET    2 AB6 2 TYR B 227  ARG B 229 -1  O  ILE B 228   N  ASN B 220           
SHEET    1 AB7 2 ILE B 312  GLY B 313  0                                        
SHEET    2 AB7 2 TYR B 328  ASN B 329  1  O  TYR B 328   N  GLY B 313           
SHEET    1 AB8 3 THR B 335  LEU B 337  0                                        
SHEET    2 AB8 3 GLY B 440  LYS B 443 -1  O  GLY B 440   N  LEU B 337           
SHEET    3 AB8 3 LYS B 455  PHE B 457 -1  O  LYS B 455   N  LYS B 443           
CISPEP   1 GLY A  374    LEU A  375          0        15.61                     
CISPEP   2 TYR A  519    PRO A  520          0        -6.33                     
CISPEP   3 GLY B  374    LEU B  375          0        16.24                     
CISPEP   4 TYR B  519    PRO B  520          0        -6.90                     
SITE     1 AC1 38 GLY A  13  GLY A  15  ALA A  16  ALA A  17                    
SITE     2 AC1 38 GLU A  37  ALA A  38  TRP A  75  ALA A  93                    
SITE     3 AC1 38 HIS A  94  GLY A  95  MET A  96  GLY A  97                    
SITE     4 AC1 38 GLY A 100  SER A 101  ASN A 105  ARG A 106                    
SITE     5 AC1 38 LEU A 107  ASN A 108  ALA A 261  VAL A 263                    
SITE     6 AC1 38 THR A 297  SER A 298  GLY A 299  SER A 577                    
SITE     7 AC1 38 HIS A 578  ASP A 605  LEU A 606  ASN A 616                    
SITE     8 AC1 38 THR A 617  TRP A 618  ALA A 621  HOH A1022                    
SITE     9 AC1 38 HOH A1083  HOH A1194  HOH A1270  HOH A1288                    
SITE    10 AC1 38 HOH A1430  HOH A1497                                          
SITE     1 AC2 38 GLY B  13  GLY B  15  ALA B  16  ALA B  17                    
SITE     2 AC2 38 GLU B  37  ALA B  38  SER B  68  TRP B  75                    
SITE     3 AC2 38 ALA B  93  HIS B  94  GLY B  95  MET B  96                    
SITE     4 AC2 38 GLY B  97  GLY B 100  SER B 101  ILE B 104                    
SITE     5 AC2 38 ASN B 105  ARG B 106  LEU B 107  ASN B 108                    
SITE     6 AC2 38 ALA B 261  VAL B 263  THR B 297  SER B 298                    
SITE     7 AC2 38 GLY B 299  SER B 577  ASP B 605  LEU B 606                    
SITE     8 AC2 38 ASN B 616  THR B 617  TRP B 618  ALA B 621                    
SITE     9 AC2 38 HOH B1093  HOH B1157  HOH B1204  HOH B1272                    
SITE    10 AC2 38 HOH B1304  HOH B1314                                          
CRYST1   64.760   77.500   94.340 111.22 109.64  94.56 P 1           2          
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      0.015442  0.001230  0.006612        0.00000                         
SCALE2      0.000000  0.012944  0.005886        0.00000                         
SCALE3      0.000000  0.000000  0.012364        0.00000                         
ATOM      1  N   ASN A   4      -5.771   2.256  49.404  1.00 35.20           N  
ATOM      2  CA  ASN A   4      -4.582   3.073  49.156  1.00 39.18           C  
ATOM      3  C   ASN A   4      -4.499   3.617  47.738  1.00 37.39           C  
ATOM      4  O   ASN A   4      -5.008   3.012  46.794  1.00 43.72           O  
ATOM      5  CB  ASN A   4      -3.292   2.281  49.440  1.00 38.74           C  
ATOM      6  CG  ASN A   4      -3.024   2.101  50.924  1.00 43.44           C  
ATOM      7  OD1 ASN A   4      -3.605   2.796  51.762  1.00 46.48           O  
ATOM      8  ND2 ASN A   4      -2.128   1.171  51.258  1.00 40.76           N  
ATOM      9  N   LEU A   5      -3.870   4.782  47.615  1.00 43.75           N  
ANISOU    9  N   LEU A   5     5968   5357   5296  -1402   -298     -1       N  
ATOM     10  CA  LEU A   5      -3.534   5.356  46.323  1.00 33.82           C  
ANISOU   10  CA  LEU A   5     4729   4101   4020  -1360   -297    -76       C  
ATOM     11  C   LEU A   5      -2.550   4.429  45.611  1.00 29.35           C  
ANISOU   11  C   LEU A   5     4276   3381   3493  -1330   -285   -134       C  
ATOM     12  O   LEU A   5      -1.626   3.908  46.233  1.00 29.45           O  
ANISOU   12  O   LEU A   5     4345   3288   3555  -1293   -267   -122       O  
ATOM     13  CB  LEU A   5      -2.932   6.747  46.496  1.00 32.62           C  
ANISOU   13  CB  LEU A   5     4524   4010   3858  -1252   -273    -82       C  
ATOM     14  CG  LEU A   5      -3.929   7.898  46.424  1.00 41.16           C  
ANISOU   14  CG  LEU A   5     5494   5254   4890  -1245   -281    -62       C  
ATOM     15  CD1 LEU A   5      -3.208   9.230  46.511  1.00 43.89           C  
ANISOU   15  CD1 LEU A   5     5802   5638   5238  -1115   -253    -73       C  
ATOM     16  CD2 LEU A   5      -4.726   7.809  45.133  1.00 50.94           C  
ANISOU   16  CD2 LEU A   5     6729   6538   6088  -1320   -312    -99       C  
ATOM     17  N   THR A   6      -2.742   4.225  44.314  1.00 25.96           N  
ANISOU   17  N   THR A   6     3876   2947   3042  -1342   -294   -194       N  
ATOM     18  CA  THR A   6      -1.843   3.383  43.542  1.00 27.99           C  
ANISOU   18  CA  THR A   6     4232   3073   3331  -1308   -279   -257       C  
ATOM     19  C   THR A   6      -1.486   4.051  42.227  1.00 24.82           C  
ANISOU   19  C   THR A   6     3835   2701   2894  -1261   -272   -327       C  
ATOM     20  O   THR A   6      -2.371   4.443  41.477  1.00 29.64           O  
ANISOU   20  O   THR A   6     4400   3409   3454  -1303   -293   -337       O  
ATOM     21  CB  THR A   6      -2.472   2.000  43.253  1.00 28.39           C  
ANISOU   21  CB  THR A   6     4332   3061   3392  -1389   -298   -263       C  
ATOM     22  OG1 THR A   6      -2.629   1.289  44.480  1.00 30.73           O  
ANISOU   22  OG1 THR A   6     4634   3314   3729  -1424   -302   -196       O  
ATOM     23  CG2 THR A   6      -1.583   1.182  42.311  1.00 25.64           C  
ANISOU   23  CG2 THR A   6     4081   2588   3074  -1350   -282   -339       C  
ATOM     24  N   GLY A   7      -0.194   4.172  41.947  1.00 21.30           N  
ANISOU   24  N   GLY A   7     3440   2177   2474  -1172   -242   -368       N  
ATOM     25  CA  GLY A   7       0.253   4.783  40.712  1.00 23.84           C  
ANISOU   25  CA  GLY A   7     3768   2528   2763  -1122   -232   -431       C  
ATOM     26  C   GLY A   7       1.358   4.002  40.034  1.00 27.44           C  
ANISOU   26  C   GLY A   7     4310   2866   3249  -1065   -205   -492       C  
ATOM     27  O   GLY A   7       2.053   3.203  40.668  1.00 25.06           O  
ANISOU   27  O   GLY A   7     4063   2455   3005  -1036   -188   -482       O  
ATOM     28  N   ASP A   8       1.509   4.225  38.731  1.00 18.70           N  
ANISOU   28  N   ASP A   8     3213   1788   2105  -1046   -202   -552       N  
ATOM     29  CA  ASP A   8       2.616   3.651  37.975  1.00 19.08           C  
ANISOU   29  CA  ASP A   8     3333   1746   2173   -980   -172   -616       C  
ATOM     30  C   ASP A   8       3.903   4.443  38.225  1.00 18.13           C  
ANISOU   30  C   ASP A   8     3208   1612   2070   -872   -137   -614       C  
ATOM     31  O   ASP A   8       4.924   3.892  38.613  1.00 23.90           O  
ANISOU   31  O   ASP A   8     3986   2243   2851   -808   -109   -619       O  
ATOM     32  CB  ASP A   8       2.266   3.618  36.484  1.00 19.68           C  
ANISOU   32  CB  ASP A   8     3415   1869   2193  -1006   -182   -678       C  
ATOM     33  CG  ASP A   8       1.068   2.733  36.196  1.00 27.57           C  
ANISOU   33  CG  ASP A   8     4427   2872   3176  -1114   -216   -683       C  
ATOM     34  OD1 ASP A   8       1.056   1.603  36.723  1.00 27.89           O  
ANISOU   34  OD1 ASP A   8     4520   2812   3264  -1142   -217   -679       O  
ATOM     35  OD2 ASP A   8       0.141   3.165  35.468  1.00 25.74           O  
ANISOU   35  OD2 ASP A   8     4151   2744   2886  -1171   -242   -686       O  
ATOM     36  N   ILE A   9       3.839   5.745  37.994  1.00 17.73           N  
ANISOU   36  N   ILE A   9     3096   1665   1977   -850   -141   -605       N  
ATOM     37  CA  ILE A   9       4.947   6.629  38.295  1.00 16.37           C  
ANISOU   37  CA  ILE A   9     2910   1492   1816   -757   -112   -596       C  
ATOM     38  C   ILE A   9       4.501   7.521  39.440  1.00 19.10           C  
ANISOU   38  C   ILE A   9     3196   1897   2163   -772   -127   -533       C  
ATOM     39  O   ILE A   9       3.473   8.202  39.348  1.00 17.08           O  
ANISOU   39  O   ILE A   9     2879   1745   1868   -825   -156   -513       O  
ATOM     40  CB  ILE A   9       5.362   7.513  37.104  1.00 18.52           C  
ANISOU   40  CB  ILE A   9     3161   1836   2039   -711   -102   -635       C  
ATOM     41  CG1 ILE A   9       5.421   6.700  35.796  1.00 24.06           C  
ANISOU   41  CG1 ILE A   9     3909   2514   2718   -722    -98   -701       C  
ATOM     42  CG2 ILE A   9       6.675   8.261  37.426  1.00 15.27           C  
ANISOU   42  CG2 ILE A   9     2747   1409   1647   -611    -68   -627       C  
ATOM     43  CD1 ILE A   9       6.550   5.689  35.719  1.00 22.58           C  
ANISOU   43  CD1 ILE A   9     3793   2209   2576   -660    -62   -739       C  
ATOM     44  N   VAL A  10       5.251   7.507  40.529  1.00 15.15           N  
ANISOU   44  N   VAL A  10     2699   1344   1712   -716   -108   -492       N  
ATOM     45  CA  VAL A  10       4.928   8.376  41.659  1.00 14.42           C  
ANISOU   45  CA  VAL A  10     2524   1328   1629   -697   -115   -420       C  
ATOM     46  C   VAL A  10       6.023   9.403  41.742  1.00 14.32           C  
ANISOU   46  C   VAL A  10     2476   1339   1624   -589    -90   -409       C  
ATOM     47  O   VAL A  10       7.200   9.050  41.794  1.00 14.72           O  
ANISOU   47  O   VAL A  10     2569   1315   1708   -525    -62   -419       O  
ATOM     48  CB  VAL A  10       4.781   7.577  42.976  1.00 14.68           C  
ANISOU   48  CB  VAL A  10     2569   1302   1706   -725   -118   -366       C  
ATOM     49  CG1 VAL A  10       4.613   8.513  44.155  1.00 13.95           C  
ANISOU   49  CG1 VAL A  10     2393   1290   1617   -692   -119   -299       C  
ATOM     50  CG2 VAL A  10       3.578   6.645  42.861  1.00 15.54           C  
ANISOU   50  CG2 VAL A  10     2704   1398   1803   -845   -148   -371       C  
ATOM     51  N   ILE A  11       5.633  10.675  41.692  1.00 12.99           N  
ANISOU   51  N   ILE A  11     2233   1277   1427   -571   -100   -388       N  
ATOM     52  CA  ILE A  11       6.575  11.787  41.642  1.00 12.27           C  
ANISOU   52  CA  ILE A  11     2106   1217   1338   -481    -82   -378       C  
ATOM     53  C   ILE A  11       6.510  12.570  42.952  1.00 13.61           C  
ANISOU   53  C   ILE A  11     2216   1430   1527   -451    -83   -319       C  
ATOM     54  O   ILE A  11       5.404  12.907  43.401  1.00 12.57           O  
ANISOU   54  O   ILE A  11     2035   1363   1378   -493   -103   -293       O  
ATOM     55  CB  ILE A  11       6.261  12.729  40.472  1.00 12.94           C  
ANISOU   55  CB  ILE A  11     2157   1384   1376   -479    -92   -402       C  
ATOM     56  CG1 ILE A  11       6.199  11.938  39.156  1.00 20.84           C  
ANISOU   56  CG1 ILE A  11     3217   2356   2345   -521    -93   -465       C  
ATOM     57  CG2 ILE A  11       7.266  13.884  40.413  1.00 11.44           C  
ANISOU   57  CG2 ILE A  11     1934   1220   1192   -392    -75   -387       C  
ATOM     58  CD1 ILE A  11       5.607  12.706  38.041  1.00 12.83           C  
ANISOU   58  CD1 ILE A  11     2165   1433   1275   -542   -111   -481       C  
ATOM     59  N   ILE A  12       7.667  12.828  43.571  1.00 11.77           N  
ANISOU   59  N   ILE A  12     1983   1164   1325   -380    -62   -299       N  
ATOM     60  CA  ILE A  12       7.717  13.555  44.854  1.00 10.78           C  
ANISOU   60  CA  ILE A  12     1807   1077   1213   -351    -63   -249       C  
ATOM     61  C   ILE A  12       8.253  14.999  44.726  1.00 13.97           C  
ANISOU   61  C   ILE A  12     2165   1535   1608   -288    -59   -243       C  
ATOM     62  O   ILE A  12       9.475  15.236  44.621  1.00 12.48           O  
ANISOU   62  O   ILE A  12     1989   1318   1436   -231    -42   -244       O  
ATOM     63  CB  ILE A  12       8.570  12.788  45.894  1.00 10.88           C  
ANISOU   63  CB  ILE A  12     1848   1020   1266   -327    -49   -218       C  
ATOM     64  CG1 ILE A  12       8.089  11.345  46.030  1.00 11.60           C  
ANISOU   64  CG1 ILE A  12     1991   1044   1373   -389    -54   -218       C  
ATOM     65  CG2 ILE A  12       8.527  13.500  47.264  1.00 10.47           C  
ANISOU   65  CG2 ILE A  12     1743   1017   1217   -308    -52   -170       C  
ATOM     66  CD1 ILE A  12       9.110  10.397  46.675  1.00 11.89           C  
ANISOU   66  CD1 ILE A  12     2073    989   1455   -356    -36   -194       C  
ATOM     67  N   GLY A  13       7.343  15.966  44.759  1.00  9.92           N  
ANISOU   67  N   GLY A  13     1599   1099   1072   -299    -74   -234       N  
ATOM     68  CA  GLY A  13       7.719  17.372  44.681  1.00  9.41           C  
ANISOU   68  CA  GLY A  13     1495   1079   1003   -245    -73   -227       C  
ATOM     69  C   GLY A  13       7.257  18.008  43.378  1.00 19.29           C  
ANISOU   69  C   GLY A  13     2729   2375   2225   -251    -84   -247       C  
ATOM     70  O   GLY A  13       7.762  17.668  42.292  1.00 11.79           O  
ANISOU   70  O   GLY A  13     1812   1402   1265   -249    -79   -275       O  
ATOM     71  N   ALA A  14       6.280  18.908  43.481  1.00 15.86           N  
ANISOU   71  N   ALA A  14     2242   2008   1774   -255    -99   -231       N  
ATOM     72  CA  ALA A  14       5.718  19.575  42.313  1.00 15.14           C  
ANISOU   72  CA  ALA A  14     2125   1970   1655   -260   -114   -238       C  
ATOM     73  C   ALA A  14       6.432  20.890  41.996  1.00 18.50           C  
ANISOU   73  C   ALA A  14     2532   2407   2089   -199   -111   -227       C  
ATOM     74  O   ALA A  14       5.781  21.918  41.842  1.00  9.05           O  
ANISOU   74  O   ALA A  14     1291   1262    885   -184   -123   -209       O  
ATOM     75  CB  ALA A  14       4.245  19.842  42.530  1.00 15.22           C  
ANISOU   75  CB  ALA A  14     2085   2052   1647   -293   -132   -221       C  
ATOM     76  N   GLY A  15       7.752  20.852  41.857  1.00  8.88           N  
ANISOU   76  N   GLY A  15     1345   1142    887   -166    -96   -234       N  
ATOM     77  CA  GLY A  15       8.508  22.065  41.634  1.00 11.78           C  
ANISOU   77  CA  GLY A  15     1695   1517   1264   -116    -95   -218       C  
ATOM     78  C   GLY A  15       8.711  22.329  40.148  1.00 16.94           C  
ANISOU   78  C   GLY A  15     2351   2194   1891   -117    -99   -225       C  
ATOM     79  O   GLY A  15       7.879  21.952  39.314  1.00  9.08           O  
ANISOU   79  O   GLY A  15     1352   1233    863   -155   -110   -239       O  
ATOM     80  N   ALA A  16       9.799  23.010  39.822  1.00 13.59           N  
ANISOU   80  N   ALA A  16     1928   1760   1476    -79    -91   -214       N  
ATOM     81  CA  ALA A  16      10.111  23.308  38.419  1.00 13.11           C  
ANISOU   81  CA  ALA A  16     1866   1729   1386    -77    -93   -215       C  
ATOM     82  C   ALA A  16      10.136  22.052  37.565  1.00 12.80           C  
ANISOU   82  C   ALA A  16     1864   1684   1315   -109    -82   -255       C  
ATOM     83  O   ALA A  16       9.662  22.037  36.416  1.00 11.25           O  
ANISOU   83  O   ALA A  16     1664   1534   1078   -134    -91   -266       O  
ATOM     84  CB  ALA A  16      11.440  24.024  38.317  1.00  9.81           C  
ANISOU   84  CB  ALA A  16     1446   1296    984    -37    -83   -194       C  
ATOM     85  N   ALA A  17      10.693  20.994  38.129  1.00 13.88           N  
ANISOU   85  N   ALA A  17     2039   1765   1469   -107    -62   -278       N  
ATOM     86  CA  ALA A  17      10.835  19.755  37.398  1.00  9.63           C  
ANISOU   86  CA  ALA A  17     1548   1203    908   -131    -47   -323       C  
ATOM     87  C   ALA A  17       9.605  18.880  37.532  1.00 14.06           C  
ANISOU   87  C   ALA A  17     2125   1760   1456   -191    -62   -345       C  
ATOM     88  O   ALA A  17       9.103  18.357  36.541  1.00 10.54           O  
ANISOU   88  O   ALA A  17     1698   1335    970   -232    -68   -379       O  
ATOM     89  CB  ALA A  17      12.066  19.012  37.866  1.00  9.64           C  
ANISOU   89  CB  ALA A  17     1585   1139    937    -94    -18   -332       C  
ATOM     90  N   GLY A  18       9.127  18.701  38.757  1.00 16.81           N  
ANISOU   90  N   GLY A  18     2465   2088   1835   -201    -68   -327       N  
ATOM     91  CA  GLY A  18       8.045  17.763  39.002  1.00 14.60           C  
ANISOU   91  CA  GLY A  18     2200   1801   1547   -263    -81   -342       C  
ATOM     92  C   GLY A  18       6.738  18.133  38.328  1.00 15.58           C  
ANISOU   92  C   GLY A  18     2288   2000   1631   -311   -109   -340       C  
ATOM     93  O   GLY A  18       6.004  17.256  37.869  1.00 15.23           O  
ANISOU   93  O   GLY A  18     2266   1959   1561   -374   -120   -368       O  
ATOM     94  N   SER A  19       6.435  19.432  38.280  1.00 12.31           N  
ANISOU   94  N   SER A  19     1818   1646   1214   -283   -122   -306       N  
ATOM     95  CA  SER A  19       5.196  19.886  37.681  1.00 11.75           C  
ANISOU   95  CA  SER A  19     1703   1654   1108   -319   -149   -292       C  
ATOM     96  C   SER A  19       5.206  19.555  36.201  1.00 16.32           C  
ANISOU   96  C   SER A  19     2302   2262   1638   -352   -156   -323       C  
ATOM     97  O   SER A  19       4.256  18.973  35.672  1.00 12.27           O  
ANISOU   97  O   SER A  19     1789   1786   1088   -417   -175   -339       O  
ATOM     98  CB  SER A  19       4.996  21.395  37.900  1.00 10.04           C  
ANISOU   98  CB  SER A  19     1426   1483    904   -269   -158   -247       C  
ATOM     99  OG  SER A  19       4.998  21.736  39.295  1.00 13.59           O  
ANISOU   99  OG  SER A  19     1860   1909   1394   -239   -150   -227       O  
ATOM    100  N   LEU A  20       6.309  19.894  35.545  1.00 15.65           N  
ANISOU  100  N   LEU A  20     2235   2164   1548   -310   -139   -331       N  
ATOM    101  CA  LEU A  20       6.444  19.645  34.117  1.00 15.67           C  
ANISOU  101  CA  LEU A  20     2256   2200   1496   -334   -141   -361       C  
ATOM    102  C   LEU A  20       6.370  18.158  33.841  1.00 18.21           C  
ANISOU  102  C   LEU A  20     2642   2479   1799   -387   -133   -422       C  
ATOM    103  O   LEU A  20       5.636  17.716  32.942  1.00 12.33           O  
ANISOU  103  O   LEU A  20     1905   1777   1003   -449   -152   -450       O  
ATOM    104  CB  LEU A  20       7.765  20.226  33.591  1.00 12.43           C  
ANISOU  104  CB  LEU A  20     1852   1783   1087   -276   -119   -356       C  
ATOM    105  CG  LEU A  20       7.962  20.192  32.062  1.00 15.72           C  
ANISOU  105  CG  LEU A  20     2279   2255   1441   -294   -119   -379       C  
ATOM    106  CD1 LEU A  20       8.968  21.266  31.652  1.00 13.75           C  
ANISOU  106  CD1 LEU A  20     2003   2029   1194   -237   -107   -342       C  
ATOM    107  CD2 LEU A  20       8.458  18.833  31.605  1.00 11.97           C  
ANISOU  107  CD2 LEU A  20     1874   1733    943   -314    -94   -450       C  
ATOM    108  N   LEU A  21       7.135  17.394  34.614  1.00 11.61           N  
ANISOU  108  N   LEU A  21     1853   1555   1005   -364   -107   -442       N  
ATOM    109  CA  LEU A  21       7.237  15.957  34.405  1.00 14.21           C  
ANISOU  109  CA  LEU A  21     2253   1818   1326   -403    -95   -500       C  
ATOM    110  C   LEU A  21       5.870  15.287  34.491  1.00 15.85           C  
ANISOU  110  C   LEU A  21     2463   2042   1516   -491   -125   -511       C  
ATOM    111  O   LEU A  21       5.518  14.464  33.642  1.00 14.66           O  
ANISOU  111  O   LEU A  21     2356   1889   1324   -551   -133   -563       O  
ATOM    112  CB  LEU A  21       8.187  15.340  35.426  1.00 16.27           C  
ANISOU  112  CB  LEU A  21     2552   1983   1645   -358    -66   -501       C  
ATOM    113  CG  LEU A  21       8.305  13.812  35.416  1.00 17.65           C  
ANISOU  113  CG  LEU A  21     2806   2069   1829   -391    -52   -554       C  
ATOM    114  CD1 LEU A  21       8.857  13.281  34.089  1.00 13.27           C  
ANISOU  114  CD1 LEU A  21     2305   1506   1232   -389    -32   -621       C  
ATOM    115  CD2 LEU A  21       9.130  13.302  36.598  1.00 13.80           C  
ANISOU  115  CD2 LEU A  21     2343   1493   1405   -343    -28   -535       C  
ATOM    116  N   ALA A  22       5.105  15.649  35.518  1.00 16.17           N  
ANISOU  116  N   ALA A  22     2457   2102   1584   -502   -142   -463       N  
ATOM    117  CA  ALA A  22       3.799  15.018  35.770  1.00 15.50           C  
ANISOU  117  CA  ALA A  22     2365   2038   1485   -587   -170   -462       C  
ATOM    118  C   ALA A  22       2.834  15.236  34.621  1.00 15.92           C  
ANISOU  118  C   ALA A  22     2390   2186   1475   -648   -202   -471       C  
ATOM    119  O   ALA A  22       2.163  14.315  34.152  1.00 14.33           O  
ANISOU  119  O   ALA A  22     2219   1984   1240   -732   -220   -507       O  
ATOM    120  CB  ALA A  22       3.196  15.563  37.061  1.00 12.38           C  
ANISOU  120  CB  ALA A  22     1911   1668   1125   -575   -178   -404       C  
ATOM    121  N   HIS A  23       2.791  16.490  34.190  1.00 17.38           N  
ANISOU  121  N   HIS A  23     2513   2447   1642   -606   -210   -435       N  
ATOM    122  CA  HIS A  23       1.916  16.977  33.149  1.00 17.23           C  
ANISOU  122  CA  HIS A  23     2448   2534   1565   -647   -241   -423       C  
ATOM    123  C   HIS A  23       2.133  16.199  31.843  1.00 14.11           C  
ANISOU  123  C   HIS A  23     2110   2140   1110   -698   -243   -488       C  
ATOM    124  O   HIS A  23       1.195  15.666  31.265  1.00 14.80           O  
ANISOU  124  O   HIS A  23     2190   2267   1168   -765   -266   -495       O  
ATOM    125  CB  HIS A  23       2.180  18.477  32.948  1.00 14.73           C  
ANISOU  125  CB  HIS A  23     2069   2274   1252   -573   -241   -371       C  
ATOM    126  CG  HIS A  23       1.440  19.093  31.798  1.00 14.63           C  
ANISOU  126  CG  HIS A  23     2007   2371   1181   -601   -272   -348       C  
ATOM    127  ND1 HIS A  23       0.337  19.900  31.972  1.00 13.38           N  
ANISOU  127  ND1 HIS A  23     1767   2296   1019   -604   -300   -289       N  
ATOM    128  CD2 HIS A  23       1.659  19.034  30.461  1.00 15.52           C  
ANISOU  128  CD2 HIS A  23     2135   2529   1232   -626   -279   -374       C  
ATOM    129  CE1 HIS A  23      -0.093  20.314  30.792  1.00 13.84           C  
ANISOU  129  CE1 HIS A  23     1792   2446   1020   -629   -326   -273       C  
ATOM    130  NE2 HIS A  23       0.685  19.795  29.859  1.00 14.10           N  
ANISOU  130  NE2 HIS A  23     1883   2459   1014   -646   -315   -325       N  
ATOM    131  N   TYR A  24       3.379  16.133  31.393  1.00 16.57           N  
ANISOU  131  N   TYR A  24     2470   2404   1423   -646   -211   -523       N  
ATOM    132  CA  TYR A  24       3.658  15.496  30.113  1.00 20.81           C  
ANISOU  132  CA  TYR A  24     3049   2942   1915   -666   -203   -575       C  
ATOM    133  C   TYR A  24       3.632  13.958  30.169  1.00 19.71           C  
ANISOU  133  C   TYR A  24     2983   2711   1796   -704   -192   -631       C  
ATOM    134  O   TYR A  24       3.320  13.306  29.172  1.00 16.19           O  
ANISOU  134  O   TYR A  24     2560   2278   1315   -743   -198   -667       O  
ATOM    135  CB  TYR A  24       4.986  16.004  29.568  1.00 14.42           C  
ANISOU  135  CB  TYR A  24     2258   2130   1092   -597   -172   -591       C  
ATOM    136  CG  TYR A  24       4.858  17.379  28.952  1.00 18.35           C  
ANISOU  136  CG  TYR A  24     2685   2735   1552   -576   -190   -537       C  
ATOM    137  CD1 TYR A  24       4.034  17.588  27.840  1.00 14.78           C  
ANISOU  137  CD1 TYR A  24     2195   2374   1045   -619   -218   -523       C  
ATOM    138  CD2 TYR A  24       5.573  18.469  29.460  1.00 13.43           C  
ANISOU  138  CD2 TYR A  24     2022   2105    975   -493   -175   -480       C  
ATOM    139  CE1 TYR A  24       3.901  18.847  27.270  1.00 17.53           C  
ANISOU  139  CE1 TYR A  24     2479   2820   1363   -598   -237   -465       C  
ATOM    140  CE2 TYR A  24       5.452  19.725  28.894  1.00 13.29           C  
ANISOU  140  CE2 TYR A  24     1941   2172    936   -470   -193   -422       C  
ATOM    141  CZ  TYR A  24       4.621  19.908  27.788  1.00 13.89           C  
ANISOU  141  CZ  TYR A  24     1988   2350    942   -524   -224   -415       C  
ATOM    142  OH  TYR A  24       4.494  21.153  27.217  1.00 21.39           O  
ANISOU  142  OH  TYR A  24     2874   3381   1873   -498   -243   -349       O  
ATOM    143  N   LEU A  25       3.928  13.372  31.326  1.00 17.25           N  
ANISOU  143  N   LEU A  25     2708   2307   1541   -694   -177   -635       N  
ATOM    144  CA  LEU A  25       3.810  11.923  31.454  1.00 15.81           C  
ANISOU  144  CA  LEU A  25     2591   2034   1383   -733   -170   -677       C  
ATOM    145  C   LEU A  25       2.357  11.509  31.285  1.00 24.44           C  
ANISOU  145  C   LEU A  25     3657   3175   2454   -825   -209   -663       C  
ATOM    146  O   LEU A  25       2.039  10.512  30.618  1.00 20.29           O  
ANISOU  146  O   LEU A  25     3174   2623   1912   -873   -214   -705       O  
ATOM    147  CB  LEU A  25       4.333  11.448  32.797  1.00 15.42           C  
ANISOU  147  CB  LEU A  25     2576   1884   1400   -706   -150   -668       C  
ATOM    148  CG  LEU A  25       5.838  11.277  32.966  1.00 15.16           C  
ANISOU  148  CG  LEU A  25     2593   1768   1400   -621   -106   -694       C  
ATOM    149  CD1 LEU A  25       6.145  10.888  34.418  1.00 16.47           C  
ANISOU  149  CD1 LEU A  25     2781   1846   1631   -605    -94   -668       C  
ATOM    150  CD2 LEU A  25       6.369  10.233  31.995  1.00 16.05           C  
ANISOU  150  CD2 LEU A  25     2768   1826   1503   -611    -85   -759       C  
ATOM    151  N   ALA A  26       1.472  12.311  31.856  1.00 19.32           N  
ANISOU  151  N   ALA A  26     2935   2603   1802   -848   -235   -603       N  
ATOM    152  CA  ALA A  26       0.055  12.037  31.766  1.00 16.62           C  
ANISOU  152  CA  ALA A  26     2555   2323   1438   -932   -271   -578       C  
ATOM    153  C   ALA A  26      -0.425  12.209  30.330  1.00 17.28           C  
ANISOU  153  C   ALA A  26     2617   2490   1459   -963   -288   -590       C  
ATOM    154  O   ALA A  26      -1.199  11.394  29.825  1.00 24.76           O  
ANISOU  154  O   ALA A  26     3579   3445   2383  -1036   -306   -608       O  
ATOM    155  CB  ALA A  26      -0.711  12.956  32.699  1.00 16.05           C  
ANISOU  155  CB  ALA A  26     2399   2323   1375   -935   -291   -509       C  
ATOM    156  N   ARG A  27       0.053  13.260  29.671  1.00 19.00           N  
ANISOU  156  N   ARG A  27     2801   2769   1647   -910   -284   -578       N  
ATOM    157  CA  ARG A  27      -0.405  13.573  28.322  1.00 17.62           C  
ANISOU  157  CA  ARG A  27     2597   2688   1411   -936   -302   -578       C  
ATOM    158  C   ARG A  27      -0.002  12.490  27.337  1.00 18.79           C  
ANISOU  158  C   ARG A  27     2821   2786   1533   -960   -289   -652       C  
ATOM    159  O   ARG A  27      -0.788  12.111  26.464  1.00 19.41           O  
ANISOU  159  O   ARG A  27     2893   2916   1566  -1025   -311   -663       O  
ATOM    160  CB  ARG A  27       0.153  14.919  27.850  1.00 16.91           C  
ANISOU  160  CB  ARG A  27     2459   2666   1298   -870   -298   -545       C  
ATOM    161  CG  ARG A  27      -0.222  15.243  26.418  1.00 17.57           C  
ANISOU  161  CG  ARG A  27     2514   2844   1317   -894   -315   -540       C  
ATOM    162  CD  ARG A  27       0.102  16.654  25.989  1.00 17.09           C  
ANISOU  162  CD  ARG A  27     2393   2864   1236   -838   -318   -488       C  
ATOM    163  NE  ARG A  27      -0.429  16.873  24.647  1.00 18.82           N  
ANISOU  163  NE  ARG A  27     2580   3179   1393   -873   -338   -475       N  
ATOM    164  CZ  ARG A  27      -0.283  17.975  23.913  1.00 25.32           C  
ANISOU  164  CZ  ARG A  27     3351   4085   2184   -840   -345   -428       C  
ATOM    165  NH1 ARG A  27       0.423  19.003  24.366  1.00 21.66           N  
ANISOU  165  NH1 ARG A  27     2863   3620   1747   -769   -336   -388       N  
ATOM    166  NH2 ARG A  27      -0.838  18.029  22.701  1.00 22.80           N  
ANISOU  166  NH2 ARG A  27     3005   3851   1807   -882   -363   -417       N  
ATOM    167  N   PHE A  28       1.228  12.007  27.491  1.00 18.20           N  
ANISOU  167  N   PHE A  28     2815   2614   1486   -906   -253   -702       N  
ATOM    168  CA  PHE A  28       1.861  11.116  26.511  1.00 21.03           C  
ANISOU  168  CA  PHE A  28     3246   2926   1820   -903   -234   -778       C  
ATOM    169  C   PHE A  28       1.792   9.619  26.865  1.00 25.70           C  
ANISOU  169  C   PHE A  28     3914   3405   2446   -942   -228   -830       C  
ATOM    170  O   PHE A  28       2.366   8.797  26.150  1.00 20.94           O  
ANISOU  170  O   PHE A  28     3377   2749   1830   -932   -209   -899       O  
ATOM    171  CB  PHE A  28       3.341  11.492  26.340  1.00 20.63           C  
ANISOU  171  CB  PHE A  28     3220   2842   1775   -809   -193   -801       C  
ATOM    172  CG  PHE A  28       3.579  12.814  25.660  1.00 18.10           C  
ANISOU  172  CG  PHE A  28     2840   2628   1410   -774   -196   -762       C  
ATOM    173  CD1 PHE A  28       2.920  13.142  24.486  1.00 18.72           C  
ANISOU  173  CD1 PHE A  28     2882   2808   1422   -816   -220   -753       C  
ATOM    174  CD2 PHE A  28       4.507  13.698  26.168  1.00 17.18           C  
ANISOU  174  CD2 PHE A  28     2704   2507   1316   -699   -173   -733       C  
ATOM    175  CE1 PHE A  28       3.162  14.352  23.843  1.00 18.40           C  
ANISOU  175  CE1 PHE A  28     2785   2863   1343   -783   -223   -709       C  
ATOM    176  CE2 PHE A  28       4.760  14.919  25.537  1.00 20.03           C  
ANISOU  176  CE2 PHE A  28     3010   2962   1637   -668   -177   -691       C  
ATOM    177  CZ  PHE A  28       4.082  15.247  24.374  1.00 22.46           C  
ANISOU  177  CZ  PHE A  28     3281   3370   1883   -709   -202   -677       C  
ATOM    178  N   SER A  29       1.125   9.253  27.961  1.00 19.61           N  
ANISOU  178  N   SER A  29     3136   2595   1718   -982   -242   -798       N  
ATOM    179  CA  SER A  29       1.025   7.835  28.323  1.00 20.37           C  
ANISOU  179  CA  SER A  29     3306   2584   1851  -1023   -239   -839       C  
ATOM    180  C   SER A  29      -0.384   7.458  28.748  1.00 21.76           C  
ANISOU  180  C   SER A  29     3453   2791   2026  -1121   -277   -802       C  
ATOM    181  O   SER A  29      -1.224   8.326  28.959  1.00 20.94           O  
ANISOU  181  O   SER A  29     3268   2786   1901  -1146   -301   -740       O  
ATOM    182  CB  SER A  29       2.007   7.498  29.446  1.00 26.13           C  
ANISOU  182  CB  SER A  29     4077   3199   2653   -959   -207   -840       C  
ATOM    183  OG  SER A  29       1.499   7.890  30.715  1.00 24.50           O  
ANISOU  183  OG  SER A  29     3826   3001   2483   -973   -219   -774       O  
ATOM    184  N   ASN A  30      -0.643   6.166  28.905  1.00 21.73           N  
ANISOU  184  N   ASN A  30     3512   2700   2044  -1174   -282   -837       N  
ATOM    185  CA  ASN A  30      -1.929   5.731  29.440  1.00 22.20           C  
ANISOU  185  CA  ASN A  30     3546   2782   2107  -1270   -316   -796       C  
ATOM    186  C   ASN A  30      -1.761   5.308  30.883  1.00 24.04           C  
ANISOU  186  C   ASN A  30     3796   2927   2409  -1261   -306   -764       C  
ATOM    187  O   ASN A  30      -2.610   4.600  31.430  1.00 26.86           O  
ANISOU  187  O   ASN A  30     4158   3265   2781  -1337   -327   -740       O  
ATOM    188  CB  ASN A  30      -2.524   4.583  28.617  1.00 24.77           C  
ANISOU  188  CB  ASN A  30     3925   3082   2403  -1355   -335   -848       C  
ATOM    189  CG  ASN A  30      -3.080   5.047  27.278  1.00 27.87           C  
ANISOU  189  CG  ASN A  30     4282   3591   2717  -1391   -356   -861       C  
ATOM    190  OD1 ASN A  30      -3.548   6.184  27.153  1.00 26.36           O  
ANISOU  190  OD1 ASN A  30     4005   3519   2493  -1385   -369   -805       O  
ATOM    191  ND2 ASN A  30      -3.028   4.169  26.266  1.00 26.87           N  
ANISOU  191  ND2 ASN A  30     4219   3431   2559  -1428   -360   -934       N  
ATOM    192  N   MET A  31      -0.657   5.742  31.487  1.00 20.85           N  
ANISOU  192  N   MET A  31     3402   2473   2046  -1169   -274   -760       N  
ATOM    193  CA  MET A  31      -0.318   5.354  32.856  1.00 23.21           C  
ANISOU  193  CA  MET A  31     3723   2684   2413  -1150   -260   -729       C  
ATOM    194  C   MET A  31      -0.976   6.222  33.922  1.00 22.04           C  
ANISOU  194  C   MET A  31     3493   2610   2270  -1163   -276   -650       C  
ATOM    195  O   MET A  31      -1.384   7.363  33.672  1.00 19.48           O  
ANISOU  195  O   MET A  31     3094   2400   1908  -1154   -288   -619       O  
ATOM    196  CB  MET A  31       1.198   5.390  33.070  1.00 19.90           C  
ANISOU  196  CB  MET A  31     3350   2177   2035  -1046   -218   -758       C  
ATOM    197  CG  MET A  31       1.974   4.362  32.251  1.00 33.15           C  
ANISOU  197  CG  MET A  31     5113   3761   3721  -1020   -196   -836       C  
ATOM    198  SD  MET A  31       3.737   4.351  32.658  1.00 34.08           S  
ANISOU  198  SD  MET A  31     5274   3780   3893   -892   -143   -855       S  
ATOM    199  CE  MET A  31       4.218   5.988  32.167  1.00 33.97           C  
ANISOU  199  CE  MET A  31     5192   3884   3831   -828   -133   -839       C  
ATOM    200  N   LYS A  32      -1.070   5.652  35.118  1.00 19.60           N  
ANISOU  200  N   LYS A  32     3200   2236   2011  -1183   -275   -617       N  
ATOM    201  CA  LYS A  32      -1.499   6.379  36.296  1.00 18.83           C  
ANISOU  201  CA  LYS A  32     3035   2194   1927  -1185   -283   -546       C  
ATOM    202  C   LYS A  32      -0.293   7.125  36.845  1.00 23.58           C  
ANISOU  202  C   LYS A  32     3638   2762   2558  -1086   -252   -543       C  
ATOM    203  O   LYS A  32       0.687   6.504  37.252  1.00 19.26           O  
ANISOU  203  O   LYS A  32     3157   2103   2059  -1042   -226   -562       O  
ATOM    204  CB  LYS A  32      -2.061   5.434  37.364  1.00 24.41           C  
ANISOU  204  CB  LYS A  32     3757   2848   2670  -1249   -294   -507       C  
ATOM    205  CG  LYS A  32      -3.254   4.591  36.926  1.00 33.13           C  
ANISOU  205  CG  LYS A  32     4863   3977   3748  -1354   -325   -506       C  
ATOM    206  CD  LYS A  32      -4.423   5.457  36.511  1.00 43.97           C  
ANISOU  206  CD  LYS A  32     6142   5504   5061  -1398   -353   -471       C  
ATOM    207  CE  LYS A  32      -5.600   4.608  36.040  1.00 54.36           C  
ANISOU  207  CE  LYS A  32     7460   6848   6346  -1505   -385   -468       C  
ATOM    208  NZ  LYS A  32      -6.506   5.365  35.123  1.00 58.07           N  
ANISOU  208  NZ  LYS A  32     7857   7458   6751  -1535   -407   -455       N  
ATOM    209  N   ILE A  33      -0.367   8.453  36.835  1.00 23.27           N  
ANISOU  209  N   ILE A  33     3529   2821   2492  -1050   -256   -518       N  
ATOM    210  CA  ILE A  33       0.690   9.301  37.353  1.00 16.00           C  
ANISOU  210  CA  ILE A  33     2603   1883   1593   -962   -231   -511       C  
ATOM    211  C   ILE A  33       0.236   9.957  38.654  1.00 15.40           C  
ANISOU  211  C   ILE A  33     2465   1855   1531   -970   -241   -450       C  
ATOM    212  O   ILE A  33      -0.830  10.572  38.698  1.00 17.16           O  
ANISOU  212  O   ILE A  33     2609   2187   1722  -1007   -267   -414       O  
ATOM    213  CB  ILE A  33       1.086  10.415  36.351  1.00 15.56           C  
ANISOU  213  CB  ILE A  33     2515   1900   1496   -908   -226   -530       C  
ATOM    214  CG1 ILE A  33       1.303   9.861  34.937  1.00 16.27           C  
ANISOU  214  CG1 ILE A  33     2650   1976   1556   -914   -221   -587       C  
ATOM    215  CG2 ILE A  33       2.314  11.172  36.855  1.00 19.60           C  
ANISOU  215  CG2 ILE A  33     3033   2380   2035   -814   -197   -526       C  
ATOM    216  CD1 ILE A  33       2.335   8.746  34.835  1.00 21.94           C  
ANISOU  216  CD1 ILE A  33     3460   2566   2312   -881   -191   -638       C  
ATOM    217  N   ILE A  34       1.040   9.823  39.707  1.00 18.54           N  
ANISOU  217  N   ILE A  34     2882   2180   1982   -912   -215   -427       N  
ATOM    218  CA  ILE A  34       0.744  10.457  40.996  1.00 17.38           C  
ANISOU  218  CA  ILE A  34     2664   2081   1857   -881   -212   -359       C  
ATOM    219  C   ILE A  34       1.831  11.453  41.388  1.00 20.16           C  
ANISOU  219  C   ILE A  34     2995   2431   2235   -765   -183   -344       C  
ATOM    220  O   ILE A  34       3.028  11.121  41.471  1.00 15.89           O  
ANISOU  220  O   ILE A  34     2509   1802   1726   -709   -157   -363       O  
ATOM    221  CB  ILE A  34       0.566   9.420  42.101  1.00 14.81           C  
ANISOU  221  CB  ILE A  34     2368   1690   1569   -929   -213   -327       C  
ATOM    222  CG1 ILE A  34      -0.638   8.530  41.767  1.00 18.06           C  
ANISOU  222  CG1 ILE A  34     2791   2118   1955  -1057   -247   -332       C  
ATOM    223  CG2 ILE A  34       0.354  10.110  43.464  1.00 16.63           C  
ANISOU  223  CG2 ILE A  34     2525   1979   1816   -891   -205   -260       C  
ATOM    224  CD1 ILE A  34      -0.952   7.516  42.823  1.00 23.07           C  
ANISOU  224  CD1 ILE A  34     3449   2695   2623  -1119   -253   -292       C  
ATOM    225  N   LEU A  35       1.405  12.696  41.583  1.00 13.75           N  
ANISOU  225  N   LEU A  35     2101   1716   1406   -728   -188   -311       N  
ATOM    226  CA  LEU A  35       2.309  13.749  42.005  1.00 12.24           C  
ANISOU  226  CA  LEU A  35     1885   1528   1236   -628   -165   -295       C  
ATOM    227  C   LEU A  35       1.986  14.148  43.448  1.00 13.31           C  
ANISOU  227  C   LEU A  35     1971   1696   1392   -609   -160   -244       C  
ATOM    228  O   LEU A  35       0.861  14.557  43.748  1.00 12.06           O  
ANISOU  228  O   LEU A  35     1749   1623   1212   -639   -175   -216       O  
ATOM    229  CB  LEU A  35       2.208  14.946  41.057  1.00 11.96           C  
ANISOU  229  CB  LEU A  35     1806   1568   1170   -591   -172   -302       C  
ATOM    230  CG  LEU A  35       2.938  16.256  41.373  1.00 11.23           C  
ANISOU  230  CG  LEU A  35     1678   1493   1096   -498   -156   -281       C  
ATOM    231  CD1 LEU A  35       4.460  16.071  41.356  1.00 10.93           C  
ANISOU  231  CD1 LEU A  35     1695   1372   1086   -441   -130   -301       C  
ATOM    232  CD2 LEU A  35       2.510  17.337  40.363  1.00 11.18           C  
ANISOU  232  CD2 LEU A  35     1624   1566   1056   -482   -171   -278       C  
ATOM    233  N   LEU A  36       2.969  13.996  44.331  1.00 15.79           N  
ANISOU  233  N   LEU A  36     2310   1948   1742   -562   -139   -231       N  
ATOM    234  CA  LEU A  36       2.830  14.348  45.753  1.00 14.23           C  
ANISOU  234  CA  LEU A  36     2071   1777   1558   -541   -132   -187       C  
ATOM    235  C   LEU A  36       3.580  15.634  46.032  1.00 15.81           C  
ANISOU  235  C   LEU A  36     2242   1999   1766   -453   -118   -182       C  
ATOM    236  O   LEU A  36       4.770  15.717  45.762  1.00 16.66           O  
ANISOU  236  O   LEU A  36     2386   2051   1894   -404   -104   -198       O  
ATOM    237  CB  LEU A  36       3.364  13.223  46.634  1.00 14.58           C  
ANISOU  237  CB  LEU A  36     2163   1742   1634   -558   -123   -168       C  
ATOM    238  CG  LEU A  36       2.816  11.848  46.233  1.00 15.68           C  
ANISOU  238  CG  LEU A  36     2351   1832   1774   -646   -137   -179       C  
ATOM    239  CD1 LEU A  36       3.518  10.708  46.974  1.00 12.68           C  
ANISOU  239  CD1 LEU A  36     2029   1352   1435   -652   -127   -159       C  
ATOM    240  CD2 LEU A  36       1.304  11.798  46.458  1.00 19.46           C  
ANISOU  240  CD2 LEU A  36     2776   2397   2222   -724   -160   -153       C  
ATOM    241  N   GLU A  37       2.873  16.631  46.567  1.00 10.50           N  
ANISOU  241  N   GLU A  37     1504   1407   1080   -434   -120   -161       N  
ATOM    242  CA  GLU A  37       3.449  17.938  46.841  1.00 11.32           C  
ANISOU  242  CA  GLU A  37     1582   1529   1191   -357   -110   -160       C  
ATOM    243  C   GLU A  37       3.164  18.365  48.289  1.00 13.88           C  
ANISOU  243  C   GLU A  37     1866   1892   1514   -339   -101   -133       C  
ATOM    244  O   GLU A  37       2.027  18.277  48.743  1.00 12.57           O  
ANISOU  244  O   GLU A  37     1658   1790   1329   -373   -106   -114       O  
ATOM    245  CB  GLU A  37       2.896  18.976  45.860  1.00  9.91           C  
ANISOU  245  CB  GLU A  37     1365   1408    993   -338   -121   -169       C  
ATOM    246  CG  GLU A  37       3.190  20.434  46.216  1.00  9.51           C  
ANISOU  246  CG  GLU A  37     1280   1381    951   -265   -114   -163       C  
ATOM    247  CD  GLU A  37       4.665  20.691  46.508  1.00 15.43           C  
ANISOU  247  CD  GLU A  37     2068   2066   1727   -217   -101   -170       C  
ATOM    248  OE1 GLU A  37       5.537  20.134  45.809  1.00 15.66           O  
ANISOU  248  OE1 GLU A  37     2142   2043   1764   -220    -98   -185       O  
ATOM    249  OE2 GLU A  37       4.961  21.450  47.453  1.00  8.85           O  
ANISOU  249  OE2 GLU A  37     1219   1240    904   -177    -92   -162       O  
ATOM    250  N   ALA A  38       4.189  18.849  48.988  1.00 13.47           N  
ANISOU  250  N   ALA A  38     1826   1811   1481   -287    -88   -131       N  
ATOM    251  CA  ALA A  38       4.073  19.223  50.411  1.00 13.99           C  
ANISOU  251  CA  ALA A  38     1863   1912   1541   -270    -78   -111       C  
ATOM    252  C   ALA A  38       3.142  20.406  50.626  1.00 18.40           C  
ANISOU  252  C   ALA A  38     2363   2548   2079   -241    -77   -114       C  
ATOM    253  O   ALA A  38       2.426  20.460  51.617  1.00 12.63           O  
ANISOU  253  O   ALA A  38     1596   1875   1330   -249    -69    -99       O  
ATOM    254  CB  ALA A  38       5.445  19.535  50.992  1.00  9.11           C  
ANISOU  254  CB  ALA A  38     1271   1248    942   -224    -69   -111       C  
ATOM    255  N   GLY A  39       3.155  21.357  49.698  1.00  9.32           N  
ANISOU  255  N   GLY A  39     1204   1403    934   -204    -82   -132       N  
ATOM    256  CA  GLY A  39       2.256  22.492  49.781  1.00 12.63           C  
ANISOU  256  CA  GLY A  39     1570   1888   1341   -168    -80   -133       C  
ATOM    257  C   GLY A  39       1.032  22.311  48.882  1.00 15.02           C  
ANISOU  257  C   GLY A  39     1835   2247   1625   -202    -94   -124       C  
ATOM    258  O   GLY A  39       0.642  21.192  48.549  1.00 11.59           O  
ANISOU  258  O   GLY A  39     1409   1814   1179   -267   -104   -115       O  
ATOM    259  N   HIS A  40       0.421  23.424  48.494  1.00 16.04           N  
ANISOU  259  N   HIS A  40     1922   2422   1752   -158    -96   -123       N  
ATOM    260  CA  HIS A  40      -0.787  23.396  47.691  1.00 20.47           C  
ANISOU  260  CA  HIS A  40     2435   3052   2292   -184   -110   -106       C  
ATOM    261  C   HIS A  40      -0.746  24.490  46.629  1.00 19.07           C  
ANISOU  261  C   HIS A  40     2245   2876   2125   -135   -121   -107       C  
ATOM    262  O   HIS A  40       0.272  25.173  46.478  1.00 12.27           O  
ANISOU  262  O   HIS A  40     1419   1956   1288    -90   -117   -120       O  
ATOM    263  CB  HIS A  40      -2.015  23.558  48.587  1.00 14.26           C  
ANISOU  263  CB  HIS A  40     1581   2353   1484   -181    -99    -87       C  
ATOM    264  CG  HIS A  40      -1.911  24.709  49.536  1.00 11.57           C  
ANISOU  264  CG  HIS A  40     1222   2020   1153   -102    -77    -99       C  
ATOM    265  ND1 HIS A  40      -1.524  24.558  50.853  1.00 17.11           N  
ANISOU  265  ND1 HIS A  40     1938   2712   1851    -96    -57   -108       N  
ATOM    266  CD2 HIS A  40      -2.160  26.028  49.366  1.00 10.82           C  
ANISOU  266  CD2 HIS A  40     1100   1940   1070    -28    -71   -104       C  
ATOM    267  CE1 HIS A  40      -1.547  25.734  51.452  1.00 10.71           C  
ANISOU  267  CE1 HIS A  40     1111   1912   1046    -23    -40   -126       C  
ATOM    268  NE2 HIS A  40      -1.923  26.646  50.568  1.00 14.20           N  
ANISOU  268  NE2 HIS A  40     1530   2363   1502     21    -47   -124       N  
ATOM    269  N   SER A  41      -1.824  24.637  45.871  1.00 10.68           N  
ANISOU  269  N   SER A  41     1132   1885   1043   -149   -136    -86       N  
ATOM    270  CA  SER A  41      -1.863  25.644  44.812  1.00 11.45           C  
ANISOU  270  CA  SER A  41     1212   1990   1147   -106   -149    -75       C  
ATOM    271  C   SER A  41      -2.174  27.039  45.377  1.00 19.63           C  
ANISOU  271  C   SER A  41     2211   3044   2205    -18   -135    -68       C  
ATOM    272  O   SER A  41      -2.883  27.179  46.384  1.00 17.04           O  
ANISOU  272  O   SER A  41     1843   2760   1870      2   -117    -65       O  
ATOM    273  CB  SER A  41      -2.892  25.266  43.740  1.00 14.65           C  
ANISOU  273  CB  SER A  41     1574   2472   1520   -156   -174    -51       C  
ATOM    274  OG  SER A  41      -4.214  25.201  44.270  1.00 15.79           O  
ANISOU  274  OG  SER A  41     1648   2708   1646   -166   -172    -26       O  
ATOM    275  N   HIS A  42      -1.625  28.060  44.726  1.00 12.36           N  
ANISOU  275  N   HIS A  42     1304   2084   1307     33   -141    -64       N  
ATOM    276  CA  HIS A  42      -1.854  29.447  45.101  1.00 13.84           C  
ANISOU  276  CA  HIS A  42     1467   2268   1522    119   -131    -58       C  
ATOM    277  C   HIS A  42      -2.416  30.252  43.931  1.00 15.06           C  
ANISOU  277  C   HIS A  42     1582   2458   1681    150   -150    -20       C  
ATOM    278  O   HIS A  42      -1.946  31.359  43.644  1.00 16.61           O  
ANISOU  278  O   HIS A  42     1793   2606   1910    207   -153    -13       O  
ATOM    279  CB  HIS A  42      -0.549  30.080  45.608  1.00 17.39           C  
ANISOU  279  CB  HIS A  42     1977   2624   2005    156   -120    -86       C  
ATOM    280  CG  HIS A  42      -0.128  29.579  46.954  1.00 15.33           C  
ANISOU  280  CG  HIS A  42     1744   2342   1740    144    -99   -118       C  
ATOM    281  ND1 HIS A  42      -0.030  30.406  48.057  1.00 10.32           N  
ANISOU  281  ND1 HIS A  42     1113   1688   1120    199    -79   -141       N  
ATOM    282  CD2 HIS A  42       0.221  28.345  47.385  1.00  9.98           C  
ANISOU  282  CD2 HIS A  42     1089   1659   1043     83    -96   -128       C  
ATOM    283  CE1 HIS A  42       0.355  29.704  49.102  1.00 13.75           C  
ANISOU  283  CE1 HIS A  42     1569   2117   1540    169    -66   -162       C  
ATOM    284  NE2 HIS A  42       0.524  28.444  48.718  1.00 14.24           N  
ANISOU  284  NE2 HIS A  42     1642   2184   1584    101    -76   -150       N  
ATOM    285  N   PHE A  43      -3.418  29.689  43.261  1.00 13.67           N  
ANISOU  285  N   PHE A  43     1355   2366   1472    107   -167      8       N  
ATOM    286  CA  PHE A  43      -3.953  30.271  42.039  1.00 15.89           C  
ANISOU  286  CA  PHE A  43     1595   2695   1749    122   -192     52       C  
ATOM    287  C   PHE A  43      -4.797  31.512  42.302  1.00 18.31           C  
ANISOU  287  C   PHE A  43     1842   3035   2080    212   -183     82       C  
ATOM    288  O   PHE A  43      -5.101  32.263  41.368  1.00 15.63           O  
ANISOU  288  O   PHE A  43     1472   2718   1749    245   -202    125       O  
ATOM    289  CB  PHE A  43      -4.751  29.215  41.254  1.00 16.84           C  
ANISOU  289  CB  PHE A  43     1679   2900   1819     37   -215     71       C  
ATOM    290  CG  PHE A  43      -3.902  28.048  40.776  1.00 13.53           C  
ANISOU  290  CG  PHE A  43     1325   2437   1377    -45   -225     38       C  
ATOM    291  CD1 PHE A  43      -2.540  28.195  40.602  1.00 12.23           C  
ANISOU  291  CD1 PHE A  43     1230   2181   1235    -32   -219     13       C  
ATOM    292  CD2 PHE A  43      -4.471  26.820  40.501  1.00 13.43           C  
ANISOU  292  CD2 PHE A  43     1304   2476   1324   -135   -239     34       C  
ATOM    293  CE1 PHE A  43      -1.754  27.134  40.187  1.00 11.13           C  
ANISOU  293  CE1 PHE A  43     1150   2002   1077    -96   -222    -18       C  
ATOM    294  CE2 PHE A  43      -3.698  25.757  40.073  1.00 13.27           C  
ANISOU  294  CE2 PHE A  43     1350   2407   1287   -203   -244     -1       C  
ATOM    295  CZ  PHE A  43      -2.333  25.911  39.922  1.00 11.41           C  
ANISOU  295  CZ  PHE A  43     1182   2080   1074   -179   -234    -28       C  
ATOM    296  N   ASN A  44      -5.199  31.715  43.556  1.00 12.74           N  
ANISOU  296  N   ASN A  44     1118   2337   1384    254   -154     62       N  
ATOM    297  CA  ASN A  44      -5.959  32.911  43.933  1.00 13.33           C  
ANISOU  297  CA  ASN A  44     1144   2437   1487    352   -138     81       C  
ATOM    298  C   ASN A  44      -5.238  33.789  44.960  1.00 21.17           C  
ANISOU  298  C   ASN A  44     2187   3336   2519    423   -111     37       C  
ATOM    299  O   ASN A  44      -5.844  34.631  45.635  1.00 16.90           O  
ANISOU  299  O   ASN A  44     1616   2808   1998    504    -87     32       O  
ATOM    300  CB  ASN A  44      -7.355  32.513  44.437  1.00 14.22           C  
ANISOU  300  CB  ASN A  44     1169   2667   1567    350   -126    100       C  
ATOM    301  CG  ASN A  44      -8.227  31.922  43.324  1.00 19.75           C  
ANISOU  301  CG  ASN A  44     1807   3469   2230    290   -159    153       C  
ATOM    302  OD1 ASN A  44      -8.935  32.657  42.625  1.00 20.14           O  
ANISOU  302  OD1 ASN A  44     1797   3570   2287    338   -172    203       O  
ATOM    303  ND2 ASN A  44      -8.151  30.607  43.134  1.00 17.55           N  
ANISOU  303  ND2 ASN A  44     1543   3214   1912    183   -174    143       N  
ATOM    304  N   ASP A  45      -3.928  33.605  45.058  1.00 22.58           N  
ANISOU  304  N   ASP A  45     2445   3425   2710    391   -114      4       N  
ATOM    305  CA  ASP A  45      -3.110  34.294  46.053  1.00 13.12           C  
ANISOU  305  CA  ASP A  45     1303   2140   1543    437    -93    -42       C  
ATOM    306  C   ASP A  45      -2.256  35.367  45.378  1.00 15.47           C  
ANISOU  306  C   ASP A  45     1645   2347   1885    474   -108    -32       C  
ATOM    307  O   ASP A  45      -1.238  35.049  44.768  1.00 12.76           O  
ANISOU  307  O   ASP A  45     1348   1958   1543    425   -127    -29       O  
ATOM    308  CB  ASP A  45      -2.250  33.263  46.788  1.00 14.06           C  
ANISOU  308  CB  ASP A  45     1471   2231   1640    370    -85    -81       C  
ATOM    309  CG  ASP A  45      -1.342  33.866  47.851  1.00 17.64           C  
ANISOU  309  CG  ASP A  45     1981   2605   2115    403    -67   -129       C  
ATOM    310  OD1 ASP A  45      -1.372  35.091  48.117  1.00 14.95           O  
ANISOU  310  OD1 ASP A  45     1649   2223   1808    476    -58   -141       O  
ATOM    311  OD2 ASP A  45      -0.585  33.073  48.439  1.00 15.58           O  
ANISOU  311  OD2 ASP A  45     1758   2324   1839    352    -63   -153       O  
ATOM    312  N   PRO A  46      -2.644  36.647  45.531  1.00 12.82           N  
ANISOU  312  N   PRO A  46     1299   1984   1588    562   -100    -25       N  
ATOM    313  CA  PRO A  46      -1.980  37.761  44.841  1.00 12.92           C  
ANISOU  313  CA  PRO A  46     1350   1911   1649    599   -118     -4       C  
ATOM    314  C   PRO A  46      -0.486  37.868  45.172  1.00 12.36           C  
ANISOU  314  C   PRO A  46     1361   1741   1594    567   -122    -41       C  
ATOM    315  O   PRO A  46       0.272  38.412  44.372  1.00 16.60           O  
ANISOU  315  O   PRO A  46     1929   2219   2158    562   -144    -14       O  
ATOM    316  CB  PRO A  46      -2.730  38.993  45.348  1.00 13.74           C  
ANISOU  316  CB  PRO A  46     1433   1996   1792    704    -99     -7       C  
ATOM    317  CG  PRO A  46      -3.315  38.568  46.683  1.00 16.51           C  
ANISOU  317  CG  PRO A  46     1764   2396   2115    718    -63    -58       C  
ATOM    318  CD  PRO A  46      -3.649  37.111  46.505  1.00 17.37           C  
ANISOU  318  CD  PRO A  46     1833   2599   2167    634    -69    -44       C  
ATOM    319  N   VAL A  47      -0.091  37.362  46.334  1.00 12.05           N  
ANISOU  319  N   VAL A  47     1350   1691   1537    545   -101    -95       N  
ATOM    320  CA  VAL A  47       1.308  37.294  46.742  1.00 11.53           C  
ANISOU  320  CA  VAL A  47     1353   1549   1478    506   -105   -127       C  
ATOM    321  C   VAL A  47       2.090  36.506  45.706  1.00 10.96           C  
ANISOU  321  C   VAL A  47     1294   1481   1391    436   -129    -98       C  
ATOM    322  O   VAL A  47       3.244  36.820  45.427  1.00 10.97           O  
ANISOU  322  O   VAL A  47     1341   1417   1411    417   -142    -96       O  
ATOM    323  CB  VAL A  47       1.469  36.626  48.141  1.00 11.32           C  
ANISOU  323  CB  VAL A  47     1341   1538   1422    484    -81   -181       C  
ATOM    324  CG1 VAL A  47       2.929  36.425  48.490  1.00 12.69           C  
ANISOU  324  CG1 VAL A  47     1576   1648   1598    437    -89   -205       C  
ATOM    325  CG2 VAL A  47       0.763  37.450  49.227  1.00 11.95           C  
ANISOU  325  CG2 VAL A  47     1413   1618   1511    556    -54   -221       C  
ATOM    326  N   VAL A  48       1.444  35.479  45.154  1.00 10.86           N  
ANISOU  326  N   VAL A  48     1239   1546   1341    397   -132    -76       N  
ATOM    327  CA  VAL A  48       2.020  34.630  44.102  1.00 13.12           C  
ANISOU  327  CA  VAL A  48     1535   1845   1605    333   -151    -54       C  
ATOM    328  C   VAL A  48       1.641  35.085  42.675  1.00 18.76           C  
ANISOU  328  C   VAL A  48     2220   2585   2322    342   -175      0       C  
ATOM    329  O   VAL A  48       2.494  35.175  41.792  1.00 10.55           O  
ANISOU  329  O   VAL A  48     1206   1518   1286    318   -191     21       O  
ATOM    330  CB  VAL A  48       1.581  33.163  44.288  1.00 15.28           C  
ANISOU  330  CB  VAL A  48     1790   2182   1834    275   -144    -66       C  
ATOM    331  CG1 VAL A  48       2.036  32.309  43.115  1.00 12.18           C  
ANISOU  331  CG1 VAL A  48     1408   1804   1417    215   -161    -50       C  
ATOM    332  CG2 VAL A  48       2.132  32.597  45.622  1.00  9.92           C  
ANISOU  332  CG2 VAL A  48     1143   1478   1149    257   -124   -110       C  
ATOM    333  N   THR A  49       0.359  35.360  42.444  1.00 11.29           N  
ANISOU  333  N   THR A  49     1215   1702   1372    375   -177     28       N  
ATOM    334  CA  THR A  49      -0.130  35.578  41.088  1.00 14.65           C  
ANISOU  334  CA  THR A  49     1602   2176   1789    373   -202     85       C  
ATOM    335  C   THR A  49       0.305  36.923  40.524  1.00 16.55           C  
ANISOU  335  C   THR A  49     1859   2356   2075    423   -216    123       C  
ATOM    336  O   THR A  49       0.505  37.051  39.326  1.00 13.97           O  
ANISOU  336  O   THR A  49     1524   2045   1738    404   -240    169       O  
ATOM    337  CB  THR A  49      -1.666  35.508  41.033  1.00 18.40           C  
ANISOU  337  CB  THR A  49     2000   2746   2246    396   -202    112       C  
ATOM    338  OG1 THR A  49      -2.200  36.548  41.870  1.00 16.50           O  
ANISOU  338  OG1 THR A  49     1744   2481   2045    482   -183    108       O  
ATOM    339  CG2 THR A  49      -2.148  34.160  41.534  1.00 12.02           C  
ANISOU  339  CG2 THR A  49     1173   2001   1391    335   -191     83       C  
ATOM    340  N   ASP A  50       0.426  37.933  41.381  1.00 16.80           N  
ANISOU  340  N   ASP A  50     1913   2316   2153    486   -203    105       N  
ATOM    341  CA  ASP A  50       0.979  39.202  40.938  1.00 14.26           C  
ANISOU  341  CA  ASP A  50     1620   1916   1881    526   -217    138       C  
ATOM    342  C   ASP A  50       2.493  39.123  41.091  1.00 12.46           C  
ANISOU  342  C   ASP A  50     1460   1614   1661    481   -220    112       C  
ATOM    343  O   ASP A  50       3.000  38.946  42.196  1.00 16.50           O  
ANISOU  343  O   ASP A  50     2008   2084   2176    474   -202     56       O  
ATOM    344  CB  ASP A  50       0.401  40.374  41.737  1.00 15.23           C  
ANISOU  344  CB  ASP A  50     1744   1989   2056    616   -203    127       C  
ATOM    345  CG  ASP A  50       0.920  41.727  41.261  1.00 23.85           C  
ANISOU  345  CG  ASP A  50     2869   2987   3205    656   -221    166       C  
ATOM    346  OD1 ASP A  50       1.923  41.770  40.520  1.00 20.77           O  
ANISOU  346  OD1 ASP A  50     2509   2565   2816    608   -242    193       O  
ATOM    347  OD2 ASP A  50       0.350  42.766  41.655  1.00 24.29           O  
ANISOU  347  OD2 ASP A  50     2923   2998   3308    737   -212    168       O  
ATOM    348  N   PRO A  51       3.225  39.249  39.974  1.00 13.29           N  
ANISOU  348  N   PRO A  51     1576   1711   1763    447   -243    156       N  
ATOM    349  CA  PRO A  51       4.688  39.170  40.036  1.00 13.62           C  
ANISOU  349  CA  PRO A  51     1671   1693   1809    403   -246    140       C  
ATOM    350  C   PRO A  51       5.281  40.141  41.058  1.00 11.47           C  
ANISOU  350  C   PRO A  51     1449   1323   1587    434   -240    109       C  
ATOM    351  O   PRO A  51       6.309  39.835  41.637  1.00 13.54           O  
ANISOU  351  O   PRO A  51     1751   1549   1845    398   -235     74       O  
ATOM    352  CB  PRO A  51       5.117  39.529  38.603  1.00 11.51           C  
ANISOU  352  CB  PRO A  51     1396   1438   1538    383   -271    207       C  
ATOM    353  CG  PRO A  51       3.966  39.087  37.764  1.00 11.77           C  
ANISOU  353  CG  PRO A  51     1370   1567   1535    384   -280    241       C  
ATOM    354  CD  PRO A  51       2.741  39.417  38.591  1.00 14.49           C  
ANISOU  354  CD  PRO A  51     1685   1919   1901    445   -267    226       C  
ATOM    355  N   MET A  52       4.639  41.283  41.274  1.00 12.13           N  
ANISOU  355  N   MET A  52     1530   1361   1716    500   -242    122       N  
ATOM    356  CA  MET A  52       5.139  42.254  42.222  1.00 17.30           C  
ANISOU  356  CA  MET A  52     2239   1916   2419    529   -238     87       C  
ATOM    357  C   MET A  52       4.967  41.779  43.681  1.00 19.23           C  
ANISOU  357  C   MET A  52     2497   2164   2646    536   -209      7       C  
ATOM    358  O   MET A  52       5.595  42.324  44.587  1.00 14.09           O  
ANISOU  358  O   MET A  52     1897   1440   2018    538   -205    -37       O  
ATOM    359  CB  MET A  52       4.448  43.603  41.997  1.00 13.29           C  
ANISOU  359  CB  MET A  52     1728   1353   1967    604   -246    122       C  
ATOM    360  CG  MET A  52       4.757  44.213  40.610  1.00 13.58           C  
ANISOU  360  CG  MET A  52     1758   1377   2026    594   -278    210       C  
ATOM    361  SD  MET A  52       6.538  44.279  40.222  1.00 19.79           S  
ANISOU  361  SD  MET A  52     2596   2110   2813    511   -299    226       S  
ATOM    362  CE  MET A  52       7.041  45.629  41.273  1.00 18.07           C  
ANISOU  362  CE  MET A  52     2451   1748   2665    542   -302    188       C  
ATOM    363  N   GLY A  53       4.152  40.744  43.898  1.00 15.46           N  
ANISOU  363  N   GLY A  53     1975   1774   2124    530   -191     -9       N  
ATOM    364  CA  GLY A  53       3.989  40.168  45.225  1.00 16.91           C  
ANISOU  364  CA  GLY A  53     2166   1977   2284    528   -165    -75       C  
ATOM    365  C   GLY A  53       5.314  39.681  45.782  1.00 19.47           C  
ANISOU  365  C   GLY A  53     2537   2267   2594    468   -166   -108       C  
ATOM    366  O   GLY A  53       5.548  39.650  47.003  1.00 15.37           O  
ANISOU  366  O   GLY A  53     2044   1729   2068    468   -151   -163       O  
ATOM    367  N   PHE A  54       6.190  39.297  44.866  1.00 16.67           N  
ANISOU  367  N   PHE A  54     2189   1913   2231    417   -185    -72       N  
ATOM    368  CA  PHE A  54       7.552  38.915  45.212  1.00 16.90           C  
ANISOU  368  CA  PHE A  54     2258   1913   2252    363   -189    -90       C  
ATOM    369  C   PHE A  54       8.258  40.013  46.022  1.00 16.01           C  
ANISOU  369  C   PHE A  54     2196   1714   2175    374   -196   -118       C  
ATOM    370  O   PHE A  54       8.937  39.722  47.000  1.00 20.61           O  
ANISOU  370  O   PHE A  54     2804   2284   2743    346   -189   -158       O  
ATOM    371  CB  PHE A  54       8.337  38.599  43.940  1.00 11.34           C  
ANISOU  371  CB  PHE A  54     1549   1221   1538    321   -207    -40       C  
ATOM    372  CG  PHE A  54       9.778  38.310  44.179  1.00 13.07           C  
ANISOU  372  CG  PHE A  54     1800   1413   1752    272   -212    -47       C  
ATOM    373  CD1 PHE A  54      10.198  37.011  44.452  1.00  9.19           C  
ANISOU  373  CD1 PHE A  54     1304    964   1223    235   -199    -66       C  
ATOM    374  CD2 PHE A  54      10.717  39.329  44.138  1.00  9.93           C  
ANISOU  374  CD2 PHE A  54     1435    950   1388    263   -230    -31       C  
ATOM    375  CE1 PHE A  54      11.513  36.738  44.676  1.00 13.21           C  
ANISOU  375  CE1 PHE A  54     1836   1456   1728    198   -202    -67       C  
ATOM    376  CE2 PHE A  54      12.053  39.059  44.367  1.00 13.76           C  
ANISOU  376  CE2 PHE A  54     1941   1421   1865    216   -235    -32       C  
ATOM    377  CZ  PHE A  54      12.453  37.770  44.627  1.00 14.03           C  
ANISOU  377  CZ  PHE A  54     1965   1504   1862    188   -220    -49       C  
ATOM    378  N   PHE A  55       8.069  41.273  45.634  1.00 14.42           N  
ANISOU  378  N   PHE A  55     2009   1451   2019    412   -209    -95       N  
ATOM    379  CA  PHE A  55       8.727  42.380  46.311  1.00 13.69           C  
ANISOU  379  CA  PHE A  55     1971   1265   1964    417   -219   -122       C  
ATOM    380  C   PHE A  55       8.009  42.867  47.575  1.00 22.83           C  
ANISOU  380  C   PHE A  55     3147   2396   3129    469   -197   -190       C  
ATOM    381  O   PHE A  55       8.442  43.837  48.198  1.00 23.56           O  
ANISOU  381  O   PHE A  55     3293   2407   3253    476   -203   -223       O  
ATOM    382  CB  PHE A  55       8.901  43.550  45.345  1.00 16.32           C  
ANISOU  382  CB  PHE A  55     2320   1531   2349    432   -244    -66       C  
ATOM    383  CG  PHE A  55       9.764  43.220  44.172  1.00 12.20           C  
ANISOU  383  CG  PHE A  55     1785   1033   1817    378   -265     -2       C  
ATOM    384  CD1 PHE A  55      11.130  43.128  44.319  1.00 13.39           C  
ANISOU  384  CD1 PHE A  55     1964   1162   1962    315   -278     -2       C  
ATOM    385  CD2 PHE A  55       9.197  42.957  42.933  1.00 12.98           C  
ANISOU  385  CD2 PHE A  55     1839   1188   1906    388   -271     57       C  
ATOM    386  CE1 PHE A  55      11.926  42.801  43.247  1.00 16.25           C  
ANISOU  386  CE1 PHE A  55     2309   1556   2311    270   -292     56       C  
ATOM    387  CE2 PHE A  55       9.986  42.629  41.851  1.00 11.53           C  
ANISOU  387  CE2 PHE A  55     1642   1035   1705    339   -286    111       C  
ATOM    388  CZ  PHE A  55      11.350  42.557  42.004  1.00 14.13           C  
ANISOU  388  CZ  PHE A  55     1999   1341   2030    283   -295    110       C  
ATOM    389  N   GLY A  56       6.923  42.202  47.959  1.00 19.26           N  
ANISOU  389  N   GLY A  56     2653   2017   2647    502   -170   -211       N  
ATOM    390  CA  GLY A  56       6.296  42.495  49.233  1.00 16.27           C  
ANISOU  390  CA  GLY A  56     2286   1634   2262    547   -144   -279       C  
ATOM    391  C   GLY A  56       5.041  43.324  49.110  1.00 17.90           C  
ANISOU  391  C   GLY A  56     2472   1829   2500    636   -129   -277       C  
ATOM    392  O   GLY A  56       4.540  43.844  50.101  1.00 18.53           O  
ANISOU  392  O   GLY A  56     2568   1889   2582    687   -106   -335       O  
ATOM    393  N   LYS A  57       4.526  43.434  47.889  1.00 23.00           N  
ANISOU  393  N   LYS A  57     3079   2494   3165    657   -142   -208       N  
ATOM    394  CA  LYS A  57       3.353  44.260  47.598  1.00 22.54           C  
ANISOU  394  CA  LYS A  57     2994   2427   3143    746   -133   -189       C  
ATOM    395  C   LYS A  57       2.153  43.934  48.490  1.00 21.84           C  
ANISOU  395  C   LYS A  57     2863   2411   3026    802    -94   -232       C  
ATOM    396  O   LYS A  57       1.395  44.830  48.879  1.00 16.81           O  
ANISOU  396  O   LYS A  57     2227   1741   2420    888    -75   -254       O  
ATOM    397  CB  LYS A  57       2.956  44.109  46.123  1.00 22.85           C  
ANISOU  397  CB  LYS A  57     2982   2511   3190    745   -155   -100       C  
ATOM    398  CG  LYS A  57       1.804  45.022  45.699  1.00 23.61           C  
ANISOU  398  CG  LYS A  57     3045   2598   3328    839   -150    -63       C  
ATOM    399  CD  LYS A  57       1.621  45.054  44.185  1.00 26.89           C  
ANISOU  399  CD  LYS A  57     3418   3046   3752    830   -180     32       C  
ATOM    400  CE  LYS A  57       0.336  45.770  43.785  1.00 27.64           C  
ANISOU  400  CE  LYS A  57     3463   3159   3881    925   -175     78       C  
ATOM    401  NZ  LYS A  57       0.069  45.656  42.315  1.00 29.03           N  
ANISOU  401  NZ  LYS A  57     3588   3393   4052    909   -205    174       N  
ATOM    402  N   TYR A  58       1.989  42.661  48.838  1.00 19.37           N  
ANISOU  402  N   TYR A  58     2512   2193   2653    755    -82   -245       N  
ATOM    403  CA  TYR A  58       0.808  42.278  49.603  1.00 22.54           C  
ANISOU  403  CA  TYR A  58     2863   2679   3022    800    -46   -274       C  
ATOM    404  C   TYR A  58       1.167  41.774  50.984  1.00 24.57           C  
ANISOU  404  C   TYR A  58     3145   2953   3236    770    -24   -345       C  
ATOM    405  O   TYR A  58       0.363  41.115  51.641  1.00 26.22           O  
ANISOU  405  O   TYR A  58     3309   3251   3402    779      4   -364       O  
ATOM    406  CB  TYR A  58       0.012  41.220  48.847  1.00 24.73           C  
ANISOU  406  CB  TYR A  58     3063   3069   3263    774    -50   -219       C  
ATOM    407  CG  TYR A  58      -0.403  41.677  47.473  1.00 18.95           C  
ANISOU  407  CG  TYR A  58     2299   2338   2564    800    -74   -144       C  
ATOM    408  CD1 TYR A  58      -1.558  42.430  47.282  1.00 20.21           C  
ANISOU  408  CD1 TYR A  58     2411   2517   2750    890    -62   -119       C  
ATOM    409  CD2 TYR A  58       0.377  41.378  46.369  1.00 15.73           C  
ANISOU  409  CD2 TYR A  58     1904   1915   2158    737   -108    -96       C  
ATOM    410  CE1 TYR A  58      -1.928  42.855  46.027  1.00 23.64           C  
ANISOU  410  CE1 TYR A  58     2813   2958   3213    913    -87    -43       C  
ATOM    411  CE2 TYR A  58       0.022  41.801  45.117  1.00 24.52           C  
ANISOU  411  CE2 TYR A  58     2986   3037   3294    756   -131    -25       C  
ATOM    412  CZ  TYR A  58      -1.129  42.534  44.947  1.00 27.86           C  
ANISOU  412  CZ  TYR A  58     3362   3480   3743    842   -123      4       C  
ATOM    413  OH  TYR A  58      -1.467  42.943  43.687  1.00 29.86           O  
ANISOU  413  OH  TYR A  58     3581   3747   4016    859   -149     83       O  
ATOM    414  N   ASN A  59       2.377  42.099  51.425  1.00 21.29           N  
ANISOU  414  N   ASN A  59     2800   2458   2830    731    -37   -381       N  
ATOM    415  CA  ASN A  59       2.794  41.755  52.776  1.00 23.34           C  
ANISOU  415  CA  ASN A  59     3089   2730   3048    703    -19   -448       C  
ATOM    416  C   ASN A  59       2.005  42.538  53.826  1.00 25.26           C  
ANISOU  416  C   ASN A  59     3338   2969   3289    783     17   -514       C  
ATOM    417  O   ASN A  59       1.852  43.753  53.716  1.00 24.03           O  
ANISOU  417  O   ASN A  59     3216   2731   3184    848     19   -531       O  
ATOM    418  CB  ASN A  59       4.282  42.033  52.972  1.00 22.36           C  
ANISOU  418  CB  ASN A  59     3036   2524   2936    643    -45   -467       C  
ATOM    419  CG  ASN A  59       5.159  41.103  52.187  1.00 19.75           C  
ANISOU  419  CG  ASN A  59     2697   2213   2594    563    -73   -413       C  
ATOM    420  OD1 ASN A  59       4.681  40.310  51.364  1.00 18.81           O  
ANISOU  420  OD1 ASN A  59     2528   2156   2464    551    -75   -363       O  
ATOM    421  ND2 ASN A  59       6.469  41.186  52.438  1.00 18.08           N  
ANISOU  421  ND2 ASN A  59     2535   1950   2384    506    -94   -425       N  
ATOM    422  N   PRO A  60       1.468  41.842  54.834  1.00 29.94           N  
ANISOU  422  N   PRO A  60     3899   3651   3825    782     49   -550       N  
ATOM    423  CA  PRO A  60       0.950  42.582  55.988  1.00 27.19           C  
ANISOU  423  CA  PRO A  60     3569   3299   3465    850     86   -627       C  
ATOM    424  C   PRO A  60       2.089  43.345  56.659  1.00 27.49           C  
ANISOU  424  C   PRO A  60     3698   3236   3513    826     73   -691       C  
ATOM    425  O   PRO A  60       3.184  42.794  56.812  1.00 28.48           O  
ANISOU  425  O   PRO A  60     3851   3353   3617    740     47   -686       O  
ATOM    426  CB  PRO A  60       0.392  41.490  56.903  1.00 30.12           C  
ANISOU  426  CB  PRO A  60     3886   3796   3761    827    115   -642       C  
ATOM    427  CG  PRO A  60       1.000  40.226  56.426  1.00 35.18           C  
ANISOU  427  CG  PRO A  60     4510   4477   4380    731     87   -586       C  
ATOM    428  CD  PRO A  60       1.251  40.394  54.955  1.00 32.60           C  
ANISOU  428  CD  PRO A  60     4183   4098   4107    722     53   -521       C  
ATOM    429  N   PRO A  61       1.847  44.610  57.016  1.00 28.07           N  
ANISOU  429  N   PRO A  61     3815   3228   3620    901     88   -747       N  
ATOM    430  CA  PRO A  61       2.863  45.502  57.589  1.00 30.14           C  
ANISOU  430  CA  PRO A  61     4166   3386   3900    864     75   -798       C  
ATOM    431  C   PRO A  61       3.513  44.969  58.875  1.00 32.09           C  
ANISOU  431  C   PRO A  61     4437   3680   4077    796     81   -856       C  
ATOM    432  O   PRO A  61       4.690  45.255  59.119  1.00 28.48           O  
ANISOU  432  O   PRO A  61     4040   3158   3622    728     53   -875       O  
ATOM    433  CB  PRO A  61       2.075  46.786  57.891  1.00 30.08           C  
ANISOU  433  CB  PRO A  61     4175   3323   3932    938    110   -827       C  
ATOM    434  CG  PRO A  61       0.875  46.725  57.002  1.00 33.30           C  
ANISOU  434  CG  PRO A  61     4510   3773   4369   1019    123   -769       C  
ATOM    435  CD  PRO A  61       0.537  45.271  56.869  1.00 29.86           C  
ANISOU  435  CD  PRO A  61     4002   3468   3875   1001    123   -740       C  
ATOM    436  N   ASN A  62       2.780  44.179  59.655  1.00 29.26           N  
ANISOU  436  N   ASN A  62     4026   3438   3653    809    116   -876       N  
ATOM    437  CA  ASN A  62       3.305  43.670  60.923  1.00 30.60           C  
ANISOU  437  CA  ASN A  62     4212   3664   3750    747    124   -924       C  
ATOM    438  C   ASN A  62       4.048  42.356  60.756  1.00 26.97           C  
ANISOU  438  C   ASN A  62     3730   3265   3254    667     95   -882       C  
ATOM    439  O   ASN A  62       4.782  41.940  61.656  1.00 22.43           O  
ANISOU  439  O   ASN A  62     3176   2720   2627    605     88   -910       O  
ATOM    440  CB  ASN A  62       2.181  43.498  61.948  1.00 41.55           C  
ANISOU  440  CB  ASN A  62     5553   5152   5081    791    177   -957       C  
ATOM    441  CG  ASN A  62       1.527  44.817  62.324  1.00 51.90           C  
ANISOU  441  CG  ASN A  62     6892   6404   6425    860    212  -1002       C  
ATOM    442  OD1 ASN A  62       2.182  45.866  62.361  1.00 51.71           O  
ANISOU  442  OD1 ASN A  62     6940   6265   6441    850    200  -1034       O  
ATOM    443  ND2 ASN A  62       0.227  44.773  62.602  1.00 57.97           N  
ANISOU  443  ND2 ASN A  62     7600   7250   7175    930    258  -1004       N  
ATOM    444  N   GLU A  63       3.849  41.708  59.606  1.00 21.90           N  
ANISOU  444  N   GLU A  63     3039   2640   2641    655     79   -798       N  
ATOM    445  CA  GLU A  63       4.590  40.494  59.255  1.00 21.74           C  
ANISOU  445  CA  GLU A  63     2998   2659   2602    568     52   -736       C  
ATOM    446  C   GLU A  63       5.156  40.644  57.847  1.00 20.55           C  
ANISOU  446  C   GLU A  63     2857   2437   2514    549     16   -673       C  
ATOM    447  O   GLU A  63       4.793  39.922  56.920  1.00 19.40           O  
ANISOU  447  O   GLU A  63     2665   2329   2378    540     10   -610       O  
ATOM    448  CB  GLU A  63       3.696  39.250  59.374  1.00 18.99           C  
ANISOU  448  CB  GLU A  63     2573   2432   2209    560     75   -698       C  
ATOM    449  CG  GLU A  63       3.248  38.995  60.820  1.00 20.28           C  
ANISOU  449  CG  GLU A  63     2723   2681   2302    566    110   -751       C  
ATOM    450  CD  GLU A  63       2.558  37.653  61.015  1.00 21.93           C  
ANISOU  450  CD  GLU A  63     2861   3008   2464    537    126   -704       C  
ATOM    451  OE1 GLU A  63       2.398  36.912  60.026  1.00 19.97           O  
ANISOU  451  OE1 GLU A  63     2578   2771   2238    512    110   -637       O  
ATOM    452  OE2 GLU A  63       2.185  37.336  62.169  1.00 27.64           O  
ANISOU  452  OE2 GLU A  63     3565   3813   3124    534    154   -736       O  
ATOM    453  N   ASN A  64       6.061  41.606  57.712  1.00 23.44           N  
ANISOU  453  N   ASN A  64     3287   2701   2917    537     -9   -694       N  
ATOM    454  CA  ASN A  64       6.592  41.995  56.425  1.00 18.10           C  
ANISOU  454  CA  ASN A  64     2626   1952   2301    526    -42   -638       C  
ATOM    455  C   ASN A  64       7.785  41.137  56.064  1.00 12.75           C  
ANISOU  455  C   ASN A  64     1947   1285   1610    439    -72   -591       C  
ATOM    456  O   ASN A  64       8.935  41.539  56.265  1.00 17.02           O  
ANISOU  456  O   ASN A  64     2535   1771   2159    391    -98   -602       O  
ATOM    457  CB  ASN A  64       6.978  43.467  56.436  1.00 19.26           C  
ANISOU  457  CB  ASN A  64     2841   1980   2497    552    -55   -677       C  
ATOM    458  CG  ASN A  64       7.396  43.955  55.066  1.00 26.78           C  
ANISOU  458  CG  ASN A  64     3802   2860   3512    545    -88   -611       C  
ATOM    459  OD1 ASN A  64       7.180  43.272  54.064  1.00 26.92           O  
ANISOU  459  OD1 ASN A  64     3772   2922   3536    537    -94   -542       O  
ATOM    460  ND2 ASN A  64       7.985  45.141  55.013  1.00 30.26           N  
ANISOU  460  ND2 ASN A  64     4308   3191   3999    545   -109   -631       N  
ATOM    461  N   ILE A  65       7.498  39.931  55.583  1.00 15.41           N  
ANISOU  461  N   ILE A  65     2231   1697   1926    419    -67   -541       N  
ATOM    462  CA  ILE A  65       8.522  38.954  55.227  1.00 11.36           C  
ANISOU  462  CA  ILE A  65     1712   1203   1401    347    -89   -495       C  
ATOM    463  C   ILE A  65       8.232  38.431  53.838  1.00 10.90           C  
ANISOU  463  C   ILE A  65     1617   1160   1365    348    -96   -431       C  
ATOM    464  O   ILE A  65       7.081  38.354  53.427  1.00 15.19           O  
ANISOU  464  O   ILE A  65     2123   1737   1912    391    -81   -419       O  
ATOM    465  CB  ILE A  65       8.574  37.761  56.225  1.00 11.12           C  
ANISOU  465  CB  ILE A  65     1659   1254   1311    310    -74   -504       C  
ATOM    466  CG1 ILE A  65       7.233  37.024  56.250  1.00 11.08           C  
ANISOU  466  CG1 ILE A  65     1599   1328   1282    340    -46   -495       C  
ATOM    467  CG2 ILE A  65       8.980  38.234  57.628  1.00 11.94           C  
ANISOU  467  CG2 ILE A  65     1799   1356   1382    299    -70   -567       C  
ATOM    468  CD1 ILE A  65       7.230  35.783  57.145  1.00 13.45           C  
ANISOU  468  CD1 ILE A  65     1875   1707   1528    298    -34   -491       C  
ATOM    469  N   SER A  66       9.285  38.095  53.110  1.00 15.35           N  
ANISOU  469  N   SER A  66     2190   1702   1941    301   -120   -389       N  
ATOM    470  CA  SER A  66       9.149  37.583  51.754  1.00 13.56           C  
ANISOU  470  CA  SER A  66     1934   1491   1728    295   -128   -332       C  
ATOM    471  C   SER A  66       8.707  36.128  51.805  1.00 17.09           C  
ANISOU  471  C   SER A  66     2342   2014   2136    273   -113   -317       C  
ATOM    472  O   SER A  66       8.816  35.487  52.857  1.00 12.59           O  
ANISOU  472  O   SER A  66     1772   1479   1534    252   -102   -340       O  
ATOM    473  CB  SER A  66      10.473  37.698  51.008  1.00 16.39           C  
ANISOU  473  CB  SER A  66     2314   1808   2106    253   -154   -296       C  
ATOM    474  OG  SER A  66      11.401  36.781  51.567  1.00 12.04           O  
ANISOU  474  OG  SER A  66     1765   1283   1525    204   -156   -296       O  
ATOM    475  N   MET A  67       8.214  35.617  50.676  1.00 15.91           N  
ANISOU  475  N   MET A  67     2162   1892   1991    274   -115   -278       N  
ATOM    476  CA  MET A  67       7.826  34.211  50.549  1.00 14.12           C  
ANISOU  476  CA  MET A  67     1906   1727   1733    244   -105   -262       C  
ATOM    477  C   MET A  67       8.976  33.292  50.909  1.00 15.25           C  
ANISOU  477  C   MET A  67     2068   1868   1860    196   -109   -257       C  
ATOM    478  O   MET A  67       8.775  32.238  51.522  1.00 12.33           O  
ANISOU  478  O   MET A  67     1686   1538   1462    173    -97   -259       O  
ATOM    479  CB  MET A  67       7.350  33.892  49.125  1.00 12.82           C  
ANISOU  479  CB  MET A  67     1715   1582   1574    242   -113   -223       C  
ATOM    480  CG  MET A  67       5.989  34.492  48.757  1.00 14.84           C  
ANISOU  480  CG  MET A  67     1935   1865   1838    289   -108   -216       C  
ATOM    481  SD  MET A  67       5.426  34.039  47.068  1.00 13.11           S  
ANISOU  481  SD  MET A  67     1681   1684   1614    275   -123   -166       S  
ATOM    482  CE  MET A  67       6.336  35.233  46.061  1.00 11.35           C  
ANISOU  482  CE  MET A  67     1487   1395   1432    290   -146   -137       C  
ATOM    483  N   SER A  68      10.190  33.681  50.520  1.00  9.43           N  
ANISOU  483  N   SER A  68     1356   1085   1141    180   -126   -243       N  
ATOM    484  CA  SER A  68      11.343  32.841  50.807  1.00  8.21           C  
ANISOU  484  CA  SER A  68     1214    932    975    140   -129   -231       C  
ATOM    485  C   SER A  68      11.710  32.874  52.314  1.00 12.29           C  
ANISOU  485  C   SER A  68     1743   1455   1471    129   -125   -261       C  
ATOM    486  O   SER A  68      12.532  32.086  52.781  1.00 15.24           O  
ANISOU  486  O   SER A  68     2120   1842   1830     99   -127   -248       O  
ATOM    487  CB  SER A  68      12.532  33.293  49.973  1.00  8.11           C  
ANISOU  487  CB  SER A  68     1216    881    984    127   -147   -204       C  
ATOM    488  OG  SER A  68      12.845  34.636  50.292  1.00 12.66           O  
ANISOU  488  OG  SER A  68     1815   1413   1582    136   -161   -219       O  
ATOM    489  N   GLN A  69      11.097  33.777  53.069  1.00 14.74           N  
ANISOU  489  N   GLN A  69     2061   1760   1779    155   -120   -299       N  
ATOM    490  CA  GLN A  69      11.309  33.818  54.526  1.00 17.32           C  
ANISOU  490  CA  GLN A  69     2400   2105   2077    143   -115   -333       C  
ATOM    491  C   GLN A  69      10.111  33.254  55.298  1.00 13.86           C  
ANISOU  491  C   GLN A  69     1935   1727   1605    157    -91   -351       C  
ATOM    492  O   GLN A  69      10.117  33.217  56.528  1.00 12.78           O  
ANISOU  492  O   GLN A  69     1801   1620   1434    149    -83   -379       O  
ATOM    493  CB  GLN A  69      11.562  35.249  54.986  1.00  9.45           C  
ANISOU  493  CB  GLN A  69     1436   1060   1093    158   -125   -373       C  
ATOM    494  CG  GLN A  69      12.789  35.898  54.382  1.00  9.40           C  
ANISOU  494  CG  GLN A  69     1457    997   1118    134   -153   -352       C  
ATOM    495  CD  GLN A  69      12.811  37.380  54.622  1.00 13.58           C  
ANISOU  495  CD  GLN A  69     2024   1464   1671    151   -164   -390       C  
ATOM    496  OE1 GLN A  69      11.763  38.011  54.774  1.00 20.19           O  
ANISOU  496  OE1 GLN A  69     2865   2290   2517    199   -149   -424       O  
ATOM    497  NE2 GLN A  69      14.011  37.952  54.695  1.00 14.13           N  
ANISOU  497  NE2 GLN A  69     2122   1494   1752    112   -190   -385       N  
ATOM    498  N   ASN A  70       9.082  32.831  54.569  1.00 13.28           N  
ANISOU  498  N   ASN A  70     1831   1678   1536    175    -80   -334       N  
ATOM    499  CA  ASN A  70       7.797  32.470  55.169  1.00  9.33           C  
ANISOU  499  CA  ASN A  70     1298   1240   1007    191    -57   -347       C  
ATOM    500  C   ASN A  70       7.514  30.964  55.037  1.00 11.07           C  
ANISOU  500  C   ASN A  70     1492   1506   1207    153    -51   -312       C  
ATOM    501  O   ASN A  70       7.321  30.451  53.933  1.00 17.20           O  
ANISOU  501  O   ASN A  70     2258   2277   1999    143    -58   -282       O  
ATOM    502  CB  ASN A  70       6.687  33.302  54.514  1.00 14.31           C  
ANISOU  502  CB  ASN A  70     1909   1870   1659    243    -49   -355       C  
ATOM    503  CG  ASN A  70       5.333  33.128  55.179  1.00 13.32           C  
ANISOU  503  CG  ASN A  70     1742   1816   1503    268    -23   -370       C  
ATOM    504  OD1 ASN A  70       5.053  32.112  55.819  1.00 11.98           O  
ANISOU  504  OD1 ASN A  70     1551   1704   1298    236    -12   -361       O  
ATOM    505  ND2 ASN A  70       4.474  34.118  55.008  1.00 10.52           N  
ANISOU  505  ND2 ASN A  70     1373   1459   1164    327    -12   -389       N  
ATOM    506  N   PRO A  71       7.476  30.261  56.175  1.00 11.19           N  
ANISOU  506  N   PRO A  71     1500   1566   1186    128    -41   -314       N  
ATOM    507  CA  PRO A  71       7.320  28.807  56.307  1.00  9.01           C  
ANISOU  507  CA  PRO A  71     1207   1325    891     86    -37   -278       C  
ATOM    508  C   PRO A  71       6.016  28.272  55.724  1.00 11.75           C  
ANISOU  508  C   PRO A  71     1517   1713   1234     84    -28   -261       C  
ATOM    509  O   PRO A  71       5.947  27.090  55.440  1.00 18.44           O  
ANISOU  509  O   PRO A  71     2360   2569   2079     44    -31   -230       O  
ATOM    510  CB  PRO A  71       7.344  28.578  57.838  1.00 14.78           C  
ANISOU  510  CB  PRO A  71     1932   2105   1578     71    -26   -289       C  
ATOM    511  CG  PRO A  71       7.896  29.785  58.419  1.00 17.59           C  
ANISOU  511  CG  PRO A  71     2313   2440   1932     96    -29   -331       C  
ATOM    512  CD  PRO A  71       7.631  30.925  57.481  1.00 13.90           C  
ANISOU  512  CD  PRO A  71     1854   1926   1501    139    -33   -353       C  
ATOM    513  N   SER A  72       5.006  29.122  55.578  1.00  9.43           N  
ANISOU  513  N   SER A  72     1197   1445    941    125    -17   -282       N  
ATOM    514  CA  SER A  72       3.780  28.760  54.897  1.00  9.59           C  
ANISOU  514  CA  SER A  72     1176   1510    958    124    -13   -262       C  
ATOM    515  C   SER A  72       3.993  28.690  53.378  1.00 15.40           C  
ANISOU  515  C   SER A  72     1921   2204   1725    118    -32   -241       C  
ATOM    516  O   SER A  72       3.178  28.104  52.676  1.00 17.16           O  
ANISOU  516  O   SER A  72     2116   2461   1943     97    -36   -219       O  
ATOM    517  CB  SER A  72       2.669  29.774  55.212  1.00 10.11           C  
ANISOU  517  CB  SER A  72     1205   1621   1016    181      6   -286       C  
ATOM    518  OG  SER A  72       2.362  29.819  56.599  1.00 10.49           O  
ANISOU  518  OG  SER A  72     1240   1721   1026    188     28   -309       O  
ATOM    519  N   TYR A  73       5.065  29.315  52.879  1.00  9.01           N  
ANISOU  519  N   TYR A  73     1150   1329    945    132    -46   -248       N  
ATOM    520  CA  TYR A  73       5.336  29.383  51.437  1.00 17.29           C  
ANISOU  520  CA  TYR A  73     2207   2343   2018    129    -63   -229       C  
ATOM    521  C   TYR A  73       6.581  28.567  51.050  1.00  9.98           C  
ANISOU  521  C   TYR A  73     1316   1375   1100     92    -73   -215       C  
ATOM    522  O   TYR A  73       6.827  28.285  49.880  1.00  8.22           O  
ANISOU  522  O   TYR A  73     1101   1134    887     80    -83   -199       O  
ATOM    523  CB  TYR A  73       5.525  30.840  50.976  1.00 10.08           C  
ANISOU  523  CB  TYR A  73     1303   1391   1134    178    -70   -239       C  
ATOM    524  CG  TYR A  73       4.251  31.648  50.863  1.00  9.59           C  
ANISOU  524  CG  TYR A  73     1204   1364   1076    226    -63   -243       C  
ATOM    525  CD1 TYR A  73       3.674  32.245  51.981  1.00 10.97           C  
ANISOU  525  CD1 TYR A  73     1366   1562   1240    264    -43   -273       C  
ATOM    526  CD2 TYR A  73       3.634  31.843  49.623  1.00  9.46           C  
ANISOU  526  CD2 TYR A  73     1162   1362   1071    237    -74   -215       C  
ATOM    527  CE1 TYR A  73       2.507  32.998  51.878  1.00 11.83           C  
ANISOU  527  CE1 TYR A  73     1437   1704   1354    318    -32   -276       C  
ATOM    528  CE2 TYR A  73       2.471  32.592  49.510  1.00  9.95           C  
ANISOU  528  CE2 TYR A  73     1184   1460   1139    286    -67   -211       C  
ATOM    529  CZ  TYR A  73       1.909  33.168  50.637  1.00 11.13           C  
ANISOU  529  CZ  TYR A  73     1319   1628   1281    331    -45   -241       C  
ATOM    530  OH  TYR A  73       0.742  33.904  50.529  1.00 10.95           O  
ANISOU  530  OH  TYR A  73     1251   1643   1266    390    -35   -235       O  
ATOM    531  N   SER A  74       7.360  28.168  52.042  1.00 12.05           N  
ANISOU  531  N   SER A  74     1599   1627   1354     76    -69   -219       N  
ATOM    532  CA  SER A  74       8.635  27.539  51.720  1.00  9.53           C  
ANISOU  532  CA  SER A  74     1309   1266   1046     54    -76   -203       C  
ATOM    533  C   SER A  74       9.210  26.725  52.837  1.00 17.22           C  
ANISOU  533  C   SER A  74     2293   2245   2006     30    -71   -195       C  
ATOM    534  O   SER A  74       8.897  26.915  54.022  1.00 18.89           O  
ANISOU  534  O   SER A  74     2494   2488   2195     31    -64   -206       O  
ATOM    535  CB  SER A  74       9.651  28.605  51.317  1.00  8.48           C  
ANISOU  535  CB  SER A  74     1196   1089    936     76    -88   -207       C  
ATOM    536  OG  SER A  74       9.691  29.597  52.316  1.00 11.96           O  
ANISOU  536  OG  SER A  74     1640   1529   1374     96    -88   -231       O  
ATOM    537  N   TRP A  75      10.109  25.847  52.422  1.00 15.32           N  
ANISOU  537  N   TRP A  75     2071   1974   1775     12    -74   -174       N  
ATOM    538  CA  TRP A  75      11.020  25.176  53.310  1.00 13.03           C  
ANISOU  538  CA  TRP A  75     1793   1677   1480     -4    -73   -156       C  
ATOM    539  C   TRP A  75      12.087  26.178  53.723  1.00 15.21           C  
ANISOU  539  C   TRP A  75     2078   1939   1761     12    -83   -163       C  
ATOM    540  O   TRP A  75      12.495  26.986  52.900  1.00 12.40           O  
ANISOU  540  O   TRP A  75     1729   1557   1424     29    -91   -169       O  
ATOM    541  CB  TRP A  75      11.653  23.981  52.585  1.00 12.67           C  
ANISOU  541  CB  TRP A  75     1766   1597   1450    -17    -71   -132       C  
ATOM    542  CG  TRP A  75      10.661  22.934  52.171  1.00  9.56           C  
ANISOU  542  CG  TRP A  75     1372   1209   1053    -43    -65   -128       C  
ATOM    543  CD1 TRP A  75       9.947  22.881  50.997  1.00  8.36           C  
ANISOU  543  CD1 TRP A  75     1219   1056    902    -49    -66   -140       C  
ATOM    544  CD2 TRP A  75      10.276  21.776  52.930  1.00 14.97           C  
ANISOU  544  CD2 TRP A  75     2058   1903   1729    -75    -60   -107       C  
ATOM    545  NE1 TRP A  75       9.139  21.758  50.993  1.00 11.14           N  
ANISOU  545  NE1 TRP A  75     1573   1415   1247    -86    -63   -133       N  
ATOM    546  CE2 TRP A  75       9.320  21.070  52.160  1.00 12.43           C  
ANISOU  546  CE2 TRP A  75     1737   1579   1404   -102    -59   -110       C  
ATOM    547  CE3 TRP A  75      10.639  21.279  54.190  1.00 17.98           C  
ANISOU  547  CE3 TRP A  75     2438   2295   2100    -87    -58    -81       C  
ATOM    548  CZ2 TRP A  75       8.726  19.879  52.612  1.00 11.82           C  
ANISOU  548  CZ2 TRP A  75     1664   1505   1321   -144    -56    -89       C  
ATOM    549  CZ3 TRP A  75      10.058  20.094  54.631  1.00 17.76           C  
ANISOU  549  CZ3 TRP A  75     2411   2271   2066   -123    -54    -55       C  
ATOM    550  CH2 TRP A  75       9.110  19.410  53.844  1.00 18.44           C  
ANISOU  550  CH2 TRP A  75     2503   2349   2156   -153    -54    -60       C  
ATOM    551  N   GLN A  76      12.522  26.140  54.989  1.00 11.66           N  
ANISOU  551  N   GLN A  76     1628   1510   1293      2    -85   -158       N  
ATOM    552  CA  GLN A  76      13.526  27.065  55.511  1.00 12.11           C  
ANISOU  552  CA  GLN A  76     1694   1560   1349      6    -98   -167       C  
ATOM    553  C   GLN A  76      14.846  26.339  55.734  1.00 10.60           C  
ANISOU  553  C   GLN A  76     1506   1361   1162     -8   -105   -128       C  
ATOM    554  O   GLN A  76      15.136  25.835  56.836  1.00 10.72           O  
ANISOU  554  O   GLN A  76     1514   1405   1154    -25   -107   -110       O  
ATOM    555  CB  GLN A  76      13.064  27.710  56.826  1.00 10.94           C  
ANISOU  555  CB  GLN A  76     1540   1450   1167      3    -97   -196       C  
ATOM    556  CG  GLN A  76      11.871  28.625  56.659  1.00  9.15           C  
ANISOU  556  CG  GLN A  76     1308   1229    939     29    -88   -237       C  
ATOM    557  CD  GLN A  76      12.196  29.842  55.828  1.00 11.77           C  
ANISOU  557  CD  GLN A  76     1656   1514   1301     51    -99   -255       C  
ATOM    558  OE1 GLN A  76      12.984  30.687  56.238  1.00 15.50           O  
ANISOU  558  OE1 GLN A  76     2147   1966   1774     47   -113   -271       O  
ATOM    559  NE2 GLN A  76      11.603  29.926  54.637  1.00 14.28           N  
ANISOU  559  NE2 GLN A  76     1969   1815   1644     70    -97   -249       N  
ATOM    560  N   GLY A  77      15.636  26.276  54.675  1.00  9.87           N  
ANISOU  560  N   GLY A  77     1419   1235   1095      1   -108   -111       N  
ATOM    561  CA  GLY A  77      16.896  25.570  54.685  1.00  7.71           C  
ANISOU  561  CA  GLY A  77     1143    955    831     -1   -111    -71       C  
ATOM    562  C   GLY A  77      17.995  26.348  55.361  1.00 16.91           C  
ANISOU  562  C   GLY A  77     2302   2134   1987    -12   -130    -62       C  
ATOM    563  O   GLY A  77      18.823  26.956  54.690  1.00 12.94           O  
ANISOU  563  O   GLY A  77     1798   1616   1501     -9   -139    -55       O  
ATOM    564  N   ALA A  78      18.010  26.313  56.693  1.00 16.56           N  
ANISOU  564  N   ALA A  78     2252   2126   1914    -31   -137    -61       N  
ATOM    565  CA  ALA A  78      19.060  26.964  57.479  1.00 13.84           C  
ANISOU  565  CA  ALA A  78     1900   1805   1552    -52   -159    -52       C  
ATOM    566  C   ALA A  78      20.362  26.176  57.424  1.00 16.43           C  
ANISOU  566  C   ALA A  78     2210   2143   1891    -51   -164      7       C  
ATOM    567  O   ALA A  78      20.427  25.061  57.926  1.00 20.24           O  
ANISOU  567  O   ALA A  78     2682   2640   2367    -49   -157     43       O  
ATOM    568  CB  ALA A  78      18.607  27.132  58.919  1.00 11.39           C  
ANISOU  568  CB  ALA A  78     1589   1541   1199    -74   -164    -71       C  
ATOM    569  N   GLN A  79      21.409  26.745  56.829  1.00 14.16           N  
ANISOU  569  N   GLN A  79     1914   1846   1619    -52   -176     21       N  
ATOM    570  CA  GLN A  79      22.664  26.003  56.729  1.00 10.79           C  
ANISOU  570  CA  GLN A  79     1461   1435   1202    -44   -178     81       C  
ATOM    571  C   GLN A  79      23.536  26.124  57.972  1.00 11.22           C  
ANISOU  571  C   GLN A  79     1494   1543   1227    -74   -202    111       C  
ATOM    572  O   GLN A  79      23.278  26.915  58.879  1.00  9.75           O  
ANISOU  572  O   GLN A  79     1315   1380   1009   -108   -221     80       O  
ATOM    573  CB  GLN A  79      23.464  26.435  55.493  1.00 11.11           C  
ANISOU  573  CB  GLN A  79     1493   1457   1269    -31   -177     93       C  
ATOM    574  CG  GLN A  79      24.012  27.846  55.534  1.00  9.09           C  
ANISOU  574  CG  GLN A  79     1237   1210   1008    -64   -205     81       C  
ATOM    575  CD  GLN A  79      25.177  28.025  54.575  1.00 15.35           C  
ANISOU  575  CD  GLN A  79     2005   2009   1819    -58   -207    120       C  
ATOM    576  OE1 GLN A  79      24.980  28.293  53.376  1.00 12.68           O  
ANISOU  576  OE1 GLN A  79     1674   1642   1501    -41   -195    110       O  
ATOM    577  NE2 GLN A  79      26.397  27.863  55.087  1.00 14.46           N  
ANISOU  577  NE2 GLN A  79     1856   1942   1697    -73   -222    170       N  
ATOM    578  N   GLU A  80      24.559  25.283  58.013  1.00 11.37           N  
ANISOU  578  N   GLU A  80     1482   1583   1254    -60   -202    173       N  
ATOM    579  CA  GLU A  80      25.515  25.287  59.098  1.00  9.56           C  
ANISOU  579  CA  GLU A  80     1221   1414    996    -87   -227    217       C  
ATOM    580  C   GLU A  80      26.409  26.516  58.966  1.00 11.68           C  
ANISOU  580  C   GLU A  80     1478   1703   1257   -122   -255    212       C  
ATOM    581  O   GLU A  80      26.525  27.071  57.867  1.00  9.52           O  
ANISOU  581  O   GLU A  80     1211   1395   1010   -112   -249    197       O  
ATOM    582  CB  GLU A  80      26.336  23.996  59.073  1.00 13.09           C  
ANISOU  582  CB  GLU A  80     1637   1875   1462    -51   -215    291       C  
ATOM    583  CG  GLU A  80      25.490  22.738  59.177  1.00 14.72           C  
ANISOU  583  CG  GLU A  80     1861   2049   1681    -22   -190    300       C  
ATOM    584  CD  GLU A  80      24.936  22.493  60.598  1.00 16.36           C  
ANISOU  584  CD  GLU A  80     2069   2298   1849    -54   -203    308       C  
ATOM    585  OE1 GLU A  80      25.021  23.390  61.456  1.00 13.65           O  
ANISOU  585  OE1 GLU A  80     1719   2004   1463    -98   -228    288       O  
ATOM    586  OE2 GLU A  80      24.410  21.396  60.854  1.00 14.16           O  
ANISOU  586  OE2 GLU A  80     1798   2003   1579    -38   -187    333       O  
ATOM    587  N   PRO A  81      27.024  26.944  60.087  1.00 11.63           N  
ANISOU  587  N   PRO A  81     1453   1755   1213   -168   -287    227       N  
ATOM    588  CA  PRO A  81      27.926  28.099  60.118  1.00 14.15           C  
ANISOU  588  CA  PRO A  81     1760   2097   1520   -216   -320    226       C  
ATOM    589  C   PRO A  81      28.891  28.116  58.938  1.00 13.68           C  
ANISOU  589  C   PRO A  81     1671   2031   1496   -196   -315    269       C  
ATOM    590  O   PRO A  81      29.566  27.128  58.652  1.00 10.50           O  
ANISOU  590  O   PRO A  81     1231   1650   1109   -158   -300    331       O  
ATOM    591  CB  PRO A  81      28.678  27.914  61.437  1.00 16.04           C  
ANISOU  591  CB  PRO A  81     1965   2415   1712   -256   -350    267       C  
ATOM    592  CG  PRO A  81      27.669  27.241  62.330  1.00 18.28           C  
ANISOU  592  CG  PRO A  81     2267   2707   1970   -246   -336    250       C  
ATOM    593  CD  PRO A  81      26.874  26.331  61.425  1.00 18.92           C  
ANISOU  593  CD  PRO A  81     2364   2728   2095   -184   -295    248       C  
ATOM    594  N   ASN A  82      28.935  29.252  58.255  1.00 17.62           N  
ANISOU  594  N   ASN A  82     2189   2499   2008   -221   -326    237       N  
ATOM    595  CA  ASN A  82      29.791  29.392  57.096  1.00 11.75           C  
ANISOU  595  CA  ASN A  82     1417   1756   1293   -208   -321    277       C  
ATOM    596  C   ASN A  82      31.160  29.843  57.545  1.00 10.93           C  
ANISOU  596  C   ASN A  82     1266   1719   1169   -259   -357    329       C  
ATOM    597  O   ASN A  82      31.354  30.997  57.938  1.00 14.16           O  
ANISOU  597  O   ASN A  82     1690   2130   1561   -324   -393    304       O  
ATOM    598  CB  ASN A  82      29.180  30.371  56.092  1.00 13.66           C  
ANISOU  598  CB  ASN A  82     1697   1935   1558   -212   -317    229       C  
ATOM    599  CG  ASN A  82      30.017  30.520  54.829  1.00 13.64           C  
ANISOU  599  CG  ASN A  82     1663   1940   1580   -201   -310    272       C  
ATOM    600  OD1 ASN A  82      31.165  30.046  54.747  1.00 13.77           O  
ANISOU  600  OD1 ASN A  82     1626   2012   1594   -195   -310    336       O  
ATOM    601  ND2 ASN A  82      29.458  31.197  53.848  1.00 12.38           N  
ANISOU  601  ND2 ASN A  82     1533   1729   1442   -196   -302    242       N  
ATOM    602  N   THR A  83      32.117  28.930  57.469  1.00 11.16           N  
ANISOU  602  N   THR A  83     1238   1802   1201   -229   -348    402       N  
ATOM    603  CA  THR A  83      33.475  29.224  57.909  1.00 11.78           C  
ANISOU  603  CA  THR A  83     1257   1960   1258   -274   -382    466       C  
ATOM    604  C   THR A  83      34.141  30.271  57.013  1.00 11.94           C  
ANISOU  604  C   THR A  83     1265   1982   1292   -312   -398    476       C  
ATOM    605  O   THR A  83      35.193  30.832  57.372  1.00 16.85           O  
ANISOU  605  O   THR A  83     1844   2666   1893   -372   -435    519       O  
ATOM    606  CB  THR A  83      34.339  27.964  57.936  1.00 14.42           C  
ANISOU  606  CB  THR A  83     1528   2353   1600   -219   -363    548       C  
ATOM    607  OG1 THR A  83      34.398  27.415  56.614  1.00 11.96           O  
ANISOU  607  OG1 THR A  83     1208   2010   1327   -149   -320    561       O  
ATOM    608  CG2 THR A  83      33.765  26.904  58.918  1.00 12.02           C  
ANISOU  608  CG2 THR A  83     1234   2049   1283   -188   -353    552       C  
ATOM    609  N   GLY A  84      33.557  30.495  55.837  1.00 14.79           N  
ANISOU  609  N   GLY A  84     1657   2280   1685   -281   -371    444       N  
ATOM    610  CA  GLY A  84      34.062  31.477  54.891  1.00 11.66           C  
ANISOU  610  CA  GLY A  84     1251   1878   1302   -315   -382    456       C  
ATOM    611  C   GLY A  84      33.408  32.838  55.008  1.00 19.63           C  
ANISOU  611  C   GLY A  84     2321   2825   2312   -376   -412    394       C  
ATOM    612  O   GLY A  84      33.736  33.763  54.251  1.00 20.08           O  
ANISOU  612  O   GLY A  84     2379   2867   2384   -412   -426    404       O  
ATOM    613  N   ALA A  85      32.473  32.961  55.953  1.00 13.70           N  
ANISOU  613  N   ALA A  85     1620   2038   1546   -386   -420    331       N  
ATOM    614  CA  ALA A  85      31.769  34.222  56.183  1.00 14.52           C  
ANISOU  614  CA  ALA A  85     1788   2077   1651   -433   -444    263       C  
ATOM    615  C   ALA A  85      31.388  34.405  57.651  1.00 13.28           C  
ANISOU  615  C   ALA A  85     1661   1929   1456   -470   -467    214       C  
ATOM    616  O   ALA A  85      30.204  34.562  57.969  1.00 13.86           O  
ANISOU  616  O   ALA A  85     1788   1951   1529   -449   -454    145       O  
ATOM    617  CB  ALA A  85      30.528  34.311  55.309  1.00 17.92           C  
ANISOU  617  CB  ALA A  85     2266   2429   2114   -381   -412    214       C  
ATOM    618  N   TYR A  86      32.398  34.366  58.525  1.00 12.93           N  
ANISOU  618  N   TYR A  86     1577   1959   1376   -523   -500    253       N  
ATOM    619  CA  TYR A  86      32.275  34.721  59.944  1.00 15.32           C  
ANISOU  619  CA  TYR A  86     1904   2285   1630   -578   -531    211       C  
ATOM    620  C   TYR A  86      31.242  33.883  60.701  1.00 18.50           C  
ANISOU  620  C   TYR A  86     2327   2690   2012   -530   -504    174       C  
ATOM    621  O   TYR A  86      30.713  34.328  61.722  1.00 17.00           O  
ANISOU  621  O   TYR A  86     2177   2498   1785   -562   -518    113       O  
ATOM    622  CB  TYR A  86      31.945  36.220  60.101  1.00 13.19           C  
ANISOU  622  CB  TYR A  86     1700   1948   1361   -642   -562    139       C  
ATOM    623  CG  TYR A  86      32.885  37.110  59.301  1.00 20.49           C  
ANISOU  623  CG  TYR A  86     2611   2862   2312   -697   -591    178       C  
ATOM    624  CD1 TYR A  86      34.224  37.253  59.673  1.00 14.21           C  
ANISOU  624  CD1 TYR A  86     1762   2146   1489   -770   -632    239       C  
ATOM    625  CD2 TYR A  86      32.442  37.775  58.153  1.00 13.32           C  
ANISOU  625  CD2 TYR A  86     1736   1871   1453   -678   -578    163       C  
ATOM    626  CE1 TYR A  86      35.100  38.054  58.930  1.00 16.97           C  
ANISOU  626  CE1 TYR A  86     2093   2494   1861   -827   -659    283       C  
ATOM    627  CE2 TYR A  86      33.315  38.571  57.396  1.00 18.35           C  
ANISOU  627  CE2 TYR A  86     2357   2503   2114   -733   -605    208       C  
ATOM    628  CZ  TYR A  86      34.641  38.701  57.791  1.00 17.99           C  
ANISOU  628  CZ  TYR A  86     2258   2538   2041   -808   -645    268       C  
ATOM    629  OH  TYR A  86      35.494  39.479  57.048  1.00 17.89           O  
ANISOU  629  OH  TYR A  86     2225   2525   2048   -868   -672    318       O  
ATOM    630  N   GLY A  87      30.983  32.669  60.220  1.00 19.19           N  
ANISOU  630  N   GLY A  87     2388   2783   2120   -455   -464    210       N  
ATOM    631  CA  GLY A  87      30.084  31.750  60.909  1.00 14.70           C  
ANISOU  631  CA  GLY A  87     1830   2221   1533   -413   -439    191       C  
ATOM    632  C   GLY A  87      28.620  32.001  60.606  1.00 15.39           C  
ANISOU  632  C   GLY A  87     1977   2233   1638   -378   -411    115       C  
ATOM    633  O   GLY A  87      27.748  31.373  61.198  1.00 13.94           O  
ANISOU  633  O   GLY A  87     1806   2055   1437   -351   -391     92       O  
ATOM    634  N   ASN A  88      28.345  32.911  59.671  1.00 17.31           N  
ANISOU  634  N   ASN A  88     2251   2410   1916   -378   -409     82       N  
ATOM    635  CA  ASN A  88      26.972  33.208  59.254  1.00 12.97           C  
ANISOU  635  CA  ASN A  88     1750   1790   1387   -339   -383     17       C  
ATOM    636  C   ASN A  88      26.193  31.979  58.821  1.00 13.24           C  
ANISOU  636  C   ASN A  88     1775   1820   1437   -272   -342     30       C  
ATOM    637  O   ASN A  88      26.769  31.015  58.320  1.00 13.96           O  
ANISOU  637  O   ASN A  88     1829   1934   1543   -245   -328     89       O  
ATOM    638  CB  ASN A  88      26.958  34.227  58.108  1.00 10.68           C  
ANISOU  638  CB  ASN A  88     1483   1435   1139   -342   -388      4       C  
ATOM    639  CG  ASN A  88      27.178  35.644  58.591  1.00 19.95           C  
ANISOU  639  CG  ASN A  88     2696   2581   2304   -405   -425    -39       C  
ATOM    640  OD1 ASN A  88      27.331  35.879  59.791  1.00 15.94           O  
ANISOU  640  OD1 ASN A  88     2199   2104   1754   -448   -447    -67       O  
ATOM    641  ND2 ASN A  88      27.193  36.601  57.663  1.00 19.73           N  
ANISOU  641  ND2 ASN A  88     2691   2491   2315   -414   -434    -44       N  
ATOM    642  N   ARG A  89      24.878  32.024  59.008  1.00  9.99           N  
ANISOU  642  N   ARG A  89     1397   1376   1022   -247   -322    -26       N  
ATOM    643  CA  ARG A  89      24.043  30.880  58.691  1.00  9.56           C  
ANISOU  643  CA  ARG A  89     1337   1317    978   -195   -287    -18       C  
ATOM    644  C   ARG A  89      22.888  31.314  57.822  1.00 11.43           C  
ANISOU  644  C   ARG A  89     1604   1496   1243   -163   -267    -63       C  
ATOM    645  O   ARG A  89      21.762  31.489  58.311  1.00 11.06           O  
ANISOU  645  O   ARG A  89     1580   1441   1183   -151   -255   -112       O  
ATOM    646  CB  ARG A  89      23.523  30.210  59.969  1.00 13.24           C  
ANISOU  646  CB  ARG A  89     1799   1828   1402   -199   -281    -26       C  
ATOM    647  CG  ARG A  89      24.606  29.621  60.846  1.00 14.28           C  
ANISOU  647  CG  ARG A  89     1895   2026   1504   -227   -301     30       C  
ATOM    648  CD  ARG A  89      23.990  28.839  62.022  1.00 15.86           C  
ANISOU  648  CD  ARG A  89     2091   2273   1663   -228   -292     31       C  
ATOM    649  NE  ARG A  89      23.242  27.666  61.570  1.00 15.91           N  
ANISOU  649  NE  ARG A  89     2094   2259   1693   -183   -259     52       N  
ATOM    650  CZ  ARG A  89      22.538  26.860  62.367  1.00 18.96           C  
ANISOU  650  CZ  ARG A  89     2477   2675   2054   -180   -247     59       C  
ATOM    651  NH1 ARG A  89      22.471  27.093  63.678  1.00 14.06           N  
ANISOU  651  NH1 ARG A  89     1852   2114   1377   -215   -261     48       N  
ATOM    652  NH2 ARG A  89      21.893  25.822  61.851  1.00 13.52           N  
ANISOU  652  NH2 ARG A  89     1788   1958   1392   -146   -220     79       N  
ATOM    653  N   PRO A  90      23.160  31.527  56.531  1.00 10.36           N  
ANISOU  653  N   PRO A  90     1465   1327   1144   -147   -263    -44       N  
ATOM    654  CA  PRO A  90      22.047  31.951  55.676  1.00  9.88           C  
ANISOU  654  CA  PRO A  90     1429   1217   1108   -117   -247    -79       C  
ATOM    655  C   PRO A  90      20.967  30.874  55.571  1.00  8.47           C  
ANISOU  655  C   PRO A  90     1247   1043    926    -80   -216    -87       C  
ATOM    656  O   PRO A  90      21.248  29.679  55.547  1.00 13.72           O  
ANISOU  656  O   PRO A  90     1893   1731   1589    -68   -203    -51       O  
ATOM    657  CB  PRO A  90      22.716  32.220  54.310  1.00 11.84           C  
ANISOU  657  CB  PRO A  90     1666   1445   1389   -112   -249    -44       C  
ATOM    658  CG  PRO A  90      24.058  31.519  54.369  1.00 10.85           C  
ANISOU  658  CG  PRO A  90     1504   1364   1256   -124   -254     14       C  
ATOM    659  CD  PRO A  90      24.455  31.505  55.824  1.00 10.28           C  
ANISOU  659  CD  PRO A  90     1427   1330   1151   -158   -274     12       C  
ATOM    660  N   ILE A  91      19.726  31.328  55.535  1.00 10.97           N  
ANISOU  660  N   ILE A  91     1585   1338   1246    -62   -206   -132       N  
ATOM    661  CA  ILE A  91      18.584  30.442  55.419  1.00 11.51           C  
ANISOU  661  CA  ILE A  91     1649   1415   1311    -35   -181   -141       C  
ATOM    662  C   ILE A  91      18.036  30.564  53.995  1.00 10.92           C  
ANISOU  662  C   ILE A  91     1576   1307   1264     -9   -170   -140       C  
ATOM    663  O   ILE A  91      17.482  31.602  53.617  1.00  8.98           O  
ANISOU  663  O   ILE A  91     1344   1033   1032      1   -175   -167       O  
ATOM    664  CB  ILE A  91      17.514  30.797  56.459  1.00 11.74           C  
ANISOU  664  CB  ILE A  91     1689   1460   1313    -33   -174   -188       C  
ATOM    665  CG1 ILE A  91      18.102  30.647  57.869  1.00 12.90           C  
ANISOU  665  CG1 ILE A  91     1831   1648   1421    -63   -186   -187       C  
ATOM    666  CG2 ILE A  91      16.261  29.952  56.271  1.00 10.47           C  
ANISOU  666  CG2 ILE A  91     1518   1312   1148    -10   -150   -193       C  
ATOM    667  CD1 ILE A  91      17.469  31.570  58.890  1.00 16.02           C  
ANISOU  667  CD1 ILE A  91     2246   2054   1786    -68   -188   -246       C  
ATOM    668  N   ILE A  92      18.211  29.495  53.219  1.00 12.97           N  
ANISOU  668  N   ILE A  92     1824   1571   1533      2   -156   -110       N  
ATOM    669  CA  ILE A  92      17.840  29.452  51.805  1.00  7.54           C  
ANISOU  669  CA  ILE A  92     1136    863    865     21   -147   -105       C  
ATOM    670  C   ILE A  92      16.589  28.593  51.594  1.00  7.42           C  
ANISOU  670  C   ILE A  92     1121    855    843     33   -128   -119       C  
ATOM    671  O   ILE A  92      16.471  27.512  52.161  1.00 13.81           O  
ANISOU  671  O   ILE A  92     1927   1679   1641     27   -118   -111       O  
ATOM    672  CB  ILE A  92      18.998  28.890  50.945  1.00  9.80           C  
ANISOU  672  CB  ILE A  92     1412   1151   1162     23   -143    -66       C  
ATOM    673  CG1 ILE A  92      20.222  29.811  51.029  1.00 13.68           C  
ANISOU  673  CG1 ILE A  92     1896   1643   1659      5   -164    -45       C  
ATOM    674  CG2 ILE A  92      18.573  28.718  49.471  1.00  8.19           C  
ANISOU  674  CG2 ILE A  92     1209    936    968     40   -131    -65       C  
ATOM    675  CD1 ILE A  92      19.939  31.244  50.633  1.00 16.35           C  
ANISOU  675  CD1 ILE A  92     2248   1954   2011     -3   -181    -61       C  
ATOM    676  N   ALA A  93      15.667  29.073  50.764  1.00  9.92           N  
ANISOU  676  N   ALA A  93     1438   1163   1167     46   -126   -135       N  
ATOM    677  CA  ALA A  93      14.368  28.416  50.591  1.00 11.94           C  
ANISOU  677  CA  ALA A  93     1689   1434   1414     51   -113   -148       C  
ATOM    678  C   ALA A  93      14.282  27.481  49.405  1.00 14.30           C  
ANISOU  678  C   ALA A  93     1988   1730   1715     50   -103   -136       C  
ATOM    679  O   ALA A  93      14.969  27.645  48.391  1.00  8.15           O  
ANISOU  679  O   ALA A  93     1212    940    946     55   -105   -122       O  
ATOM    680  CB  ALA A  93      13.270  29.463  50.459  1.00 11.03           C  
ANISOU  680  CB  ALA A  93     1569   1321   1302     68   -117   -172       C  
ATOM    681  N   HIS A  94      13.403  26.504  49.545  1.00 15.73           N  
ANISOU  681  N   HIS A  94     2168   1925   1885     40    -92   -142       N  
ATOM    682  CA  HIS A  94      12.744  25.898  48.402  1.00 14.01           C  
ANISOU  682  CA  HIS A  94     1950   1710   1663     34    -87   -145       C  
ATOM    683  C   HIS A  94      11.280  26.303  48.548  1.00 10.35           C  
ANISOU  683  C   HIS A  94     1468   1275   1189     33    -89   -160       C  
ATOM    684  O   HIS A  94      10.733  26.182  49.646  1.00 10.97           O  
ANISOU  684  O   HIS A  94     1538   1373   1258     27    -86   -167       O  
ATOM    685  CB  HIS A  94      12.886  24.374  48.387  1.00 11.68           C  
ANISOU  685  CB  HIS A  94     1670   1403   1364     16    -74   -139       C  
ATOM    686  CG  HIS A  94      14.229  23.872  47.930  1.00  7.34           C  
ANISOU  686  CG  HIS A  94     1137    827    826     28    -67   -125       C  
ATOM    687  ND1 HIS A  94      14.558  23.726  46.601  1.00  7.58           N  
ANISOU  687  ND1 HIS A  94     1176    851    856     35    -61   -129       N  
ATOM    688  CD2 HIS A  94      15.285  23.397  48.633  1.00 14.75           C  
ANISOU  688  CD2 HIS A  94     2079   1751   1773     35    -62   -104       C  
ATOM    689  CE1 HIS A  94      15.785  23.233  46.500  1.00 10.01           C  
ANISOU  689  CE1 HIS A  94     1491   1140   1172     51    -50   -114       C  
ATOM    690  NE2 HIS A  94      16.245  23.021  47.721  1.00  7.43           N  
ANISOU  690  NE2 HIS A  94     1161    808    854     52    -51    -96       N  
ATOM    691  N   GLY A  95      10.656  26.792  47.478  1.00  8.38           N  
ANISOU  691  N   GLY A  95     1207   1037    939     40    -95   -162       N  
ATOM    692  CA  GLY A  95       9.224  27.061  47.487  1.00  7.66           C  
ANISOU  692  CA  GLY A  95     1091    983    837     41    -97   -170       C  
ATOM    693  C   GLY A  95       8.422  25.823  47.869  1.00  9.13           C  
ANISOU  693  C   GLY A  95     1271   1193   1004      8    -90   -172       C  
ATOM    694  O   GLY A  95       8.837  24.701  47.611  1.00  7.77           O  
ANISOU  694  O   GLY A  95     1120   1002    829    -18    -85   -169       O  
ATOM    695  N   MET A  96       7.263  26.015  48.492  1.00  9.44           N  
ANISOU  695  N   MET A  96     1281   1274   1032      8    -87   -176       N  
ATOM    696  CA  MET A  96       6.464  24.891  48.939  1.00  8.19           C  
ANISOU  696  CA  MET A  96     1113   1145    855    -31    -82   -172       C  
ATOM    697  C   MET A  96       5.034  25.046  48.427  1.00  8.49           C  
ANISOU  697  C   MET A  96     1111   1239    877    -39    -87   -168       C  
ATOM    698  O   MET A  96       4.213  25.713  49.065  1.00 11.91           O  
ANISOU  698  O   MET A  96     1508   1714   1302    -16    -81   -170       O  
ATOM    699  CB  MET A  96       6.467  24.799  50.488  1.00  8.26           C  
ANISOU  699  CB  MET A  96     1116   1168    855    -30    -71   -172       C  
ATOM    700  CG  MET A  96       5.846  23.509  51.032  1.00  8.71           C  
ANISOU  700  CG  MET A  96     1167   1249    895    -78    -66   -157       C  
ATOM    701  SD  MET A  96       5.499  23.415  52.837  1.00 15.15           S  
ANISOU  701  SD  MET A  96     1960   2109   1686    -83    -53   -149       S  
ATOM    702  CE  MET A  96       6.985  24.110  53.533  1.00 13.76           C  
ANISOU  702  CE  MET A  96     1813   1893   1522    -49    -53   -159       C  
ATOM    703  N   GLY A  97       4.731  24.430  47.289  1.00  8.59           N  
ANISOU  703  N   GLY A  97     1127   1256    882    -71    -96   -164       N  
ATOM    704  CA  GLY A  97       3.409  24.537  46.709  1.00 16.44           C  
ANISOU  704  CA  GLY A  97     2079   2312   1857    -85   -106   -156       C  
ATOM    705  C   GLY A  97       3.472  24.092  45.262  1.00 12.04           C  
ANISOU  705  C   GLY A  97     1536   1749   1289   -115   -120   -157       C  
ATOM    706  O   GLY A  97       4.499  23.570  44.820  1.00 10.58           O  
ANISOU  706  O   GLY A  97     1397   1513   1112   -124   -117   -168       O  
ATOM    707  N   PHE A  98       2.368  24.236  44.543  1.00 10.03           N  
ANISOU  707  N   PHE A  98     1242   1555   1014   -131   -133   -145       N  
ATOM    708  CA  PHE A  98       2.360  23.903  43.115  1.00 13.61           C  
ANISOU  708  CA  PHE A  98     1707   2016   1449   -162   -149   -148       C  
ATOM    709  C   PHE A  98       3.376  24.801  42.437  1.00 12.96           C  
ANISOU  709  C   PHE A  98     1644   1900   1382   -116   -150   -147       C  
ATOM    710  O   PHE A  98       3.259  26.027  42.515  1.00 12.43           O  
ANISOU  710  O   PHE A  98     1549   1844   1331    -66   -152   -130       O  
ATOM    711  CB  PHE A  98       0.980  24.089  42.483  1.00 12.67           C  
ANISOU  711  CB  PHE A  98     1532   1981   1302   -184   -168   -128       C  
ATOM    712  CG  PHE A  98      -0.023  23.014  42.843  1.00 10.37           C  
ANISOU  712  CG  PHE A  98     1223   1731    988   -252   -173   -126       C  
ATOM    713  CD1 PHE A  98       0.071  22.308  44.037  1.00 11.35           C  
ANISOU  713  CD1 PHE A  98     1363   1830   1122   -270   -159   -131       C  
ATOM    714  CD2 PHE A  98      -1.063  22.717  41.978  1.00 14.01           C  
ANISOU  714  CD2 PHE A  98     1648   2262   1414   -302   -196   -113       C  
ATOM    715  CE1 PHE A  98      -0.863  21.322  44.370  1.00 11.00           C  
ANISOU  715  CE1 PHE A  98     1300   1823   1056   -339   -165   -121       C  
ATOM    716  CE2 PHE A  98      -2.000  21.732  42.295  1.00 20.77           C  
ANISOU  716  CE2 PHE A  98     2485   3158   2247   -374   -204   -107       C  
ATOM    717  CZ  PHE A  98      -1.900  21.035  43.501  1.00 12.61           C  
ANISOU  717  CZ  PHE A  98     1470   2094   1228   -392   -188   -110       C  
ATOM    718  N   GLY A  99       4.401  24.203  41.831  1.00 10.61           N  
ANISOU  718  N   GLY A  99     1393   1557   1082   -131   -145   -165       N  
ATOM    719  CA  GLY A  99       5.423  24.975  41.145  1.00  8.86           C  
ANISOU  719  CA  GLY A  99     1185   1310    871    -94   -145   -159       C  
ATOM    720  C   GLY A  99       6.716  25.115  41.923  1.00 11.28           C  
ANISOU  720  C   GLY A  99     1524   1555   1208    -63   -128   -165       C  
ATOM    721  O   GLY A  99       7.713  25.598  41.390  1.00  8.33           O  
ANISOU  721  O   GLY A  99     1164   1159    842    -40   -126   -159       O  
ATOM    722  N   GLY A 100       6.701  24.701  43.189  1.00 10.16           N  
ANISOU  722  N   GLY A 100     1388   1394   1079    -65   -118   -171       N  
ATOM    723  CA  GLY A 100       7.882  24.778  44.024  1.00  8.07           C  
ANISOU  723  CA  GLY A 100     1147   1081    838    -41   -106   -172       C  
ATOM    724  C   GLY A 100       8.506  26.154  44.094  1.00  7.90           C  
ANISOU  724  C   GLY A 100     1117   1047    836      2   -110   -160       C  
ATOM    725  O   GLY A 100       7.850  27.165  44.357  1.00  7.98           O  
ANISOU  725  O   GLY A 100     1101   1077    854     26   -118   -152       O  
ATOM    726  N   SER A 101       9.797  26.211  43.836  1.00  7.73           N  
ANISOU  726  N   SER A 101     1118    992    825     13   -106   -156       N  
ATOM    727  CA  SER A 101      10.475  27.481  43.942  1.00  8.94           C  
ANISOU  727  CA  SER A 101     1268   1129    999     44   -113   -141       C  
ATOM    728  C   SER A 101      10.065  28.473  42.852  1.00  7.78           C  
ANISOU  728  C   SER A 101     1102   1003    851     57   -127   -123       C  
ATOM    729  O   SER A 101      10.167  29.677  43.082  1.00 11.35           O  
ANISOU  729  O   SER A 101     1546   1440   1324     82   -136   -110       O  
ATOM    730  CB  SER A 101      11.990  27.277  43.959  1.00 10.70           C  
ANISOU  730  CB  SER A 101     1513   1321   1232     48   -105   -134       C  
ATOM    731  OG  SER A 101      12.383  26.738  45.218  1.00  9.31           O  
ANISOU  731  OG  SER A 101     1348   1128   1064     45    -97   -141       O  
ATOM    732  N   THR A 102       9.533  27.999  41.714  1.00 13.08           N  
ANISOU  732  N   THR A 102     1765   1707   1496     38   -131   -121       N  
ATOM    733  CA  THR A 102       9.084  28.938  40.670  1.00  8.18           C  
ANISOU  733  CA  THR A 102     1121   1116    871     49   -147    -95       C  
ATOM    734  C   THR A 102       7.823  29.676  41.126  1.00 15.97           C  
ANISOU  734  C   THR A 102     2075   2124   1868     69   -157    -86       C  
ATOM    735  O   THR A 102       7.476  30.709  40.571  1.00 14.55           O  
ANISOU  735  O   THR A 102     1875   1957   1698     93   -171    -58       O  
ATOM    736  CB  THR A 102       8.834  28.247  39.313  1.00  8.40           C  
ANISOU  736  CB  THR A 102     1146   1185    859     19   -150    -95       C  
ATOM    737  OG1 THR A 102       7.635  27.465  39.353  1.00  8.59           O  
ANISOU  737  OG1 THR A 102     1158   1245    861    -10   -153   -111       O  
ATOM    738  CG2 THR A 102      10.033  27.357  38.946  1.00  8.71           C  
ANISOU  738  CG2 THR A 102     1220   1203    886      6   -133   -113       C  
ATOM    739  N   MET A 103       7.168  29.160  42.163  1.00 13.64           N  
ANISOU  739  N   MET A 103     1775   1835   1572     64   -148   -107       N  
ATOM    740  CA  MET A 103       6.054  29.858  42.804  1.00  8.58           C  
ANISOU  740  CA  MET A 103     1101   1217    941     92   -150   -103       C  
ATOM    741  C   MET A 103       6.490  31.149  43.516  1.00  8.58           C  
ANISOU  741  C   MET A 103     1110   1173    977    138   -150   -102       C  
ATOM    742  O   MET A 103       5.704  32.092  43.649  1.00  8.89           O  
ANISOU  742  O   MET A 103     1125   1221   1032    176   -154    -92       O  
ATOM    743  CB  MET A 103       5.363  28.937  43.829  1.00  8.59           C  
ANISOU  743  CB  MET A 103     1095   1242    929     71   -138   -125       C  
ATOM    744  CG  MET A 103       4.075  29.504  44.437  1.00 16.71           C  
ANISOU  744  CG  MET A 103     2079   2312   1958     99   -136   -121       C  
ATOM    745  SD  MET A 103       3.273  28.398  45.633  1.00 14.48           S  
ANISOU  745  SD  MET A 103     1781   2070   1653     66   -120   -138       S  
ATOM    746  CE  MET A 103       4.389  28.517  47.022  1.00 13.15           C  
ANISOU  746  CE  MET A 103     1651   1844   1501     82   -104   -162       C  
ATOM    747  N   ILE A 104       7.745  31.187  43.965  1.00  8.30           N  
ANISOU  747  N   ILE A 104     1110   1089    956    134   -146   -112       N  
ATOM    748  CA  ILE A 104       8.211  32.244  44.843  1.00 15.08           C  
ANISOU  748  CA  ILE A 104     1984   1903   1843    164   -146   -120       C  
ATOM    749  C   ILE A 104       9.480  32.936  44.348  1.00 16.01           C  
ANISOU  749  C   ILE A 104     2126   1976   1982    163   -158   -101       C  
ATOM    750  O   ILE A 104       9.994  33.822  45.035  1.00  8.36           O  
ANISOU  750  O   ILE A 104     1175    963   1037    177   -163   -108       O  
ATOM    751  CB  ILE A 104       8.491  31.700  46.282  1.00 14.19           C  
ANISOU  751  CB  ILE A 104     1886   1782   1724    154   -132   -152       C  
ATOM    752  CG1 ILE A 104       9.809  30.925  46.343  1.00 13.56           C  
ANISOU  752  CG1 ILE A 104     1833   1681   1640    123   -130   -150       C  
ATOM    753  CG2 ILE A 104       7.324  30.842  46.778  1.00 10.14           C  
ANISOU  753  CG2 ILE A 104     1347   1319   1186    144   -120   -164       C  
ATOM    754  CD1 ILE A 104      10.257  30.557  47.769  1.00 18.77           C  
ANISOU  754  CD1 ILE A 104     2507   2332   2295    114   -120   -171       C  
ATOM    755  N   ASN A 105       9.968  32.555  43.163  1.00 12.35           N  
ANISOU  755  N   ASN A 105     1661   1526   1505    142   -163    -77       N  
ATOM    756  CA  ASN A 105      11.259  33.058  42.702  1.00 16.46           C  
ANISOU  756  CA  ASN A 105     2198   2017   2038    135   -171    -54       C  
ATOM    757  C   ASN A 105      11.125  34.406  41.997  1.00 15.71           C  
ANISOU  757  C   ASN A 105     2097   1905   1968    155   -191    -18       C  
ATOM    758  O   ASN A 105      10.015  34.953  41.902  1.00 16.59           O  
ANISOU  758  O   ASN A 105     2191   2025   2089    182   -196    -12       O  
ATOM    759  CB  ASN A 105      11.962  32.013  41.811  1.00 12.85           C  
ANISOU  759  CB  ASN A 105     1743   1585   1553    107   -163    -47       C  
ATOM    760  CG  ASN A 105      11.358  31.873  40.420  1.00 12.59           C  
ANISOU  760  CG  ASN A 105     1691   1597   1495    101   -169    -26       C  
ATOM    761  OD1 ASN A 105      10.513  32.655  40.012  1.00 11.31           O  
ANISOU  761  OD1 ASN A 105     1510   1448   1341    117   -183     -6       O  
ATOM    762  ND2 ASN A 105      11.789  30.838  39.691  1.00  9.96           N  
ANISOU  762  ND2 ASN A 105     1364   1290   1131     78   -157    -34       N  
ATOM    763  N   ARG A 106      12.248  34.945  41.521  1.00 11.61           N  
ANISOU  763  N   ARG A 106     1588   1361   1460    142   -201     11       N  
ATOM    764  CA  ARG A 106      12.248  36.270  40.900  1.00  8.91           C  
ANISOU  764  CA  ARG A 106     1245    993   1146    156   -221     53       C  
ATOM    765  C   ARG A 106      12.030  36.177  39.363  1.00 11.99           C  
ANISOU  765  C   ARG A 106     1611   1434   1513    149   -229     98       C  
ATOM    766  O   ARG A 106      12.080  37.192  38.646  1.00 11.73           O  
ANISOU  766  O   ARG A 106     1571   1387   1498    156   -248    146       O  
ATOM    767  CB  ARG A 106      13.557  37.000  41.218  1.00  8.97           C  
ANISOU  767  CB  ARG A 106     1277    952   1180    138   -233     68       C  
ATOM    768  CG  ARG A 106      13.522  38.515  40.979  1.00 13.32           C  
ANISOU  768  CG  ARG A 106     1839   1449   1774    152   -256    104       C  
ATOM    769  CD  ARG A 106      14.689  39.232  41.692  1.00 14.73           C  
ANISOU  769  CD  ARG A 106     2049   1569   1980    127   -269    103       C  
ATOM    770  NE  ARG A 106      14.774  40.639  41.298  1.00 13.08           N  
ANISOU  770  NE  ARG A 106     1855   1301   1813    130   -295    145       N  
ATOM    771  CZ  ARG A 106      15.505  41.566  41.908  1.00 14.01           C  
ANISOU  771  CZ  ARG A 106     2006   1351   1965    110   -313    144       C  
ATOM    772  NH1 ARG A 106      16.194  41.282  43.011  1.00 18.76           N  
ANISOU  772  NH1 ARG A 106     2627   1940   2559     85   -309    102       N  
ATOM    773  NH2 ARG A 106      15.509  42.803  41.442  1.00 12.98           N  
ANISOU  773  NH2 ARG A 106     1893   1163   1877    112   -337    187       N  
ATOM    774  N   LEU A 107      11.806  34.959  38.876  1.00  9.28           N  
ANISOU  774  N   LEU A 107     1254   1145   1126    131   -215     81       N  
ATOM    775  CA  LEU A 107      11.271  34.718  37.516  1.00  9.80           C  
ANISOU  775  CA  LEU A 107     1294   1272   1157    122   -221    109       C  
ATOM    776  C   LEU A 107      12.213  35.074  36.352  1.00 13.90           C  
ANISOU  776  C   LEU A 107     1809   1812   1662    104   -228    156       C  
ATOM    777  O   LEU A 107      11.773  35.181  35.203  1.00 15.17           O  
ANISOU  777  O   LEU A 107     1947   2023   1794     98   -238    190       O  
ATOM    778  CB  LEU A 107       9.950  35.482  37.342  1.00  9.46           C  
ANISOU  778  CB  LEU A 107     1226   1239   1129    152   -237    133       C  
ATOM    779  CG  LEU A 107       8.793  35.070  38.263  1.00 14.35           C  
ANISOU  779  CG  LEU A 107     1836   1866   1751    170   -228     94       C  
ATOM    780  CD1 LEU A 107       7.669  36.089  38.212  1.00 10.32           C  
ANISOU  780  CD1 LEU A 107     1298   1357   1266    212   -243    123       C  
ATOM    781  CD2 LEU A 107       8.262  33.688  37.901  1.00  9.95           C  
ANISOU  781  CD2 LEU A 107     1266   1371   1144    137   -218     67       C  
ATOM    782  N   ASN A 108      13.496  35.276  36.635  1.00 12.94           N  
ANISOU  782  N   ASN A 108     1704   1659   1554     93   -224    163       N  
ATOM    783  CA  ASN A 108      14.460  35.519  35.570  1.00  9.38           C  
ANISOU  783  CA  ASN A 108     1243   1237   1084     73   -227    209       C  
ATOM    784  C   ASN A 108      14.770  34.200  34.867  1.00 15.85           C  
ANISOU  784  C   ASN A 108     2058   2118   1847     57   -202    183       C  
ATOM    785  O   ASN A 108      15.406  33.310  35.433  1.00 17.12           O  
ANISOU  785  O   ASN A 108     2234   2269   2002     54   -181    144       O  
ATOM    786  CB  ASN A 108      15.741  36.169  36.119  1.00 10.95           C  
ANISOU  786  CB  ASN A 108     1455   1389   1314     62   -231    229       C  
ATOM    787  CG  ASN A 108      16.676  36.637  35.012  1.00 13.08           C  
ANISOU  787  CG  ASN A 108     1707   1694   1567     39   -238    290       C  
ATOM    788  OD1 ASN A 108      16.451  36.340  33.845  1.00 14.18           O  
ANISOU  788  OD1 ASN A 108     1826   1897   1664     33   -234    311       O  
ATOM    789  ND2 ASN A 108      17.727  37.375  35.374  1.00 11.69           N  
ANISOU  789  ND2 ASN A 108     1538   1483   1421     21   -248    320       N  
ATOM    790  N   LEU A 109      14.332  34.075  33.619  1.00 18.16           N  
ANISOU  790  N   LEU A 109     2331   2473   2097     47   -206    204       N  
ATOM    791  CA  LEU A 109      14.409  32.789  32.945  1.00  9.58           C  
ANISOU  791  CA  LEU A 109     1246   1440    953     32   -183    167       C  
ATOM    792  C   LEU A 109      15.591  32.732  31.998  1.00 18.19           C  
ANISOU  792  C   LEU A 109     2328   2575   2008     20   -169    193       C  
ATOM    793  O   LEU A 109      15.584  33.348  30.914  1.00 14.02           O  
ANISOU  793  O   LEU A 109     1776   2097   1453      9   -182    243       O  
ATOM    794  CB  LEU A 109      13.102  32.516  32.218  1.00 17.43           C  
ANISOU  794  CB  LEU A 109     2226   2487   1911     23   -195    161       C  
ATOM    795  CG  LEU A 109      12.798  31.108  31.714  1.00 19.51           C  
ANISOU  795  CG  LEU A 109     2502   2794   2119      1   -176    106       C  
ATOM    796  CD1 LEU A 109      12.863  30.103  32.843  1.00 19.49           C  
ANISOU  796  CD1 LEU A 109     2529   2740   2136      6   -155     45       C  
ATOM    797  CD2 LEU A 109      11.418  31.103  31.077  1.00 14.67           C  
ANISOU  797  CD2 LEU A 109     1866   2234   1474    -15   -197    112       C  
ATOM    798  N   VAL A 110      16.597  31.964  32.413  1.00 17.40           N  
ANISOU  798  N   VAL A 110     2243   2462   1906     24   -141    161       N  
ATOM    799  CA  VAL A 110      17.877  31.864  31.714  1.00 17.96           C  
ANISOU  799  CA  VAL A 110     2302   2575   1949     21   -121    184       C  
ATOM    800  C   VAL A 110      18.239  30.400  31.430  1.00 15.81           C  
ANISOU  800  C   VAL A 110     2046   2329   1634     29    -83    124       C  
ATOM    801  O   VAL A 110      18.250  29.565  32.331  1.00 11.67           O  
ANISOU  801  O   VAL A 110     1546   1759   1131     42    -68     76       O  
ATOM    802  CB  VAL A 110      19.030  32.504  32.532  1.00  9.74           C  
ANISOU  802  CB  VAL A 110     1255   1493    953     24   -124    216       C  
ATOM    803  CG1 VAL A 110      20.314  32.437  31.759  1.00 10.07           C  
ANISOU  803  CG1 VAL A 110     1274   1592    962     19   -103    247       C  
ATOM    804  CG2 VAL A 110      18.707  33.959  32.915  1.00 10.70           C  
ANISOU  804  CG2 VAL A 110     1372   1570   1123     15   -162    267       C  
ATOM    805  N   VAL A 111      18.523  30.088  30.174  1.00 10.35           N  
ANISOU  805  N   VAL A 111     1343   1709    882     22    -66    126       N  
ATOM    806  CA  VAL A 111      18.902  28.730  29.801  1.00 13.14           C  
ANISOU  806  CA  VAL A 111     1717   2083   1193     35    -27     64       C  
ATOM    807  C   VAL A 111      20.241  28.311  30.412  1.00 17.08           C  
ANISOU  807  C   VAL A 111     2217   2560   1715     64      4     60       C  
ATOM    808  O   VAL A 111      20.327  27.264  31.060  1.00 13.05           O  
ANISOU  808  O   VAL A 111     1735   2006   1219     83     25      8       O  
ATOM    809  CB  VAL A 111      18.962  28.588  28.269  1.00 12.61           C  
ANISOU  809  CB  VAL A 111     1636   2106   1048     22    -14     66       C  
ATOM    810  CG1 VAL A 111      19.648  27.278  27.871  1.00 11.47           C  
ANISOU  810  CG1 VAL A 111     1515   1981    861     44     35      2       C  
ATOM    811  CG2 VAL A 111      17.550  28.656  27.724  1.00 12.25           C  
ANISOU  811  CG2 VAL A 111     1594   2086    974     -7    -42     57       C  
ATOM    812  N   GLY A 112      21.282  29.123  30.214  1.00 14.24           N  
ANISOU  812  N   GLY A 112     1822   2230   1359     64      4    121       N  
ATOM    813  CA  GLY A 112      22.556  28.855  30.855  1.00 10.58           C  
ANISOU  813  CA  GLY A 112     1347   1754    919     88     27    129       C  
ATOM    814  C   GLY A 112      23.738  28.663  29.926  1.00 16.14           C  
ANISOU  814  C   GLY A 112     2020   2536   1576    104     62    150       C  
ATOM    815  O   GLY A 112      24.868  28.457  30.383  1.00 18.31           O  
ANISOU  815  O   GLY A 112     2276   2814   1868    127     83    165       O  
ATOM    816  N   GLY A 113      23.474  28.710  28.622  1.00 11.58           N  
ANISOU  816  N   GLY A 113     1433   2030    936     92     70    151       N  
ATOM    817  CA  GLY A 113      24.519  28.673  27.628  1.00 12.19           C  
ANISOU  817  CA  GLY A 113     1474   2197    959    104    103    177       C  
ATOM    818  C   GLY A 113      24.939  27.302  27.145  1.00 17.32           C  
ANISOU  818  C   GLY A 113     2143   2875   1563    146    159    105       C  
ATOM    819  O   GLY A 113      24.854  26.303  27.864  1.00 14.31           O  
ANISOU  819  O   GLY A 113     1799   2429   1210    176    177     45       O  
ATOM    820  N   ARG A 114      25.390  27.269  25.899  1.00 18.08           N  
ANISOU  820  N   ARG A 114     2214   3068   1586    149    186    113       N  
ATOM    821  CA  ARG A 114      25.909  26.064  25.273  1.00 15.97           C  
ANISOU  821  CA  ARG A 114     1962   2840   1266    195    245     45       C  
ATOM    822  C   ARG A 114      27.172  25.524  25.919  1.00 16.70           C  
ANISOU  822  C   ARG A 114     2037   2919   1390    251    285     46       C  
ATOM    823  O   ARG A 114      27.332  24.306  26.053  1.00 18.48           O  
ANISOU  823  O   ARG A 114     2299   3110   1613    299    325    -26       O  
ATOM    824  CB  ARG A 114      26.208  26.326  23.786  1.00 14.63           C  
ANISOU  824  CB  ARG A 114     1760   2795   1005    184    266     64       C  
ATOM    825  CG  ARG A 114      27.199  25.331  23.183  1.00 19.81           C  
ANISOU  825  CG  ARG A 114     2412   3509   1607    242    336     14       C  
ATOM    826  CD  ARG A 114      27.519  25.648  21.713  1.00 21.62           C  
ANISOU  826  CD  ARG A 114     2602   3875   1737    230    359     36       C  
ATOM    827  NE  ARG A 114      26.384  25.449  20.829  1.00 18.68           N  
ANISOU  827  NE  ARG A 114     2266   3529   1300    192    345    -14       N  
ATOM    828  CZ  ARG A 114      26.000  24.264  20.350  1.00 25.40           C  
ANISOU  828  CZ  ARG A 114     3173   4375   2103    213    379   -121       C  
ATOM    829  NH1 ARG A 114      26.665  23.159  20.677  1.00 19.63           N  
ANISOU  829  NH1 ARG A 114     2471   3602   1385    279    433   -191       N  
ATOM    830  NH2 ARG A 114      24.951  24.182  19.536  1.00 23.24           N  
ANISOU  830  NH2 ARG A 114     2928   4137   1767    167    358   -158       N  
ATOM    831  N   THR A 115      28.089  26.418  26.279  1.00 13.91           N  
ANISOU  831  N   THR A 115     1627   2595   1063    243    273    132       N  
ATOM    832  CA  THR A 115      29.446  25.991  26.653  1.00 14.22           C  
ANISOU  832  CA  THR A 115     1630   2657   1116    295    314    148       C  
ATOM    833  C   THR A 115      29.468  25.045  27.856  1.00 13.86           C  
ANISOU  833  C   THR A 115     1621   2513   1132    337    323    101       C  
ATOM    834  O   THR A 115      30.149  24.020  27.847  1.00 18.53           O  
ANISOU  834  O   THR A 115     2216   3108   1716    401    374     63       O  
ATOM    835  CB  THR A 115      30.337  27.201  26.954  1.00 16.15           C  
ANISOU  835  CB  THR A 115     1807   2945   1385    263    288    254       C  
ATOM    836  OG1 THR A 115      30.413  28.034  25.795  1.00 14.65           O  
ANISOU  836  OG1 THR A 115     1578   2852   1136    225    282    307       O  
ATOM    837  CG2 THR A 115      31.750  26.759  27.334  1.00 14.59           C  
ANISOU  837  CG2 THR A 115     1561   2785   1197    315    328    279       C  
ATOM    838  N   VAL A 116      28.690  25.379  28.876  1.00 13.12           N  
ANISOU  838  N   VAL A 116     1556   2331   1097    304    276    105       N  
ATOM    839  CA  VAL A 116      28.687  24.604  30.113  1.00 12.77           C  
ANISOU  839  CA  VAL A 116     1542   2197   1112    334    278     74       C  
ATOM    840  C   VAL A 116      28.176  23.180  29.864  1.00 13.02           C  
ANISOU  840  C   VAL A 116     1635   2184   1128    375    315    -20       C  
ATOM    841  O   VAL A 116      28.772  22.228  30.328  1.00 13.26           O  
ANISOU  841  O   VAL A 116     1675   2181   1180    431    349    -44       O  
ATOM    842  CB  VAL A 116      27.857  25.312  31.219  1.00 12.89           C  
ANISOU  842  CB  VAL A 116     1576   2137   1185    285    219     94       C  
ATOM    843  CG1 VAL A 116      26.365  25.363  30.852  1.00 12.29           C  
ANISOU  843  CG1 VAL A 116     1546   2028   1094    249    194     49       C  
ATOM    844  CG2 VAL A 116      28.084  24.624  32.564  1.00 14.40           C  
ANISOU  844  CG2 VAL A 116     1784   2255   1433    314    221     80       C  
ATOM    845  N   PHE A 117      27.132  23.020  29.056  1.00 18.14           N  
ANISOU  845  N   PHE A 117     2323   2834   1734    347    309    -71       N  
ATOM    846  CA  PHE A 117      26.645  21.684  28.735  1.00 13.45           C  
ANISOU  846  CA  PHE A 117     1793   2197   1121    375    341   -164       C  
ATOM    847  C   PHE A 117      27.614  20.908  27.840  1.00 16.21           C  
ANISOU  847  C   PHE A 117     2136   2602   1420    438    407   -199       C  
ATOM    848  O   PHE A 117      27.793  19.704  28.012  1.00 18.23           O  
ANISOU  848  O   PHE A 117     2435   2803   1689    490    445   -261       O  
ATOM    849  CB  PHE A 117      25.252  21.771  28.097  1.00 15.38           C  
ANISOU  849  CB  PHE A 117     2076   2439   1329    319    313   -206       C  
ATOM    850  CG  PHE A 117      24.198  22.130  29.092  1.00 12.59           C  
ANISOU  850  CG  PHE A 117     1743   2013   1029    275    260   -195       C  
ATOM    851  CD1 PHE A 117      23.645  21.150  29.907  1.00 12.42           C  
ANISOU  851  CD1 PHE A 117     1773   1898   1046    282    261   -246       C  
ATOM    852  CD2 PHE A 117      23.835  23.447  29.287  1.00 15.82           C  
ANISOU  852  CD2 PHE A 117     2115   2443   1453    230    214   -128       C  
ATOM    853  CE1 PHE A 117      22.713  21.483  30.879  1.00 18.78           C  
ANISOU  853  CE1 PHE A 117     2590   2647   1899    244    216   -232       C  
ATOM    854  CE2 PHE A 117      22.904  23.790  30.251  1.00 19.11           C  
ANISOU  854  CE2 PHE A 117     2546   2795   1918    199    171   -120       C  
ATOM    855  CZ  PHE A 117      22.344  22.803  31.054  1.00 14.28           C  
ANISOU  855  CZ  PHE A 117     1982   2104   1340    206    173   -172       C  
ATOM    856  N   ASP A 118      28.262  21.600  26.912  1.00 14.77           N  
ANISOU  856  N   ASP A 118     1899   2529   1183    436    421   -157       N  
ATOM    857  CA  ASP A 118      29.221  20.943  26.036  1.00 17.70           C  
ANISOU  857  CA  ASP A 118     2255   2969   1501    499    487   -187       C  
ATOM    858  C   ASP A 118      30.460  20.459  26.774  1.00 18.88           C  
ANISOU  858  C   ASP A 118     2373   3104   1695    573    524   -162       C  
ATOM    859  O   ASP A 118      31.092  19.482  26.370  1.00 21.45           O  
ANISOU  859  O   ASP A 118     2710   3441   1999    647    585   -212       O  
ATOM    860  CB  ASP A 118      29.646  21.889  24.916  1.00 22.12           C  
ANISOU  860  CB  ASP A 118     2753   3661   1989    473    492   -134       C  
ATOM    861  CG  ASP A 118      28.674  21.882  23.754  1.00 22.93           C  
ANISOU  861  CG  ASP A 118     2891   3806   2015    430    485   -185       C  
ATOM    862  OD1 ASP A 118      27.742  21.055  23.776  1.00 22.40           O  
ANISOU  862  OD1 ASP A 118     2896   3667   1948    423    482   -269       O  
ATOM    863  OD2 ASP A 118      28.859  22.681  22.816  1.00 22.56           O  
ANISOU  863  OD2 ASP A 118     2798   3869   1907    400    482   -138       O  
ATOM    864  N   ASN A 119      30.829  21.148  27.846  1.00 20.39           N  
ANISOU  864  N   ASN A 119     2522   3275   1948    556    488    -84       N  
ATOM    865  CA  ASN A 119      32.094  20.839  28.513  1.00 15.61           C  
ANISOU  865  CA  ASN A 119     1870   2680   1379    620    518    -42       C  
ATOM    866  C   ASN A 119      31.962  20.210  29.904  1.00 15.17           C  
ANISOU  866  C   ASN A 119     1846   2513   1403    641    502    -49       C  
ATOM    867  O   ASN A 119      32.737  19.331  30.261  1.00 17.66           O  
ANISOU  867  O   ASN A 119     2156   2810   1742    717    543    -56       O  
ATOM    868  CB  ASN A 119      32.952  22.106  28.610  1.00 17.62           C  
ANISOU  868  CB  ASN A 119     2036   3025   1634    586    494     66       C  
ATOM    869  CG  ASN A 119      33.515  22.529  27.260  1.00 20.86           C  
ANISOU  869  CG  ASN A 119     2396   3565   1965    588    527     87       C  
ATOM    870  OD1 ASN A 119      34.585  22.071  26.853  1.00 21.80           O  
ANISOU  870  OD1 ASN A 119     2471   3757   2056    655    583     94       O  
ATOM    871  ND2 ASN A 119      32.799  23.406  26.563  1.00 16.02           N  
ANISOU  871  ND2 ASN A 119     1787   2988   1314    517    492    102       N  
ATOM    872  N   ASP A 120      30.982  20.652  30.681  1.00 14.33           N  
ANISOU  872  N   ASP A 120     1772   2337   1336    578    445    -43       N  
ATOM    873  CA  ASP A 120      30.918  20.275  32.096  1.00 14.93           C  
ANISOU  873  CA  ASP A 120     1865   2325   1484    587    423    -31       C  
ATOM    874  C   ASP A 120      29.869  19.201  32.374  1.00 20.65           C  
ANISOU  874  C   ASP A 120     2674   2943   2229    592    425   -111       C  
ATOM    875  O   ASP A 120      29.759  18.704  33.490  1.00 17.73           O  
ANISOU  875  O   ASP A 120     2325   2498   1914    603    412   -106       O  
ATOM    876  CB  ASP A 120      30.633  21.515  32.937  1.00 13.10           C  
ANISOU  876  CB  ASP A 120     1605   2090   1284    515    359     34       C  
ATOM    877  CG  ASP A 120      31.655  22.608  32.696  1.00 16.05           C  
ANISOU  877  CG  ASP A 120     1898   2560   1640    498    352    117       C  
ATOM    878  OD1 ASP A 120      32.845  22.369  32.981  1.00 17.73           O  
ANISOU  878  OD1 ASP A 120     2059   2813   1863    544    378    158       O  
ATOM    879  OD2 ASP A 120      31.275  23.692  32.209  1.00 20.75           O  
ANISOU  879  OD2 ASP A 120     2479   3191   2213    438    320    144       O  
ATOM    880  N   TRP A 121      29.076  18.882  31.359  1.00 18.15           N  
ANISOU  880  N   TRP A 121     2406   2626   1865    575    436   -180       N  
ATOM    881  CA  TRP A 121      28.099  17.815  31.456  1.00 20.22           C  
ANISOU  881  CA  TRP A 121     2750   2794   2138    573    439   -259       C  
ATOM    882  C   TRP A 121      28.575  16.639  30.598  1.00 27.56           C  
ANISOU  882  C   TRP A 121     3716   3719   3037    643    505   -330       C  
ATOM    883  O   TRP A 121      29.286  16.851  29.617  1.00 25.46           O  
ANISOU  883  O   TRP A 121     3414   3542   2716    673    541   -330       O  
ATOM    884  CB  TRP A 121      26.729  18.310  31.016  1.00 13.66           C  
ANISOU  884  CB  TRP A 121     1951   1962   1279    493    398   -288       C  
ATOM    885  CG  TRP A 121      26.075  19.268  31.975  1.00 12.76           C  
ANISOU  885  CG  TRP A 121     1818   1828   1204    433    338   -235       C  
ATOM    886  CD1 TRP A 121      26.556  20.475  32.390  1.00 14.99           C  
ANISOU  886  CD1 TRP A 121     2038   2155   1501    413    309   -156       C  
ATOM    887  CD2 TRP A 121      24.782  19.119  32.594  1.00 12.51           C  
ANISOU  887  CD2 TRP A 121     1830   1726   1198    384    299   -260       C  
ATOM    888  NE1 TRP A 121      25.658  21.075  33.252  1.00 12.09           N  
ANISOU  888  NE1 TRP A 121     1679   1745   1168    361    259   -137       N  
ATOM    889  CE2 TRP A 121      24.560  20.270  33.379  1.00 14.66           C  
ANISOU  889  CE2 TRP A 121     2065   2007   1499    344    253   -198       C  
ATOM    890  CE3 TRP A 121      23.796  18.127  32.550  1.00 12.43           C  
ANISOU  890  CE3 TRP A 121     1888   1649   1187    367    300   -329       C  
ATOM    891  CZ2 TRP A 121      23.392  20.451  34.128  1.00 17.34           C  
ANISOU  891  CZ2 TRP A 121     2427   2296   1865    297    212   -203       C  
ATOM    892  CZ3 TRP A 121      22.631  18.311  33.297  1.00 13.81           C  
ANISOU  892  CZ3 TRP A 121     2081   1778   1388    312    256   -328       C  
ATOM    893  CH2 TRP A 121      22.447  19.464  34.072  1.00 12.81           C  
ANISOU  893  CH2 TRP A 121     1911   1669   1289    283    215   -265       C  
ATOM    894  N   PRO A 122      28.205  15.399  30.979  1.00 15.38           N  
ANISOU  894  N   PRO A 122     2244   2071   1527    671    521   -391       N  
ATOM    895  CA  PRO A 122      28.692  14.181  30.323  1.00 16.43           C  
ANISOU  895  CA  PRO A 122     2422   2176   1644    747    585   -463       C  
ATOM    896  C   PRO A 122      28.085  13.931  28.930  1.00 24.25           C  
ANISOU  896  C   PRO A 122     3461   3197   2556    722    604   -552       C  
ATOM    897  O   PRO A 122      27.158  14.628  28.502  1.00 16.54           O  
ANISOU  897  O   PRO A 122     2486   2259   1541    641    563   -556       O  
ATOM    898  CB  PRO A 122      28.264  13.080  31.295  1.00 21.83           C  
ANISOU  898  CB  PRO A 122     3173   2724   2396    762    580   -490       C  
ATOM    899  CG  PRO A 122      26.994  13.628  31.905  1.00 18.34           C  
ANISOU  899  CG  PRO A 122     2747   2251   1971    664    513   -475       C  
ATOM    900  CD  PRO A 122      27.295  15.088  32.100  1.00 18.83           C  
ANISOU  900  CD  PRO A 122     2725   2409   2023    630    479   -391       C  
ATOM    901  N   VAL A 123      28.606  12.921  28.243  1.00 20.85           N  
ANISOU  901  N   VAL A 123     3068   2750   2103    791    665   -622       N  
ATOM    902  CA  VAL A 123      28.019  12.466  26.987  1.00 27.79           C  
ANISOU  902  CA  VAL A 123     3993   3642   2922    748    674   -712       C  
ATOM    903  C   VAL A 123      26.519  12.203  27.176  1.00 26.94           C  
ANISOU  903  C   VAL A 123     3960   3459   2819    663    626   -761       C  
ATOM    904  O   VAL A 123      26.097  11.680  28.223  1.00 18.03           O  
ANISOU  904  O   VAL A 123     2869   2223   1759    657    604   -755       O  
ATOM    905  CB  VAL A 123      28.712  11.178  26.471  1.00 28.84           C  
ANISOU  905  CB  VAL A 123     4153   3730   3075    805    727   -777       C  
ATOM    906  CG1 VAL A 123      27.995  10.622  25.237  1.00 29.80           C  
ANISOU  906  CG1 VAL A 123     4329   3855   3137    752    735   -881       C  
ATOM    907  CG2 VAL A 123      30.191  11.444  26.158  1.00 29.37           C  
ANISOU  907  CG2 VAL A 123     4142   3887   3131    885    775   -729       C  
ATOM    908  N   GLY A 124      25.724  12.602  26.181  1.00 21.61           N  
ANISOU  908  N   GLY A 124     3296   2847   2067    595    608   -800       N  
ATOM    909  CA  GLY A 124      24.276  12.458  26.226  1.00 24.02           C  
ANISOU  909  CA  GLY A 124     3658   3104   2363    506    559   -841       C  
ATOM    910  C   GLY A 124      23.581  13.664  26.838  1.00 24.68           C  
ANISOU  910  C   GLY A 124     3697   3222   2456    444    498   -761       C  
ATOM    911  O   GLY A 124      22.350  13.802  26.743  1.00 19.25           O  
ANISOU  911  O   GLY A 124     3035   2528   1753    362    452   -779       O  
ATOM    912  N   TRP A 125      24.369  14.539  27.465  1.00 22.61           N  
ANISOU  912  N   TRP A 125     3360   3001   2232    474    492   -668       N  
ATOM    913  CA  TRP A 125      23.836  15.738  28.124  1.00 18.19           C  
ANISOU  913  CA  TRP A 125     2747   2468   1698    415    432   -585       C  
ATOM    914  C   TRP A 125      24.540  16.984  27.580  1.00 18.37           C  
ANISOU  914  C   TRP A 125     2687   2609   1683    419    431   -515       C  
ATOM    915  O   TRP A 125      24.537  18.038  28.224  1.00 17.24           O  
ANISOU  915  O   TRP A 125     2493   2486   1574    393    392   -435       O  
ATOM    916  CB  TRP A 125      23.975  15.643  29.679  1.00 14.68           C  
ANISOU  916  CB  TRP A 125     2295   1938   1345    431    412   -535       C  
ATOM    917  CG  TRP A 125      22.959  14.677  30.283  1.00 14.67           C  
ANISOU  917  CG  TRP A 125     2367   1828   1380    398    394   -585       C  
ATOM    918  CD1 TRP A 125      23.086  13.322  30.403  1.00 16.03           C  
ANISOU  918  CD1 TRP A 125     2607   1908   1575    436    428   -647       C  
ATOM    919  CD2 TRP A 125      21.644  14.998  30.783  1.00 14.06           C  
ANISOU  919  CD2 TRP A 125     2300   1726   1316    319    339   -576       C  
ATOM    920  NE1 TRP A 125      21.940  12.782  30.957  1.00 16.08           N  
ANISOU  920  NE1 TRP A 125     2666   1834   1609    377    394   -673       N  
ATOM    921  CE2 TRP A 125      21.042  13.790  31.190  1.00 14.39           C  
ANISOU  921  CE2 TRP A 125     2415   1667   1387    306    341   -630       C  
ATOM    922  CE3 TRP A 125      20.928  16.191  30.934  1.00 15.20           C  
ANISOU  922  CE3 TRP A 125     2398   1924   1452    262    290   -524       C  
ATOM    923  CZ2 TRP A 125      19.756  13.739  31.746  1.00 17.11           C  
ANISOU  923  CZ2 TRP A 125     2780   1972   1749    233    295   -632       C  
ATOM    924  CZ3 TRP A 125      19.639  16.135  31.473  1.00 12.97           C  
ANISOU  924  CZ3 TRP A 125     2137   1602   1187    198    248   -531       C  
ATOM    925  CH2 TRP A 125      19.072  14.919  31.868  1.00 13.29           C  
ANISOU  925  CH2 TRP A 125     2245   1554   1253    182    251   -582       C  
ATOM    926  N   LYS A 126      25.134  16.864  26.390  1.00 23.59           N  
ANISOU  926  N   LYS A 126     3340   3350   2273    448    475   -546       N  
ATOM    927  CA  LYS A 126      25.783  18.003  25.733  1.00 15.95           C  
ANISOU  927  CA  LYS A 126     2295   2505   1261    445    476   -478       C  
ATOM    928  C   LYS A 126      24.722  18.974  25.267  1.00 22.17           C  
ANISOU  928  C   LYS A 126     3069   3343   2013    361    421   -451       C  
ATOM    929  O   LYS A 126      23.531  18.648  25.295  1.00 22.43           O  
ANISOU  929  O   LYS A 126     3150   3329   2043    311    391   -496       O  
ATOM    930  CB  LYS A 126      26.646  17.559  24.555  1.00 17.00           C  
ANISOU  930  CB  LYS A 126     2421   2717   1319    499    540   -521       C  
ATOM    931  CG  LYS A 126      27.689  16.513  24.901  1.00 21.60           C  
ANISOU  931  CG  LYS A 126     3021   3253   1935    595    601   -554       C  
ATOM    932  CD  LYS A 126      28.643  17.020  25.977  1.00 21.98           C  
ANISOU  932  CD  LYS A 126     3002   3296   2053    632    595   -459       C  
ATOM    933  CE  LYS A 126      29.734  15.996  26.269  1.00 23.74           C  
ANISOU  933  CE  LYS A 126     3230   3483   2306    735    658   -481       C  
ATOM    934  NZ  LYS A 126      30.743  16.510  27.236  1.00 24.27           N  
ANISOU  934  NZ  LYS A 126     3223   3568   2432    769    652   -383       N  
ATOM    935  N   TYR A 127      25.128  20.160  24.823  1.00 15.43           N  
ANISOU  935  N   TYR A 127     2145   2585   1131    343    407   -373       N  
ATOM    936  CA  TYR A 127      24.126  21.178  24.529  1.00 22.64           C  
ANISOU  936  CA  TYR A 127     3041   3536   2026    269    351   -332       C  
ATOM    937  C   TYR A 127      23.171  20.750  23.393  1.00 22.06           C  
ANISOU  937  C   TYR A 127     3007   3504   1870    227    349   -401       C  
ATOM    938  O   TYR A 127      21.961  20.976  23.480  1.00 15.22           O  
ANISOU  938  O   TYR A 127     2159   2618   1008    169    302   -404       O  
ATOM    939  CB  TYR A 127      24.773  22.534  24.192  1.00 19.24           C  
ANISOU  939  CB  TYR A 127     2532   3198   1581    255    336   -230       C  
ATOM    940  CG  TYR A 127      23.706  23.580  23.979  1.00 19.96           C  
ANISOU  940  CG  TYR A 127     2607   3311   1664    186    277   -183       C  
ATOM    941  CD1 TYR A 127      22.983  24.093  25.062  1.00 13.73           C  
ANISOU  941  CD1 TYR A 127     1823   2443    949    160    227   -151       C  
ATOM    942  CD2 TYR A 127      23.369  24.014  22.696  1.00 17.15           C  
ANISOU  942  CD2 TYR A 127     2233   3057   1225    151    270   -171       C  
ATOM    943  CE1 TYR A 127      21.970  25.015  24.867  1.00 17.77           C  
ANISOU  943  CE1 TYR A 127     2322   2973   1458    107    176   -109       C  
ATOM    944  CE2 TYR A 127      22.361  24.953  22.492  1.00 18.27           C  
ANISOU  944  CE2 TYR A 127     2359   3220   1364     93    215   -122       C  
ATOM    945  CZ  TYR A 127      21.665  25.452  23.580  1.00 20.47           C  
ANISOU  945  CZ  TYR A 127     2642   3413   1722     75    169    -91       C  
ATOM    946  OH  TYR A 127      20.655  26.381  23.388  1.00 18.05           O  
ANISOU  946  OH  TYR A 127     2319   3125   1416     28    117    -41       O  
ATOM    947  N   ASP A 128      23.691  20.125  22.342  1.00 17.69           N  
ANISOU  947  N   ASP A 128     2467   3013   1241    255    399   -458       N  
ATOM    948  CA  ASP A 128      22.809  19.674  21.259  1.00 17.11           C  
ANISOU  948  CA  ASP A 128     2435   2982   1082    210    396   -531       C  
ATOM    949  C   ASP A 128      21.835  18.582  21.713  1.00 19.26           C  
ANISOU  949  C   ASP A 128     2789   3146   1381    188    385   -619       C  
ATOM    950  O   ASP A 128      20.797  18.375  21.087  1.00 17.43           O  
ANISOU  950  O   ASP A 128     2589   2937   1096    128    359   -665       O  
ATOM    951  CB  ASP A 128      23.627  19.180  20.068  1.00 19.67           C  
ANISOU  951  CB  ASP A 128     2762   3384   1327    246    455   -577       C  
ATOM    952  CG  ASP A 128      24.372  20.301  19.371  1.00 25.06           C  
ANISOU  952  CG  ASP A 128     3362   4191   1968    245    457   -486       C  
ATOM    953  OD1 ASP A 128      23.873  21.447  19.356  1.00 22.97           O  
ANISOU  953  OD1 ASP A 128     3052   3982   1696    194    408   -406       O  
ATOM    954  OD2 ASP A 128      25.473  20.039  18.853  1.00 35.02           O  
ANISOU  954  OD2 ASP A 128     4603   5492   3211    294    509   -489       O  
ATOM    955  N   ASP A 129      22.157  17.902  22.811  1.00 16.79           N  
ANISOU  955  N   ASP A 129     2508   2721   1151    232    400   -637       N  
ATOM    956  CA  ASP A 129      21.236  16.932  23.400  1.00 19.52           C  
ANISOU  956  CA  ASP A 129     2927   2956   1534    206    384   -703       C  
ATOM    957  C   ASP A 129      20.089  17.622  24.153  1.00 21.64           C  
ANISOU  957  C   ASP A 129     3178   3198   1848    140    316   -649       C  
ATOM    958  O   ASP A 129      18.981  17.096  24.231  1.00 21.25           O  
ANISOU  958  O   ASP A 129     3174   3105   1795     87    288   -696       O  
ATOM    959  CB  ASP A 129      21.980  15.996  24.362  1.00 18.83           C  
ANISOU  959  CB  ASP A 129     2874   2758   1521    276    421   -728       C  
ATOM    960  CG  ASP A 129      23.022  15.137  23.661  1.00 20.60           C  
ANISOU  960  CG  ASP A 129     3126   2995   1708    350    493   -794       C  
ATOM    961  OD1 ASP A 129      22.687  14.525  22.632  1.00 19.37           O  
ANISOU  961  OD1 ASP A 129     3017   2853   1490    322    510   -868       O  
ATOM    962  OD2 ASP A 129      24.173  15.067  24.149  1.00 17.78           O  
ANISOU  962  OD2 ASP A 129     2739   2625   1393    428    530   -760       O  
ATOM    963  N   VAL A 130      20.337  18.802  24.706  1.00 19.17           N  
ANISOU  963  N   VAL A 130     2798   2910   1575    143    289   -552       N  
ATOM    964  CA  VAL A 130      19.320  19.397  25.563  1.00 14.30           C  
ANISOU  964  CA  VAL A 130     2169   2256   1010     96    233   -506       C  
ATOM    965  C   VAL A 130      18.631  20.631  25.007  1.00 14.10           C  
ANISOU  965  C   VAL A 130     2092   2315    950     46    188   -444       C  
ATOM    966  O   VAL A 130      17.605  21.044  25.549  1.00 19.36           O  
ANISOU  966  O   VAL A 130     2751   2957   1647      6    143   -418       O  
ATOM    967  CB  VAL A 130      19.906  19.746  26.968  1.00 13.56           C  
ANISOU  967  CB  VAL A 130     2050   2094   1008    134    228   -448       C  
ATOM    968  CG1 VAL A 130      20.404  18.484  27.630  1.00 13.77           C  
ANISOU  968  CG1 VAL A 130     2128   2028   1076    180    265   -501       C  
ATOM    969  CG2 VAL A 130      21.038  20.795  26.852  1.00 13.42           C  
ANISOU  969  CG2 VAL A 130     1967   2140    993    167    238   -370       C  
ATOM    970  N   LYS A 131      19.157  21.207  23.922  1.00 19.36           N  
ANISOU  970  N   LYS A 131     2722   3083   1552     49    200   -418       N  
ATOM    971  CA  LYS A 131      18.655  22.493  23.445  1.00 19.31           C  
ANISOU  971  CA  LYS A 131     2660   3154   1522      9    157   -339       C  
ATOM    972  C   LYS A 131      17.154  22.464  23.111  1.00 16.92           C  
ANISOU  972  C   LYS A 131     2371   2869   1189    -55    113   -358       C  
ATOM    973  O   LYS A 131      16.459  23.460  23.301  1.00 17.82           O  
ANISOU  973  O   LYS A 131     2446   3001   1324    -82     68   -290       O  
ATOM    974  CB  LYS A 131      19.457  22.980  22.229  1.00 25.05           C  
ANISOU  974  CB  LYS A 131     3349   3997   2173     18    181   -310       C  
ATOM    975  CG  LYS A 131      19.383  22.114  20.968  1.00 15.94           C  
ANISOU  975  CG  LYS A 131     2228   2911    918      5    212   -392       C  
ATOM    976  CD  LYS A 131      20.425  22.599  19.973  1.00 16.52           C  
ANISOU  976  CD  LYS A 131     2256   3097    925     27    244   -355       C  
ATOM    977  CE  LYS A 131      20.382  21.851  18.645  1.00 17.58           C  
ANISOU  977  CE  LYS A 131     2419   3294    965     15    273   -427       C  
ATOM    978  NZ  LYS A 131      21.490  22.294  17.760  1.00 18.17           N  
ANISOU  978  NZ  LYS A 131     2446   3460    999     42    306   -383       N  
ATOM    979  N   ASN A 132      16.640  21.341  22.625  1.00 16.28           N  
ANISOU  979  N   ASN A 132     2344   2783   1058    -81    125   -448       N  
ATOM    980  CA  ASN A 132      15.204  21.281  22.324  1.00 16.42           C  
ANISOU  980  CA  ASN A 132     2370   2826   1045   -149     80   -463       C  
ATOM    981  C   ASN A 132      14.335  21.163  23.579  1.00 20.33           C  
ANISOU  981  C   ASN A 132     2875   3230   1619   -164     49   -456       C  
ATOM    982  O   ASN A 132      13.185  21.604  23.599  1.00 22.21           O  
ANISOU  982  O   ASN A 132     3090   3495   1854   -210      3   -426       O  
ATOM    983  CB  ASN A 132      14.914  20.137  21.349  1.00 16.08           C  
ANISOU  983  CB  ASN A 132     2383   2812    916   -183     99   -564       C  
ATOM    984  CG  ASN A 132      15.384  20.455  19.930  1.00 33.89           C  
ANISOU  984  CG  ASN A 132     4613   5167   3098   -181    113   -548       C  
ATOM    985  OD1 ASN A 132      16.137  21.405  19.718  1.00 34.76           O  
ANISOU  985  OD1 ASN A 132     4669   5342   3195   -154    122   -480       O  
ATOM    986  ND2 ASN A 132      14.953  19.656  18.961  1.00 36.65           N  
ANISOU  986  ND2 ASN A 132     5000   5527   3400   -211    114   -607       N  
ATOM    987  N   TYR A 133      14.881  20.572  24.630  1.00 14.12           N  
ANISOU  987  N   TYR A 133     2121   2343    902   -124     73   -479       N  
ATOM    988  CA  TYR A 133      14.166  20.537  25.899  1.00 13.49           C  
ANISOU  988  CA  TYR A 133     2045   2185    897   -135     47   -464       C  
ATOM    989  C   TYR A 133      14.150  21.942  26.512  1.00 16.45           C  
ANISOU  989  C   TYR A 133     2357   2572   1321   -118     18   -368       C  
ATOM    990  O   TYR A 133      13.124  22.394  27.029  1.00 13.10           O  
ANISOU  990  O   TYR A 133     1912   2141    924   -145    -20   -338       O  
ATOM    991  CB  TYR A 133      14.787  19.493  26.829  1.00 13.38           C  
ANISOU  991  CB  TYR A 133     2081   2065    938    -98     81   -510       C  
ATOM    992  CG  TYR A 133      14.581  18.072  26.324  1.00 14.14           C  
ANISOU  992  CG  TYR A 133     2250   2128    996   -120    103   -608       C  
ATOM    993  CD1 TYR A 133      13.375  17.402  26.529  1.00 15.74           C  
ANISOU  993  CD1 TYR A 133     2487   2298   1197   -183     75   -647       C  
ATOM    994  CD2 TYR A 133      15.585  17.413  25.626  1.00 14.78           C  
ANISOU  994  CD2 TYR A 133     2364   2211   1040    -80    152   -662       C  
ATOM    995  CE1 TYR A 133      13.180  16.107  26.052  1.00 16.75           C  
ANISOU  995  CE1 TYR A 133     2687   2387   1289   -212     92   -739       C  
ATOM    996  CE2 TYR A 133      15.401  16.120  25.145  1.00 19.33           C  
ANISOU  996  CE2 TYR A 133     3016   2748   1582    -99    174   -760       C  
ATOM    997  CZ  TYR A 133      14.195  15.471  25.359  1.00 22.07           C  
ANISOU  997  CZ  TYR A 133     3402   3054   1930   -169    142   -799       C  
ATOM    998  OH  TYR A 133      14.010  14.191  24.882  1.00 16.64           O  
ANISOU  998  OH  TYR A 133     2773   2310   1238   -176    148   -868       O  
ATOM    999  N   PHE A 134      15.275  22.649  26.427  1.00 14.01           N  
ANISOU  999  N   PHE A 134     2018   2282   1023    -75     36   -322       N  
ATOM   1000  CA  PHE A 134      15.306  24.050  26.821  1.00 12.17           C  
ANISOU 1000  CA  PHE A 134     1731   2063    830    -65      8   -233       C  
ATOM   1001  C   PHE A 134      14.316  24.892  26.033  1.00 14.99           C  
ANISOU 1001  C   PHE A 134     2051   2496   1147   -105    -33   -189       C  
ATOM   1002  O   PHE A 134      13.603  25.719  26.602  1.00 15.37           O  
ANISOU 1002  O   PHE A 134     2072   2530   1238   -110    -67   -139       O  
ATOM   1003  CB  PHE A 134      16.716  24.614  26.658  1.00 14.48           C  
ANISOU 1003  CB  PHE A 134     1997   2375   1128    -25     33   -190       C  
ATOM   1004  CG  PHE A 134      17.573  24.442  27.871  1.00 11.71           C  
ANISOU 1004  CG  PHE A 134     1655   1946    847     16     52   -186       C  
ATOM   1005  CD1 PHE A 134      17.134  24.889  29.105  1.00 11.09           C  
ANISOU 1005  CD1 PHE A 134     1571   1805    837     16     25   -160       C  
ATOM   1006  CD2 PHE A 134      18.814  23.826  27.781  1.00 16.68           C  
ANISOU 1006  CD2 PHE A 134     2295   2573   1471     57     97   -209       C  
ATOM   1007  CE1 PHE A 134      17.916  24.743  30.234  1.00 10.71           C  
ANISOU 1007  CE1 PHE A 134     1529   1694    848     49     39   -154       C  
ATOM   1008  CE2 PHE A 134      19.599  23.672  28.893  1.00 12.84           C  
ANISOU 1008  CE2 PHE A 134     1809   2023   1045     94    111   -198       C  
ATOM   1009  CZ  PHE A 134      19.156  24.131  30.128  1.00 18.07           C  
ANISOU 1009  CZ  PHE A 134     2468   2625   1773     86     80   -169       C  
ATOM   1010  N   ARG A 135      14.257  24.674  24.722  1.00 15.00           N  
ANISOU 1010  N   ARG A 135     2052   2583   1065   -130    -27   -207       N  
ATOM   1011  CA  ARG A 135      13.317  25.396  23.891  1.00 15.06           C  
ANISOU 1011  CA  ARG A 135     2021   2674   1026   -170    -67   -162       C  
ATOM   1012  C   ARG A 135      11.892  25.141  24.369  1.00 15.40           C  
ANISOU 1012  C   ARG A 135     2069   2697   1086   -206   -102   -178       C  
ATOM   1013  O   ARG A 135      11.085  26.067  24.498  1.00 15.30           O  
ANISOU 1013  O   ARG A 135     2014   2706   1095   -214   -140   -114       O  
ATOM   1014  CB  ARG A 135      13.472  24.988  22.423  1.00 14.21           C  
ANISOU 1014  CB  ARG A 135     1918   2666    814   -197    -53   -193       C  
ATOM   1015  CG  ARG A 135      12.503  25.672  21.503  1.00 15.18           C  
ANISOU 1015  CG  ARG A 135     1998   2887    881   -242    -96   -142       C  
ATOM   1016  CD  ARG A 135      12.825  25.364  20.036  1.00 20.04           C  
ANISOU 1016  CD  ARG A 135     2615   3613   1385   -268    -80   -167       C  
ATOM   1017  NE  ARG A 135      12.652  23.944  19.742  1.00 23.43           N  
ANISOU 1017  NE  ARG A 135     3105   4018   1779   -290    -55   -278       N  
ATOM   1018  CZ  ARG A 135      13.044  23.347  18.617  1.00 32.34           C  
ANISOU 1018  CZ  ARG A 135     4252   5185   2849   -296    -27   -324       C  
ATOM   1019  NH1 ARG A 135      13.636  24.048  17.654  1.00 27.53           N  
ANISOU 1019  NH1 ARG A 135     3602   4660   2199   -288    -20   -270       N  
ATOM   1020  NH2 ARG A 135      12.835  22.043  18.450  1.00 31.82           N  
ANISOU 1020  NH2 ARG A 135     4249   5072   2769   -311     -8   -422       N  
ATOM   1021  N   ARG A 136      11.598  23.876  24.639  1.00 13.37           N  
ANISOU 1021  N   ARG A 136     1862   2395    821   -226    -87   -260       N  
ATOM   1022  CA  ARG A 136      10.310  23.491  25.192  1.00 16.54           C  
ANISOU 1022  CA  ARG A 136     2269   2775   1240   -264   -117   -278       C  
ATOM   1023  C   ARG A 136      10.009  24.216  26.497  1.00 12.56           C  
ANISOU 1023  C   ARG A 136     1738   2210    824   -235   -133   -226       C  
ATOM   1024  O   ARG A 136       8.922  24.769  26.660  1.00 18.08           O  
ANISOU 1024  O   ARG A 136     2400   2938   1533   -253   -169   -186       O  
ATOM   1025  CB  ARG A 136      10.265  21.976  25.411  1.00 20.38           C  
ANISOU 1025  CB  ARG A 136     2823   3203   1718   -288    -94   -374       C  
ATOM   1026  CG  ARG A 136       9.052  21.447  26.193  1.00 17.63           C  
ANISOU 1026  CG  ARG A 136     2484   2818   1398   -330   -120   -391       C  
ATOM   1027  CD  ARG A 136       7.732  21.954  25.663  1.00 13.74           C  
ANISOU 1027  CD  ARG A 136     1943   2413    864   -382   -167   -354       C  
ATOM   1028  NE  ARG A 136       7.578  21.720  24.230  1.00 18.23           N  
ANISOU 1028  NE  ARG A 136     2516   3075   1338   -428   -175   -380       N  
ATOM   1029  CZ  ARG A 136       6.540  22.143  23.514  1.00 21.39           C  
ANISOU 1029  CZ  ARG A 136     2869   3564   1696   -471   -214   -342       C  
ATOM   1030  NH1 ARG A 136       5.550  22.811  24.115  1.00 14.70           N  
ANISOU 1030  NH1 ARG A 136     1969   2740    877   -479   -251   -283       N  
ATOM   1031  NH2 ARG A 136       6.478  21.876  22.207  1.00 19.52           N  
ANISOU 1031  NH2 ARG A 136     2633   3383   1401   -498   -213   -357       N  
ATOM   1032  N   VAL A 137      10.971  24.238  27.410  1.00 12.05           N  
ANISOU 1032  N   VAL A 137     1689   2069    820   -187   -107   -225       N  
ATOM   1033  CA  VAL A 137      10.772  24.907  28.685  1.00 11.42           C  
ANISOU 1033  CA  VAL A 137     1590   1932    817   -160   -120   -184       C  
ATOM   1034  C   VAL A 137      10.410  26.374  28.485  1.00 21.65           C  
ANISOU 1034  C   VAL A 137     2831   3270   2126   -148   -151   -103       C  
ATOM   1035  O   VAL A 137       9.463  26.866  29.098  1.00 16.04           O  
ANISOU 1035  O   VAL A 137     2095   2551   1449   -147   -176    -76       O  
ATOM   1036  CB  VAL A 137      12.023  24.813  29.582  1.00 20.62           C  
ANISOU 1036  CB  VAL A 137     2776   3022   2036   -113    -89   -189       C  
ATOM   1037  CG1 VAL A 137      11.872  25.725  30.811  1.00 12.88           C  
ANISOU 1037  CG1 VAL A 137     1772   1995   1128    -87   -106   -142       C  
ATOM   1038  CG2 VAL A 137      12.269  23.372  29.996  1.00 15.23           C  
ANISOU 1038  CG2 VAL A 137     2148   2282   1357   -118    -61   -261       C  
ATOM   1039  N   LEU A 138      11.142  27.058  27.606  1.00 18.69           N  
ANISOU 1039  N   LEU A 138     2436   2942   1724   -136   -148    -63       N  
ATOM   1040  CA  LEU A 138      10.910  28.477  27.349  1.00 16.75           C  
ANISOU 1040  CA  LEU A 138     2143   2728   1495   -124   -178     22       C  
ATOM   1041  C   LEU A 138       9.552  28.774  26.681  1.00 19.84           C  
ANISOU 1041  C   LEU A 138     2498   3192   1848   -154   -214     51       C  
ATOM   1042  O   LEU A 138       8.853  29.706  27.098  1.00 15.52           O  
ANISOU 1042  O   LEU A 138     1917   2637   1344   -137   -241    105       O  
ATOM   1043  CB  LEU A 138      12.033  29.032  26.480  1.00 24.84           C  
ANISOU 1043  CB  LEU A 138     3154   3792   2491   -114   -166     62       C  
ATOM   1044  CG  LEU A 138      13.449  29.080  27.065  1.00 24.93           C  
ANISOU 1044  CG  LEU A 138     3182   3749   2542    -81   -135     60       C  
ATOM   1045  CD1 LEU A 138      14.422  29.685  26.043  1.00 27.08           C  
ANISOU 1045  CD1 LEU A 138     3429   4083   2775    -80   -127    111       C  
ATOM   1046  CD2 LEU A 138      13.479  29.867  28.337  1.00 22.90           C  
ANISOU 1046  CD2 LEU A 138     2921   3412   2369    -53   -148     92       C  
ATOM   1047  N   VAL A 139       9.186  28.018  25.637  1.00 12.60           N  
ANISOU 1047  N   VAL A 139     1586   2349    851   -199   -216     16       N  
ATOM   1048  CA  VAL A 139       7.957  28.323  24.911  1.00 16.48           C  
ANISOU 1048  CA  VAL A 139     2036   2925   1299   -233   -255     52       C  
ATOM   1049  C   VAL A 139       6.710  28.038  25.767  1.00 14.91           C  
ANISOU 1049  C   VAL A 139     1828   2704   1133   -245   -274     37       C  
ATOM   1050  O   VAL A 139       5.669  28.681  25.588  1.00 13.48           O  
ANISOU 1050  O   VAL A 139     1597   2574    950   -249   -308     92       O  
ATOM   1051  CB  VAL A 139       7.849  27.557  23.540  1.00 21.54           C  
ANISOU 1051  CB  VAL A 139     2687   3663   1836   -288   -255     13       C  
ATOM   1052  CG1 VAL A 139       8.968  27.991  22.601  1.00 29.39           C  
ANISOU 1052  CG1 VAL A 139     3676   4703   2788   -275   -237     42       C  
ATOM   1053  CG2 VAL A 139       7.835  26.024  23.713  1.00 19.10           C  
ANISOU 1053  CG2 VAL A 139     2437   3320   1499   -322   -231    -93       C  
ATOM   1054  N   ASP A 140       6.806  27.076  26.683  1.00 16.89           N  
ANISOU 1054  N   ASP A 140     2122   2883   1412   -249   -252    -30       N  
ATOM   1055  CA  ASP A 140       5.699  26.775  27.595  1.00 20.06           C  
ANISOU 1055  CA  ASP A 140     2512   3263   1845   -261   -267    -41       C  
ATOM   1056  C   ASP A 140       5.406  27.976  28.496  1.00 15.86           C  
ANISOU 1056  C   ASP A 140     1942   2698   1386   -207   -278     21       C  
ATOM   1057  O   ASP A 140       4.253  28.283  28.786  1.00 12.86           O  
ANISOU 1057  O   ASP A 140     1521   2348   1017   -209   -302     50       O  
ATOM   1058  CB  ASP A 140       6.010  25.540  28.454  1.00 15.50           C  
ANISOU 1058  CB  ASP A 140     1992   2608   1288   -273   -239   -118       C  
ATOM   1059  CG  ASP A 140       5.763  24.238  27.711  1.00 14.72           C  
ANISOU 1059  CG  ASP A 140     1932   2539   1122   -338   -236   -187       C  
ATOM   1060  OD1 ASP A 140       5.395  24.303  26.516  1.00 14.37           O  
ANISOU 1060  OD1 ASP A 140     1869   2582   1008   -375   -255   -179       O  
ATOM   1061  OD2 ASP A 140       5.928  23.151  28.315  1.00 13.98           O  
ANISOU 1061  OD2 ASP A 140     1888   2379   1044   -354   -216   -248       O  
ATOM   1062  N   ILE A 141       6.463  28.658  28.917  1.00 13.68           N  
ANISOU 1062  N   ILE A 141     1679   2362   1158   -159   -261     42       N  
ATOM   1063  CA  ILE A 141       6.328  29.848  29.751  1.00 16.39           C  
ANISOU 1063  CA  ILE A 141     1996   2661   1570   -107   -270     94       C  
ATOM   1064  C   ILE A 141       5.990  31.053  28.872  1.00 17.55           C  
ANISOU 1064  C   ILE A 141     2095   2864   1708    -92   -299    175       C  
ATOM   1065  O   ILE A 141       5.012  31.765  29.125  1.00 14.69           O  
ANISOU 1065  O   ILE A 141     1693   2516   1373    -69   -321    218       O  
ATOM   1066  CB  ILE A 141       7.630  30.102  30.571  1.00 19.08           C  
ANISOU 1066  CB  ILE A 141     2372   2914   1964    -71   -244     83       C  
ATOM   1067  CG1 ILE A 141       7.950  28.907  31.490  1.00 14.77           C  
ANISOU 1067  CG1 ILE A 141     1869   2313   1429    -81   -218     13       C  
ATOM   1068  CG2 ILE A 141       7.567  31.439  31.350  1.00 11.51           C  
ANISOU 1068  CG2 ILE A 141     1394   1906   1074    -21   -256    134       C  
ATOM   1069  CD1 ILE A 141       6.817  28.522  32.433  1.00 11.85           C  
ANISOU 1069  CD1 ILE A 141     1490   1933   1078    -88   -224     -8       C  
ATOM   1070  N   ASN A 142       6.789  31.245  27.821  1.00 12.07           N  
ANISOU 1070  N   ASN A 142     1405   2207    975   -104   -297    197       N  
ATOM   1071  CA  ASN A 142       6.691  32.399  26.909  1.00 14.78           C  
ANISOU 1071  CA  ASN A 142     1706   2601   1308    -92   -324    284       C  
ATOM   1072  C   ASN A 142       6.972  33.706  27.659  1.00 14.05           C  
ANISOU 1072  C   ASN A 142     1608   2432   1300    -37   -330    339       C  
ATOM   1073  O   ASN A 142       6.082  34.537  27.850  1.00 13.29           O  
ANISOU 1073  O   ASN A 142     1476   2335   1237     -7   -353    389       O  
ATOM   1074  CB  ASN A 142       5.318  32.437  26.203  1.00 16.28           C  
ANISOU 1074  CB  ASN A 142     1847   2886   1454   -116   -357    318       C  
ATOM   1075  CG  ASN A 142       5.318  33.322  24.973  1.00 17.33           C  
ANISOU 1075  CG  ASN A 142     1940   3094   1552   -119   -383    403       C  
ATOM   1076  OD1 ASN A 142       6.358  33.829  24.562  1.00 19.63           O  
ANISOU 1076  OD1 ASN A 142     2241   3372   1844   -110   -375    434       O  
ATOM   1077  ND2 ASN A 142       4.155  33.519  24.387  1.00 20.62           N  
ANISOU 1077  ND2 ASN A 142     2305   3596   1935   -132   -416    448       N  
ATOM   1078  N   PRO A 143       8.223  33.877  28.096  1.00 11.96           N  
ANISOU 1078  N   PRO A 143     1377   2100   1068    -23   -308    328       N  
ATOM   1079  CA  PRO A 143       8.607  35.021  28.921  1.00 13.76           C  
ANISOU 1079  CA  PRO A 143     1610   2242   1374     21   -313    365       C  
ATOM   1080  C   PRO A 143       8.654  36.298  28.097  1.00 15.06           C  
ANISOU 1080  C   PRO A 143     1745   2427   1549     33   -340    460       C  
ATOM   1081  O   PRO A 143       8.668  36.243  26.877  1.00 12.76           O  
ANISOU 1081  O   PRO A 143     1431   2220   1198      5   -350    497       O  
ATOM   1082  CB  PRO A 143       9.990  34.631  29.434  1.00 11.32           C  
ANISOU 1082  CB  PRO A 143     1342   1879   1079     16   -284    325       C  
ATOM   1083  CG  PRO A 143      10.547  33.742  28.354  1.00 16.62           C  
ANISOU 1083  CG  PRO A 143     2017   2623   1673    -22   -268    304       C  
ATOM   1084  CD  PRO A 143       9.363  32.974  27.837  1.00 16.32           C  
ANISOU 1084  CD  PRO A 143     1964   2655   1582    -47   -278    277       C  
ATOM   1085  N   VAL A 144       8.655  37.438  28.770  1.00 18.95           N  
ANISOU 1085  N   VAL A 144     2242   2842   2117     73   -352    500       N  
ATOM   1086  CA  VAL A 144       8.606  38.719  28.081  1.00 12.95           C  
ANISOU 1086  CA  VAL A 144     1457   2084   1380     88   -380    596       C  
ATOM   1087  C   VAL A 144       9.879  39.514  28.329  1.00 14.94           C  
ANISOU 1087  C   VAL A 144     1738   2261   1678     89   -378    626       C  
ATOM   1088  O   VAL A 144      10.619  39.248  29.277  1.00 14.23           O  
ANISOU 1088  O   VAL A 144     1684   2106   1616     88   -358    571       O  
ATOM   1089  CB  VAL A 144       7.405  39.545  28.544  1.00 15.05           C  
ANISOU 1089  CB  VAL A 144     1701   2317   1701    140   -401    630       C  
ATOM   1090  CG1 VAL A 144       6.145  38.728  28.458  1.00 13.33           C  
ANISOU 1090  CG1 VAL A 144     1449   2175   1440    137   -402    599       C  
ATOM   1091  CG2 VAL A 144       7.623  39.990  29.992  1.00 19.68           C  
ANISOU 1091  CG2 VAL A 144     2326   2786   2366    179   -388    589       C  
ATOM   1092  N   ARG A 145      10.136  40.490  27.470  1.00 14.58           N  
ANISOU 1092  N   ARG A 145     1674   2229   1637     84   -402    718       N  
ATOM   1093  CA  ARG A 145      11.246  41.401  27.673  1.00 15.90           C  
ANISOU 1093  CA  ARG A 145     1865   2323   1853     78   -407    760       C  
ATOM   1094  C   ARG A 145      10.792  42.615  28.475  1.00 16.14           C  
ANISOU 1094  C   ARG A 145     1912   2244   1976    125   -427    789       C  
ATOM   1095  O   ARG A 145       9.606  42.891  28.579  1.00 15.25           O  
ANISOU 1095  O   ARG A 145     1781   2129   1884    166   -439    800       O  
ATOM   1096  CB  ARG A 145      11.841  41.844  26.333  1.00 14.67           C  
ANISOU 1096  CB  ARG A 145     1682   2237   1656     43   -423    849       C  
ATOM   1097  CG  ARG A 145      12.498  40.715  25.551  1.00 18.16           C  
ANISOU 1097  CG  ARG A 145     2113   2783   2005      0   -397    815       C  
ATOM   1098  CD  ARG A 145      13.116  41.193  24.235  1.00 17.52           C  
ANISOU 1098  CD  ARG A 145     2001   2780   1876    -35   -410    907       C  
ATOM   1099  NE  ARG A 145      14.244  42.103  24.454  1.00 16.42           N  
ANISOU 1099  NE  ARG A 145     1876   2577   1786    -49   -416    961       N  
ATOM   1100  CZ  ARG A 145      14.168  43.427  24.327  1.00 16.38           C  
ANISOU 1100  CZ  ARG A 145     1867   2516   1839    -43   -450   1056       C  
ATOM   1101  NH1 ARG A 145      13.022  43.990  23.978  1.00 20.71           N  
ANISOU 1101  NH1 ARG A 145     2397   3064   2409    -15   -471   1093       N  
ATOM   1102  NH2 ARG A 145      15.235  44.183  24.550  1.00 16.45           N  
ANISOU 1102  NH2 ARG A 145     1893   2465   1893    -66   -455   1098       N  
ATOM   1103  N   ASP A 146      11.758  43.336  29.028  1.00 19.54           N  
ANISOU 1103  N   ASP A 146     2378   2584   2460    117   -430    801       N  
ATOM   1104  CA  ASP A 146      11.513  44.591  29.732  1.00 18.98           C  
ANISOU 1104  CA  ASP A 146     2335   2397   2481    155   -450    828       C  
ATOM   1105  C   ASP A 146      10.682  45.524  28.848  1.00 23.14           C  
ANISOU 1105  C   ASP A 146     2831   2936   3026    184   -481    927       C  
ATOM   1106  O   ASP A 146      11.020  45.730  27.685  1.00 15.52           O  
ANISOU 1106  O   ASP A 146     1837   2035   2023    151   -497   1007       O  
ATOM   1107  CB  ASP A 146      12.864  45.223  30.111  1.00 17.04           C  
ANISOU 1107  CB  ASP A 146     2127   2074   2274    120   -455    844       C  
ATOM   1108  CG  ASP A 146      12.732  46.406  31.048  1.00 15.93           C  
ANISOU 1108  CG  ASP A 146     2031   1795   2226    152   -472    846       C  
ATOM   1109  OD1 ASP A 146      11.604  46.892  31.266  1.00 17.88           O  
ANISOU 1109  OD1 ASP A 146     2277   2005   2512    211   -479    851       O  
ATOM   1110  OD2 ASP A 146      13.781  46.862  31.550  1.00 17.05           O  
ANISOU 1110  OD2 ASP A 146     2209   1867   2401    118   -477    843       O  
ATOM   1111  N   ASN A 147       9.582  46.058  29.382  1.00 22.35           N  
ANISOU 1111  N   ASN A 147     2731   2782   2979    247   -488    924       N  
ATOM   1112  CA  ASN A 147       8.722  46.945  28.607  1.00 16.26           C  
ANISOU 1112  CA  ASN A 147     1927   2020   2232    285   -518   1022       C  
ATOM   1113  C   ASN A 147       9.150  48.416  28.646  1.00 20.12           C  
ANISOU 1113  C   ASN A 147     2452   2391   2800    296   -535   1079       C  
ATOM   1114  O   ASN A 147       8.456  49.277  28.112  1.00 22.71           O  
ANISOU 1114  O   ASN A 147     2766   2709   3154    328   -545   1131       O  
ATOM   1115  CB  ASN A 147       7.263  46.847  29.096  1.00 17.90           C  
ANISOU 1115  CB  ASN A 147     2109   2234   2457    355   -512    992       C  
ATOM   1116  CG  ASN A 147       7.055  47.431  30.507  1.00 22.67           C  
ANISOU 1116  CG  ASN A 147     2761   2707   3144    412   -499    931       C  
ATOM   1117  OD1 ASN A 147       7.989  47.918  31.150  1.00 24.03           O  
ANISOU 1117  OD1 ASN A 147     2991   2778   3362    395   -497    907       O  
ATOM   1118  ND2 ASN A 147       5.807  47.403  30.976  1.00 20.17           N  
ANISOU 1118  ND2 ASN A 147     2420   2398   2844    478   -490    907       N  
ATOM   1119  N   THR A 148      10.270  48.707  29.301  1.00 22.41           N  
ANISOU 1119  N   THR A 148     2794   2594   3128    264   -535   1058       N  
ATOM   1120  CA  THR A 148      10.676  50.095  29.530  1.00 22.60           C  
ANISOU 1120  CA  THR A 148     2865   2494   3229    267   -546   1087       C  
ATOM   1121  C   THR A 148      12.165  50.326  29.312  1.00 23.48           C  
ANISOU 1121  C   THR A 148     2999   2589   3334    188   -553   1111       C  
ATOM   1122  O   THR A 148      13.002  49.801  30.050  1.00 22.77           O  
ANISOU 1122  O   THR A 148     2935   2477   3240    155   -547   1062       O  
ATOM   1123  CB  THR A 148      10.327  50.554  30.956  1.00 22.55           C  
ANISOU 1123  CB  THR A 148     2913   2356   3299    323   -540   1018       C  
ATOM   1124  OG1 THR A 148       8.906  50.493  31.141  1.00 25.28           O  
ANISOU 1124  OG1 THR A 148     3232   2718   3655    403   -532   1002       O  
ATOM   1125  CG2 THR A 148      10.796  51.989  31.173  1.00 19.66           C  
ANISOU 1125  CG2 THR A 148     2603   1861   3005    319   -551   1040       C  
ATOM   1126  N   LYS A 149      12.488  51.131  28.304  1.00 18.56           N  
ANISOU 1126  N   LYS A 149     2970   1825   2259   -629   -536   1042       N  
ATOM   1127  CA  LYS A 149      13.876  51.443  28.003  1.00 25.32           C  
ANISOU 1127  CA  LYS A 149     3813   2760   3049   -675   -541   1065       C  
ATOM   1128  C   LYS A 149      14.385  52.525  28.930  1.00 22.87           C  
ANISOU 1128  C   LYS A 149     3536   2410   2745   -697   -555   1063       C  
ATOM   1129  O   LYS A 149      13.746  53.557  29.097  1.00 26.51           O  
ANISOU 1129  O   LYS A 149     4037   2791   3244   -700   -606   1071       O  
ATOM   1130  CB  LYS A 149      14.038  51.877  26.542  1.00 30.57           C  
ANISOU 1130  CB  LYS A 149     4473   3462   3678   -710   -607   1114       C  
ATOM   1131  CG  LYS A 149      13.877  50.736  25.528  1.00 33.80           C  
ANISOU 1131  CG  LYS A 149     4849   3935   4058   -698   -592   1120       C  
ATOM   1132  CD  LYS A 149      14.122  51.218  24.098  1.00 38.36           C  
ANISOU 1132  CD  LYS A 149     5428   4554   4592   -730   -651   1171       C  
ATOM   1133  CE  LYS A 149      13.862  50.111  23.076  1.00 44.03           C  
ANISOU 1133  CE  LYS A 149     6121   5331   5277   -714   -643   1177       C  
ATOM   1134  NZ  LYS A 149      14.067  50.577  21.661  1.00 52.56           N  
ANISOU 1134  NZ  LYS A 149     7211   6452   6309   -737   -696   1228       N  
ATOM   1135  N   ALA A 150      15.546  52.282  29.529  1.00 25.48           N  
ANISOU 1135  N   ALA A 150     3849   2793   3041   -712   -514   1053       N  
ATOM   1136  CA  ALA A 150      16.191  53.263  30.390  1.00 28.21           C  
ANISOU 1136  CA  ALA A 150     4225   3109   3383   -750   -545   1059       C  
ATOM   1137  C   ALA A 150      17.492  53.725  29.758  1.00 31.33           C  
ANISOU 1137  C   ALA A 150     4604   3572   3731   -823   -594   1103       C  
ATOM   1138  O   ALA A 150      18.247  52.911  29.229  1.00 31.45           O  
ANISOU 1138  O   ALA A 150     4572   3671   3707   -837   -570   1113       O  
ATOM   1139  CB  ALA A 150      16.452  52.681  31.753  1.00 18.64           C  
ANISOU 1139  CB  ALA A 150     3016   1893   2175   -726   -484   1021       C  
ATOM   1140  N   SER A 151      17.743  55.031  29.799  1.00 20.53           N  
ANISOU 1140  N   SER A 151     3270   2161   2369   -869   -660   1132       N  
ATOM   1141  CA  SER A 151      18.944  55.590  29.195  1.00 29.78           C  
ANISOU 1141  CA  SER A 151     4426   3386   3505   -941   -708   1182       C  
ATOM   1142  C   SER A 151      20.206  54.952  29.775  1.00 29.90           C  
ANISOU 1142  C   SER A 151     4404   3472   3485   -970   -679   1177       C  
ATOM   1143  O   SER A 151      21.172  54.687  29.039  1.00 21.24           O  
ANISOU 1143  O   SER A 151     3263   2453   2354  -1008   -683   1210       O  
ATOM   1144  CB  SER A 151      18.998  57.112  29.391  1.00 29.91           C  
ANISOU 1144  CB  SER A 151     4492   3332   3542   -984   -780   1211       C  
ATOM   1145  OG  SER A 151      17.986  57.765  28.645  1.00 36.38           O  
ANISOU 1145  OG  SER A 151     5338   4095   4389   -964   -814   1228       O  
ATOM   1146  N   ILE A 152      20.186  54.694  31.086  1.00 30.21           N  
ANISOU 1146  N   ILE A 152     4461   3483   3534   -947   -648   1136       N  
ATOM   1147  CA  ILE A 152      21.371  54.188  31.757  1.00 20.40           C  
ANISOU 1147  CA  ILE A 152     3190   2300   2262   -974   -628   1132       C  
ATOM   1148  C   ILE A 152      21.782  52.846  31.172  1.00 24.58           C  
ANISOU 1148  C   ILE A 152     3655   2920   2765   -954   -571   1128       C  
ATOM   1149  O   ILE A 152      22.974  52.532  31.111  1.00 27.73           O  
ANISOU 1149  O   ILE A 152     4012   3390   3134   -991   -571   1148       O  
ATOM   1150  CB  ILE A 152      21.179  54.080  33.300  1.00 28.15           C  
ANISOU 1150  CB  ILE A 152     4208   3233   3256   -944   -597   1089       C  
ATOM   1151  CG1 ILE A 152      22.506  53.708  33.978  1.00 25.22           C  
ANISOU 1151  CG1 ILE A 152     3809   2921   2851   -980   -591   1093       C  
ATOM   1152  CG2 ILE A 152      20.061  53.111  33.684  1.00 19.20           C  
ANISOU 1152  CG2 ILE A 152     3076   2073   2146   -861   -520   1043       C  
ATOM   1153  CD1 ILE A 152      22.433  53.656  35.509  1.00 19.77           C  
ANISOU 1153  CD1 ILE A 152     3161   2186   2165   -956   -566   1057       C  
ATOM   1154  N   THR A 153      20.802  52.067  30.726  1.00 22.26           N  
ANISOU 1154  N   THR A 153     3353   2621   2483   -895   -526   1104       N  
ATOM   1155  CA  THR A 153      21.074  50.794  30.062  1.00 23.50           C  
ANISOU 1155  CA  THR A 153     3454   2857   2616   -872   -474   1099       C  
ATOM   1156  C   THR A 153      21.873  50.996  28.767  1.00 23.73           C  
ANISOU 1156  C   THR A 153     3450   2953   2614   -921   -508   1149       C  
ATOM   1157  O   THR A 153      22.773  50.219  28.455  1.00 23.78           O  
ANISOU 1157  O   THR A 153     3406   3037   2591   -930   -480   1157       O  
ATOM   1158  CB  THR A 153      19.773  50.030  29.756  1.00 22.03           C  
ANISOU 1158  CB  THR A 153     3273   2644   2454   -803   -427   1067       C  
ATOM   1159  OG1 THR A 153      19.076  49.773  30.979  1.00 20.11           O  
ANISOU 1159  OG1 THR A 153     3056   2340   2243   -754   -383   1025       O  
ATOM   1160  CG2 THR A 153      20.069  48.700  29.069  1.00 19.36           C  
ANISOU 1160  CG2 THR A 153     2883   2383   2089   -780   -375   1060       C  
ATOM   1161  N   SER A 154      21.528  52.019  27.999  1.00 20.16           N  
ANISOU 1161  N   SER A 154     3025   2468   2169   -948   -565   1184       N  
ATOM   1162  CA  SER A 154      22.252  52.294  26.760  1.00 24.46           C  
ANISOU 1162  CA  SER A 154     3542   3069   2682   -992   -594   1239       C  
ATOM   1163  C   SER A 154      23.646  52.826  27.057  1.00 28.19           C  
ANISOU 1163  C   SER A 154     3994   3578   3140  -1057   -623   1275       C  
ATOM   1164  O   SER A 154      24.606  52.484  26.367  1.00 23.27           O  
ANISOU 1164  O   SER A 154     3324   3031   2487  -1084   -614   1309       O  
ATOM   1165  CB  SER A 154      21.477  53.275  25.879  1.00 26.46           C  
ANISOU 1165  CB  SER A 154     3834   3273   2948   -999   -646   1271       C  
ATOM   1166  OG  SER A 154      20.211  52.737  25.547  1.00 23.81           O  
ANISOU 1166  OG  SER A 154     3512   2908   2626   -938   -623   1242       O  
ATOM   1167  N   VAL A 155      23.753  53.642  28.103  1.00 27.18           N  
ANISOU 1167  N   VAL A 155     3900   3394   3032  -1082   -659   1269       N  
ATOM   1168  CA  VAL A 155      25.046  54.162  28.531  1.00 30.90           C  
ANISOU 1168  CA  VAL A 155     4355   3894   3493  -1146   -692   1302       C  
ATOM   1169  C   VAL A 155      25.969  53.015  28.950  1.00 31.75           C  
ANISOU 1169  C   VAL A 155     4405   4079   3578  -1139   -642   1286       C  
ATOM   1170  O   VAL A 155      27.164  53.005  28.616  1.00 29.74           O  
ANISOU 1170  O   VAL A 155     4106   3889   3304  -1184   -653   1327       O  
ATOM   1171  CB  VAL A 155      24.887  55.175  29.679  1.00 27.14           C  
ANISOU 1171  CB  VAL A 155     3935   3336   3042  -1168   -738   1290       C  
ATOM   1172  CG1 VAL A 155      26.225  55.491  30.298  1.00 24.33           C  
ANISOU 1172  CG1 VAL A 155     3559   3011   2673  -1228   -768   1315       C  
ATOM   1173  CG2 VAL A 155      24.235  56.459  29.151  1.00 27.07           C  
ANISOU 1173  CG2 VAL A 155     3976   3255   3056  -1187   -797   1320       C  
ATOM   1174  N   ALA A 156      25.409  52.049  29.679  1.00 26.81           N  
ANISOU 1174  N   ALA A 156     3782   3445   2958  -1079   -586   1229       N  
ATOM   1175  CA  ALA A 156      26.174  50.898  30.137  1.00 20.44           C  
ANISOU 1175  CA  ALA A 156     2925   2705   2134  -1062   -533   1210       C  
ATOM   1176  C   ALA A 156      26.596  50.018  28.964  1.00 20.46           C  
ANISOU 1176  C   ALA A 156     2870   2790   2113  -1051   -499   1229       C  
ATOM   1177  O   ALA A 156      27.729  49.551  28.907  1.00 20.65           O  
ANISOU 1177  O   ALA A 156     2843   2885   2119  -1072   -487   1249       O  
ATOM   1178  CB  ALA A 156      25.364  50.076  31.159  1.00 23.68           C  
ANISOU 1178  CB  ALA A 156     3357   3081   2559   -994   -475   1148       C  
ATOM   1179  N   LEU A 157      25.669  49.761  28.050  1.00 25.56           N  
ANISOU 1179  N   LEU A 157     3528   3425   2760  -1016   -481   1222       N  
ATOM   1180  CA  LEU A 157      25.972  48.959  26.870  1.00 26.69           C  
ANISOU 1180  CA  LEU A 157     3627   3639   2876  -1003   -449   1238       C  
ATOM   1181  C   LEU A 157      27.098  49.586  26.052  1.00 23.68           C  
ANISOU 1181  C   LEU A 157     3217   3310   2472  -1064   -486   1305       C  
ATOM   1182  O   LEU A 157      28.070  48.914  25.699  1.00 22.76           O  
ANISOU 1182  O   LEU A 157     3046   3268   2332  -1069   -458   1324       O  
ATOM   1183  CB  LEU A 157      24.727  48.783  26.011  1.00 20.12           C  
ANISOU 1183  CB  LEU A 157     2822   2777   2045   -961   -438   1225       C  
ATOM   1184  CG  LEU A 157      23.714  47.788  26.593  1.00 27.63           C  
ANISOU 1184  CG  LEU A 157     3784   3698   3015   -892   -383   1163       C  
ATOM   1185  CD1 LEU A 157      22.421  47.800  25.790  1.00 23.51           C  
ANISOU 1185  CD1 LEU A 157     3294   3137   2501   -858   -387   1156       C  
ATOM   1186  CD2 LEU A 157      24.301  46.373  26.658  1.00 18.72           C  
ANISOU 1186  CD2 LEU A 157     2605   2637   1869   -860   -317   1139       C  
ATOM   1187  N   ASP A 158      26.998  50.882  25.805  1.00 21.98           N  
ANISOU 1187  N   ASP A 158     3035   3051   2265  -1109   -547   1344       N  
ATOM   1188  CA  ASP A 158      28.024  51.562  25.015  1.00 23.36           C  
ANISOU 1188  CA  ASP A 158     3186   3269   2423  -1168   -581   1415       C  
ATOM   1189  C   ASP A 158      29.381  51.509  25.730  1.00 25.77           C  
ANISOU 1189  C   ASP A 158     3446   3620   2725  -1208   -587   1435       C  
ATOM   1190  O   ASP A 158      30.429  51.455  25.083  1.00 26.63           O  
ANISOU 1190  O   ASP A 158     3508   3795   2814  -1238   -585   1486       O  
ATOM   1191  CB  ASP A 158      27.609  53.009  24.727  1.00 28.00           C  
ANISOU 1191  CB  ASP A 158     3823   3790   3026  -1207   -646   1453       C  
ATOM   1192  CG  ASP A 158      26.565  53.109  23.619  1.00 35.14           C  
ANISOU 1192  CG  ASP A 158     4759   4671   3922  -1175   -645   1460       C  
ATOM   1193  OD1 ASP A 158      26.495  52.188  22.776  1.00 31.89           O  
ANISOU 1193  OD1 ASP A 158     4323   4313   3481  -1140   -599   1457       O  
ATOM   1194  OD2 ASP A 158      25.810  54.109  23.594  1.00 39.02           O  
ANISOU 1194  OD2 ASP A 158     5301   5090   4436  -1184   -691   1470       O  
ATOM   1195  N   ALA A 159      29.361  51.501  27.063  1.00 24.29           N  
ANISOU 1195  N   ALA A 159     3273   3398   2556  -1207   -594   1396       N  
ATOM   1196  CA  ALA A 159      30.598  51.388  27.839  1.00 22.96           C  
ANISOU 1196  CA  ALA A 159     3065   3273   2385  -1241   -602   1411       C  
ATOM   1197  C   ALA A 159      31.228  50.005  27.674  1.00 22.60           C  
ANISOU 1197  C   ALA A 159     2956   3311   2320  -1205   -539   1400       C  
ATOM   1198  O   ALA A 159      32.445  49.870  27.507  1.00 23.11           O  
ANISOU 1198  O   ALA A 159     2967   3442   2373  -1237   -543   1442       O  
ATOM   1199  CB  ALA A 159      30.337  51.685  29.307  1.00 22.57           C  
ANISOU 1199  CB  ALA A 159     3057   3164   2355  -1242   -622   1371       C  
ATOM   1200  N   LEU A 160      30.385  48.981  27.726  1.00 21.76           N  
ANISOU 1200  N   LEU A 160     2856   3198   2213  -1137   -482   1344       N  
ATOM   1201  CA  LEU A 160      30.811  47.604  27.517  1.00 24.83           C  
ANISOU 1201  CA  LEU A 160     3193   3656   2586  -1093   -419   1327       C  
ATOM   1202  C   LEU A 160      31.287  47.388  26.069  1.00 21.97           C  
ANISOU 1202  C   LEU A 160     2794   3357   2196  -1100   -405   1372       C  
ATOM   1203  O   LEU A 160      32.221  46.619  25.820  1.00 22.97           O  
ANISOU 1203  O   LEU A 160     2865   3555   2306  -1092   -373   1389       O  
ATOM   1204  CB  LEU A 160      29.664  46.642  27.864  1.00 20.41           C  
ANISOU 1204  CB  LEU A 160     2656   3062   2035  -1020   -363   1258       C  
ATOM   1205  CG  LEU A 160      29.173  46.647  29.326  1.00 29.43           C  
ANISOU 1205  CG  LEU A 160     3835   4147   3202   -999   -358   1211       C  
ATOM   1206  CD1 LEU A 160      27.901  45.806  29.496  1.00 18.94           C  
ANISOU 1206  CD1 LEU A 160     2533   2777   1886   -925   -302   1152       C  
ATOM   1207  CD2 LEU A 160      30.257  46.156  30.290  1.00 20.20           C  
ANISOU 1207  CD2 LEU A 160     2626   3020   2027  -1006   -346   1211       C  
ATOM   1208  N   ARG A 161      30.649  48.066  25.122  1.00 22.48           N  
ANISOU 1208  N   ARG A 161     2893   3394   2255  -1110   -427   1394       N  
ATOM   1209  CA  ARG A 161      31.089  48.017  23.716  1.00 24.36           C  
ANISOU 1209  CA  ARG A 161     3108   3687   2462  -1118   -416   1445       C  
ATOM   1210  C   ARG A 161      32.550  48.439  23.623  1.00 25.54           C  
ANISOU 1210  C   ARG A 161     3209   3892   2604  -1173   -437   1511       C  
ATOM   1211  O   ARG A 161      33.362  47.761  22.991  1.00 24.22           O  
ANISOU 1211  O   ARG A 161     2994   3798   2412  -1163   -400   1538       O  
ATOM   1212  CB  ARG A 161      30.221  48.912  22.825  1.00 23.42           C  
ANISOU 1212  CB  ARG A 161     3040   3520   2337  -1129   -448   1468       C  
ATOM   1213  CG  ARG A 161      30.353  48.640  21.316  1.00 26.93           C  
ANISOU 1213  CG  ARG A 161     3476   4015   2741  -1116   -421   1508       C  
ATOM   1214  CD  ARG A 161      29.470  49.570  20.492  1.00 24.43           C  
ANISOU 1214  CD  ARG A 161     3215   3650   2418  -1124   -457   1534       C  
ATOM   1215  NE  ARG A 161      28.197  49.806  21.159  1.00 30.94           N  
ANISOU 1215  NE  ARG A 161     4089   4394   3275  -1102   -478   1482       N  
ATOM   1216  CZ  ARG A 161      27.205  48.920  21.222  1.00 33.31           C  
ANISOU 1216  CZ  ARG A 161     4404   4677   3576  -1043   -443   1423       C  
ATOM   1217  NH1 ARG A 161      27.324  47.746  20.616  1.00 30.18           N  
ANISOU 1217  NH1 ARG A 161     3981   4336   3148  -1003   -388   1407       N  
ATOM   1218  NH2 ARG A 161      26.088  49.215  21.884  1.00 27.59           N  
ANISOU 1218  NH2 ARG A 161     3721   3876   2885  -1024   -463   1382       N  
ATOM   1219  N   ILE A 162      32.878  49.551  24.275  1.00 24.30           N  
ANISOU 1219  N   ILE A 162     3066   3699   2468  -1230   -497   1538       N  
ATOM   1220  CA  ILE A 162      34.250  50.075  24.280  1.00 25.19           C  
ANISOU 1220  CA  ILE A 162     3135   3857   2579  -1289   -527   1606       C  
ATOM   1221  C   ILE A 162      35.264  49.087  24.859  1.00 24.99           C  
ANISOU 1221  C   ILE A 162     3046   3900   2550  -1276   -494   1599       C  
ATOM   1222  O   ILE A 162      36.304  48.817  24.246  1.00 25.63           O  
ANISOU 1222  O   ILE A 162     3073   4051   2613  -1287   -477   1651       O  
ATOM   1223  CB  ILE A 162      34.327  51.399  25.060  1.00 29.64           C  
ANISOU 1223  CB  ILE A 162     3731   4359   3170  -1351   -601   1626       C  
ATOM   1224  CG1 ILE A 162      33.531  52.484  24.328  1.00 32.54           C  
ANISOU 1224  CG1 ILE A 162     4155   4666   3542  -1369   -637   1652       C  
ATOM   1225  CG2 ILE A 162      35.763  51.862  25.191  1.00 31.58           C  
ANISOU 1225  CG2 ILE A 162     3929   4653   3419  -1412   -633   1695       C  
ATOM   1226  CD1 ILE A 162      33.522  53.801  25.052  1.00 33.43           C  
ANISOU 1226  CD1 ILE A 162     4309   4710   3685  -1426   -710   1670       C  
ATOM   1227  N   ILE A 163      34.953  48.551  26.045  1.00 24.16           N  
ANISOU 1227  N   ILE A 163     2948   3770   2459  -1248   -484   1538       N  
ATOM   1228  CA  ILE A 163      35.832  47.603  26.714  1.00 23.93           C  
ANISOU 1228  CA  ILE A 163     2865   3799   2428  -1230   -455   1529       C  
ATOM   1229  C   ILE A 163      36.001  46.343  25.861  1.00 26.90           C  
ANISOU 1229  C   ILE A 163     3200   4238   2782  -1174   -386   1522       C  
ATOM   1230  O   ILE A 163      37.118  45.849  25.676  1.00 27.08           O  
ANISOU 1230  O   ILE A 163     3164   4333   2794  -1177   -368   1559       O  
ATOM   1231  CB  ILE A 163      35.291  47.223  28.127  1.00 23.04           C  
ANISOU 1231  CB  ILE A 163     2780   3641   2333  -1202   -448   1462       C  
ATOM   1232  CG1 ILE A 163      35.136  48.486  28.987  1.00 23.25           C  
ANISOU 1232  CG1 ILE A 163     2855   3601   2378  -1256   -517   1468       C  
ATOM   1233  CG2 ILE A 163      36.203  46.186  28.782  1.00 23.75           C  
ANISOU 1233  CG2 ILE A 163     2813   3791   2419  -1178   -416   1455       C  
ATOM   1234  CD1 ILE A 163      34.472  48.267  30.332  1.00 22.46           C  
ANISOU 1234  CD1 ILE A 163     2798   3445   2292  -1227   -509   1404       C  
ATOM   1235  N   ALA A 164      34.882  45.831  25.351  1.00 23.21           N  
ANISOU 1235  N   ALA A 164     2768   3743   2307  -1123   -348   1476       N  
ATOM   1236  CA  ALA A 164      34.894  44.673  24.461  1.00 26.25           C  
ANISOU 1236  CA  ALA A 164     3127   4178   2668  -1070   -285   1465       C  
ATOM   1237  C   ALA A 164      35.834  44.929  23.280  1.00 25.00           C  
ANISOU 1237  C   ALA A 164     2935   4083   2483  -1098   -283   1539       C  
ATOM   1238  O   ALA A 164      36.646  44.071  22.909  1.00 24.36           O  
ANISOU 1238  O   ALA A 164     2804   4067   2383  -1074   -241   1556       O  
ATOM   1239  CB  ALA A 164      33.477  44.347  23.974  1.00 22.47           C  
ANISOU 1239  CB  ALA A 164     2701   3652   2185  -1023   -259   1414       C  
ATOM   1240  N   GLU A 165      35.721  46.118  22.701  1.00 24.79           N  
ANISOU 1240  N   GLU A 165     2935   4031   2452  -1145   -327   1586       N  
ATOM   1241  CA  GLU A 165      36.594  46.508  21.613  1.00 25.88           C  
ANISOU 1241  CA  GLU A 165     3046   4221   2565  -1175   -325   1664       C  
ATOM   1242  C   GLU A 165      38.061  46.468  22.061  1.00 26.51           C  
ANISOU 1242  C   GLU A 165     3059   4360   2653  -1207   -333   1713       C  
ATOM   1243  O   GLU A 165      38.910  45.926  21.352  1.00 27.00           O  
ANISOU 1243  O   GLU A 165     3076   4490   2691  -1194   -294   1754       O  
ATOM   1244  CB  GLU A 165      36.218  47.896  21.094  1.00 26.53           C  
ANISOU 1244  CB  GLU A 165     3173   4257   2649  -1224   -376   1709       C  
ATOM   1245  CG  GLU A 165      37.017  48.320  19.870  1.00 39.05           C  
ANISOU 1245  CG  GLU A 165     4739   5892   4206  -1249   -367   1794       C  
ATOM   1246  CD  GLU A 165      37.199  47.175  18.871  1.00 45.95           C  
ANISOU 1246  CD  GLU A 165     5594   6829   5037  -1194   -294   1792       C  
ATOM   1247  OE1 GLU A 165      38.348  46.916  18.445  1.00 49.96           O  
ANISOU 1247  OE1 GLU A 165     6051   7404   5529  -1201   -268   1847       O  
ATOM   1248  OE2 GLU A 165      36.192  46.521  18.518  1.00 45.56           O  
ANISOU 1248  OE2 GLU A 165     5581   6761   4971  -1142   -264   1737       O  
ATOM   1249  N   GLN A 166      38.333  46.975  23.268  1.00 26.27           N  
ANISOU 1249  N   GLN A 166     3024   4305   2654  -1244   -382   1708       N  
ATOM   1250  CA  GLN A 166      39.692  46.997  23.819  1.00 26.80           C  
ANISOU 1250  CA  GLN A 166     3029   4423   2730  -1279   -399   1756       C  
ATOM   1251  C   GLN A 166      40.245  45.583  23.923  1.00 32.80           C  
ANISOU 1251  C   GLN A 166     3737   5247   3479  -1223   -340   1735       C  
ATOM   1252  O   GLN A 166      41.355  45.305  23.474  1.00 29.18           O  
ANISOU 1252  O   GLN A 166     3222   4857   3009  -1228   -321   1792       O  
ATOM   1253  CB  GLN A 166      39.713  47.619  25.229  1.00 38.58           C  
ANISOU 1253  CB  GLN A 166     4536   5870   4252  -1319   -459   1738       C  
ATOM   1254  CG  GLN A 166      39.448  49.117  25.369  1.00 39.20           C  
ANISOU 1254  CG  GLN A 166     4662   5885   4349  -1385   -530   1767       C  
ATOM   1255  CD  GLN A 166      39.166  49.557  26.835  1.00 51.79           C  
ANISOU 1255  CD  GLN A 166     6290   7420   5967  -1409   -579   1726       C  
ATOM   1256  OE1 GLN A 166      39.136  48.734  27.764  1.00 46.41           O  
ANISOU 1256  OE1 GLN A 166     5599   6746   5288  -1374   -557   1676       O  
ATOM   1257  NE2 GLN A 166      38.944  50.859  27.028  1.00 49.16           N  
ANISOU 1257  NE2 GLN A 166     6002   7025   5650  -1466   -644   1749       N  
ATOM   1258  N   GLN A 167      39.440  44.685  24.488  1.00 25.44           N  
ANISOU 1258  N   GLN A 167     2826   4289   2551  -1166   -308   1657       N  
ATOM   1259  CA  GLN A 167      39.814  43.287  24.659  1.00 31.89           C  
ANISOU 1259  CA  GLN A 167     3601   5154   3360  -1106   -250   1629       C  
ATOM   1260  C   GLN A 167      40.028  42.552  23.331  1.00 25.45           C  
ANISOU 1260  C   GLN A 167     2766   4389   2513  -1068   -192   1649       C  
ATOM   1261  O   GLN A 167      41.030  41.868  23.154  1.00 25.85           O  
ANISOU 1261  O   GLN A 167     2762   4505   2555  -1050   -161   1680       O  
ATOM   1262  CB  GLN A 167      38.748  42.558  25.495  1.00 26.30           C  
ANISOU 1262  CB  GLN A 167     2930   4396   2667  -1054   -227   1541       C  
ATOM   1263  CG  GLN A 167      38.575  43.100  26.909  1.00 23.48           C  
ANISOU 1263  CG  GLN A 167     2595   3991   2336  -1081   -272   1517       C  
ATOM   1264  CD  GLN A 167      37.600  42.267  27.739  1.00 22.41           C  
ANISOU 1264  CD  GLN A 167     2492   3810   2213  -1021   -235   1436       C  
ATOM   1265  OE1 GLN A 167      37.009  41.304  27.241  1.00 21.95           O  
ANISOU 1265  OE1 GLN A 167     2441   3752   2147   -961   -180   1397       O  
ATOM   1266  NE2 GLN A 167      37.425  42.641  29.004  1.00 22.06           N  
ANISOU 1266  NE2 GLN A 167     2471   3724   2186  -1036   -264   1412       N  
ATOM   1267  N   ILE A 168      39.059  42.652  22.426  1.00 25.33           N  
ANISOU 1267  N   ILE A 168     2800   4344   2479  -1051   -175   1629       N  
ATOM   1268  CA  ILE A 168      39.208  42.067  21.084  1.00 30.37           C  
ANISOU 1268  CA  ILE A 168     3433   5027   3080  -1018   -122   1650       C  
ATOM   1269  C   ILE A 168      40.497  42.536  20.396  1.00 27.03           C  
ANISOU 1269  C   ILE A 168     2964   4666   2640  -1056   -124   1742       C  
ATOM   1270  O   ILE A 168      41.304  41.723  19.943  1.00 29.37           O  
ANISOU 1270  O   ILE A 168     3218   5023   2917  -1026    -77   1765       O  
ATOM   1271  CB  ILE A 168      38.010  42.401  20.181  1.00 25.69           C  
ANISOU 1271  CB  ILE A 168     2906   4389   2465  -1008   -118   1630       C  
ATOM   1272  CG1 ILE A 168      36.748  41.711  20.700  1.00 24.52           C  
ANISOU 1272  CG1 ILE A 168     2798   4188   2331   -959   -101   1541       C  
ATOM   1273  CG2 ILE A 168      38.271  41.949  18.752  1.00 26.38           C  
ANISOU 1273  CG2 ILE A 168     2993   4525   2504   -982    -67   1662       C  
ATOM   1274  CD1 ILE A 168      35.478  42.247  20.089  1.00 24.34           C  
ANISOU 1274  CD1 ILE A 168     2842   4110   2297   -958   -116   1522       C  
ATOM   1275  N   ALA A 169      40.706  43.845  20.370  1.00 27.66           N  
ANISOU 1275  N   ALA A 169     3052   4727   2729  -1121   -179   1795       N  
ATOM   1276  CA  ALA A 169      41.874  44.429  19.702  1.00 28.91           C  
ANISOU 1276  CA  ALA A 169     3170   4937   2877  -1162   -183   1890       C  
ATOM   1277  C   ALA A 169      43.202  43.950  20.283  1.00 29.25           C  
ANISOU 1277  C   ALA A 169     3137   5041   2934  -1166   -176   1925       C  
ATOM   1278  O   ALA A 169      44.191  43.821  19.564  1.00 30.18           O  
ANISOU 1278  O   ALA A 169     3214   5220   3035  -1167   -146   1992       O  
ATOM   1279  CB  ALA A 169      41.801  45.949  19.762  1.00 29.46           C  
ANISOU 1279  CB  ALA A 169     3265   4963   2964  -1234   -250   1937       C  
ATOM   1280  N   SER A 170      43.219  43.685  21.587  1.00 33.80           N  
ANISOU 1280  N   SER A 170     3699   5602   3541  -1165   -203   1883       N  
ATOM   1281  CA  SER A 170      44.448  43.349  22.289  1.00 28.84           C  
ANISOU 1281  CA  SER A 170     3002   5028   2929  -1174   -210   1919       C  
ATOM   1282  C   SER A 170      44.980  41.966  21.923  1.00 33.06           C  
ANISOU 1282  C   SER A 170     3494   5623   3445  -1108   -139   1913       C  
ATOM   1283  O   SER A 170      46.144  41.657  22.173  1.00 29.38           O  
ANISOU 1283  O   SER A 170     2964   5213   2985  -1110   -134   1962       O  
ATOM   1284  CB  SER A 170      44.227  43.423  23.802  1.00 28.06           C  
ANISOU 1284  CB  SER A 170     2908   4892   2861  -1187   -256   1873       C  
ATOM   1285  OG  SER A 170      43.587  42.248  24.283  1.00 27.74           O  
ANISOU 1285  OG  SER A 170     2881   4839   2820  -1119   -214   1792       O  
ATOM   1286  N   GLY A 171      44.114  41.116  21.381  1.00 30.25           N  
ANISOU 1286  N   GLY A 171     3174   5251   3066  -1047    -87   1853       N  
ATOM   1287  CA  GLY A 171      44.495  39.764  21.009  1.00 28.23           C  
ANISOU 1287  CA  GLY A 171     2890   5043   2793   -981    -18   1840       C  
ATOM   1288  C   GLY A 171      44.644  38.824  22.198  1.00 29.87           C  
ANISOU 1288  C   GLY A 171     3071   5253   3025   -943    -12   1793       C  
ATOM   1289  O   GLY A 171      45.021  37.658  22.038  1.00 28.55           O  
ANISOU 1289  O   GLY A 171     2877   5122   2848   -886     42   1783       O  
ATOM   1290  N   GLU A 172      44.327  39.327  23.387  1.00 26.91           N  
ANISOU 1290  N   GLU A 172     2707   4837   2679   -972    -65   1766       N  
ATOM   1291  CA  GLU A 172      44.362  38.528  24.609  1.00 28.76           C  
ANISOU 1291  CA  GLU A 172     2926   5067   2936   -938    -62   1721       C  
ATOM   1292  C   GLU A 172      43.383  37.378  24.487  1.00 27.96           C  
ANISOU 1292  C   GLU A 172     2861   4935   2829   -864     -5   1642       C  
ATOM   1293  O   GLU A 172      42.249  37.586  24.095  1.00 33.36           O  
ANISOU 1293  O   GLU A 172     3602   5567   3505   -858     -1   1598       O  
ATOM   1294  CB  GLU A 172      44.028  39.404  25.809  1.00 37.65           C  
ANISOU 1294  CB  GLU A 172     4074   6145   4087   -985   -127   1704       C  
ATOM   1295  CG  GLU A 172      44.168  38.745  27.163  1.00 52.50           C  
ANISOU 1295  CG  GLU A 172     5939   8022   5987   -958   -129   1668       C  
ATOM   1296  CD  GLU A 172      45.126  39.497  28.079  1.00 54.88           C  
ANISOU 1296  CD  GLU A 172     6203   8345   6303  -1020   -191   1721       C  
ATOM   1297  OE1 GLU A 172      45.808  38.840  28.899  1.00 48.84           O  
ANISOU 1297  OE1 GLU A 172     5397   7615   5547   -998   -186   1727       O  
ATOM   1298  OE2 GLU A 172      45.178  40.746  27.992  1.00 60.22           O  
ANISOU 1298  OE2 GLU A 172     6894   9003   6984  -1089   -247   1756       O  
ATOM   1299  N   PRO A 173      43.829  36.159  24.804  1.00 26.94           N  
ANISOU 1299  N   PRO A 173     2699   4836   2703   -807     38   1628       N  
ATOM   1300  CA  PRO A 173      43.049  34.932  24.577  1.00 24.47           C  
ANISOU 1300  CA  PRO A 173     2416   4498   2384   -735     99   1561       C  
ATOM   1301  C   PRO A 173      41.756  34.838  25.391  1.00 23.39           C  
ANISOU 1301  C   PRO A 173     2334   4285   2267   -716     93   1483       C  
ATOM   1302  O   PRO A 173      40.746  34.330  24.887  1.00 23.03           O  
ANISOU 1302  O   PRO A 173     2334   4202   2215   -680    128   1430       O  
ATOM   1303  CB  PRO A 173      44.016  33.812  24.997  1.00 24.65           C  
ANISOU 1303  CB  PRO A 173     2383   4569   2413   -688    133   1577       C  
ATOM   1304  CG  PRO A 173      45.050  34.483  25.851  1.00 25.10           C  
ANISOU 1304  CG  PRO A 173     2390   4661   2486   -736     80   1634       C  
ATOM   1305  CD  PRO A 173      45.171  35.881  25.346  1.00 25.99           C  
ANISOU 1305  CD  PRO A 173     2509   4776   2591   -810     31   1682       C  
ATOM   1306  N   VAL A 174      41.795  35.264  26.651  1.00 25.40           N  
ANISOU 1306  N   VAL A 174     2586   4518   2546   -739     52   1475       N  
ATOM   1307  CA  VAL A 174      40.610  35.225  27.502  1.00 22.10           C  
ANISOU 1307  CA  VAL A 174     2221   4027   2148   -722     51   1406       C  
ATOM   1308  C   VAL A 174      40.447  36.512  28.310  1.00 23.63           C  
ANISOU 1308  C   VAL A 174     2436   4187   2355   -784    -14   1414       C  
ATOM   1309  O   VAL A 174      41.374  36.952  28.982  1.00 26.25           O  
ANISOU 1309  O   VAL A 174     2731   4550   2692   -822    -53   1457       O  
ATOM   1310  CB  VAL A 174      40.643  34.031  28.474  1.00 21.56           C  
ANISOU 1310  CB  VAL A 174     2142   3953   2098   -660     89   1368       C  
ATOM   1311  CG1 VAL A 174      39.338  33.944  29.248  1.00 20.62           C  
ANISOU 1311  CG1 VAL A 174     2083   3755   1998   -636     98   1297       C  
ATOM   1312  CG2 VAL A 174      40.898  32.737  27.731  1.00 21.68           C  
ANISOU 1312  CG2 VAL A 174     2137   3999   2103   -600    151   1363       C  
ATOM   1313  N   ASP A 175      39.260  37.106  28.234  1.00 21.59           N  
ANISOU 1313  N   ASP A 175     2238   3864   2100   -795    -27   1375       N  
ATOM   1314  CA  ASP A 175      38.906  38.268  29.041  1.00 21.46           C  
ANISOU 1314  CA  ASP A 175     2257   3801   2097   -848    -83   1373       C  
ATOM   1315  C   ASP A 175      37.380  38.378  29.032  1.00 20.71           C  
ANISOU 1315  C   ASP A 175     2232   3628   2011   -824    -70   1311       C  
ATOM   1316  O   ASP A 175      36.717  37.709  28.236  1.00 20.44           O  
ANISOU 1316  O   ASP A 175     2213   3584   1969   -781    -26   1282       O  
ATOM   1317  CB  ASP A 175      39.579  39.544  28.524  1.00 23.86           C  
ANISOU 1317  CB  ASP A 175     2545   4128   2392   -925   -142   1440       C  
ATOM   1318  CG  ASP A 175      39.875  40.535  29.633  1.00 26.99           C  
ANISOU 1318  CG  ASP A 175     2950   4502   2802   -983   -204   1457       C  
ATOM   1319  OD1 ASP A 175      39.354  40.350  30.755  1.00 28.39           O  
ANISOU 1319  OD1 ASP A 175     3159   4637   2994   -964   -201   1409       O  
ATOM   1320  OD2 ASP A 175      40.633  41.501  29.386  1.00 25.14           O  
ANISOU 1320  OD2 ASP A 175     2695   4292   2565  -1049   -256   1519       O  
ATOM   1321  N   PHE A 176      36.818  39.181  29.930  1.00 26.31           N  
ANISOU 1321  N   PHE A 176     2984   4279   2734   -851   -105   1291       N  
ATOM   1322  CA  PHE A 176      35.427  38.954  30.325  1.00 22.06           C  
ANISOU 1322  CA  PHE A 176     2505   3666   2210   -810    -77   1226       C  
ATOM   1323  C   PHE A 176      34.359  39.371  29.324  1.00 24.75           C  
ANISOU 1323  C   PHE A 176     2890   3968   2547   -811    -78   1211       C  
ATOM   1324  O   PHE A 176      33.179  39.039  29.523  1.00 18.78           O  
ANISOU 1324  O   PHE A 176     2178   3155   1803   -769    -49   1159       O  
ATOM   1325  CB  PHE A 176      35.140  39.613  31.691  1.00 20.29           C  
ANISOU 1325  CB  PHE A 176     2319   3389   2000   -830   -106   1207       C  
ATOM   1326  CG  PHE A 176      35.300  41.114  31.721  1.00 19.82           C  
ANISOU 1326  CG  PHE A 176     2281   3309   1939   -907   -179   1244       C  
ATOM   1327  CD1 PHE A 176      34.218  41.947  31.473  1.00 19.65           C  
ANISOU 1327  CD1 PHE A 176     2320   3222   1924   -920   -200   1226       C  
ATOM   1328  CD2 PHE A 176      36.518  41.688  32.060  1.00 22.24           C  
ANISOU 1328  CD2 PHE A 176     2551   3660   2241   -965   -228   1297       C  
ATOM   1329  CE1 PHE A 176      34.357  43.319  31.530  1.00 20.16           C  
ANISOU 1329  CE1 PHE A 176     2409   3261   1990   -989   -269   1260       C  
ATOM   1330  CE2 PHE A 176      36.665  43.058  32.118  1.00 21.01           C  
ANISOU 1330  CE2 PHE A 176     2417   3479   2085  -1037   -296   1331       C  
ATOM   1331  CZ  PHE A 176      35.582  43.877  31.852  1.00 20.84           C  
ANISOU 1331  CZ  PHE A 176     2460   3389   2071  -1049   -317   1312       C  
ATOM   1332  N   LEU A 177      34.745  40.038  28.239  1.00 20.14           N  
ANISOU 1332  N   LEU A 177     2293   3415   1944   -853   -108   1259       N  
ATOM   1333  CA  LEU A 177      33.756  40.422  27.223  1.00 20.10           C  
ANISOU 1333  CA  LEU A 177     2330   3377   1931   -853   -110   1251       C  
ATOM   1334  C   LEU A 177      34.001  39.759  25.870  1.00 20.45           C  
ANISOU 1334  C   LEU A 177     2350   3473   1948   -832    -75   1269       C  
ATOM   1335  O   LEU A 177      33.318  40.066  24.898  1.00 20.57           O  
ANISOU 1335  O   LEU A 177     2395   3471   1948   -834    -77   1271       O  
ATOM   1336  CB  LEU A 177      33.717  41.940  27.047  1.00 20.63           C  
ANISOU 1336  CB  LEU A 177     2423   3418   1999   -921   -177   1291       C  
ATOM   1337  CG  LEU A 177      32.809  42.698  28.023  1.00 20.96           C  
ANISOU 1337  CG  LEU A 177     2522   3379   2064   -932   -208   1258       C  
ATOM   1338  CD1 LEU A 177      33.248  44.154  28.127  1.00 20.87           C  
ANISOU 1338  CD1 LEU A 177     2522   3352   2055  -1008   -281   1307       C  
ATOM   1339  CD2 LEU A 177      31.339  42.626  27.638  1.00 19.63           C  
ANISOU 1339  CD2 LEU A 177     2407   3150   1902   -895   -189   1215       C  
ATOM   1340  N   LEU A 178      34.948  38.828  25.822  1.00 23.74           N  
ANISOU 1340  N   LEU A 178     2715   3950   2356   -807    -40   1281       N  
ATOM   1341  CA  LEU A 178      35.258  38.092  24.597  1.00 21.77           C  
ANISOU 1341  CA  LEU A 178     2444   3750   2077   -781      1   1296       C  
ATOM   1342  C   LEU A 178      34.233  36.983  24.336  1.00 20.33           C  
ANISOU 1342  C   LEU A 178     2291   3538   1894   -717     55   1234       C  
ATOM   1343  O   LEU A 178      33.820  36.290  25.257  1.00 19.63           O  
ANISOU 1343  O   LEU A 178     2210   3418   1832   -678     80   1186       O  
ATOM   1344  CB  LEU A 178      36.656  37.477  24.681  1.00 21.53           C  
ANISOU 1344  CB  LEU A 178     2348   3791   2040   -775     19   1334       C  
ATOM   1345  CG  LEU A 178      37.817  38.457  24.803  1.00 22.44           C  
ANISOU 1345  CG  LEU A 178     2426   3948   2154   -838    -31   1405       C  
ATOM   1346  CD1 LEU A 178      39.131  37.713  24.744  1.00 22.87           C  
ANISOU 1346  CD1 LEU A 178     2414   4075   2200   -823     -5   1444       C  
ATOM   1347  CD2 LEU A 178      37.733  39.521  23.699  1.00 23.04           C  
ANISOU 1347  CD2 LEU A 178     2521   4025   2209   -886    -60   1452       C  
ATOM   1348  N   ASN A 179      33.821  36.823  23.079  1.00 18.38           N  
ANISOU 1348  N   ASN A 179     1918   3451   1613   -509    125    648       N  
ATOM   1349  CA  ASN A 179      32.903  35.748  22.715  1.00 17.98           C  
ANISOU 1349  CA  ASN A 179     1910   3371   1549   -435    167    563       C  
ATOM   1350  C   ASN A 179      33.302  35.098  21.405  1.00 20.06           C  
ANISOU 1350  C   ASN A 179     2146   3733   1744   -441    272    522       C  
ATOM   1351  O   ASN A 179      33.274  35.741  20.354  1.00 24.73           O  
ANISOU 1351  O   ASN A 179     2760   4387   2248   -521    275    556       O  
ATOM   1352  CB  ASN A 179      31.479  36.269  22.629  1.00 17.32           C  
ANISOU 1352  CB  ASN A 179     1931   3208   1441   -449     92    560       C  
ATOM   1353  CG  ASN A 179      30.470  35.165  22.370  1.00 16.91           C  
ANISOU 1353  CG  ASN A 179     1922   3127   1377   -384    124    473       C  
ATOM   1354  OD1 ASN A 179      30.265  34.275  23.201  1.00 16.39           O  
ANISOU 1354  OD1 ASN A 179     1846   3007   1375   -307    136    421       O  
ATOM   1355  ND2 ASN A 179      29.854  35.202  21.192  1.00 18.33           N  
ANISOU 1355  ND2 ASN A 179     2145   3350   1468   -425    137    460       N  
ATOM   1356  N   LYS A 180      33.673  33.822  21.466  1.00 19.10           N  
ANISOU 1356  N   LYS A 180     1974   3621   1661   -358    363    451       N  
ATOM   1357  CA  LYS A 180      34.313  33.169  20.331  1.00 22.53           C  
ANISOU 1357  CA  LYS A 180     2365   4152   2043   -359    485    402       C  
ATOM   1358  C   LYS A 180      33.434  33.143  19.095  1.00 21.83           C  
ANISOU 1358  C   LYS A 180     2358   4096   1840   -413    504    351       C  
ATOM   1359  O   LYS A 180      33.916  33.379  17.984  1.00 21.46           O  
ANISOU 1359  O   LYS A 180     2293   4161   1701   -480    563    356       O  
ATOM   1360  CB  LYS A 180      34.741  31.742  20.694  1.00 23.26           C  
ANISOU 1360  CB  LYS A 180     2400   4219   2221   -245    584    327       C  
ATOM   1361  N   ALA A 181      32.143  32.909  19.281  1.00 19.66           N  
ANISOU 1361  N   ALA A 181     2168   3740   1561   -394    450    310       N  
ATOM   1362  CA  ALA A 181      31.275  32.638  18.141  1.00 24.23           C  
ANISOU 1362  CA  ALA A 181     2815   4361   2032   -441    473    251       C  
ATOM   1363  C   ALA A 181      30.904  33.868  17.311  1.00 24.15           C  
ANISOU 1363  C   ALA A 181     2843   4418   1914   -550    403    339       C  
ATOM   1364  O   ALA A 181      30.335  33.727  16.232  1.00 24.49           O  
ANISOU 1364  O   ALA A 181     2929   4533   1845   -608    422    307       O  
ATOM   1365  CB  ALA A 181      29.995  31.938  18.614  1.00 21.45           C  
ANISOU 1365  CB  ALA A 181     2530   3908   1711   -389    437    184       C  
ATOM   1366  N   THR A 182      31.218  35.069  17.786  1.00 21.12           N  
ANISOU 1366  N   THR A 182     2446   4015   1562   -586    322    452       N  
ATOM   1367  CA  THR A 182      30.746  36.251  17.070  1.00 20.41           C  
ANISOU 1367  CA  THR A 182     2399   3962   1392   -681    248    550       C  
ATOM   1368  C   THR A 182      31.872  37.033  16.369  1.00 26.15           C  
ANISOU 1368  C   THR A 182     3076   4798   2061   -770    278    633       C  
ATOM   1369  O   THR A 182      31.716  38.206  16.031  1.00 24.31           O  
ANISOU 1369  O   THR A 182     2868   4556   1813   -839    202    735       O  
ATOM   1370  CB  THR A 182      29.945  37.179  18.018  1.00 26.11           C  
ANISOU 1370  CB  THR A 182     3169   4559   2192   -667    125    622       C  
ATOM   1371  OG1 THR A 182      30.622  37.317  19.272  1.00 18.93           O  
ANISOU 1371  OG1 THR A 182     2222   3577   1393   -623    110    630       O  
ATOM   1372  CG2 THR A 182      28.540  36.596  18.272  1.00 18.71           C  
ANISOU 1372  CG2 THR A 182     2291   3551   1266   -611     87    561       C  
ATOM   1373  N   GLY A 183      33.008  36.377  16.162  1.00 22.15           N  
ANISOU 1373  N   GLY A 183     2494   4371   1552   -756    387    584       N  
ATOM   1374  CA  GLY A 183      34.054  36.915  15.312  1.00 31.25           C  
ANISOU 1374  CA  GLY A 183     3594   5624   2657   -829    426    632       C  
ATOM   1375  C   GLY A 183      34.676  38.220  15.774  1.00 23.44           C  
ANISOU 1375  C   GLY A 183     2579   4612   1716   -889    350    758       C  
ATOM   1376  O   GLY A 183      35.016  38.340  16.940  1.00 22.79           O  
ANISOU 1376  O   GLY A 183     2464   4481   1712   -862    327    789       O  
ATOM   1377  N   ASN A 184      34.793  39.195  14.861  1.00 24.34           N  
ANISOU 1377  N   ASN A 184     2708   4755   1783   -974    308    829       N  
ATOM   1378  CA  ASN A 184      35.538  40.451  15.106  1.00 24.77           C  
ANISOU 1378  CA  ASN A 184     2736   4794   1879  -1046    250    942       C  
ATOM   1379  C   ASN A 184      34.785  41.539  15.883  1.00 28.69           C  
ANISOU 1379  C   ASN A 184     3301   5156   2443  -1066    130   1025       C  
ATOM   1380  O   ASN A 184      35.372  42.545  16.278  1.00 28.85           O  
ANISOU 1380  O   ASN A 184     3310   5140   2514  -1125     84   1105       O  
ATOM   1381  CB  ASN A 184      35.983  41.075  13.771  1.00 26.21           C  
ANISOU 1381  CB  ASN A 184     2907   5064   1987  -1132    258    989       C  
ATOM   1382  CG  ASN A 184      37.117  40.323  13.119  1.00 27.26           C  
ANISOU 1382  CG  ASN A 184     2958   5328   2072  -1129    378    928       C  
ATOM   1383  OD1 ASN A 184      37.753  39.480  13.742  1.00 34.37           O  
ANISOU 1383  OD1 ASN A 184     3795   6248   3016  -1065    452    867       O  
ATOM   1384  ND2 ASN A 184      37.376  40.622  11.852  1.00 28.83           N  
ANISOU 1384  ND2 ASN A 184     3152   5617   2185  -1197    399    946       N  
ATOM   1385  N   VAL A 185      33.484  41.357  16.066  1.00 23.21           N  
ANISOU 1385  N   VAL A 185     2681   4384   1754  -1019     83   1002       N  
ATOM   1386  CA  VAL A 185      32.623  42.424  16.559  1.00 26.90           C  
ANISOU 1386  CA  VAL A 185     3218   4719   2284  -1030    -24   1077       C  
ATOM   1387  C   VAL A 185      32.282  42.222  18.052  1.00 21.56           C  
ANISOU 1387  C   VAL A 185     2565   3940   1687   -971    -55   1053       C  
ATOM   1388  O   VAL A 185      32.065  41.094  18.500  1.00 25.93           O  
ANISOU 1388  O   VAL A 185     3105   4502   2244   -891    -14    960       O  
ATOM   1389  CB  VAL A 185      31.341  42.500  15.695  1.00 26.13           C  
ANISOU 1389  CB  VAL A 185     3178   4606   2145  -1018    -65   1083       C  
ATOM   1390  CG1 VAL A 185      30.311  43.453  16.276  1.00 32.95           C  
ANISOU 1390  CG1 VAL A 185     4108   5323   3090  -1000   -163   1150       C  
ATOM   1391  CG2 VAL A 185      31.698  42.897  14.260  1.00 27.58           C  
ANISOU 1391  CG2 VAL A 185     3339   4890   2250  -1094    -49   1127       C  
ATOM   1392  N   PRO A 186      32.280  43.315  18.835  1.00 21.48           N  
ANISOU 1392  N   PRO A 186     2588   3819   1755  -1005   -126   1121       N  
ATOM   1393  CA  PRO A 186      31.841  43.189  20.234  1.00 24.86           C  
ANISOU 1393  CA  PRO A 186     3043   4124   2279   -935   -166   1064       C  
ATOM   1394  C   PRO A 186      30.437  42.596  20.297  1.00 22.79           C  
ANISOU 1394  C   PRO A 186     2834   3806   2020   -844   -187   1006       C  
ATOM   1395  O   PRO A 186      29.563  43.057  19.576  1.00 22.11           O  
ANISOU 1395  O   PRO A 186     2794   3705   1900   -859   -224   1064       O  
ATOM   1396  CB  PRO A 186      31.864  44.630  20.744  1.00 25.61           C  
ANISOU 1396  CB  PRO A 186     3186   4100   2445  -1001   -237   1145       C  
ATOM   1397  CG  PRO A 186      32.895  45.315  19.871  1.00 27.26           C  
ANISOU 1397  CG  PRO A 186     3356   4394   2607  -1114   -218   1235       C  
ATOM   1398  CD  PRO A 186      32.733  44.683  18.514  1.00 22.47           C  
ANISOU 1398  CD  PRO A 186     2723   3904   1910  -1095   -170   1217       C  
ATOM   1399  N   ASN A 187      30.220  41.576  21.118  1.00 18.70           N  
ANISOU 1399  N   ASN A 187     2301   3265   1538   -755   -166    904       N  
ATOM   1400  CA  ASN A 187      28.894  40.989  21.166  1.00 22.11           C  
ANISOU 1400  CA  ASN A 187     2778   3651   1970   -680   -185    850       C  
ATOM   1401  C   ASN A 187      28.044  41.755  22.167  1.00 20.11           C  
ANISOU 1401  C   ASN A 187     2582   3254   1807   -649   -259    862       C  
ATOM   1402  O   ASN A 187      27.588  41.203  23.166  1.00 22.41           O  
ANISOU 1402  O   ASN A 187     2879   3485   2149   -577   -265    789       O  
ATOM   1403  CB  ASN A 187      28.951  39.512  21.525  1.00 23.23           C  
ANISOU 1403  CB  ASN A 187     2884   3827   2113   -601   -124    740       C  
ATOM   1404  CG  ASN A 187      27.705  38.769  21.086  1.00 26.40           C  
ANISOU 1404  CG  ASN A 187     3325   4229   2478   -554   -124    688       C  
ATOM   1405  OD1 ASN A 187      27.064  39.152  20.100  1.00 19.26           O  
ANISOU 1405  OD1 ASN A 187     2451   3362   1507   -595   -148    736       O  
ATOM   1406  ND2 ASN A 187      27.342  37.712  21.818  1.00 16.27           N  
ANISOU 1406  ND2 ASN A 187     2038   2910   1236   -475   -102    598       N  
ATOM   1407  N   VAL A 188      27.867  43.040  21.883  1.00 20.19           N  
ANISOU 1407  N   VAL A 188     2630   3205   1835   -705   -309    958       N  
ATOM   1408  CA  VAL A 188      27.128  43.971  22.724  1.00 17.98           C  
ANISOU 1408  CA  VAL A 188     2408   2775   1649   -683   -369    975       C  
ATOM   1409  C   VAL A 188      25.984  44.565  21.916  1.00 27.74           C  
ANISOU 1409  C   VAL A 188     3686   3976   2878   -675   -413   1057       C  
ATOM   1410  O   VAL A 188      26.186  44.994  20.766  1.00 23.54           O  
ANISOU 1410  O   VAL A 188     3148   3510   2285   -740   -417   1154       O  
ATOM   1411  CB  VAL A 188      28.032  45.104  23.232  1.00 19.65           C  
ANISOU 1411  CB  VAL A 188     2631   2920   1916   -762   -387   1021       C  
ATOM   1412  CG1 VAL A 188      27.261  46.042  24.148  1.00 19.21           C  
ANISOU 1412  CG1 VAL A 188     2642   2695   1962   -737   -434   1017       C  
ATOM   1413  CG2 VAL A 188      29.239  44.534  23.941  1.00 18.36           C  
ANISOU 1413  CG2 VAL A 188     2408   2820   1747   -782   -350    960       C  
ATOM   1414  N   GLU A 189      24.786  44.563  22.501  1.00 27.24           N  
ANISOU 1414  N   GLU A 189     3655   3821   2873   -596   -445   1027       N  
ATOM   1415  CA  GLU A 189      23.589  45.080  21.837  1.00 21.82           C  
ANISOU 1415  CA  GLU A 189     2994   3102   2194   -572   -491   1111       C  
ATOM   1416  C   GLU A 189      23.772  46.542  21.484  1.00 22.82           C  
ANISOU 1416  C   GLU A 189     3153   3144   2374   -629   -527   1238       C  
ATOM   1417  O   GLU A 189      24.318  47.318  22.278  1.00 19.76           O  
ANISOU 1417  O   GLU A 189     2794   2647   2068   -654   -528   1230       O  
ATOM   1418  CB  GLU A 189      22.363  44.907  22.726  1.00 18.84           C  
ANISOU 1418  CB  GLU A 189     2637   2632   1891   -473   -513   1052       C  
ATOM   1419  CG  GLU A 189      21.016  45.285  22.097  1.00 22.60           C  
ANISOU 1419  CG  GLU A 189     3119   3088   2378   -432   -561   1137       C  
ATOM   1420  CD  GLU A 189      19.842  44.931  23.022  1.00 23.69           C  
ANISOU 1420  CD  GLU A 189     3262   3158   2583   -333   -569   1065       C  
ATOM   1421  OE1 GLU A 189      19.733  43.743  23.386  1.00 21.20           O  
ANISOU 1421  OE1 GLU A 189     2925   2905   2223   -304   -542    962       O  
ATOM   1422  OE2 GLU A 189      19.052  45.830  23.406  1.00 19.88           O  
ANISOU 1422  OE2 GLU A 189     2802   2554   2200   -283   -598   1110       O  
ATOM   1423  N   LYS A 190      23.313  46.911  20.293  1.00 20.42           N  
ANISOU 1423  N   LYS A 190     2833   2885   2042   -640   -543   1316       N  
ATOM   1424  CA  LYS A 190      23.453  48.278  19.813  1.00 23.49           C  
ANISOU 1424  CA  LYS A 190     3239   3194   2491   -682   -568   1427       C  
ATOM   1425  C   LYS A 190      22.426  49.169  20.478  1.00 22.00           C  
ANISOU 1425  C   LYS A 190     3096   2830   2433   -611   -607   1466       C  
ATOM   1426  O   LYS A 190      21.436  48.682  21.018  1.00 21.31           O  
ANISOU 1426  O   LYS A 190     3011   2715   2372   -526   -618   1418       O  
ATOM   1427  CB  LYS A 190      23.319  48.328  18.288  1.00 22.67           C  
ANISOU 1427  CB  LYS A 190     3094   3211   2309   -717   -570   1491       C  
ATOM   1428  CG  LYS A 190      24.470  47.615  17.598  1.00 28.89           C  
ANISOU 1428  CG  LYS A 190     3841   4158   2980   -795   -521   1454       C  
ATOM   1429  CD  LYS A 190      24.381  47.678  16.090  1.00 34.44           C  
ANISOU 1429  CD  LYS A 190     4506   4982   3597   -842   -523   1513       C  
ATOM   1430  CE  LYS A 190      25.643  47.070  15.489  1.00 42.11           C  
ANISOU 1430  CE  LYS A 190     5438   6097   4464   -920   -464   1472       C  
ATOM   1431  NZ  LYS A 190      25.727  47.244  14.011  1.00 48.37           N  
ANISOU 1431  NZ  LYS A 190     6197   7012   5171   -985   -464   1533       N  
ATOM   1432  N   THR A 191      22.681  50.471  20.463  1.00 23.12           N  
ANISOU 1432  N   THR A 191     3272   2849   2664   -645   -621   1548       N  
ATOM   1433  CA  THR A 191      21.835  51.409  21.185  1.00 31.55           C  
ANISOU 1433  CA  THR A 191     4388   3721   3877   -577   -642   1574       C  
ATOM   1434  C   THR A 191      21.188  52.442  20.250  1.00 35.14           C  
ANISOU 1434  C   THR A 191     4835   4129   4387   -554   -664   1696       C  
ATOM   1435  O   THR A 191      20.614  53.436  20.690  1.00 37.79           O  
ANISOU 1435  O   THR A 191     5210   4290   4857   -501   -670   1734       O  
ATOM   1436  CB  THR A 191      22.647  52.091  22.292  1.00 28.28           C  
ANISOU 1436  CB  THR A 191     4040   3155   3550   -632   -630   1540       C  
ATOM   1437  OG1 THR A 191      23.843  52.626  21.728  1.00 25.97           O  
ANISOU 1437  OG1 THR A 191     3744   2899   3225   -745   -620   1591       O  
ATOM   1438  CG2 THR A 191      23.067  51.057  23.321  1.00 22.30           C  
ANISOU 1438  CG2 THR A 191     3278   2447   2746   -630   -606   1398       C  
ATOM   1439  N   THR A 192      21.271  52.174  18.953  1.00 39.24           N  
ANISOU 1439  N   THR A 192     5301   4806   4802   -593   -672   1753       N  
ATOM   1440  CA  THR A 192      20.603  52.972  17.931  1.00 41.83           C  
ANISOU 1440  CA  THR A 192     5607   5130   5156   -577   -702   1877       C  
ATOM   1441  C   THR A 192      19.078  52.779  18.049  1.00 43.93           C  
ANISOU 1441  C   THR A 192     5850   5373   5468   -461   -724   1880       C  
ATOM   1442  O   THR A 192      18.635  51.828  18.694  1.00 41.50           O  
ANISOU 1442  O   THR A 192     5534   5097   5136   -410   -715   1782       O  
ATOM   1443  CB  THR A 192      21.109  52.562  16.543  1.00 42.53           C  
ANISOU 1443  CB  THR A 192     5641   5415   5102   -661   -704   1919       C  
ATOM   1444  OG1 THR A 192      20.832  51.170  16.330  1.00 45.83           O  
ANISOU 1444  OG1 THR A 192     6019   5991   5404   -649   -692   1828       O  
ATOM   1445  CG2 THR A 192      22.611  52.797  16.441  1.00 27.80           C  
ANISOU 1445  CG2 THR A 192     3788   3576   3197   -771   -678   1919       C  
ATOM   1446  N   PRO A 193      18.271  53.672  17.432  1.00 47.83           N  
ANISOU 1446  N   PRO A 193     6328   5817   6028   -420   -753   1997       N  
ATOM   1447  CA  PRO A 193      16.804  53.631  17.557  1.00 50.22           C  
ANISOU 1447  CA  PRO A 193     6600   6093   6389   -308   -773   2014       C  
ATOM   1448  C   PRO A 193      16.142  52.263  17.340  1.00 54.78           C  
ANISOU 1448  C   PRO A 193     7122   6839   6853   -289   -781   1939       C  
ATOM   1449  O   PRO A 193      15.390  51.799  18.206  1.00 53.75           O  
ANISOU 1449  O   PRO A 193     6991   6666   6766   -206   -775   1865       O  
ATOM   1450  CB  PRO A 193      16.350  54.608  16.473  1.00 48.05           C  
ANISOU 1450  CB  PRO A 193     6294   5816   6145   -311   -808   2171       C  
ATOM   1451  CG  PRO A 193      17.422  55.622  16.439  1.00 49.47           C  
ANISOU 1451  CG  PRO A 193     6527   5891   6378   -379   -794   2226       C  
ATOM   1452  CD  PRO A 193      18.706  54.880  16.700  1.00 50.51           C  
ANISOU 1452  CD  PRO A 193     6679   6101   6410   -473   -765   2126       C  
ATOM   1453  N   ASP A 194      16.412  51.631  16.205  1.00 53.81           N  
ANISOU 1453  N   ASP A 194     6956   6901   6589   -369   -792   1953       N  
ATOM   1454  CA  ASP A 194      15.754  50.373  15.879  1.00 57.40           C  
ANISOU 1454  CA  ASP A 194     7363   7510   6937   -364   -796   1883       C  
ATOM   1455  C   ASP A 194      16.642  49.169  16.170  1.00 55.87           C  
ANISOU 1455  C   ASP A 194     7184   7404   6639   -415   -755   1748       C  
ATOM   1456  O   ASP A 194      16.656  48.205  15.399  1.00 54.30           O  
ANISOU 1456  O   ASP A 194     6952   7366   6315   -468   -747   1703       O  
ATOM   1457  CB  ASP A 194      15.354  50.367  14.409  1.00 63.67           C  
ANISOU 1457  CB  ASP A 194     8098   8454   7641   -421   -830   1974       C  
ATOM   1458  CG  ASP A 194      16.519  50.705  13.494  1.00 68.24           C  
ANISOU 1458  CG  ASP A 194     8681   9103   8145   -531   -823   2027       C  
ATOM   1459  OD1 ASP A 194      17.665  50.790  13.999  1.00 62.83           O  
ANISOU 1459  OD1 ASP A 194     8040   8366   7467   -567   -788   1980       O  
ATOM   1460  OD2 ASP A 194      16.286  50.897  12.276  1.00 68.89           O  
ANISOU 1460  OD2 ASP A 194     8717   9298   8161   -587   -853   2120       O  
ATOM   1461  N   ALA A 195      17.383  49.229  17.275  1.00 46.57           N  
ANISOU 1461  N   ALA A 195     6057   6122   5516   -404   -726   1683       N  
ATOM   1462  CA  ALA A 195      18.359  48.189  17.585  1.00 36.38           C  
ANISOU 1462  CA  ALA A 195     4778   4909   4138   -453   -685   1570       C  
ATOM   1463  C   ALA A 195      17.659  46.854  17.789  1.00 31.47           C  
ANISOU 1463  C   ALA A 195     4131   4373   3453   -414   -675   1465       C  
ATOM   1464  O   ALA A 195      16.592  46.792  18.388  1.00 35.82           O  
ANISOU 1464  O   ALA A 195     4678   4867   4067   -332   -694   1451       O  
ATOM   1465  CB  ALA A 195      19.161  48.564  18.814  1.00 33.46           C  
ANISOU 1465  CB  ALA A 195     4461   4406   3847   -449   -666   1532       C  
ATOM   1466  N   VAL A 196      18.268  45.788  17.288  1.00 24.43           N  
ANISOU 1466  N   VAL A 196     3224   3616   2441   -473   -640   1389       N  
ATOM   1467  CA  VAL A 196      17.751  44.441  17.493  1.00 25.34           C  
ANISOU 1467  CA  VAL A 196     3326   3806   2497   -448   -621   1278       C  
ATOM   1468  C   VAL A 196      18.238  43.881  18.835  1.00 25.68           C  
ANISOU 1468  C   VAL A 196     3400   3784   2574   -410   -592   1181       C  
ATOM   1469  O   VAL A 196      19.431  43.961  19.150  1.00 26.23           O  
ANISOU 1469  O   VAL A 196     3488   3841   2638   -449   -563   1164       O  
ATOM   1470  CB  VAL A 196      18.180  43.517  16.343  1.00 28.85           C  
ANISOU 1470  CB  VAL A 196     3745   4412   2803   -528   -587   1231       C  
ATOM   1471  CG1 VAL A 196      17.637  42.111  16.532  1.00 28.48           C  
ANISOU 1471  CG1 VAL A 196     3692   4428   2702   -508   -563   1113       C  
ATOM   1472  CG2 VAL A 196      17.735  44.103  15.003  1.00 37.77           C  
ANISOU 1472  CG2 VAL A 196     4842   5619   3891   -578   -621   1334       C  
ATOM   1473  N   PRO A 197      17.320  43.326  19.641  1.00 23.33           N  
ANISOU 1473  N   PRO A 197     3100   3450   2312   -338   -601   1122       N  
ATOM   1474  CA  PRO A 197      17.749  42.774  20.931  1.00 21.67           C  
ANISOU 1474  CA  PRO A 197     2915   3186   2130   -305   -579   1035       C  
ATOM   1475  C   PRO A 197      18.688  41.594  20.757  1.00 20.58           C  
ANISOU 1475  C   PRO A 197     2773   3150   1898   -351   -526    944       C  
ATOM   1476  O   PRO A 197      18.480  40.784  19.854  1.00 18.01           O  
ANISOU 1476  O   PRO A 197     2425   2931   1486   -382   -505    908       O  
ATOM   1477  CB  PRO A 197      16.438  42.318  21.581  1.00 17.08           C  
ANISOU 1477  CB  PRO A 197     2322   2577   1590   -226   -600    995       C  
ATOM   1478  CG  PRO A 197      15.377  43.059  20.863  1.00 20.73           C  
ANISOU 1478  CG  PRO A 197     2757   3034   2083   -205   -639   1086       C  
ATOM   1479  CD  PRO A 197      15.863  43.208  19.458  1.00 23.23           C  
ANISOU 1479  CD  PRO A 197     3059   3450   2318   -287   -635   1138       C  
ATOM   1480  N   LEU A 198      19.722  41.511  21.584  1.00 16.45           N  
ANISOU 1480  N   LEU A 198     2266   2592   1393   -359   -500    907       N  
ATOM   1481  CA  LEU A 198      20.508  40.290  21.637  1.00 22.66           C  
ANISOU 1481  CA  LEU A 198     3036   3452   2123   -373   -436    801       C  
ATOM   1482  C   LEU A 198      19.865  39.391  22.696  1.00 17.78           C  
ANISOU 1482  C   LEU A 198     2417   2786   1552   -298   -423    699       C  
ATOM   1483  O   LEU A 198      19.422  39.870  23.738  1.00 18.60           O  
ANISOU 1483  O   LEU A 198     2534   2787   1744   -247   -447    692       O  
ATOM   1484  CB  LEU A 198      21.980  40.582  21.938  1.00 15.96           C  
ANISOU 1484  CB  LEU A 198     2181   2592   1290   -410   -398    796       C  
ATOM   1485  CG  LEU A 198      22.720  41.427  20.894  1.00 16.96           C  
ANISOU 1485  CG  LEU A 198     2305   2775   1365   -495   -403    899       C  
ATOM   1486  CD1 LEU A 198      24.218  41.438  21.200  1.00 20.12           C  
ANISOU 1486  CD1 LEU A 198     2682   3191   1771   -534   -355    876       C  
ATOM   1487  CD2 LEU A 198      22.464  40.926  19.443  1.00 17.63           C  
ANISOU 1487  CD2 LEU A 198     2369   2987   1341   -538   -384    906       C  
ATOM   1488  N   ASN A 199      19.794  38.101  22.391  1.00 16.41           N  
ANISOU 1488  N   ASN A 199     2230   2687   1318   -300   -382    619       N  
ATOM   1489  CA  ASN A 199      19.056  37.128  23.179  1.00 16.05           C  
ANISOU 1489  CA  ASN A 199     2183   2612   1303   -242   -371    533       C  
ATOM   1490  C   ASN A 199      20.024  36.173  23.853  1.00 16.63           C  
ANISOU 1490  C   ASN A 199     2244   2677   1397   -223   -307    447       C  
ATOM   1491  O   ASN A 199      20.609  35.292  23.198  1.00 13.73           O  
ANISOU 1491  O   ASN A 199     1865   2378    972   -249   -250    400       O  
ATOM   1492  CB  ASN A 199      18.065  36.375  22.266  1.00 14.68           C  
ANISOU 1492  CB  ASN A 199     2005   2523   1050   -266   -379    516       C  
ATOM   1493  CG  ASN A 199      17.262  35.288  23.003  1.00 16.67           C  
ANISOU 1493  CG  ASN A 199     2256   2748   1331   -220   -366    429       C  
ATOM   1494  OD1 ASN A 199      17.451  35.034  24.182  1.00 16.59           O  
ANISOU 1494  OD1 ASN A 199     2246   2663   1394   -168   -349    384       O  
ATOM   1495  ND2 ASN A 199      16.334  34.668  22.291  1.00 17.79           N  
ANISOU 1495  ND2 ASN A 199     2394   2959   1407   -250   -378    411       N  
ATOM   1496  N   LEU A 200      20.183  36.318  25.165  1.00 13.58           N  
ANISOU 1496  N   LEU A 200     1858   2211   1091   -177   -313    426       N  
ATOM   1497  CA  LEU A 200      21.146  35.487  25.859  1.00 12.56           C  
ANISOU 1497  CA  LEU A 200     1707   2080    987   -157   -262    369       C  
ATOM   1498  C   LEU A 200      20.723  34.015  25.798  1.00 14.98           C  
ANISOU 1498  C   LEU A 200     2008   2407   1278   -130   -219    292       C  
ATOM   1499  O   LEU A 200      21.556  33.125  25.952  1.00 12.89           O  
ANISOU 1499  O   LEU A 200     1720   2153   1023   -116   -162    250       O  
ATOM   1500  CB  LEU A 200      21.327  35.942  27.317  1.00 16.56           C  
ANISOU 1500  CB  LEU A 200     2214   2512   1568   -126   -285    367       C  
ATOM   1501  CG  LEU A 200      20.370  35.378  28.367  1.00 20.87           C  
ANISOU 1501  CG  LEU A 200     2766   3011   2154    -71   -295    320       C  
ATOM   1502  CD1 LEU A 200      20.828  35.777  29.769  1.00 11.29           C  
ANISOU 1502  CD1 LEU A 200     1549   1750    992    -59   -308    313       C  
ATOM   1503  CD2 LEU A 200      18.947  35.855  28.138  1.00 15.32           C  
ANISOU 1503  CD2 LEU A 200     2085   2284   1452    -56   -337    338       C  
ATOM   1504  N   ASN A 201      19.443  33.765  25.527  1.00 14.35           N  
ANISOU 1504  N   ASN A 201     1945   2329   1177   -126   -245    280       N  
ATOM   1505  CA  ASN A 201      18.930  32.398  25.403  1.00 18.69           C  
ANISOU 1505  CA  ASN A 201     2497   2893   1710   -117   -207    205       C  
ATOM   1506  C   ASN A 201      18.843  31.902  23.949  1.00 16.96           C  
ANISOU 1506  C   ASN A 201     2289   2758   1398   -177   -177    177       C  
ATOM   1507  O   ASN A 201      18.050  31.007  23.647  1.00 19.60           O  
ANISOU 1507  O   ASN A 201     2636   3109   1703   -191   -164    121       O  
ATOM   1508  CB  ASN A 201      17.534  32.301  26.049  1.00 17.38           C  
ANISOU 1508  CB  ASN A 201     2340   2692   1573    -88   -251    199       C  
ATOM   1509  CG  ASN A 201      17.558  32.515  27.559  1.00 16.27           C  
ANISOU 1509  CG  ASN A 201     2192   2478   1512    -33   -265    201       C  
ATOM   1510  OD1 ASN A 201      18.570  32.288  28.229  1.00 11.05           O  
ANISOU 1510  OD1 ASN A 201     1519   1796    886    -16   -236    190       O  
ATOM   1511  ND2 ASN A 201      16.442  32.993  28.096  1.00 13.78           N  
ANISOU 1511  ND2 ASN A 201     1879   2135   1222     -9   -310    218       N  
ATOM   1512  N   ASP A 202      19.643  32.480  23.052  1.00 18.04           N  
ANISOU 1512  N   ASP A 202     2421   2954   1481   -222   -164    214       N  
ATOM   1513  CA  ASP A 202      19.560  32.127  21.629  1.00 18.95           C  
ANISOU 1513  CA  ASP A 202     2546   3167   1488   -293   -136    191       C  
ATOM   1514  C   ASP A 202      19.702  30.612  21.437  1.00 16.23           C  
ANISOU 1514  C   ASP A 202     2211   2826   1131   -293    -51     73       C  
ATOM   1515  O   ASP A 202      20.543  29.970  22.066  1.00 18.22           O  
ANISOU 1515  O   ASP A 202     2448   3024   1450   -243     10     29       O  
ATOM   1516  CB  ASP A 202      20.617  32.892  20.812  1.00 14.96           C  
ANISOU 1516  CB  ASP A 202     2028   2727    929   -342   -118    245       C  
ATOM   1517  CG  ASP A 202      21.996  32.264  20.898  1.00 19.19           C  
ANISOU 1517  CG  ASP A 202     2540   3265   1486   -325    -27    191       C  
ATOM   1518  OD1 ASP A 202      22.672  32.411  21.948  1.00 17.67           O  
ANISOU 1518  OD1 ASP A 202     2323   3006   1383   -271    -24    206       O  
ATOM   1519  OD2 ASP A 202      22.407  31.614  19.910  1.00 15.89           O  
ANISOU 1519  OD2 ASP A 202     2122   2922    993   -368     45    132       O  
ATOM   1520  N   TYR A 203      18.851  30.054  20.584  1.00 18.98           N  
ANISOU 1520  N   TYR A 203     2582   3233   1397   -351    -49     25       N  
ATOM   1521  CA  TYR A 203      18.689  28.601  20.449  1.00 20.12           C  
ANISOU 1521  CA  TYR A 203     2748   3359   1536   -360     25    -96       C  
ATOM   1522  C   TYR A 203      20.004  27.824  20.259  1.00 23.04           C  
ANISOU 1522  C   TYR A 203     3114   3714   1928   -340    141   -172       C  
ATOM   1523  O   TYR A 203      20.229  26.814  20.931  1.00 21.97           O  
ANISOU 1523  O   TYR A 203     2980   3491   1877   -285    199   -236       O  
ATOM   1524  CB  TYR A 203      17.725  28.307  19.286  1.00 20.43           C  
ANISOU 1524  CB  TYR A 203     2813   3497   1451   -459      9   -134       C  
ATOM   1525  CG  TYR A 203      17.548  26.837  18.961  1.00 17.86           C  
ANISOU 1525  CG  TYR A 203     2524   3157   1107   -493     92   -274       C  
ATOM   1526  CD1 TYR A 203      16.946  25.965  19.863  1.00 16.42           C  
ANISOU 1526  CD1 TYR A 203     2353   2875   1010   -452     98   -323       C  
ATOM   1527  CD2 TYR A 203      17.995  26.321  17.737  1.00 19.79           C  
ANISOU 1527  CD2 TYR A 203     2792   3483   1244   -573    172   -362       C  
ATOM   1528  CE1 TYR A 203      16.793  24.612  19.558  1.00 20.88           C  
ANISOU 1528  CE1 TYR A 203     2957   3407   1568   -489    179   -452       C  
ATOM   1529  CE2 TYR A 203      17.849  24.979  17.422  1.00 18.80           C  
ANISOU 1529  CE2 TYR A 203     2709   3329   1107   -610    259   -505       C  
ATOM   1530  CZ  TYR A 203      17.247  24.127  18.331  1.00 22.48           C  
ANISOU 1530  CZ  TYR A 203     3190   3680   1671   -567    262   -549       C  
ATOM   1531  OH  TYR A 203      17.104  22.794  18.001  1.00 22.58           O  
ANISOU 1531  OH  TYR A 203     3250   3647   1681   -610    352   -692       O  
ATOM   1532  N   GLU A 204      20.879  28.292  19.370  1.00 21.23           N  
ANISOU 1532  N   GLU A 204     2871   3566   1628   -381    176   -156       N  
ATOM   1533  CA  GLU A 204      22.114  27.551  19.091  1.00 22.39           C  
ANISOU 1533  CA  GLU A 204     3003   3711   1794   -360    297   -231       C  
ATOM   1534  C   GLU A 204      23.265  27.879  20.033  1.00 18.80           C  
ANISOU 1534  C   GLU A 204     2496   3201   1447   -278    311   -173       C  
ATOM   1535  O   GLU A 204      24.354  27.321  19.883  1.00 21.50           O  
ANISOU 1535  O   GLU A 204     2807   3542   1820   -247    410   -217       O  
ATOM   1536  CB  GLU A 204      22.577  27.781  17.648  1.00 30.72           C  
ANISOU 1536  CB  GLU A 204     4063   4897   2713   -450    347   -254       C  
ATOM   1537  CG  GLU A 204      21.751  27.059  16.586  1.00 33.37           C  
ANISOU 1537  CG  GLU A 204     4449   5302   2929   -543    376   -355       C  
ATOM   1538  CD  GLU A 204      21.783  25.530  16.715  1.00 38.77           C  
ANISOU 1538  CD  GLU A 204     5163   5901   3667   -516    485   -506       C  
ATOM   1539  OE1 GLU A 204      22.642  24.975  17.430  1.00 37.95           O  
ANISOU 1539  OE1 GLU A 204     5033   5700   3687   -422    558   -532       O  
ATOM   1540  OE2 GLU A 204      20.942  24.870  16.077  1.00 45.61           O  
ANISOU 1540  OE2 GLU A 204     6078   6799   4454   -594    498   -597       O  
ATOM   1541  N   GLY A 205      23.017  28.745  21.015  1.00 15.73           N  
ANISOU 1541  N   GLY A 205     2093   2768   1117   -244    217    -78       N  
ATOM   1542  CA  GLY A 205      24.012  29.103  22.013  1.00 21.12           C  
ANISOU 1542  CA  GLY A 205     2725   3405   1892   -181    215    -20       C  
ATOM   1543  C   GLY A 205      25.176  29.967  21.539  1.00 22.34           C  
ANISOU 1543  C   GLY A 205     2840   3634   2015   -212    230     40       C  
ATOM   1544  O   GLY A 205      26.253  29.935  22.128  1.00 17.52           O  
ANISOU 1544  O   GLY A 205     2176   3010   1472   -169    261     65       O  
ATOM   1545  N   VAL A 206      24.965  30.731  20.469  1.00 25.85           N  
ANISOU 1545  N   VAL A 206     3303   4163   2354   -292    205     74       N  
ATOM   1546  CA  VAL A 206      25.979  31.659  19.966  1.00 23.01           C  
ANISOU 1546  CA  VAL A 206     2909   3877   1956   -338    211    145       C  
ATOM   1547  C   VAL A 206      26.396  32.670  21.017  1.00 19.49           C  
ANISOU 1547  C   VAL A 206     2437   3379   1588   -315    141    238       C  
ATOM   1548  O   VAL A 206      27.576  32.974  21.195  1.00 19.29           O  
ANISOU 1548  O   VAL A 206     2359   3380   1589   -317    169    274       O  
ATOM   1549  CB  VAL A 206      25.467  32.429  18.729  1.00 17.38           C  
ANISOU 1549  CB  VAL A 206     2226   3260   1117   -434    174    191       C  
ATOM   1550  CG1 VAL A 206      26.438  33.584  18.380  1.00 17.85           C  
ANISOU 1550  CG1 VAL A 206     2252   3379   1150   -485    161    291       C  
ATOM   1551  CG2 VAL A 206      25.316  31.476  17.575  1.00 18.30           C  
ANISOU 1551  CG2 VAL A 206     2363   3459   1132   -479    257     91       C  
ATOM   1552  N   ASN A 207      25.411  33.185  21.730  1.00 15.36           N  
ANISOU 1552  N   ASN A 207     1950   2786   1102   -299     53    272       N  
ATOM   1553  CA  ASN A 207      25.667  34.228  22.697  1.00 15.55           C  
ANISOU 1553  CA  ASN A 207     1964   2755   1191   -292    -14    347       C  
ATOM   1554  C   ASN A 207      26.090  33.699  24.073  1.00 19.35           C  
ANISOU 1554  C   ASN A 207     2414   3171   1767   -224     -6    323       C  
ATOM   1555  O   ASN A 207      25.352  33.828  25.032  1.00 15.47           O  
ANISOU 1555  O   ASN A 207     1946   2609   1324   -191    -59    323       O  
ATOM   1556  CB  ASN A 207      24.431  35.101  22.835  1.00 16.66           C  
ANISOU 1556  CB  ASN A 207     2154   2846   1331   -302   -104    395       C  
ATOM   1557  CG  ASN A 207      24.151  35.899  21.575  1.00 22.60           C  
ANISOU 1557  CG  ASN A 207     2925   3665   1998   -375   -130    460       C  
ATOM   1558  OD1 ASN A 207      25.077  36.353  20.902  1.00 17.90           O  
ANISOU 1558  OD1 ASN A 207     2309   3134   1360   -430   -105    504       O  
ATOM   1559  ND2 ASN A 207      22.875  36.100  21.268  1.00 15.24           N  
ANISOU 1559  ND2 ASN A 207     2026   2724   1041   -378   -184    480       N  
ATOM   1560  N   SER A 208      27.276  33.104  24.151  1.00 22.29           N  
ANISOU 1560  N   SER A 208     2727   3578   2163   -203     62    308       N  
ATOM   1561  CA  SER A 208      27.854  32.666  25.421  1.00 16.99           C  
ANISOU 1561  CA  SER A 208     2008   2868   1577   -146     65    311       C  
ATOM   1562  C   SER A 208      28.174  33.878  26.289  1.00 15.23           C  
ANISOU 1562  C   SER A 208     1779   2627   1380   -181    -11    381       C  
ATOM   1563  O   SER A 208      27.642  34.033  27.386  1.00 23.47           O  
ANISOU 1563  O   SER A 208     2843   3609   2465   -159    -65    382       O  
ATOM   1564  CB  SER A 208      29.114  31.833  25.187  1.00 15.85           C  
ANISOU 1564  CB  SER A 208     1788   2776   1458   -115    157    297       C  
ATOM   1565  OG  SER A 208      29.586  31.290  26.410  1.00 17.91           O  
ANISOU 1565  OG  SER A 208     1997   3004   1804    -54    154    313       O  
ATOM   1566  N   VAL A 209      29.068  34.727  25.803  1.00 16.47           N  
ANISOU 1566  N   VAL A 209     1909   2840   1509   -244    -11    435       N  
ATOM   1567  CA  VAL A 209      29.277  36.029  26.421  1.00 16.38           C  
ANISOU 1567  CA  VAL A 209     1908   2802   1512   -300    -83    495       C  
ATOM   1568  C   VAL A 209      28.570  37.077  25.573  1.00 17.72           C  
ANISOU 1568  C   VAL A 209     2143   2952   1636   -357   -122    530       C  
ATOM   1569  O   VAL A 209      28.701  37.096  24.343  1.00 18.51           O  
ANISOU 1569  O   VAL A 209     2242   3116   1674   -392    -89    546       O  
ATOM   1570  CB  VAL A 209      30.776  36.343  26.586  1.00 20.03           C  
ANISOU 1570  CB  VAL A 209     2292   3334   1985   -344    -65    544       C  
ATOM   1571  CG1 VAL A 209      31.012  37.831  26.834  1.00 20.57           C  
ANISOU 1571  CG1 VAL A 209     2386   3379   2052   -433   -131    605       C  
ATOM   1572  CG2 VAL A 209      31.332  35.534  27.755  1.00 21.13           C  
ANISOU 1572  CG2 VAL A 209     2366   3479   2184   -288    -56    534       C  
ATOM   1573  N   VAL A 210      27.791  37.936  26.221  1.00 14.52           N  
ANISOU 1573  N   VAL A 210     1792   2462   1262   -364   -191    546       N  
ATOM   1574  CA  VAL A 210      26.886  38.823  25.492  1.00 14.70           C  
ANISOU 1574  CA  VAL A 210     1876   2449   1262   -393   -231    587       C  
ATOM   1575  C   VAL A 210      26.346  39.937  26.396  1.00 19.08           C  
ANISOU 1575  C   VAL A 210     2479   2895   1876   -401   -295    606       C  
ATOM   1576  O   VAL A 210      26.061  39.717  27.579  1.00 15.12           O  
ANISOU 1576  O   VAL A 210     1984   2342   1420   -361   -310    559       O  
ATOM   1577  CB  VAL A 210      25.705  38.012  24.888  1.00 14.39           C  
ANISOU 1577  CB  VAL A 210     1862   2419   1188   -346   -221    546       C  
ATOM   1578  CG1 VAL A 210      24.930  37.254  25.999  1.00 21.54           C  
ANISOU 1578  CG1 VAL A 210     2777   3265   2143   -271   -230    479       C  
ATOM   1579  CG2 VAL A 210      24.781  38.889  24.072  1.00 14.75           C  
ANISOU 1579  CG2 VAL A 210     1953   2448   1205   -375   -268    607       C  
ATOM   1580  N   ALA A 211      26.232  41.149  25.864  1.00 16.66           N  
ANISOU 1580  N   ALA A 211     2208   2550   1571   -455   -329    677       N  
ATOM   1581  CA  ALA A 211      25.581  42.201  26.636  1.00 16.37           C  
ANISOU 1581  CA  ALA A 211     2226   2390   1603   -452   -378    687       C  
ATOM   1582  C   ALA A 211      24.305  42.609  25.917  1.00 20.74           C  
ANISOU 1582  C   ALA A 211     2819   2901   2160   -422   -407    731       C  
ATOM   1583  O   ALA A 211      24.257  42.670  24.678  1.00 17.40           O  
ANISOU 1583  O   ALA A 211     2390   2541   1681   -451   -407    795       O  
ATOM   1584  CB  ALA A 211      26.500  43.383  26.854  1.00 15.96           C  
ANISOU 1584  CB  ALA A 211     2186   2297   1581   -538   -395    734       C  
ATOM   1585  N   PHE A 212      23.272  42.872  26.712  1.00 17.49           N  
ANISOU 1585  N   PHE A 212     2442   2394   1810   -365   -432    699       N  
ATOM   1586  CA  PHE A 212      21.911  43.029  26.220  1.00 15.20           C  
ANISOU 1586  CA  PHE A 212     2171   2072   1531   -314   -459    733       C  
ATOM   1587  C   PHE A 212      21.165  44.025  27.102  1.00 15.44           C  
ANISOU 1587  C   PHE A 212     2245   1961   1660   -277   -483    729       C  
ATOM   1588  O   PHE A 212      21.572  44.262  28.243  1.00 15.35           O  
ANISOU 1588  O   PHE A 212     2252   1891   1690   -284   -473    666       O  
ATOM   1589  CB  PHE A 212      21.201  41.671  26.242  1.00 15.29           C  
ANISOU 1589  CB  PHE A 212     2156   2152   1502   -255   -442    667       C  
ATOM   1590  CG  PHE A 212      21.463  40.879  27.510  1.00 13.67           C  
ANISOU 1590  CG  PHE A 212     1938   1938   1317   -222   -416    571       C  
ATOM   1591  CD1 PHE A 212      20.784  41.178  28.692  1.00 13.42           C  
ANISOU 1591  CD1 PHE A 212     1930   1820   1348   -178   -429    526       C  
ATOM   1592  CD2 PHE A 212      22.394  39.854  27.528  1.00 18.98           C  
ANISOU 1592  CD2 PHE A 212     2574   2691   1948   -235   -376    531       C  
ATOM   1593  CE1 PHE A 212      21.007  40.450  29.878  1.00 12.82           C  
ANISOU 1593  CE1 PHE A 212     1841   1751   1280   -156   -410    449       C  
ATOM   1594  CE2 PHE A 212      22.638  39.126  28.709  1.00 15.31           C  
ANISOU 1594  CE2 PHE A 212     2091   2222   1506   -204   -359    463       C  
ATOM   1595  CZ  PHE A 212      21.939  39.436  29.887  1.00 18.69           C  
ANISOU 1595  CZ  PHE A 212     2543   2575   1983   -170   -380    426       C  
ATOM   1596  N   SER A 213      20.058  44.573  26.608  1.00 23.59           N  
ANISOU 1596  N   SER A 213     3291   2945   2728   -236   -512    792       N  
ATOM   1597  CA  SER A 213      19.284  45.524  27.401  1.00 16.32           C  
ANISOU 1597  CA  SER A 213     2408   1880   1914   -186   -522    786       C  
ATOM   1598  C   SER A 213      18.268  44.828  28.317  1.00 23.22           C  
ANISOU 1598  C   SER A 213     3269   2746   2807   -103   -510    697       C  
ATOM   1599  O   SER A 213      17.824  45.424  29.307  1.00 18.15           O  
ANISOU 1599  O   SER A 213     2657   1995   2244    -66   -498    648       O  
ATOM   1600  CB  SER A 213      18.548  46.522  26.505  1.00 22.81           C  
ANISOU 1600  CB  SER A 213     3240   2641   2786   -168   -557    911       C  
ATOM   1601  OG  SER A 213      17.572  45.879  25.716  1.00 21.81           O  
ANISOU 1601  OG  SER A 213     3071   2605   2612   -125   -580    956       O  
ATOM   1602  N   SER A 214      17.899  43.584  27.983  1.00 16.07           N  
ANISOU 1602  N   SER A 214     2322   1953   1829    -81   -507    671       N  
ATOM   1603  CA  SER A 214      16.822  42.894  28.685  1.00 14.37           C  
ANISOU 1603  CA  SER A 214     2090   1742   1629    -10   -499    606       C  
ATOM   1604  C   SER A 214      17.007  41.382  28.879  1.00 13.44           C  
ANISOU 1604  C   SER A 214     1943   1727   1438    -11   -476    534       C  
ATOM   1605  O   SER A 214      17.368  40.657  27.955  1.00 16.89           O  
ANISOU 1605  O   SER A 214     2359   2257   1802    -45   -473    551       O  
ATOM   1606  CB  SER A 214      15.504  43.142  27.943  1.00 14.88           C  
ANISOU 1606  CB  SER A 214     2132   1809   1714     41   -531    682       C  
ATOM   1607  OG  SER A 214      14.401  42.579  28.633  1.00 14.50           O  
ANISOU 1607  OG  SER A 214     2060   1763   1687    109   -523    626       O  
ATOM   1608  N   PHE A 215      16.748  40.922  30.102  1.00 14.44           N  
ANISOU 1608  N   PHE A 215     2068   1831   1586     23   -456    451       N  
ATOM   1609  CA  PHE A 215      16.521  39.506  30.397  1.00 12.19           C  
ANISOU 1609  CA  PHE A 215     1755   1620   1256     40   -437    392       C  
ATOM   1610  C   PHE A 215      15.087  39.150  29.987  1.00 12.24           C  
ANISOU 1610  C   PHE A 215     1738   1650   1262     86   -453    408       C  
ATOM   1611  O   PHE A 215      14.348  40.000  29.479  1.00 12.85           O  
ANISOU 1611  O   PHE A 215     1813   1696   1373    108   -481    471       O  
ATOM   1612  CB  PHE A 215      16.718  39.199  31.900  1.00 11.77           C  
ANISOU 1612  CB  PHE A 215     1707   1542   1224     54   -414    315       C  
ATOM   1613  CG  PHE A 215      18.150  39.249  32.364  1.00 18.03           C  
ANISOU 1613  CG  PHE A 215     2505   2343   2001      2   -403    299       C  
ATOM   1614  CD1 PHE A 215      18.987  38.154  32.201  1.00 11.34           C  
ANISOU 1614  CD1 PHE A 215     1626   1571   1109    -17   -384    290       C  
ATOM   1615  CD2 PHE A 215      18.643  40.379  32.996  1.00 12.18           C  
ANISOU 1615  CD2 PHE A 215     1797   1536   1297    -29   -408    291       C  
ATOM   1616  CE1 PHE A 215      20.295  38.202  32.652  1.00 11.41           C  
ANISOU 1616  CE1 PHE A 215     1624   1601   1110    -61   -376    288       C  
ATOM   1617  CE2 PHE A 215      19.938  40.442  33.422  1.00 13.64           C  
ANISOU 1617  CE2 PHE A 215     1978   1744   1463    -89   -404    283       C  
ATOM   1618  CZ  PHE A 215      20.771  39.349  33.267  1.00 11.85           C  
ANISOU 1618  CZ  PHE A 215     1707   1606   1191   -102   -391    287       C  
ATOM   1619  N   TYR A 216      14.697  37.894  30.199  1.00 22.41           N  
ANISOU 1619  N   TYR A 216     3004   2996   2516     97   -438    358       N  
ATOM   1620  CA  TYR A 216      13.327  37.450  29.940  1.00 16.12           C  
ANISOU 1620  CA  TYR A 216     2178   2232   1714    128   -453    365       C  
ATOM   1621  C   TYR A 216      12.646  37.032  31.248  1.00 14.96           C  
ANISOU 1621  C   TYR A 216     2020   2062   1601    171   -434    303       C  
ATOM   1622  O   TYR A 216      13.153  36.177  31.957  1.00 12.31           O  
ANISOU 1622  O   TYR A 216     1689   1740   1249    160   -407    249       O  
ATOM   1623  CB  TYR A 216      13.323  36.294  28.935  1.00 17.55           C  
ANISOU 1623  CB  TYR A 216     2345   2506   1819     87   -450    359       C  
ATOM   1624  CG  TYR A 216      13.956  36.663  27.609  1.00 12.15           C  
ANISOU 1624  CG  TYR A 216     1668   1866   1084     35   -463    416       C  
ATOM   1625  CD1 TYR A 216      15.342  36.661  27.450  1.00 15.78           C  
ANISOU 1625  CD1 TYR A 216     2146   2328   1523     -1   -436    407       C  
ATOM   1626  CD2 TYR A 216      13.175  37.026  26.526  1.00 22.62           C  
ANISOU 1626  CD2 TYR A 216     2975   3243   2377     19   -504    488       C  
ATOM   1627  CE1 TYR A 216      15.933  37.012  26.229  1.00 21.12           C  
ANISOU 1627  CE1 TYR A 216     2826   3055   2145    -55   -442    460       C  
ATOM   1628  CE2 TYR A 216      13.745  37.379  25.308  1.00 26.61           C  
ANISOU 1628  CE2 TYR A 216     3486   3802   2822    -37   -517    548       C  
ATOM   1629  CZ  TYR A 216      15.121  37.372  25.164  1.00 25.21           C  
ANISOU 1629  CZ  TYR A 216     3332   3625   2623    -75   -483    530       C  
ATOM   1630  OH  TYR A 216      15.676  37.722  23.952  1.00 28.43           O  
ANISOU 1630  OH  TYR A 216     3742   4098   2964   -136   -490    591       O  
ATOM   1631  N   MET A 217      11.507  37.639  31.562  1.00 13.86           N  
ANISOU 1631  N   MET A 217     1864   1892   1512    222   -445    319       N  
ATOM   1632  CA  MET A 217      10.813  37.341  32.813  1.00 18.95           C  
ANISOU 1632  CA  MET A 217     2494   2522   2183    260   -420    261       C  
ATOM   1633  C   MET A 217       9.672  36.347  32.597  1.00 15.96           C  
ANISOU 1633  C   MET A 217     2069   2215   1779    268   -428    260       C  
ATOM   1634  O   MET A 217       8.935  36.467  31.631  1.00 14.89           O  
ANISOU 1634  O   MET A 217     1903   2118   1636    271   -459    316       O  
ATOM   1635  CB  MET A 217      10.261  38.625  33.440  1.00 12.23           C  
ANISOU 1635  CB  MET A 217     1649   1589   1411    315   -412    263       C  
ATOM   1636  CG  MET A 217      11.326  39.614  33.855  1.00 14.55           C  
ANISOU 1636  CG  MET A 217     1994   1800   1733    296   -399    246       C  
ATOM   1637  SD  MET A 217      12.492  38.914  35.042  1.00 15.47           S  
ANISOU 1637  SD  MET A 217     2138   1939   1801    245   -372    165       S  
ATOM   1638  CE  MET A 217      14.012  39.198  34.144  1.00 14.61           C  
ANISOU 1638  CE  MET A 217     2056   1830   1666    180   -391    210       C  
ATOM   1639  N   GLY A 218       9.525  35.388  33.506  1.00 12.90           N  
ANISOU 1639  N   GLY A 218     1675   1849   1377    265   -401    203       N  
ATOM   1640  CA  GLY A 218       8.414  34.449  33.460  1.00 14.91           C  
ANISOU 1640  CA  GLY A 218     1887   2165   1614    263   -404    197       C  
ATOM   1641  C   GLY A 218       7.092  35.074  33.902  1.00 18.67           C  
ANISOU 1641  C   GLY A 218     2317   2639   2139    321   -405    211       C  
ATOM   1642  O   GLY A 218       6.540  34.728  34.953  1.00 15.08           O  
ANISOU 1642  O   GLY A 218     1843   2193   1695    340   -376    170       O  
ATOM   1643  N   VAL A 219       6.605  36.026  33.114  1.00 12.27           N  
ANISOU 1643  N   VAL A 219     1483   1819   1361    352   -434    276       N  
ATOM   1644  CA  VAL A 219       5.285  36.599  33.306  1.00 19.64           C  
ANISOU 1644  CA  VAL A 219     2355   2757   2350    416   -437    308       C  
ATOM   1645  C   VAL A 219       4.536  36.615  31.970  1.00 23.66           C  
ANISOU 1645  C   VAL A 219     2810   3337   2842    405   -492    399       C  
ATOM   1646  O   VAL A 219       5.152  36.594  30.909  1.00 22.27           O  
ANISOU 1646  O   VAL A 219     2658   3184   2620    356   -526    439       O  
ATOM   1647  CB  VAL A 219       5.354  38.034  33.890  1.00 17.97           C  
ANISOU 1647  CB  VAL A 219     2161   2440   2226    486   -411    308       C  
ATOM   1648  CG1 VAL A 219       6.323  38.094  35.068  1.00 13.07           C  
ANISOU 1648  CG1 VAL A 219     1605   1761   1601    470   -365    219       C  
ATOM   1649  CG2 VAL A 219       5.771  39.034  32.837  1.00 23.89           C  
ANISOU 1649  CG2 VAL A 219     2929   3144   3005    492   -447    390       C  
ATOM   1650  N   ASN A 220       3.207  36.606  32.025  1.00 14.20           N  
ANISOU 1650  N   ASN A 220     1533   2191   1672    443   -502    433       N  
ATOM   1651  CA  ASN A 220       2.406  36.830  30.835  1.00 15.02           C  
ANISOU 1651  CA  ASN A 220     1570   2370   1768    440   -562    537       C  
ATOM   1652  C   ASN A 220       1.493  38.015  31.087  1.00 28.15           C  
ANISOU 1652  C   ASN A 220     3168   3990   3538    546   -559    603       C  
ATOM   1653  O   ASN A 220       1.033  38.226  32.216  1.00 29.18           O  
ANISOU 1653  O   ASN A 220     3280   4076   3730    610   -505    550       O  
ATOM   1654  CB  ASN A 220       1.554  35.616  30.463  1.00 15.08           C  
ANISOU 1654  CB  ASN A 220     1520   2504   1704    375   -589    535       C  
ATOM   1655  CG  ASN A 220       2.367  34.447  29.941  1.00 15.94           C  
ANISOU 1655  CG  ASN A 220     1691   2653   1714    269   -592    480       C  
ATOM   1656  OD1 ASN A 220       1.816  33.382  29.702  1.00 14.86           O  
ANISOU 1656  OD1 ASN A 220     1528   2599   1521    203   -604    458       O  
ATOM   1657  ND2 ASN A 220       3.679  34.627  29.792  1.00 16.89           N  
ANISOU 1657  ND2 ASN A 220     1891   2709   1819    252   -577    453       N  
ATOM   1658  N   GLN A 221       1.201  38.771  30.037  1.00 19.40           N  
ANISOU 1658  N   GLN A 221     2020   2898   2453    566   -612    723       N  
ATOM   1659  CA  GLN A 221       0.248  39.856  30.147  1.00 19.57           C  
ANISOU 1659  CA  GLN A 221     1966   2880   2591    676   -611    806       C  
ATOM   1660  C   GLN A 221      -1.135  39.305  29.841  1.00 24.57           C  
ANISOU 1660  C   GLN A 221     2499   3632   3206    660   -634    837       C  
ATOM   1661  O   GLN A 221      -1.299  38.495  28.937  1.00 30.58           O  
ANISOU 1661  O   GLN A 221     3254   4498   3868    558   -677    847       O  
ATOM   1662  CB  GLN A 221       0.606  41.011  29.213  1.00 18.99           C  
ANISOU 1662  CB  GLN A 221     1919   2736   2561    688   -641    899       C  
ATOM   1663  CG  GLN A 221      -0.229  42.266  29.444  1.00 21.45           C  
ANISOU 1663  CG  GLN A 221     2180   2956   3014    805   -617    959       C  
ATOM   1664  CD  GLN A 221       0.225  43.440  28.583  1.00 29.74           C  
ANISOU 1664  CD  GLN A 221     3269   3922   4110    813   -641   1048       C  
ATOM   1665  OE1 GLN A 221       0.675  43.262  27.450  1.00 30.93           O  
ANISOU 1665  OE1 GLN A 221     3443   4138   4169    724   -690   1097       O  
ATOM   1666  NE2 GLN A 221       0.115  44.648  29.127  1.00 30.15           N  
ANISOU 1666  NE2 GLN A 221     3330   3824   4301    918   -596   1063       N  
ATOM   1667  N   LEU A 222      -2.109  39.680  30.657  1.00 25.94           N  
ANISOU 1667  N   LEU A 222     2599   3787   3472    755   -594    836       N  
ATOM   1668  CA  LEU A 222      -3.490  39.251  30.467  1.00 25.71           C  
ANISOU 1668  CA  LEU A 222     2465   3865   3437    745   -609    868       C  
ATOM   1669  C   LEU A 222      -4.228  40.251  29.586  1.00 29.81           C  
ANISOU 1669  C   LEU A 222     2930   4376   4021    787   -640    979       C  
ATOM   1670  O   LEU A 222      -3.730  41.347  29.349  1.00 29.40           O  
ANISOU 1670  O   LEU A 222     2919   4215   4038    842   -637   1022       O  
ATOM   1671  CB  LEU A 222      -4.184  39.101  31.822  1.00 30.21           C  
ANISOU 1671  CB  LEU A 222     2974   4435   4067    824   -541    807       C  
ATOM   1672  CG  LEU A 222      -3.547  38.111  32.802  1.00 33.01           C  
ANISOU 1672  CG  LEU A 222     3384   4805   4354    781   -500    690       C  
ATOM   1673  CD1 LEU A 222      -4.192  38.208  34.178  1.00 37.38           C  
ANISOU 1673  CD1 LEU A 222     3899   5334   4969    854   -412    613       C  
ATOM   1674  CD2 LEU A 222      -3.648  36.696  32.265  1.00 35.18           C  
ANISOU 1674  CD2 LEU A 222     3651   5211   4503    650   -550    681       C  
ATOM   1675  N   SER A 223      -5.426  39.894  29.127  1.00 34.41           N  
ANISOU 1675  N   SER A 223     3418   5072   4584    761   -668   1031       N  
ATOM   1676  CA  SER A 223      -6.146  40.732  28.170  1.00 37.92           C  
ANISOU 1676  CA  SER A 223     3802   5535   5072    787   -706   1152       C  
ATOM   1677  C   SER A 223      -6.571  42.069  28.778  1.00 40.19           C  
ANISOU 1677  C   SER A 223     4052   5696   5520    939   -658   1187       C  
ATOM   1678  O   SER A 223      -6.867  43.015  28.050  1.00 38.87           O  
ANISOU 1678  O   SER A 223     3859   5500   5411    980   -682   1291       O  
ATOM   1679  CB  SER A 223      -7.365  39.996  27.611  1.00 40.53           C  
ANISOU 1679  CB  SER A 223     4032   6024   5343    721   -745   1200       C  
ATOM   1680  OG  SER A 223      -8.136  39.416  28.645  1.00 46.21           O  
ANISOU 1680  OG  SER A 223     4687   6784   6086    749   -702   1142       O  
ATOM   1681  N   ASP A 224      -6.600  42.154  30.106  1.00 37.05           N  
ANISOU 1681  N   ASP A 224     3655   5225   5196   1022   -582   1098       N  
ATOM   1682  CA  ASP A 224      -6.945  43.417  30.755  1.00 37.96           C  
ANISOU 1682  CA  ASP A 224     3749   5204   5469   1166   -518   1104       C  
ATOM   1683  C   ASP A 224      -5.707  44.288  30.948  1.00 33.29           C  
ANISOU 1683  C   ASP A 224     3274   4444   4931   1202   -490   1074       C  
ATOM   1684  O   ASP A 224      -5.798  45.409  31.442  1.00 34.12           O  
ANISOU 1684  O   ASP A 224     3389   4407   5166   1311   -432   1066       O  
ATOM   1685  CB  ASP A 224      -7.635  43.176  32.100  1.00 42.39           C  
ANISOU 1685  CB  ASP A 224     4252   5767   6086   1239   -434   1013       C  
ATOM   1686  CG  ASP A 224      -6.800  42.342  33.049  1.00 44.43           C  
ANISOU 1686  CG  ASP A 224     4577   6024   6279   1199   -392    890       C  
ATOM   1687  OD1 ASP A 224      -5.750  41.813  32.632  1.00 45.85           O  
ANISOU 1687  OD1 ASP A 224     4841   6217   6364   1109   -436    878       O  
ATOM   1688  OD2 ASP A 224      -7.201  42.210  34.224  1.00 50.52           O  
ANISOU 1688  OD2 ASP A 224     5316   6791   7091   1257   -310    805       O  
ATOM   1689  N   GLY A 225      -4.549  43.765  30.563  1.00 26.30           N  
ANISOU 1689  N   GLY A 225     2478   3570   3943   1106   -528   1052       N  
ATOM   1690  CA  GLY A 225      -3.320  44.534  30.634  1.00 27.67           C  
ANISOU 1690  CA  GLY A 225     2762   3597   4155   1120   -510   1035       C  
ATOM   1691  C   GLY A 225      -2.489  44.229  31.867  1.00 33.40           C  
ANISOU 1691  C   GLY A 225     3557   4250   4884   1135   -443    909       C  
ATOM   1692  O   GLY A 225      -1.336  44.645  31.961  1.00 38.55           O  
ANISOU 1692  O   GLY A 225     4307   4796   5546   1122   -432    885       O  
ATOM   1693  N   ASN A 226      -3.081  43.511  32.819  1.00 30.22           N  
ANISOU 1693  N   ASN A 226     3101   3911   4470   1158   -395    831       N  
ATOM   1694  CA  ASN A 226      -2.363  43.074  34.013  1.00 30.08           C  
ANISOU 1694  CA  ASN A 226     3156   3854   4418   1144   -326    689       C  
ATOM   1695  C   ASN A 226      -1.400  41.940  33.707  1.00 29.25           C  
ANISOU 1695  C   ASN A 226     3127   3829   4159   1001   -374    644       C  
ATOM   1696  O   ASN A 226      -1.523  41.245  32.693  1.00 26.14           O  
ANISOU 1696  O   ASN A 226     2696   3553   3683    932   -453    722       O  
ATOM   1697  CB  ASN A 226      -3.339  42.629  35.098  1.00 34.83           C  
ANISOU 1697  CB  ASN A 226     3687   4514   5033   1188   -256    609       C  
ATOM   1698  CG  ASN A 226      -4.272  43.739  35.529  1.00 45.28           C  
ANISOU 1698  CG  ASN A 226     4936   5751   6518   1338   -185    632       C  
ATOM   1699  OD1 ASN A 226      -3.910  44.917  35.500  1.00 47.41           O  
ANISOU 1699  OD1 ASN A 226     5263   5862   6890   1395   -156    633       O  
ATOM   1700  ND2 ASN A 226      -5.488  43.370  35.920  1.00 46.00           N  
ANISOU 1700  ND2 ASN A 226     4919   5939   6620   1368   -158    623       N  
ATOM   1701  N   TYR A 227      -0.432  41.761  34.590  1.00 19.03           N  
ANISOU 1701  N   TYR A 227     1935   2471   2825    956   -325    516       N  
ATOM   1702  CA  TYR A 227       0.532  40.699  34.425  1.00 19.25           C  
ANISOU 1702  CA  TYR A 227     2031   2560   2724    837   -357    470       C  
ATOM   1703  C   TYR A 227       0.310  39.589  35.448  1.00 22.53           C  
ANISOU 1703  C   TYR A 227     2439   3049   3071    797   -318    369       C  
ATOM   1704  O   TYR A 227      -0.098  39.850  36.577  1.00 21.66           O  
ANISOU 1704  O   TYR A 227     2318   2908   3003    848   -247    296       O  
ATOM   1705  CB  TYR A 227       1.939  41.275  34.535  1.00 17.19           C  
ANISOU 1705  CB  TYR A 227     1884   2186   2462    803   -346    426       C  
ATOM   1706  CG  TYR A 227       2.354  41.988  33.272  1.00 28.46           C  
ANISOU 1706  CG  TYR A 227     3325   3576   3913    799   -405    540       C  
ATOM   1707  CD1 TYR A 227       2.947  41.291  32.232  1.00 26.09           C  
ANISOU 1707  CD1 TYR A 227     3041   3360   3513    708   -468    587       C  
ATOM   1708  CD2 TYR A 227       2.116  43.346  33.098  1.00 29.35           C  
ANISOU 1708  CD2 TYR A 227     3432   3571   4150    884   -392    604       C  
ATOM   1709  CE1 TYR A 227       3.324  41.922  31.071  1.00 17.45           C  
ANISOU 1709  CE1 TYR A 227     1956   2250   2425    694   -521    696       C  
ATOM   1710  CE2 TYR A 227       2.490  43.991  31.920  1.00 26.08           C  
ANISOU 1710  CE2 TYR A 227     3027   3128   3755    873   -451    727       C  
ATOM   1711  CZ  TYR A 227       3.091  43.263  30.911  1.00 27.24           C  
ANISOU 1711  CZ  TYR A 227     3188   3378   3784    774   -517    773       C  
ATOM   1712  OH  TYR A 227       3.483  43.857  29.721  1.00 35.04           O  
ANISOU 1712  OH  TYR A 227     4184   4359   4772    750   -574    898       O  
ATOM   1713  N   ILE A 228       0.595  38.353  35.053  1.00 16.03           N  
ANISOU 1713  N   ILE A 228     1625   2321   2144    702   -358    366       N  
ATOM   1714  CA  ILE A 228       0.508  37.231  35.959  1.00 17.70           C  
ANISOU 1714  CA  ILE A 228     1839   2594   2293    653   -326    286       C  
ATOM   1715  C   ILE A 228       1.852  36.511  35.950  1.00 15.07           C  
ANISOU 1715  C   ILE A 228     1598   2247   1882    566   -337    239       C  
ATOM   1716  O   ILE A 228       2.528  36.440  34.917  1.00 13.97           O  
ANISOU 1716  O   ILE A 228     1492   2106   1711    524   -383    281       O  
ATOM   1717  CB  ILE A 228      -0.645  36.257  35.567  1.00 24.18           C  
ANISOU 1717  CB  ILE A 228     2566   3544   3077    623   -357    329       C  
ATOM   1718  CG1 ILE A 228      -0.908  35.234  36.677  1.00 29.10           C  
ANISOU 1718  CG1 ILE A 228     3183   4218   3655    584   -312    254       C  
ATOM   1719  CG2 ILE A 228      -0.337  35.542  34.240  1.00 15.25           C  
ANISOU 1719  CG2 ILE A 228     1445   2476   1872    537   -430    384       C  
ATOM   1720  CD1 ILE A 228      -2.231  34.443  36.517  1.00 24.43           C  
ANISOU 1720  CD1 ILE A 228     2487   3750   3047    561   -329    293       C  
ATOM   1721  N   ARG A 229       2.253  36.022  37.117  1.00 13.78           N  
ANISOU 1721  N   ARG A 229     1470   2076   1687    543   -291    157       N  
ATOM   1722  CA  ARG A 229       3.385  35.126  37.237  1.00 12.85           C  
ANISOU 1722  CA  ARG A 229     1418   1963   1501    466   -298    123       C  
ATOM   1723  C   ARG A 229       3.073  33.901  36.387  1.00 20.80           C  
ANISOU 1723  C   ARG A 229     2398   3049   2455    404   -337    157       C  
ATOM   1724  O   ARG A 229       2.003  33.308  36.524  1.00 12.86           O  
ANISOU 1724  O   ARG A 229     1331   2114   1444    398   -336    166       O  
ATOM   1725  CB  ARG A 229       3.618  34.741  38.709  1.00 14.84           C  
ANISOU 1725  CB  ARG A 229     1691   2219   1728    452   -247     49       C  
ATOM   1726  CG  ARG A 229       4.665  33.656  38.945  1.00 11.82           C  
ANISOU 1726  CG  ARG A 229     1357   1851   1283    380   -254     31       C  
ATOM   1727  CD  ARG A 229       4.728  33.209  40.434  1.00 11.78           C  
ANISOU 1727  CD  ARG A 229     1358   1874   1246    361   -211    -20       C  
ATOM   1728  NE  ARG A 229       5.267  34.279  41.266  1.00 13.21           N  
ANISOU 1728  NE  ARG A 229     1577   2005   1437    382   -180    -71       N  
ATOM   1729  CZ  ARG A 229       6.556  34.417  41.563  1.00 12.38           C  
ANISOU 1729  CZ  ARG A 229     1529   1870   1306    346   -186    -89       C  
ATOM   1730  NH1 ARG A 229       7.449  33.543  41.109  1.00 11.13           N  
ANISOU 1730  NH1 ARG A 229     1389   1722   1117    301   -217    -55       N  
ATOM   1731  NH2 ARG A 229       6.948  35.436  42.306  1.00 12.18           N  
ANISOU 1731  NH2 ARG A 229     1539   1803   1286    352   -158   -144       N  
ATOM   1732  N   LYS A 230       3.994  33.554  35.491  1.00 13.68           N  
ANISOU 1732  N   LYS A 230     1542   2139   1517    355   -368    172       N  
ATOM   1733  CA  LYS A 230       3.849  32.388  34.627  1.00 11.97           C  
ANISOU 1733  CA  LYS A 230     1317   1985   1246    285   -395    186       C  
ATOM   1734  C   LYS A 230       4.938  31.424  35.030  1.00 16.93           C  
ANISOU 1734  C   LYS A 230     2003   2587   1840    238   -371    139       C  
ATOM   1735  O   LYS A 230       6.117  31.616  34.698  1.00 10.95           O  
ANISOU 1735  O   LYS A 230     1298   1789   1074    227   -372    134       O  
ATOM   1736  CB  LYS A 230       3.933  32.794  33.137  1.00 12.29           C  
ANISOU 1736  CB  LYS A 230     1354   2048   1267    267   -444    244       C  
ATOM   1737  CG  LYS A 230       3.800  31.634  32.136  1.00 12.69           C  
ANISOU 1737  CG  LYS A 230     1403   2168   1249    180   -469    243       C  
ATOM   1738  CD  LYS A 230       2.382  31.065  32.087  1.00 13.88           C  
ANISOU 1738  CD  LYS A 230     1480   2405   1389    156   -487    260       C  
ATOM   1739  CE  LYS A 230       2.206  30.081  30.890  1.00 13.53           C  
ANISOU 1739  CE  LYS A 230     1438   2435   1268     55   -518    257       C  
ATOM   1740  NZ  LYS A 230       2.459  30.731  29.554  1.00 13.60           N  
ANISOU 1740  NZ  LYS A 230     1448   2481   1238     35   -564    312       N  
ATOM   1741  N   TYR A 231       4.556  30.404  35.795  1.00 12.85           N  
ANISOU 1741  N   TYR A 231     1475   2096   1313    212   -348    112       N  
ATOM   1742  CA  TYR A 231       5.548  29.575  36.464  1.00 12.25           C  
ANISOU 1742  CA  TYR A 231     1444   1987   1223    185   -320     82       C  
ATOM   1743  C   TYR A 231       5.140  28.124  36.325  1.00 10.74           C  
ANISOU 1743  C   TYR A 231     1246   1823   1012    125   -313     74       C  
ATOM   1744  O   TYR A 231       4.125  27.830  35.688  1.00 13.49           O  
ANISOU 1744  O   TYR A 231     1556   2221   1348     96   -333     85       O  
ATOM   1745  CB  TYR A 231       5.706  29.983  37.932  1.00 11.58           C  
ANISOU 1745  CB  TYR A 231     1361   1888   1151    218   -289     61       C  
ATOM   1746  CG  TYR A 231       4.471  29.789  38.776  1.00 14.60           C  
ANISOU 1746  CG  TYR A 231     1691   2320   1536    226   -269     55       C  
ATOM   1747  CD1 TYR A 231       3.359  30.579  38.586  1.00 11.54           C  
ANISOU 1747  CD1 TYR A 231     1249   1960   1174    268   -273     66       C  
ATOM   1748  CD2 TYR A 231       4.424  28.810  39.767  1.00 14.25           C  
ANISOU 1748  CD2 TYR A 231     1644   2299   1473    193   -244     48       C  
ATOM   1749  CE1 TYR A 231       2.222  30.413  39.344  1.00 13.80           C  
ANISOU 1749  CE1 TYR A 231     1477   2302   1465    279   -248     61       C  
ATOM   1750  CE2 TYR A 231       3.276  28.637  40.552  1.00 11.41           C  
ANISOU 1750  CE2 TYR A 231     1230   1996   1108    194   -221     45       C  
ATOM   1751  CZ  TYR A 231       2.184  29.442  40.316  1.00 17.49           C  
ANISOU 1751  CZ  TYR A 231     1945   2799   1903    237   -221     47       C  
ATOM   1752  OH  TYR A 231       1.035  29.302  41.034  1.00 13.63           O  
ANISOU 1752  OH  TYR A 231     1391   2374   1412    242   -193     45       O  
ATOM   1753  N   ALA A 232       5.914  27.209  36.887  1.00 10.47           N  
ANISOU 1753  N   ALA A 232     1246   1755    979    103   -287     61       N  
ATOM   1754  CA  ALA A 232       5.670  25.804  36.575  1.00 13.51           C  
ANISOU 1754  CA  ALA A 232     1638   2139   1358     43   -276     53       C  
ATOM   1755  C   ALA A 232       4.319  25.339  37.117  1.00 17.18           C  
ANISOU 1755  C   ALA A 232     2053   2654   1820     17   -274     61       C  
ATOM   1756  O   ALA A 232       3.680  24.466  36.524  1.00 14.65           O  
ANISOU 1756  O   ALA A 232     1725   2352   1489    -45   -279     53       O  
ATOM   1757  CB  ALA A 232       6.784  24.933  37.102  1.00 10.46           C  
ANISOU 1757  CB  ALA A 232     1291   1693    990     37   -245     52       C  
ATOM   1758  N   GLY A 233       3.875  25.964  38.211  1.00 16.00           N  
ANISOU 1758  N   GLY A 233     1868   2534   1676     57   -264     71       N  
ATOM   1759  CA  GLY A 233       2.629  25.609  38.874  1.00 14.15           C  
ANISOU 1759  CA  GLY A 233     1578   2360   1438     37   -254     81       C  
ATOM   1760  C   GLY A 233       1.387  25.879  38.043  1.00 14.66           C  
ANISOU 1760  C   GLY A 233     1583   2490   1498     25   -282     92       C  
ATOM   1761  O   GLY A 233       0.596  24.976  37.791  1.00 17.81           O  
ANISOU 1761  O   GLY A 233     1954   2927   1885    -40   -288     98       O  
ATOM   1762  N   ASN A 234       1.194  27.123  37.618  1.00 13.38           N  
ANISOU 1762  N   ASN A 234     1395   2342   1347     85   -301    102       N  
ATOM   1763  CA  ASN A 234      -0.006  27.441  36.883  1.00 12.76           C  
ANISOU 1763  CA  ASN A 234     1243   2337   1270     82   -333    132       C  
ATOM   1764  C   ASN A 234       0.134  27.050  35.402  1.00 12.88           C  
ANISOU 1764  C   ASN A 234     1277   2364   1252     20   -377    141       C  
ATOM   1765  O   ASN A 234      -0.856  26.883  34.717  1.00 13.51           O  
ANISOU 1765  O   ASN A 234     1297   2522   1313    -21   -410    167       O  
ATOM   1766  CB  ASN A 234      -0.383  28.927  37.058  1.00 13.06           C  
ANISOU 1766  CB  ASN A 234     1236   2380   1347    178   -332    153       C  
ATOM   1767  CG  ASN A 234       0.640  29.901  36.476  1.00 16.95           C  
ANISOU 1767  CG  ASN A 234     1783   2804   1854    222   -348    156       C  
ATOM   1768  OD1 ASN A 234       1.735  29.526  36.032  1.00 13.71           O  
ANISOU 1768  OD1 ASN A 234     1443   2347   1420    186   -356    140       O  
ATOM   1769  ND2 ASN A 234       0.289  31.183  36.513  1.00 13.15           N  
ANISOU 1769  ND2 ASN A 234     1267   2310   1420    302   -348    179       N  
ATOM   1770  N   THR A 235       1.359  26.866  34.924  1.00 13.13           N  
ANISOU 1770  N   THR A 235     1387   2330   1271      6   -374    117       N  
ATOM   1771  CA  THR A 235       1.548  26.451  33.529  1.00 15.16           C  
ANISOU 1771  CA  THR A 235     1668   2605   1485    -61   -404    110       C  
ATOM   1772  C   THR A 235       1.121  24.992  33.377  1.00 18.25           C  
ANISOU 1772  C   THR A 235     2069   3012   1853   -160   -393     78       C  
ATOM   1773  O   THR A 235       0.470  24.630  32.396  1.00 13.93           O  
ANISOU 1773  O   THR A 235     1501   2530   1263   -236   -425     77       O  
ATOM   1774  CB  THR A 235       3.008  26.642  33.049  1.00 14.38           C  
ANISOU 1774  CB  THR A 235     1646   2436   1380    -48   -392     89       C  
ATOM   1775  OG1 THR A 235       3.367  28.032  33.139  1.00 13.80           O  
ANISOU 1775  OG1 THR A 235     1566   2345   1331     31   -405    122       O  
ATOM   1776  CG2 THR A 235       3.196  26.144  31.594  1.00 12.47           C  
ANISOU 1776  CG2 THR A 235     1432   2223   1082   -127   -411     70       C  
ATOM   1777  N   TYR A 236       1.477  24.148  34.347  1.00 18.14           N  
ANISOU 1777  N   TYR A 236     2088   2938   1866   -168   -349     54       N  
ATOM   1778  CA  TYR A 236       1.266  22.713  34.151  1.00 18.63           C  
ANISOU 1778  CA  TYR A 236     2177   2981   1919   -264   -330     21       C  
ATOM   1779  C   TYR A 236       0.124  22.091  34.955  1.00 16.97           C  
ANISOU 1779  C   TYR A 236     1914   2816   1719   -306   -324     39       C  
ATOM   1780  O   TYR A 236      -0.411  21.047  34.571  1.00 15.56           O  
ANISOU 1780  O   TYR A 236     1740   2645   1526   -405   -323     17       O  
ATOM   1781  CB  TYR A 236       2.568  21.968  34.438  1.00 12.72           C  
ANISOU 1781  CB  TYR A 236     1509   2122   1203   -256   -283    -10       C  
ATOM   1782  CG  TYR A 236       3.661  22.351  33.456  1.00 12.47           C  
ANISOU 1782  CG  TYR A 236     1528   2057   1155   -238   -282    -36       C  
ATOM   1783  CD1 TYR A 236       3.535  22.049  32.098  1.00 13.00           C  
ANISOU 1783  CD1 TYR A 236     1614   2152   1172   -311   -294    -75       C  
ATOM   1784  CD2 TYR A 236       4.803  23.027  33.878  1.00 15.69           C  
ANISOU 1784  CD2 TYR A 236     1958   2417   1587   -158   -269    -22       C  
ATOM   1785  CE1 TYR A 236       4.518  22.386  31.195  1.00 12.88           C  
ANISOU 1785  CE1 TYR A 236     1642   2119   1134   -301   -287    -99       C  
ATOM   1786  CE2 TYR A 236       5.800  23.368  32.973  1.00 11.70           C  
ANISOU 1786  CE2 TYR A 236     1491   1889   1064   -148   -265    -42       C  
ATOM   1787  CZ  TYR A 236       5.642  23.052  31.634  1.00 20.26           C  
ANISOU 1787  CZ  TYR A 236     2594   3004   2100   -217   -272    -79       C  
ATOM   1788  OH  TYR A 236       6.611  23.395  30.734  1.00 18.19           O  
ANISOU 1788  OH  TYR A 236     2367   2733   1813   -211   -262    -98       O  
ATOM   1789  N   LEU A 237      -0.279  22.747  36.036  1.00 13.84           N  
ANISOU 1789  N   LEU A 237     1465   2452   1343   -239   -317     74       N  
ATOM   1790  CA  LEU A 237      -1.217  22.132  36.969  1.00 13.82           C  
ANISOU 1790  CA  LEU A 237     1413   2490   1349   -276   -299     94       C  
ATOM   1791  C   LEU A 237      -2.459  22.987  37.163  1.00 16.56           C  
ANISOU 1791  C   LEU A 237     1655   2947   1689   -243   -319    129       C  
ATOM   1792  O   LEU A 237      -3.139  22.864  38.176  1.00 14.79           O  
ANISOU 1792  O   LEU A 237     1378   2767   1472   -240   -294    148       O  
ATOM   1793  CB  LEU A 237      -0.530  21.885  38.322  1.00 15.17           C  
ANISOU 1793  CB  LEU A 237     1616   2602   1544   -238   -255    104       C  
ATOM   1794  CG  LEU A 237       0.776  21.078  38.293  1.00 15.08           C  
ANISOU 1794  CG  LEU A 237     1694   2479   1556   -250   -232     88       C  
ATOM   1795  CD1 LEU A 237       1.433  21.041  39.651  1.00 14.71           C  
ANISOU 1795  CD1 LEU A 237     1661   2401   1526   -206   -202    118       C  
ATOM   1796  CD2 LEU A 237       0.550  19.657  37.775  1.00 13.67           C  
ANISOU 1796  CD2 LEU A 237     1550   2256   1390   -352   -220     70       C  
ATOM   1797  N   ASN A 238      -2.746  23.851  36.193  1.00 14.84           N  
ANISOU 1797  N   ASN A 238     1401   2778   1459   -216   -361    143       N  
ATOM   1798  CA  ASN A 238      -3.920  24.711  36.254  1.00 15.05           C  
ANISOU 1798  CA  ASN A 238     1317   2905   1495   -171   -380    188       C  
ATOM   1799  C   ASN A 238      -5.211  23.936  35.994  1.00 15.97           C  
ANISOU 1799  C   ASN A 238     1353   3126   1588   -268   -403    211       C  
ATOM   1800  O   ASN A 238      -5.179  22.751  35.664  1.00 16.16           O  
ANISOU 1800  O   ASN A 238     1419   3135   1585   -380   -406    184       O  
ATOM   1801  CB  ASN A 238      -3.783  25.873  35.256  1.00 15.10           C  
ANISOU 1801  CB  ASN A 238     1306   2925   1504   -111   -424    217       C  
ATOM   1802  CG  ASN A 238      -3.862  25.420  33.805  1.00 17.83           C  
ANISOU 1802  CG  ASN A 238     1662   3314   1797   -205   -478    222       C  
ATOM   1803  OD1 ASN A 238      -4.892  24.910  33.353  1.00 16.31           O  
ANISOU 1803  OD1 ASN A 238     1402   3220   1574   -286   -511    244       O  
ATOM   1804  ND2 ASN A 238      -2.776  25.621  33.067  1.00 15.02           N  
ANISOU 1804  ND2 ASN A 238     1387   2896   1423   -201   -488    200       N  
ATOM   1805  N   ARG A 239      -6.341  24.628  36.110  1.00 19.95           N  
ANISOU 1805  N   ARG A 239     1739   3734   2107   -226   -416    261       N  
ATOM   1806  CA  ARG A 239      -7.655  23.986  36.060  1.00 17.66           C  
ANISOU 1806  CA  ARG A 239     1349   3562   1798   -312   -434    292       C  
ATOM   1807  C   ARG A 239      -8.089  23.435  34.704  1.00 22.37           C  
ANISOU 1807  C   ARG A 239     1928   4229   2341   -432   -501    304       C  
ATOM   1808  O   ARG A 239      -9.157  22.816  34.621  1.00 22.40           O  
ANISOU 1808  O   ARG A 239     1851   4337   2322   -526   -521    328       O  
ATOM   1809  CB  ARG A 239      -8.745  24.961  36.541  1.00 21.71           C  
ANISOU 1809  CB  ARG A 239     1724   4174   2351   -219   -425    349       C  
ATOM   1810  CG  ARG A 239      -8.762  25.296  38.047  1.00 18.19           C  
ANISOU 1810  CG  ARG A 239     1265   3703   1942   -135   -347    329       C  
ATOM   1811  CD  ARG A 239      -9.306  24.156  38.910  1.00 18.53           C  
ANISOU 1811  CD  ARG A 239     1287   3791   1962   -229   -311    323       C  
ATOM   1812  NE  ARG A 239     -10.739  23.970  38.687  1.00 25.54           N  
ANISOU 1812  NE  ARG A 239     2033   4825   2845   -279   -333    376       N  
ATOM   1813  CZ  ARG A 239     -11.699  24.735  39.203  1.00 29.73           C  
ANISOU 1813  CZ  ARG A 239     2434   5450   3411   -196   -303    412       C  
ATOM   1814  NH1 ARG A 239     -11.398  25.755  39.997  1.00 34.96           N  
ANISOU 1814  NH1 ARG A 239     3100   6067   4115    -60   -244    389       N  
ATOM   1815  NH2 ARG A 239     -12.968  24.483  38.909  1.00 24.98           N  
ANISOU 1815  NH2 ARG A 239     1696   4992   2804   -252   -330    469       N  
ATOM   1816  N   ASN A 240      -7.318  23.668  33.642  1.00 18.15           N  
ANISOU 1816  N   ASN A 240     1461   3655   1778   -440   -536    288       N  
ATOM   1817  CA  ASN A 240      -7.611  23.000  32.377  1.00 19.27           C  
ANISOU 1817  CA  ASN A 240     1607   3865   1850   -578   -592    279       C  
ATOM   1818  C   ASN A 240      -7.139  21.555  32.437  1.00 22.64           C  
ANISOU 1818  C   ASN A 240     2139   4209   2255   -700   -557    198       C  
ATOM   1819  O   ASN A 240      -7.626  20.716  31.682  1.00 19.47           O  
ANISOU 1819  O   ASN A 240     1736   3864   1799   -843   -587    174       O  
ATOM   1820  CB  ASN A 240      -6.933  23.700  31.185  1.00 18.60           C  
ANISOU 1820  CB  ASN A 240     1568   3766   1734   -553   -630    287       C  
ATOM   1821  CG  ASN A 240      -7.544  25.048  30.866  1.00 24.93           C  
ANISOU 1821  CG  ASN A 240     2286   4614   2572   -443   -652    376       C  
ATOM   1822  OD1 ASN A 240      -8.751  25.260  31.020  1.00 19.98           O  
ANISOU 1822  OD1 ASN A 240     1555   4069   1967   -432   -658    433       O  
ATOM   1823  ND2 ASN A 240      -6.701  25.979  30.427  1.00 22.08           N  
ANISOU 1823  ND2 ASN A 240     1970   4196   2223   -363   -661    390       N  
ATOM   1824  N   TYR A 241      -6.182  21.281  33.329  1.00 17.72           N  
ANISOU 1824  N   TYR A 241     1605   3451   1678   -644   -494    159       N  
ATOM   1825  CA  TYR A 241      -5.491  19.988  33.376  1.00 20.30           C  
ANISOU 1825  CA  TYR A 241     2042   3664   2006   -732   -453     89       C  
ATOM   1826  C   TYR A 241      -5.771  19.205  34.660  1.00 19.80           C  
ANISOU 1826  C   TYR A 241     1975   3561   1986   -750   -405     98       C  
ATOM   1827  O   TYR A 241      -5.855  17.981  34.632  1.00 18.16           O  
ANISOU 1827  O   TYR A 241     1815   3306   1780   -863   -385     64       O  
ATOM   1828  CB  TYR A 241      -3.967  20.197  33.207  1.00 16.66           C  
ANISOU 1828  CB  TYR A 241     1693   3075   1563   -661   -423     47       C  
ATOM   1829  CG  TYR A 241      -3.648  20.874  31.890  1.00 16.73           C  
ANISOU 1829  CG  TYR A 241     1711   3125   1520   -660   -467     40       C  
ATOM   1830  CD1 TYR A 241      -3.697  20.161  30.701  1.00 17.46           C  
ANISOU 1830  CD1 TYR A 241     1843   3241   1549   -788   -486    -13       C  
ATOM   1831  CD2 TYR A 241      -3.345  22.232  31.829  1.00 16.22           C  
ANISOU 1831  CD2 TYR A 241     1617   3081   1466   -542   -489     87       C  
ATOM   1832  CE1 TYR A 241      -3.457  20.766  29.486  1.00 21.01           C  
ANISOU 1832  CE1 TYR A 241     2296   3751   1936   -801   -528    -13       C  
ATOM   1833  CE2 TYR A 241      -3.086  22.854  30.605  1.00 16.41           C  
ANISOU 1833  CE2 TYR A 241     1646   3150   1440   -549   -533     97       C  
ATOM   1834  CZ  TYR A 241      -3.147  22.109  29.441  1.00 18.13           C  
ANISOU 1834  CZ  TYR A 241     1897   3408   1583   -680   -554     50       C  
ATOM   1835  OH  TYR A 241      -2.906  22.692  28.221  1.00 19.22           O  
ANISOU 1835  OH  TYR A 241     2039   3609   1656   -701   -598     64       O  
ATOM   1836  N   VAL A 242      -5.892  19.913  35.779  1.00 17.42           N  
ANISOU 1836  N   VAL A 242     1623   3278   1719   -643   -382    141       N  
ATOM   1837  CA  VAL A 242      -6.119  19.286  37.084  1.00 17.76           C  
ANISOU 1837  CA  VAL A 242     1658   3300   1791   -655   -335    160       C  
ATOM   1838  C   VAL A 242      -7.264  20.012  37.792  1.00 21.19           C  
ANISOU 1838  C   VAL A 242     1962   3864   2226   -607   -335    213       C  
ATOM   1839  O   VAL A 242      -7.240  21.240  37.887  1.00 17.42           O  
ANISOU 1839  O   VAL A 242     1441   3420   1759   -491   -339    229       O  
ATOM   1840  CB  VAL A 242      -4.852  19.336  37.968  1.00 18.68           C  
ANISOU 1840  CB  VAL A 242     1859   3297   1942   -571   -288    151       C  
ATOM   1841  CG1 VAL A 242      -5.092  18.606  39.277  1.00 20.71           C  
ANISOU 1841  CG1 VAL A 242     2107   3545   2217   -600   -245    183       C  
ATOM   1842  CG2 VAL A 242      -3.671  18.721  37.249  1.00 18.22           C  
ANISOU 1842  CG2 VAL A 242     1916   3112   1895   -597   -281    102       C  
ATOM   1843  N   ASP A 243      -8.266  19.290  38.294  1.00 18.56           N  
ANISOU 1843  N   ASP A 243     1563   3602   1886   -693   -324    240       N  
ATOM   1844  CA  ASP A 243      -9.384  19.996  38.924  1.00 19.11           C  
ANISOU 1844  CA  ASP A 243     1497   3807   1959   -643   -315    289       C  
ATOM   1845  C   ASP A 243      -9.016  20.402  40.363  1.00 18.65           C  
ANISOU 1845  C   ASP A 243     1446   3721   1919   -548   -251    293       C  
ATOM   1846  O   ASP A 243      -7.912  20.117  40.831  1.00 17.92           O  
ANISOU 1846  O   ASP A 243     1457   3516   1835   -528   -225    271       O  
ATOM   1847  CB  ASP A 243     -10.681  19.158  38.876  1.00 20.32           C  
ANISOU 1847  CB  ASP A 243     1558   4072   2091   -777   -330    321       C  
ATOM   1848  CG  ASP A 243     -10.651  17.900  39.767  1.00 26.07           C  
ANISOU 1848  CG  ASP A 243     2334   4749   2825   -876   -286    324       C  
ATOM   1849  OD1 ASP A 243      -9.850  17.800  40.722  1.00 19.94           O  
ANISOU 1849  OD1 ASP A 243     1627   3885   2066   -822   -239    321       O  
ATOM   1850  OD2 ASP A 243     -11.487  17.000  39.515  1.00 23.12           O  
ANISOU 1850  OD2 ASP A 243     1919   4429   2434  -1016   -303    339       O  
ATOM   1851  N   GLU A 244      -9.934  21.067  41.051  1.00 19.20           N  
ANISOU 1851  N   GLU A 244     1400   3903   1994   -491   -224    322       N  
ATOM   1852  CA  GLU A 244      -9.652  21.617  42.376  1.00 19.19           C  
ANISOU 1852  CA  GLU A 244     1400   3895   1997   -401   -158    314       C  
ATOM   1853  C   GLU A 244      -9.407  20.549  43.444  1.00 19.00           C  
ANISOU 1853  C   GLU A 244     1423   3845   1951   -480   -118    326       C  
ATOM   1854  O   GLU A 244      -8.893  20.851  44.520  1.00 29.18           O  
ANISOU 1854  O   GLU A 244     2741   5117   3228   -425    -70    316       O  
ATOM   1855  CB  GLU A 244     -10.803  22.527  42.825  1.00 20.99           C  
ANISOU 1855  CB  GLU A 244     1484   4254   2237   -327   -126    334       C  
ATOM   1856  CG  GLU A 244     -12.110  21.793  43.155  1.00 20.95           C  
ANISOU 1856  CG  GLU A 244     1362   4382   2214   -423   -114    379       C  
ATOM   1857  CD  GLU A 244     -12.990  21.521  41.934  1.00 39.49           C  
ANISOU 1857  CD  GLU A 244     3630   6811   4564   -499   -183    417       C  
ATOM   1858  OE1 GLU A 244     -12.464  21.466  40.795  1.00 30.57           O  
ANISOU 1858  OE1 GLU A 244     2565   5618   3433   -522   -245    404       O  
ATOM   1859  OE2 GLU A 244     -14.222  21.375  42.118  1.00 40.27           O  
ANISOU 1859  OE2 GLU A 244     3592   7050   4659   -541   -175    461       O  
ATOM   1860  N   ASN A 245      -9.806  19.317  43.147  1.00 19.52           N  
ANISOU 1860  N   ASN A 245     1494   3912   2011   -614   -137    351       N  
ATOM   1861  CA  ASN A 245      -9.601  18.174  44.035  1.00 22.60           C  
ANISOU 1861  CA  ASN A 245     1932   4264   2392   -702   -105    380       C  
ATOM   1862  C   ASN A 245      -8.395  17.343  43.635  1.00 22.96           C  
ANISOU 1862  C   ASN A 245     2116   4146   2461   -741   -121    365       C  
ATOM   1863  O   ASN A 245      -8.153  16.264  44.194  1.00 20.79           O  
ANISOU 1863  O   ASN A 245     1890   3812   2197   -819   -101    400       O  
ATOM   1864  CB  ASN A 245     -10.841  17.291  44.069  1.00 24.73           C  
ANISOU 1864  CB  ASN A 245     2118   4628   2650   -835   -107    423       C  
ATOM   1865  CG  ASN A 245     -12.057  18.030  44.562  1.00 28.02           C  
ANISOU 1865  CG  ASN A 245     2383   5216   3049   -796    -80    445       C  
ATOM   1866  OD1 ASN A 245     -11.973  18.830  45.502  1.00 26.24           O  
ANISOU 1866  OD1 ASN A 245     2127   5032   2810   -696    -29    438       O  
ATOM   1867  ND2 ASN A 245     -13.202  17.756  43.952  1.00 25.26           N  
ANISOU 1867  ND2 ASN A 245     1931   4971   2696   -878   -110    470       N  
ATOM   1868  N   GLY A 246      -7.663  17.827  42.641  1.00 18.44           N  
ANISOU 1868  N   GLY A 246     1601   3501   1903   -686   -154    319       N  
ATOM   1869  CA  GLY A 246      -6.422  17.187  42.245  1.00 20.08           C  
ANISOU 1869  CA  GLY A 246     1935   3556   2140   -699   -159    297       C  
ATOM   1870  C   GLY A 246      -6.518  16.099  41.197  1.00 21.27           C  
ANISOU 1870  C   GLY A 246     2135   3639   2307   -818   -181    273       C  
ATOM   1871  O   GLY A 246      -5.511  15.472  40.857  1.00 18.11           O  
ANISOU 1871  O   GLY A 246     1838   3102   1940   -829   -172    249       O  
ATOM   1872  N   ARG A 247      -7.716  15.886  40.662  1.00 19.23           N  
ANISOU 1872  N   ARG A 247     1801   3479   2027   -910   -207    275       N  
ATOM   1873  CA  ARG A 247      -7.903  14.848  39.657  1.00 27.38           C  
ANISOU 1873  CA  ARG A 247     2880   4459   3063  -1046   -227    239       C  
ATOM   1874  C   ARG A 247      -7.736  15.433  38.265  1.00 23.17           C  
ANISOU 1874  C   ARG A 247     2359   3943   2502  -1033   -273    183       C  
ATOM   1875  O   ARG A 247      -8.378  16.417  37.926  1.00 20.53           O  
ANISOU 1875  O   ARG A 247     1930   3734   2135   -987   -310    199       O  
ATOM   1876  CB  ARG A 247      -9.278  14.185  39.800  1.00 30.11           C  
ANISOU 1876  CB  ARG A 247     3140   4909   3391  -1181   -235    272       C  
ATOM   1877  CG  ARG A 247      -9.395  13.376  41.075  1.00 36.87           C  
ANISOU 1877  CG  ARG A 247     4001   5734   4274  -1224   -188    331       C  
ATOM   1878  CD  ARG A 247     -10.712  12.647  41.193  1.00 51.37           C  
ANISOU 1878  CD  ARG A 247     5757   7668   6095  -1373   -193    367       C  
ATOM   1879  NE  ARG A 247     -10.717  11.819  42.395  1.00 57.52           N  
ANISOU 1879  NE  ARG A 247     6552   8404   6900  -1421   -147    432       N  
ATOM   1880  CZ  ARG A 247     -11.183  12.220  43.573  1.00 63.55           C  
ANISOU 1880  CZ  ARG A 247     7229   9278   7638  -1377   -118    497       C  
ATOM   1881  NH1 ARG A 247     -11.696  13.439  43.708  1.00 61.39           N  
ANISOU 1881  NH1 ARG A 247     6847   9151   7325  -1277   -123    494       N  
ATOM   1882  NH2 ARG A 247     -11.141  11.402  44.618  1.00 64.37           N  
ANISOU 1882  NH2 ARG A 247     7354   9344   7758  -1433    -79    565       N  
ATOM   1883  N   GLY A 248      -6.842  14.832  37.488  1.00 19.57           N  
ANISOU 1883  N   GLY A 248     2016   3358   2062  -1069   -267    124       N  
ATOM   1884  CA  GLY A 248      -6.625  15.214  36.105  1.00 26.39           C  
ANISOU 1884  CA  GLY A 248     2903   4237   2886  -1082   -306     66       C  
ATOM   1885  C   GLY A 248      -7.876  15.154  35.252  1.00 25.78           C  
ANISOU 1885  C   GLY A 248     2743   4303   2750  -1202   -360     63       C  
ATOM   1886  O   GLY A 248      -8.778  14.351  35.503  1.00 26.47           O  
ANISOU 1886  O   GLY A 248     2792   4431   2835  -1323   -360     78       O  
ATOM   1887  N   ILE A 249      -7.894  15.993  34.222  1.00 25.78           N  
ANISOU 1887  N   ILE A 249     2714   4380   2699  -1176   -410     51       N  
ATOM   1888  CA  ILE A 249      -9.046  16.212  33.364  1.00 26.21           C  
ANISOU 1888  CA  ILE A 249     2667   4603   2688  -1268   -477     70       C  
ATOM   1889  C   ILE A 249      -8.798  15.707  31.935  1.00 22.96           C  
ANISOU 1889  C   ILE A 249     2328   4182   2213  -1394   -505     -9       C  
ATOM   1890  O   ILE A 249      -7.709  15.888  31.384  1.00 21.51           O  
ANISOU 1890  O   ILE A 249     2240   3909   2026  -1345   -489    -62       O  
ATOM   1891  CB  ILE A 249      -9.415  17.716  33.319  1.00 27.50           C  
ANISOU 1891  CB  ILE A 249     2716   4891   2841  -1134   -520    142       C  
ATOM   1892  CG1 ILE A 249      -9.841  18.192  34.706  1.00 28.50           C  
ANISOU 1892  CG1 ILE A 249     2762   5046   3021  -1028   -484    205       C  
ATOM   1893  CG2 ILE A 249     -10.514  17.991  32.301  1.00 30.53           C  
ANISOU 1893  CG2 ILE A 249     3016   5417   3168  -1190   -576    179       C  
ATOM   1894  CD1 ILE A 249     -10.117  19.666  34.776  1.00 31.28           C  
ANISOU 1894  CD1 ILE A 249     3015   5484   3385   -880   -506    265       C  
ATOM   1895  N   GLY A 250      -9.809  15.040  31.376  1.00 23.47           N  
ANISOU 1895  N   GLY A 250     2366   4318   2234  -1528   -523    -16       N  
ATOM   1896  CA  GLY A 250      -9.792  14.545  30.006  1.00 31.76           C  
ANISOU 1896  CA  GLY A 250     3489   5361   3217  -1629   -529    -85       C  
ATOM   1897  C   GLY A 250      -8.608  13.659  29.675  1.00 28.38           C  
ANISOU 1897  C   GLY A 250     3215   4764   2805  -1690   -476   -203       C  
ATOM   1898  O   GLY A 250      -8.393  12.607  30.278  1.00 28.83           O  
ANISOU 1898  O   GLY A 250     3338   4697   2918  -1764   -427   -248       O  
ATOM   1899  N   LYS A 251      -7.834  14.113  28.703  1.00 26.25           N  
ANISOU 1899  N   LYS A 251     3001   4480   2491  -1654   -479   -247       N  
ATOM   1900  CA  LYS A 251      -6.602  13.463  28.270  1.00 30.29           C  
ANISOU 1900  CA  LYS A 251     3655   4838   3017  -1683   -421   -362       C  
ATOM   1901  C   LYS A 251      -5.584  13.323  29.420  1.00 29.87           C  
ANISOU 1901  C   LYS A 251     3658   4625   3068  -1584   -366   -363       C  
ATOM   1902  O   LYS A 251      -4.669  12.494  29.370  1.00 26.38           O  
ANISOU 1902  O   LYS A 251     3334   4011   2678  -1594   -292   -443       O  
ATOM   1903  CB  LYS A 251      -6.023  14.271  27.102  1.00 36.59           C  
ANISOU 1903  CB  LYS A 251     4472   5686   3745  -1629   -437   -377       C  
ATOM   1904  CG  LYS A 251      -4.682  13.833  26.572  1.00 46.44           C  
ANISOU 1904  CG  LYS A 251     5852   6794   4998  -1631   -372   -489       C  
ATOM   1905  CD  LYS A 251      -4.260  14.672  25.360  1.00 41.51           C  
ANISOU 1905  CD  LYS A 251     5229   6249   4295  -1590   -392   -487       C  
ATOM   1906  CE  LYS A 251      -5.020  14.262  24.118  1.00 44.71           C  
ANISOU 1906  CE  LYS A 251     5630   6747   4610  -1713   -400   -513       C  
ATOM   1907  NZ  LYS A 251      -4.676  12.868  23.716  1.00 47.66           N  
ANISOU 1907  NZ  LYS A 251     6123   6998   4990  -1829   -319   -650       N  
ATOM   1908  N   PHE A 252      -5.755  14.135  30.460  1.00 26.97           N  
ANISOU 1908  N   PHE A 252     3207   4296   2744  -1448   -382   -258       N  
ATOM   1909  CA  PHE A 252      -4.852  14.125  31.611  1.00 21.46           C  
ANISOU 1909  CA  PHE A 252     2554   3457   2143  -1312   -323   -228       C  
ATOM   1910  C   PHE A 252      -5.473  13.379  32.806  1.00 20.97           C  
ANISOU 1910  C   PHE A 252     2465   3362   2142  -1347   -297   -179       C  
ATOM   1911  O   PHE A 252      -5.007  13.512  33.942  1.00 23.76           O  
ANISOU 1911  O   PHE A 252     2819   3650   2560  -1239   -264   -123       O  
ATOM   1912  CB  PHE A 252      -4.486  15.558  32.011  1.00 19.42           C  
ANISOU 1912  CB  PHE A 252     2236   3255   1887  -1140   -349   -156       C  
ATOM   1913  CG  PHE A 252      -3.578  16.255  31.025  1.00 20.71           C  
ANISOU 1913  CG  PHE A 252     2444   3413   2011  -1086   -359   -193       C  
ATOM   1914  CD1 PHE A 252      -4.028  16.594  29.757  1.00 19.62           C  
ANISOU 1914  CD1 PHE A 252     2278   3395   1780  -1166   -414   -214       C  
ATOM   1915  CD2 PHE A 252      -2.276  16.565  31.371  1.00 17.97           C  
ANISOU 1915  CD2 PHE A 252     2161   2952   1714   -965   -316   -199       C  
ATOM   1916  CE1 PHE A 252      -3.180  17.227  28.849  1.00 19.77           C  
ANISOU 1916  CE1 PHE A 252     2339   3416   1756  -1124   -422   -241       C  
ATOM   1917  CE2 PHE A 252      -1.432  17.198  30.485  1.00 17.61           C  
ANISOU 1917  CE2 PHE A 252     2153   2906   1632   -921   -322   -228       C  
ATOM   1918  CZ  PHE A 252      -1.882  17.528  29.217  1.00 20.73           C  
ANISOU 1918  CZ  PHE A 252     2526   3418   1934  -1001   -373   -250       C  
ATOM   1919  N   SER A 253      -6.530  12.608  32.559  1.00 22.21           N  
ANISOU 1919  N   SER A 253     2592   3575   2271  -1508   -315   -194       N  
ATOM   1920  CA  SER A 253      -7.290  12.003  33.658  1.00 28.52           C  
ANISOU 1920  CA  SER A 253     3345   4376   3115  -1554   -299   -132       C  
ATOM   1921  C   SER A 253      -6.479  10.919  34.396  1.00 23.74           C  
ANISOU 1921  C   SER A 253     2849   3564   2608  -1551   -221   -143       C  
ATOM   1922  O   SER A 253      -6.847  10.493  35.494  1.00 22.89           O  
ANISOU 1922  O   SER A 253     2712   3438   2546  -1558   -201    -74       O  
ATOM   1923  CB  SER A 253      -8.617  11.424  33.146  1.00 24.12           C  
ANISOU 1923  CB  SER A 253     2727   3935   2502  -1744   -340   -145       C  
ATOM   1924  OG  SER A 253      -8.400  10.359  32.247  1.00 25.49           O  
ANISOU 1924  OG  SER A 253     3010   4009   2667  -1894   -315   -253       O  
ATOM   1925  N   GLY A 254      -5.378  10.487  33.781  1.00 24.69           N  
ANISOU 1925  N   GLY A 254     3087   3533   2760  -1538   -177   -224       N  
ATOM   1926  CA  GLY A 254      -4.434   9.580  34.406  1.00 24.31           C  
ANISOU 1926  CA  GLY A 254     3138   3280   2820  -1502   -102   -224       C  
ATOM   1927  C   GLY A 254      -3.603  10.240  35.499  1.00 23.08           C  
ANISOU 1927  C   GLY A 254     2962   3097   2710  -1323    -89   -137       C  
ATOM   1928  O   GLY A 254      -2.898   9.561  36.243  1.00 21.47           O  
ANISOU 1928  O   GLY A 254     2814   2749   2596  -1283    -37   -100       O  
ATOM   1929  N   LEU A 255      -3.652  11.568  35.565  1.00 21.03           N  
ANISOU 1929  N   LEU A 255     2626   2974   2392  -1220   -136   -102       N  
ATOM   1930  CA  LEU A 255      -2.920  12.327  36.573  1.00 21.74           C  
ANISOU 1930  CA  LEU A 255     2694   3057   2508  -1064   -128    -30       C  
ATOM   1931  C   LEU A 255      -3.699  12.536  37.877  1.00 19.20           C  
ANISOU 1931  C   LEU A 255     2285   2827   2183  -1049   -138     65       C  
ATOM   1932  O   LEU A 255      -4.874  12.898  37.852  1.00 20.30           O  
ANISOU 1932  O   LEU A 255     2334   3108   2270  -1099   -174     82       O  
ATOM   1933  CB  LEU A 255      -2.524  13.693  36.015  1.00 22.24           C  
ANISOU 1933  CB  LEU A 255     2728   3205   2516   -961   -165    -47       C  
ATOM   1934  CG  LEU A 255      -1.765  14.614  36.975  1.00 20.54           C  
ANISOU 1934  CG  LEU A 255     2493   2994   2319   -810   -161     13       C  
ATOM   1935  CD1 LEU A 255      -0.486  13.950  37.494  1.00 17.34           C  
ANISOU 1935  CD1 LEU A 255     2167   2432   1989   -758   -109     26       C  
ATOM   1936  CD2 LEU A 255      -1.453  15.936  36.276  1.00 16.40           C  
ANISOU 1936  CD2 LEU A 255     1946   2541   1746   -728   -198     -9       C  
ATOM   1937  N   ARG A 256      -3.019  12.356  39.007  1.00 21.74           N  
ANISOU 1937  N   ARG A 256     2625   3078   2555   -977   -105    130       N  
ATOM   1938  CA  ARG A 256      -3.569  12.720  40.319  1.00 20.23           C  
ANISOU 1938  CA  ARG A 256     2355   2985   2345   -946   -108    216       C  
ATOM   1939  C   ARG A 256      -2.554  13.551  41.103  1.00 18.45           C  
ANISOU 1939  C   ARG A 256     2133   2755   2122   -805   -101    253       C  
ATOM   1940  O   ARG A 256      -1.429  13.105  41.336  1.00 17.98           O  
ANISOU 1940  O   ARG A 256     2143   2575   2116   -762    -75    271       O  
ATOM   1941  CB  ARG A 256      -3.953  11.473  41.119  1.00 19.73           C  
ANISOU 1941  CB  ARG A 256     2304   2864   2329  -1041    -77    279       C  
ATOM   1942  N   VAL A 257      -2.936  14.767  41.483  1.00 13.80           N  
ANISOU 1942  N   VAL A 257     1695   2044   1505   -708   -182   -361       N  
ATOM   1943  CA  VAL A 257      -2.047  15.624  42.263  1.00 13.02           C  
ANISOU 1943  CA  VAL A 257     1590   1914   1444   -601   -156   -348       C  
ATOM   1944  C   VAL A 257      -2.559  15.692  43.702  1.00 17.33           C  
ANISOU 1944  C   VAL A 257     2099   2483   2003   -605   -137   -314       C  
ATOM   1945  O   VAL A 257      -3.667  16.162  43.949  1.00 13.32           O  
ANISOU 1945  O   VAL A 257     1507   2071   1483   -624   -140   -287       O  
ATOM   1946  CB  VAL A 257      -1.940  17.057  41.676  1.00 12.59           C  
ANISOU 1946  CB  VAL A 257     1470   1920   1395   -521   -160   -337       C  
ATOM   1947  CG1 VAL A 257      -0.923  17.877  42.461  1.00 11.87           C  
ANISOU 1947  CG1 VAL A 257     1386   1782   1340   -422   -135   -330       C  
ATOM   1948  CG2 VAL A 257      -1.514  17.015  40.204  1.00 12.67           C  
ANISOU 1948  CG2 VAL A 257     1508   1923   1382   -524   -180   -365       C  
ATOM   1949  N   VAL A 258      -1.741  15.256  44.651  1.00 17.82           N  
ANISOU 1949  N   VAL A 258     2220   2465   2088   -581   -116   -314       N  
ATOM   1950  CA  VAL A 258      -2.140  15.302  46.059  1.00 12.80           C  
ANISOU 1950  CA  VAL A 258     1554   1852   1458   -583    -96   -282       C  
ATOM   1951  C   VAL A 258      -1.526  16.508  46.741  1.00 14.42           C  
ANISOU 1951  C   VAL A 258     1727   2064   1687   -480    -75   -274       C  
ATOM   1952  O   VAL A 258      -0.301  16.647  46.832  1.00 13.84           O  
ANISOU 1952  O   VAL A 258     1704   1920   1634   -421    -67   -287       O  
ATOM   1953  CB  VAL A 258      -1.736  14.035  46.808  1.00 16.20           C  
ANISOU 1953  CB  VAL A 258     2065   2197   1894   -630    -87   -278       C  
ATOM   1954  CG1 VAL A 258      -2.323  14.037  48.236  1.00 13.23           C  
ANISOU 1954  CG1 VAL A 258     1650   1864   1514   -647    -68   -239       C  
ATOM   1955  CG2 VAL A 258      -2.207  12.803  46.037  1.00 14.66           C  
ANISOU 1955  CG2 VAL A 258     1922   1971   1679   -733   -109   -294       C  
ATOM   1956  N   SER A 259      -2.390  17.413  47.178  1.00 13.87           N  
ANISOU 1956  N   SER A 259     1573   2084   1612   -459    -67   -254       N  
ATOM   1957  CA  SER A 259      -1.932  18.631  47.818  1.00 11.70           C  
ANISOU 1957  CA  SER A 259     1270   1818   1357   -365    -48   -251       C  
ATOM   1958  C   SER A 259      -1.634  18.360  49.282  1.00 13.16           C  
ANISOU 1958  C   SER A 259     1477   1980   1545   -360    -24   -239       C  
ATOM   1959  O   SER A 259      -2.195  17.424  49.857  1.00 12.11           O  
ANISOU 1959  O   SER A 259     1349   1857   1394   -430    -20   -222       O  
ATOM   1960  CB  SER A 259      -2.977  19.737  47.691  1.00 15.12           C  
ANISOU 1960  CB  SER A 259     1608   2351   1785   -333    -46   -237       C  
ATOM   1961  OG  SER A 259      -3.033  20.218  46.362  1.00 19.20           O  
ANISOU 1961  OG  SER A 259     2107   2886   2303   -318    -69   -243       O  
ATOM   1962  N   ASP A 260      -0.730  19.161  49.844  1.00 15.84           N  
ANISOU 1962  N   ASP A 260     1829   2287   1902   -283    -11   -247       N  
ATOM   1963  CA  ASP A 260      -0.359  19.120  51.265  1.00 15.57           C  
ANISOU 1963  CA  ASP A 260     1810   2240   1866   -268     11   -237       C  
ATOM   1964  C   ASP A 260      -0.030  17.708  51.717  1.00 18.21           C  
ANISOU 1964  C   ASP A 260     2208   2520   2194   -329     10   -223       C  
ATOM   1965  O   ASP A 260      -0.508  17.247  52.751  1.00 17.71           O  
ANISOU 1965  O   ASP A 260     2135   2482   2111   -366     24   -200       O  
ATOM   1966  CB  ASP A 260      -1.481  19.717  52.118  1.00 11.43           C  
ANISOU 1966  CB  ASP A 260     1212   1807   1323   -263     32   -224       C  
ATOM   1967  CG  ASP A 260      -1.833  21.126  51.691  1.00 17.79           C  
ANISOU 1967  CG  ASP A 260     1960   2659   2139   -193     35   -236       C  
ATOM   1968  OD1 ASP A 260      -0.922  21.982  51.640  1.00 11.58           O  
ANISOU 1968  OD1 ASP A 260     1198   1829   1374   -126     35   -254       O  
ATOM   1969  OD2 ASP A 260      -3.017  21.379  51.382  1.00 21.93           O  
ANISOU 1969  OD2 ASP A 260     2416   3265   2652   -205     36   -225       O  
ATOM   1970  N   ALA A 261       0.810  17.046  50.924  1.00 14.13           N  
ANISOU 1970  N   ALA A 261     1754   1924   1690   -335     -5   -236       N  
ATOM   1971  CA  ALA A 261       1.227  15.669  51.161  1.00 12.42           C  
ANISOU 1971  CA  ALA A 261     1611   1636   1473   -383     -8   -225       C  
ATOM   1972  C   ALA A 261       2.723  15.686  51.420  1.00 14.33           C  
ANISOU 1972  C   ALA A 261     1905   1805   1734   -320     -5   -229       C  
ATOM   1973  O   ALA A 261       3.511  15.800  50.479  1.00 13.20           O  
ANISOU 1973  O   ALA A 261     1790   1621   1607   -284    -14   -251       O  
ATOM   1974  CB  ALA A 261       0.901  14.786  49.953  1.00 11.80           C  
ANISOU 1974  CB  ALA A 261     1565   1526   1390   -443    -28   -241       C  
ATOM   1975  N   VAL A 262       3.114  15.635  52.694  1.00 10.97           N  
ANISOU 1975  N   VAL A 262     1489   1375   1306   -305      8   -206       N  
ATOM   1976  CA  VAL A 262       4.521  15.725  53.052  1.00 10.62           C  
ANISOU 1976  CA  VAL A 262     1483   1277   1276   -245      9   -203       C  
ATOM   1977  C   VAL A 262       5.122  14.336  53.030  1.00 12.42           C  
ANISOU 1977  C   VAL A 262     1786   1422   1512   -267      5   -187       C  
ATOM   1978  O   VAL A 262       4.883  13.519  53.936  1.00 11.53           O  
ANISOU 1978  O   VAL A 262     1697   1296   1389   -307     10   -154       O  
ATOM   1979  CB  VAL A 262       4.723  16.360  54.431  1.00 16.12           C  
ANISOU 1979  CB  VAL A 262     2154   2013   1959   -217     22   -186       C  
ATOM   1980  CG1 VAL A 262       6.211  16.436  54.757  1.00 11.40           C  
ANISOU 1980  CG1 VAL A 262     1591   1368   1373   -162     19   -180       C  
ATOM   1981  CG2 VAL A 262       4.067  17.756  54.484  1.00 10.30           C  
ANISOU 1981  CG2 VAL A 262     1348   1350   1214   -190     30   -207       C  
ATOM   1982  N   VAL A 263       5.892  14.049  51.990  1.00 10.84           N  
ANISOU 1982  N   VAL A 263     1627   1164   1329   -239     -2   -209       N  
ATOM   1983  CA  VAL A 263       6.474  12.716  51.843  1.00 16.12           C  
ANISOU 1983  CA  VAL A 263     2373   1742   2008   -249     -4   -200       C  
ATOM   1984  C   VAL A 263       7.624  12.508  52.817  1.00 18.22           C  
ANISOU 1984  C   VAL A 263     2664   1974   2282   -198      2   -168       C  
ATOM   1985  O   VAL A 263       8.468  13.383  52.997  1.00 10.74           O  
ANISOU 1985  O   VAL A 263     1689   1053   1340   -137      3   -170       O  
ATOM   1986  CB  VAL A 263       6.960  12.468  50.399  1.00 12.57           C  
ANISOU 1986  CB  VAL A 263     1960   1247   1570   -229     -9   -239       C  
ATOM   1987  CG1 VAL A 263       7.872  11.226  50.313  1.00 11.67           C  
ANISOU 1987  CG1 VAL A 263     1931   1033   1472   -209     -5   -233       C  
ATOM   1988  CG2 VAL A 263       5.764  12.304  49.485  1.00 12.62           C  
ANISOU 1988  CG2 VAL A 263     1956   1277   1562   -298    -19   -265       C  
ATOM   1989  N   ASP A 264       7.645  11.331  53.438  1.00 11.76           N  
ANISOU 1989  N   ASP A 264     1901   1101   1466   -228      4   -134       N  
ATOM   1990  CA  ASP A 264       8.707  10.950  54.340  1.00 16.01           C  
ANISOU 1990  CA  ASP A 264     2467   1604   2011   -182      7    -95       C  
ATOM   1991  C   ASP A 264       9.783  10.166  53.585  1.00 18.81           C  
ANISOU 1991  C   ASP A 264     2886   1870   2390   -130      7   -103       C  
ATOM   1992  O   ASP A 264      10.890  10.653  53.384  1.00 24.11           O  
ANISOU 1992  O   ASP A 264     3545   2547   3071    -57      9   -108       O  
ATOM   1993  CB  ASP A 264       8.146  10.121  55.509  1.00 12.43           C  
ANISOU 1993  CB  ASP A 264     2037   1143   1545   -238      9    -43       C  
ATOM   1994  CG  ASP A 264       9.231   9.437  56.305  1.00 15.89           C  
ANISOU 1994  CG  ASP A 264     2519   1529   1992   -194      8      5       C  
ATOM   1995  OD1 ASP A 264      10.366   9.953  56.330  1.00 16.69           O  
ANISOU 1995  OD1 ASP A 264     2604   1638   2100   -119      7      4       O  
ATOM   1996  OD2 ASP A 264       8.958   8.377  56.907  1.00 16.55           O  
ANISOU 1996  OD2 ASP A 264     2650   1565   2074   -236      8     49       O  
ATOM   1997  N   ARG A 265       9.463   8.952  53.170  1.00 21.82           N  
ANISOU 1997  N   ARG A 265     3338   2170   2781   -169      8   -105       N  
ATOM   1998  CA  ARG A 265      10.470   8.099  52.546  1.00 20.65           C  
ANISOU 1998  CA  ARG A 265     3261   1930   2656   -113     13   -113       C  
ATOM   1999  C   ARG A 265       9.894   7.198  51.472  1.00 22.89           C  
ANISOU 1999  C   ARG A 265     3611   2141   2945   -161     13   -153       C  
ATOM   2000  O   ARG A 265       8.675   7.150  51.265  1.00 13.77           O  
ANISOU 2000  O   ARG A 265     2449   1010   1775   -249      5   -168       O  
ATOM   2001  CB  ARG A 265      11.170   7.239  53.612  1.00 16.72           C  
ANISOU 2001  CB  ARG A 265     2807   1376   2170    -83     15    -52       C  
ATOM   2002  CG  ARG A 265      10.301   6.143  54.193  1.00 17.78           C  
ANISOU 2002  CG  ARG A 265     2998   1454   2303   -163     12    -17       C  
ATOM   2003  CD  ARG A 265      10.903   5.647  55.493  1.00 19.88           C  
ANISOU 2003  CD  ARG A 265     3282   1701   2573   -136     11     57       C  
ATOM   2004  NE  ARG A 265      10.885   6.703  56.500  1.00 20.48           N  
ANISOU 2004  NE  ARG A 265     3274   1887   2622   -132      8     82       N  
ATOM   2005  CZ  ARG A 265      11.748   6.789  57.509  1.00 20.08           C  
ANISOU 2005  CZ  ARG A 265     3207   1858   2566    -82      5    135       C  
ATOM   2006  NH1 ARG A 265      12.690   5.865  57.655  1.00 19.33           N  
ANISOU 2006  NH1 ARG A 265     3169   1682   2493    -26      5    174       N  
ATOM   2007  NH2 ARG A 265      11.670   7.796  58.371  1.00 14.06           N  
ANISOU 2007  NH2 ARG A 265     2372   1196   1773    -86      2    147       N  
ATOM   2008  N   ILE A 266      10.798   6.499  50.788  1.00 18.21           N  
ANISOU 2008  N   ILE A 266     3084   1465   2371   -103     22   -173       N  
ATOM   2009  CA  ILE A 266      10.437   5.509  49.794  1.00 14.68           C  
ANISOU 2009  CA  ILE A 266     2720    932   1927   -140     24   -216       C  
ATOM   2010  C   ILE A 266      10.587   4.112  50.404  1.00 15.61           C  
ANISOU 2010  C   ILE A 266     2933    933   2066   -150     27   -178       C  
ATOM   2011  O   ILE A 266      11.599   3.809  51.027  1.00 15.77           O  
ANISOU 2011  O   ILE A 266     2971    917   2105    -72     36   -137       O  
ATOM   2012  CB  ILE A 266      11.322   5.614  48.530  1.00 15.59           C  
ANISOU 2012  CB  ILE A 266     2852   1026   2045    -64     37   -271       C  
ATOM   2013  CG1 ILE A 266      11.242   7.023  47.928  1.00 13.75           C  
ANISOU 2013  CG1 ILE A 266     2526    905   1793    -53     32   -299       C  
ATOM   2014  CG2 ILE A 266      10.906   4.577  47.505  1.00 16.25           C  
ANISOU 2014  CG2 ILE A 266     3028   1019   2126   -108     39   -324       C  
ATOM   2015  CD1 ILE A 266      12.322   7.287  46.834  1.00 18.88           C  
ANISOU 2015  CD1 ILE A 266     3177   1554   2441     33     47   -339       C  
ATOM   2016  N   ILE A 267       9.578   3.272  50.221  1.00 16.29           N  
ANISOU 2016  N   ILE A 267     3079    963   2148   -247     19   -189       N  
ATOM   2017  CA  ILE A 267       9.608   1.904  50.726  1.00 17.30           C  
ANISOU 2017  CA  ILE A 267     3310    967   2297   -270     20   -154       C  
ATOM   2018  C   ILE A 267      10.084   0.931  49.643  1.00 21.36           C  
ANISOU 2018  C   ILE A 267     3932   1355   2827   -238     31   -209       C  
ATOM   2019  O   ILE A 267       9.617   0.988  48.496  1.00 22.26           O  
ANISOU 2019  O   ILE A 267     4045   1489   2925   -275     28   -276       O  
ATOM   2020  CB  ILE A 267       8.227   1.484  51.228  1.00 25.31           C  
ANISOU 2020  CB  ILE A 267     4333   1986   3297   -406      3   -128       C  
ATOM   2021  CG1 ILE A 267       7.734   2.478  52.284  1.00 26.79           C  
ANISOU 2021  CG1 ILE A 267     4411   2306   3464   -431     -2    -80       C  
ATOM   2022  CG2 ILE A 267       8.260   0.063  51.785  1.00 24.75           C  
ANISOU 2022  CG2 ILE A 267     4373   1780   3249   -436      3    -84       C  
ATOM   2023  CD1 ILE A 267       8.647   2.574  53.485  1.00 30.10           C  
ANISOU 2023  CD1 ILE A 267     4812   2731   3893   -354      4    -13       C  
ATOM   2024  N   PHE A 268      10.997   0.038  50.032  1.00 22.73           N  
ANISOU 2024  N   PHE A 268     4157   1448   3032   -161     43   -174       N  
ATOM   2025  CA  PHE A 268      11.671  -0.888  49.126  1.00 20.89           C  
ANISOU 2025  CA  PHE A 268     3970   1149   2819    -97     57   -215       C  
ATOM   2026  C   PHE A 268      11.403  -2.358  49.442  1.00 28.17           C  
ANISOU 2026  C   PHE A 268     4974   1963   3767   -135     54   -189       C  
ATOM   2027  O   PHE A 268      11.202  -2.744  50.598  1.00 26.59           O  
ANISOU 2027  O   PHE A 268     4793   1731   3578   -165     45   -116       O  
ATOM   2028  CB  PHE A 268      13.189  -0.657  49.171  1.00 19.38           C  
ANISOU 2028  CB  PHE A 268     3753    964   2646     49     78   -199       C  
ATOM   2029  CG  PHE A 268      13.635   0.610  48.490  1.00 19.20           C  
ANISOU 2029  CG  PHE A 268     3657   1037   2601    100     85   -241       C  
ATOM   2030  CD1 PHE A 268      13.632   1.817  49.173  1.00 19.72           C  
ANISOU 2030  CD1 PHE A 268     3662   1179   2652    104     78   -210       C  
ATOM   2031  CD2 PHE A 268      14.058   0.593  47.172  1.00 18.51           C  
ANISOU 2031  CD2 PHE A 268     3563    963   2506    142    100   -308       C  
ATOM   2032  CE1 PHE A 268      14.051   2.977  48.564  1.00 18.46           C  
ANISOU 2032  CE1 PHE A 268     3421   1119   2475    148     83   -242       C  
ATOM   2033  CE2 PHE A 268      14.470   1.759  46.545  1.00 19.60           C  
ANISOU 2033  CE2 PHE A 268     3632   1192   2622    185    106   -340       C  
ATOM   2034  CZ  PHE A 268      14.461   2.951  47.235  1.00 21.43           C  
ANISOU 2034  CZ  PHE A 268     3803   1496   2843    188     97   -308       C  
ATOM   2035  N   LYS A 269      11.412  -3.169  48.388  1.00 22.68           N  
ANISOU 2035  N   LYS A 269     4327   1212   3077   -134     60   -248       N  
ATOM   2036  CA  LYS A 269      11.541  -4.606  48.499  1.00 23.10           C  
ANISOU 2036  CA  LYS A 269     4465   1150   3163   -132     63   -235       C  
ATOM   2037  C   LYS A 269      12.830  -4.948  47.777  1.00 28.16           C  
ANISOU 2037  C   LYS A 269     5120   1756   3824     -1     89   -270       C  
ATOM   2038  O   LYS A 269      12.899  -4.840  46.555  1.00 31.22           O  
ANISOU 2038  O   LYS A 269     5506   2162   4194     10     98   -346       O  
ATOM   2039  CB  LYS A 269      10.340  -5.322  47.881  1.00 28.12           C  
ANISOU 2039  CB  LYS A 269     5151   1747   3785   -256     47   -278       C  
ATOM   2040  CG  LYS A 269      10.407  -6.843  47.959  1.00 41.42           C  
ANISOU 2040  CG  LYS A 269     6932   3301   5505   -261     49   -268       C  
ATOM   2041  CD  LYS A 269       9.149  -7.481  47.363  1.00 51.12           C  
ANISOU 2041  CD  LYS A 269     8207   4502   6715   -396     30   -310       C  
ATOM   2042  CE  LYS A 269       7.869  -6.802  47.878  1.00 58.28           C  
ANISOU 2042  CE  LYS A 269     9059   5496   7587   -526      5   -280       C  
ATOM   2043  NZ  LYS A 269       7.264  -5.847  46.887  1.00 55.62           N  
ANISOU 2043  NZ  LYS A 269     8663   5264   7207   -572     -4   -345       N  
ATOM   2044  N   GLY A 270      13.860  -5.327  48.527  1.00 26.55           N  
ANISOU 2044  N   GLY A 270     4922   1512   3652     97    101   -212       N  
ATOM   2045  CA  GLY A 270      15.202  -5.404  47.975  1.00 28.65           C  
ANISOU 2045  CA  GLY A 270     5176   1777   3934    232    126   -234       C  
ATOM   2046  C   GLY A 270      15.597  -4.025  47.472  1.00 28.13           C  
ANISOU 2046  C   GLY A 270     5020   1830   3836    273    134   -263       C  
ATOM   2047  O   GLY A 270      15.497  -3.047  48.212  1.00 26.67           O  
ANISOU 2047  O   GLY A 270     4777   1719   3637    262    123   -221       O  
ATOM   2048  N   ASN A 271      16.026  -3.930  46.213  1.00 28.02           N  
ANISOU 2048  N   ASN A 271     4999   1838   3808    316    151   -336       N  
ATOM   2049  CA  ASN A 271      16.404  -2.623  45.668  1.00 31.73           C  
ANISOU 2049  CA  ASN A 271     5384   2424   4249    352    158   -363       C  
ATOM   2050  C   ASN A 271      15.354  -2.068  44.703  1.00 30.63           C  
ANISOU 2050  C   ASN A 271     5234   2333   4071    256    146   -431       C  
ATOM   2051  O   ASN A 271      15.637  -1.188  43.889  1.00 20.62           O  
ANISOU 2051  O   ASN A 271     3910   1147   2776    283    154   -470       O  
ATOM   2052  CB  ASN A 271      17.777  -2.697  44.992  1.00 31.67           C  
ANISOU 2052  CB  ASN A 271     5354   2433   4248    478    188   -384       C  
ATOM   2053  CG  ASN A 271      17.776  -3.556  43.749  1.00 30.57           C  
ANISOU 2053  CG  ASN A 271     5273   2237   4104    481    204   -462       C  
ATOM   2054  OD1 ASN A 271      16.870  -4.352  43.532  1.00 28.04           O  
ANISOU 2054  OD1 ASN A 271     5026   1843   3787    399    192   -490       O  
ATOM   2055  ND2 ASN A 271      18.806  -3.403  42.927  1.00 36.08           N  
ANISOU 2055  ND2 ASN A 271     5942   2973   4795    573    231   -495       N  
ATOM   2056  N   ARG A 272      14.130  -2.567  44.836  1.00 28.99           N  
ANISOU 2056  N   ARG A 272     5075   2081   3859    141    125   -437       N  
ATOM   2057  CA  ARG A 272      13.001  -2.072  44.069  1.00 21.27           C  
ANISOU 2057  CA  ARG A 272     4082   1156   2843     38    107   -489       C  
ATOM   2058  C   ARG A 272      12.066  -1.254  44.956  1.00 23.55           C  
ANISOU 2058  C   ARG A 272     4328   1502   3119    -47     84   -446       C  
ATOM   2059  O   ARG A 272      11.590  -1.736  45.982  1.00 22.43           O  
ANISOU 2059  O   ARG A 272     4216   1313   2993    -98     72   -392       O  
ATOM   2060  CB  ARG A 272      12.230  -3.228  43.432  1.00 23.88           C  
ANISOU 2060  CB  ARG A 272     4494   1409   3172    -41     99   -534       C  
ATOM   2061  CG  ARG A 272      10.941  -2.785  42.768  1.00 28.13           C  
ANISOU 2061  CG  ARG A 272     5012   2006   3669   -162     75   -576       C  
ATOM   2062  CD  ARG A 272      10.261  -3.908  42.008  1.00 29.31           C  
ANISOU 2062  CD  ARG A 272     5239   2086   3812   -236     66   -627       C  
ATOM   2063  NE  ARG A 272       9.178  -3.376  41.194  1.00 33.03           N  
ANISOU 2063  NE  ARG A 272     5677   2635   4237   -336     43   -670       N  
ATOM   2064  CZ  ARG A 272       9.330  -2.916  39.953  1.00 39.00           C  
ANISOU 2064  CZ  ARG A 272     6409   3450   4960   -317     47   -734       C  
ATOM   2065  NH1 ARG A 272      10.526  -2.919  39.372  1.00 35.73           N  
ANISOU 2065  NH1 ARG A 272     5997   3026   4552   -202     76   -764       N  
ATOM   2066  NH2 ARG A 272       8.285  -2.442  39.289  1.00 36.28           N  
ANISOU 2066  NH2 ARG A 272     6031   3180   4573   -412     22   -764       N  
ATOM   2067  N   ALA A 273      11.801  -0.021  44.552  1.00 19.34           N  
ANISOU 2067  N   ALA A 273     3725   1069   2555    -63     78   -468       N  
ATOM   2068  CA  ALA A 273      10.844   0.822  45.249  1.00 19.87           C  
ANISOU 2068  CA  ALA A 273     3748   1197   2606   -146     56   -438       C  
ATOM   2069  C   ALA A 273       9.425   0.289  45.021  1.00 26.50           C  
ANISOU 2069  C   ALA A 273     4616   2024   3427   -283     33   -456       C  
ATOM   2070  O   ALA A 273       9.028   0.049  43.875  1.00 19.53           O  
ANISOU 2070  O   ALA A 273     3747   1151   2524   -319     28   -515       O  
ATOM   2071  CB  ALA A 273      10.964   2.242  44.768  1.00 17.46           C  
ANISOU 2071  CB  ALA A 273     3363    998   2275   -122     56   -462       C  
ATOM   2072  N   VAL A 274       8.654   0.104  46.093  1.00 19.19           N  
ANISOU 2072  N   VAL A 274     3698   1087   2508   -362     18   -402       N  
ATOM   2073  CA  VAL A 274       7.298  -0.425  45.932  1.00 19.82           C  
ANISOU 2073  CA  VAL A 274     3795   1166   2569   -497     -5   -411       C  
ATOM   2074  C   VAL A 274       6.231   0.504  46.503  1.00 20.99           C  
ANISOU 2074  C   VAL A 274     3873   1410   2691   -590    -23   -383       C  
ATOM   2075  O   VAL A 274       5.035   0.350  46.247  1.00 20.23           O  
ANISOU 2075  O   VAL A 274     3763   1351   2571   -703    -44   -392       O  
ATOM   2076  CB  VAL A 274       7.163  -1.812  46.586  1.00 20.98           C  
ANISOU 2076  CB  VAL A 274     4022   1206   2743   -531     -6   -372       C  
ATOM   2077  CG1 VAL A 274       8.035  -2.821  45.851  1.00 22.57           C  
ANISOU 2077  CG1 VAL A 274     4295   1312   2967   -454     11   -411       C  
ATOM   2078  CG2 VAL A 274       7.520  -1.760  48.087  1.00 20.76           C  
ANISOU 2078  CG2 VAL A 274     3992   1158   2739   -505     -2   -288       C  
ATOM   2079  N   GLY A 275       6.666   1.489  47.267  1.00 18.34           N  
ANISOU 2079  N   GLY A 275     3490   1120   2359   -542    -16   -350       N  
ATOM   2080  CA  GLY A 275       5.726   2.386  47.903  1.00 18.67           C  
ANISOU 2080  CA  GLY A 275     3436   1278   2381   -608    -30   -316       C  
ATOM   2081  C   GLY A 275       6.379   3.674  48.337  1.00 16.47           C  
ANISOU 2081  C   GLY A 275     3055   1099   2104   -511    -20   -294       C  
ATOM   2082  O   GLY A 275       7.598   3.759  48.414  1.00 17.97           O  
ANISOU 2082  O   GLY A 275     3259   1255   2314   -404     -4   -290       O  
ATOM   2083  N   VAL A 276       5.542   4.667  48.616  1.00 15.90           N  
ANISOU 2083  N   VAL A 276     2881   1150   2011   -552    -29   -280       N  
ATOM   2084  CA  VAL A 276       5.952   5.959  49.144  1.00 14.94           C  
ANISOU 2084  CA  VAL A 276     2662   1126   1889   -479    -22   -259       C  
ATOM   2085  C   VAL A 276       5.012   6.322  50.297  1.00 20.22           C  
ANISOU 2085  C   VAL A 276     3265   1875   2543   -539    -26   -208       C  
ATOM   2086  O   VAL A 276       3.800   6.184  50.164  1.00 21.08           O  
ANISOU 2086  O   VAL A 276     3353   2024   2632   -635    -38   -210       O  
ATOM   2087  CB  VAL A 276       5.890   7.073  48.071  1.00 14.31           C  
ANISOU 2087  CB  VAL A 276     2516   1128   1793   -451    -26   -307       C  
ATOM   2088  CG1 VAL A 276       6.223   8.416  48.690  1.00 13.43           C  
ANISOU 2088  CG1 VAL A 276     2311   1109   1682   -387    -20   -283       C  
ATOM   2089  CG2 VAL A 276       6.811   6.767  46.868  1.00 15.79           C  
ANISOU 2089  CG2 VAL A 276     2763   1252   1986   -392    -19   -359       C  
ATOM   2090  N   ASN A 277       5.571   6.760  51.425  1.00 18.68           N  
ANISOU 2090  N   ASN A 277     3036   1708   2355   -483    -16   -163       N  
ATOM   2091  CA  ASN A 277       4.781   7.246  52.562  1.00 19.56           C  
ANISOU 2091  CA  ASN A 277     3078   1907   2447   -525    -15   -120       C  
ATOM   2092  C   ASN A 277       4.668   8.759  52.602  1.00 16.41           C  
ANISOU 2092  C   ASN A 277     2579   1622   2035   -481    -11   -135       C  
ATOM   2093  O   ASN A 277       5.641   9.462  52.352  1.00 13.98           O  
ANISOU 2093  O   ASN A 277     2256   1316   1738   -395     -7   -152       O  
ATOM   2094  CB  ASN A 277       5.398   6.775  53.887  1.00 23.11           C  
ANISOU 2094  CB  ASN A 277     3556   2322   2903   -500     -8    -59       C  
ATOM   2095  CG  ASN A 277       5.184   5.303  54.139  1.00 33.08           C  
ANISOU 2095  CG  ASN A 277     4910   3484   4176   -564    -12    -26       C  
ATOM   2096  OD1 ASN A 277       4.244   4.705  53.625  1.00 41.70           O  
ANISOU 2096  OD1 ASN A 277     6029   4556   5260   -656    -21    -40       O  
ATOM   2097  ND2 ASN A 277       6.061   4.707  54.937  1.00 35.09           N  
ANISOU 2097  ND2 ASN A 277     5213   3674   4446   -519     -7     21       N  
ATOM   2098  N   TYR A 278       3.503   9.275  52.967  1.00 17.14           N  
ANISOU 2098  N   TYR A 278     2602   1807   2104   -536    -12   -125       N  
ATOM   2099  CA  TYR A 278       3.408  10.708  53.239  1.00 19.17           C  
ANISOU 2099  CA  TYR A 278     2769   2162   2350   -486     -4   -133       C  
ATOM   2100  C   TYR A 278       2.409  10.957  54.378  1.00 17.75           C  
ANISOU 2100  C   TYR A 278     2531   2069   2145   -533      5    -97       C  
ATOM   2101  O   TYR A 278       1.628  10.072  54.740  1.00 23.39           O  
ANISOU 2101  O   TYR A 278     3262   2779   2845   -617      4    -68       O  
ATOM   2102  CB  TYR A 278       3.020  11.491  51.967  1.00 12.55           C  
ANISOU 2102  CB  TYR A 278     1889   1368   1511   -477    -13   -179       C  
ATOM   2103  CG  TYR A 278       1.553  11.374  51.574  1.00 16.37           C  
ANISOU 2103  CG  TYR A 278     2332   1915   1974   -565    -22   -182       C  
ATOM   2104  CD1 TYR A 278       0.594  12.216  52.129  1.00 12.94           C  
ANISOU 2104  CD1 TYR A 278     1809   1588   1520   -576    -14   -167       C  
ATOM   2105  CD2 TYR A 278       1.127  10.425  50.644  1.00 16.51           C  
ANISOU 2105  CD2 TYR A 278     2397   1887   1988   -636    -37   -200       C  
ATOM   2106  CE1 TYR A 278      -0.742  12.111  51.787  1.00 13.43           C  
ANISOU 2106  CE1 TYR A 278     1822   1719   1560   -654    -22   -163       C  
ATOM   2107  CE2 TYR A 278      -0.219  10.317  50.288  1.00 15.28           C  
ANISOU 2107  CE2 TYR A 278     2198   1800   1809   -725    -49   -199       C  
ATOM   2108  CZ  TYR A 278      -1.147  11.163  50.865  1.00 15.66           C  
ANISOU 2108  CZ  TYR A 278     2149   1964   1839   -732    -41   -177       C  
ATOM   2109  OH  TYR A 278      -2.485  11.071  50.519  1.00 17.30           O  
ANISOU 2109  OH  TYR A 278     2300   2251   2020   -817    -53   -170       O  
ATOM   2110  N   ILE A 279       2.429  12.170  54.925  1.00 17.50           N  
ANISOU 2110  N   ILE A 279     2432   2115   2103   -481     17   -101       N  
ATOM   2111  CA  ILE A 279       1.541  12.559  56.020  1.00 12.83           C  
ANISOU 2111  CA  ILE A 279     1778   1615   1480   -509     32    -74       C  
ATOM   2112  C   ILE A 279       0.672  13.728  55.590  1.00 18.72           C  
ANISOU 2112  C   ILE A 279     2441   2456   2218   -494     37   -103       C  
ATOM   2113  O   ILE A 279       1.200  14.748  55.139  1.00 15.34           O  
ANISOU 2113  O   ILE A 279     1993   2033   1804   -422     36   -134       O  
ATOM   2114  CB  ILE A 279       2.330  12.973  57.287  1.00 23.10           C  
ANISOU 2114  CB  ILE A 279     3078   2928   2771   -456     45    -53       C  
ATOM   2115  CG1 ILE A 279       3.188  11.819  57.801  1.00 29.02           C  
ANISOU 2115  CG1 ILE A 279     3906   3592   3530   -464     39    -14       C  
ATOM   2116  CG2 ILE A 279       1.393  13.455  58.376  1.00 12.87           C  
ANISOU 2116  CG2 ILE A 279     1718   1735   1438   -479     65    -34       C  
ATOM   2117  CD1 ILE A 279       4.656  12.054  57.612  1.00 32.81           C  
ANISOU 2117  CD1 ILE A 279     4421   4012   4033   -381     32    -26       C  
ATOM   2118  N   ASP A 280      -0.648  13.601  55.732  1.00 14.83           N  
ANISOU 2118  N   ASP A 280     1895   2038   1700   -560     43    -87       N  
ATOM   2119  CA  ASP A 280      -1.554  14.634  55.230  1.00 13.04           C  
ANISOU 2119  CA  ASP A 280     1584   1903   1465   -543     47   -109       C  
ATOM   2120  C   ASP A 280      -1.692  15.756  56.249  1.00 15.65           C  
ANISOU 2120  C   ASP A 280     1857   2310   1780   -483     73   -110       C  
ATOM   2121  O   ASP A 280      -1.022  15.755  57.282  1.00 13.66           O  
ANISOU 2121  O   ASP A 280     1631   2040   1519   -458     85    -98       O  
ATOM   2122  CB  ASP A 280      -2.929  14.026  54.834  1.00 13.74           C  
ANISOU 2122  CB  ASP A 280     1635   2052   1535   -640     40    -91       C  
ATOM   2123  CG  ASP A 280      -3.753  13.497  56.017  1.00 21.20           C  
ANISOU 2123  CG  ASP A 280     2549   3060   2445   -707     57    -46       C  
ATOM   2124  OD1 ASP A 280      -3.515  13.867  57.197  1.00 17.67           O  
ANISOU 2124  OD1 ASP A 280     2089   2642   1983   -670     81    -31       O  
ATOM   2125  OD2 ASP A 280      -4.676  12.684  55.748  1.00 18.15           O  
ANISOU 2125  OD2 ASP A 280     2152   2699   2044   -805     47    -23       O  
ATOM   2126  N   ARG A 281      -2.536  16.737  55.976  1.00 18.85           N  
ANISOU 2126  N   ARG A 281     2185   2800   2178   -456     82   -126       N  
ATOM   2127  CA  ARG A 281      -2.548  17.898  56.868  1.00 21.09           C  
ANISOU 2127  CA  ARG A 281     2424   3139   2449   -385    108   -138       C  
ATOM   2128  C   ARG A 281      -3.234  17.621  58.212  1.00 19.76           C  
ANISOU 2128  C   ARG A 281     2223   3046   2239   -420    136   -108       C  
ATOM   2129  O   ARG A 281      -3.158  18.428  59.142  1.00 14.70           O  
ANISOU 2129  O   ARG A 281     1559   2447   1580   -367    161   -120       O  
ATOM   2130  CB  ARG A 281      -3.150  19.101  56.147  1.00 24.59           C  
ANISOU 2130  CB  ARG A 281     2803   3639   2903   -329    111   -164       C  
ATOM   2131  CG  ARG A 281      -4.497  18.927  55.527  1.00 26.80           C  
ANISOU 2131  CG  ARG A 281     3013   4000   3171   -377    107   -148       C  
ATOM   2132  CD  ARG A 281      -4.797  20.166  54.683  1.00 24.02           C  
ANISOU 2132  CD  ARG A 281     2609   3681   2837   -305    104   -171       C  
ATOM   2133  NE  ARG A 281      -6.095  20.053  54.030  1.00 22.00           N  
ANISOU 2133  NE  ARG A 281     2277   3514   2566   -347     97   -152       N  
ATOM   2134  CZ  ARG A 281      -7.241  20.367  54.615  1.00 24.35           C  
ANISOU 2134  CZ  ARG A 281     2489   3924   2837   -346    123   -134       C  
ATOM   2135  NH1 ARG A 281      -7.256  20.825  55.863  1.00 25.41           N  
ANISOU 2135  NH1 ARG A 281     2610   4091   2954   -303    159   -138       N  
ATOM   2136  NH2 ARG A 281      -8.372  20.222  53.954  1.00 20.85           N  
ANISOU 2136  NH2 ARG A 281     1973   3567   2381   -388    112   -112       N  
ATOM   2137  N   GLU A 282      -3.862  16.456  58.321  1.00 19.10           N  
ANISOU 2137  N   GLU A 282     2142   2976   2138   -515    131    -70       N  
ATOM   2138  CA  GLU A 282      -4.503  16.026  59.558  1.00 20.85           C  
ANISOU 2138  CA  GLU A 282     2336   3271   2317   -563    156    -31       C  
ATOM   2139  C   GLU A 282      -3.536  15.207  60.413  1.00 17.42           C  
ANISOU 2139  C   GLU A 282     1980   2764   1877   -583    153     -4       C  
ATOM   2140  O   GLU A 282      -3.873  14.742  61.496  1.00 21.35           O  
ANISOU 2140  O   GLU A 282     2467   3307   2337   -627    171     35       O  
ATOM   2141  CB  GLU A 282      -5.761  15.203  59.220  1.00 19.70           C  
ANISOU 2141  CB  GLU A 282     2147   3186   2154   -666    151      4       C  
ATOM   2142  CG  GLU A 282      -6.742  15.052  60.338  1.00 29.94           C  
ANISOU 2142  CG  GLU A 282     3380   4597   3401   -711    182     43       C  
ATOM   2143  CD  GLU A 282      -8.093  14.518  59.879  1.00 32.28           C  
ANISOU 2143  CD  GLU A 282     3609   4977   3678   -805    177     74       C  
ATOM   2144  OE1 GLU A 282      -8.293  14.328  58.660  1.00 27.05           O  
ANISOU 2144  OE1 GLU A 282     2951   4287   3041   -833    147     61       O  
ATOM   2145  OE2 GLU A 282      -8.952  14.302  60.751  1.00 37.43           O  
ANISOU 2145  OE2 GLU A 282     4203   5732   4287   -853    202    112       O  
ATOM   2146  N   GLY A 283      -2.318  15.044  59.917  1.00 20.73           N  
ANISOU 2146  N   GLY A 283     2472   3074   2332   -548    130    -20       N  
ATOM   2147  CA  GLY A 283      -1.297  14.289  60.619  1.00 13.94           C  
ANISOU 2147  CA  GLY A 283     1685   2140   1472   -555    124      8       C  
ATOM   2148  C   GLY A 283      -1.487  12.800  60.414  1.00 19.30           C  
ANISOU 2148  C   GLY A 283     2417   2759   2156   -646    108     51       C  
ATOM   2149  O   GLY A 283      -0.943  11.988  61.155  1.00 18.04           O  
ANISOU 2149  O   GLY A 283     2311   2553   1990   -669    105     92       O  
ATOM   2150  N   ILE A 284      -2.258  12.431  59.396  1.00 20.11           N  
ANISOU 2150  N   ILE A 284     2509   2862   2271   -701     94     43       N  
ATOM   2151  CA  ILE A 284      -2.544  11.023  59.140  1.00 23.08           C  
ANISOU 2151  CA  ILE A 284     2940   3178   2652   -800     77     79       C  
ATOM   2152  C   ILE A 284      -1.611  10.513  58.061  1.00 21.50           C  
ANISOU 2152  C   ILE A 284     2823   2850   2494   -779     52     51       C  
ATOM   2153  O   ILE A 284      -1.412  11.177  57.029  1.00 16.41           O  
ANISOU 2153  O   ILE A 284     2166   2200   1870   -731     43      3       O  
ATOM   2154  CB  ILE A 284      -4.021  10.792  58.731  1.00 19.20           C  
ANISOU 2154  CB  ILE A 284     2386   2768   2139   -892     76     90       C  
ATOM   2155  CG1 ILE A 284      -4.947  11.160  59.890  1.00 28.86           C  
ANISOU 2155  CG1 ILE A 284     3526   4123   3316   -914    106    124       C  
ATOM   2156  CG2 ILE A 284      -4.271   9.335  58.338  1.00 16.69           C  
ANISOU 2156  CG2 ILE A 284     2139   2374   1830  -1002     53    119       C  
ATOM   2157  CD1 ILE A 284      -6.416  10.945  59.585  1.00 30.23           C  
ANISOU 2157  CD1 ILE A 284     3625   4397   3464  -1005    107    144       C  
ATOM   2158  N   MET A 285      -1.015   9.349  58.313  1.00 16.62           N  
ANISOU 2158  N   MET A 285     2293   2132   1889   -811     43     84       N  
ATOM   2159  CA  MET A 285      -0.040   8.781  57.383  1.00 21.21           C  
ANISOU 2159  CA  MET A 285     2961   2588   2509   -782     24     58       C  
ATOM   2160  C   MET A 285      -0.698   7.916  56.323  1.00 18.98           C  
ANISOU 2160  C   MET A 285     2716   2259   2235   -868      5     44       C  
ATOM   2161  O   MET A 285      -1.629   7.163  56.612  1.00 18.60           O  
ANISOU 2161  O   MET A 285     2669   2228   2169   -972      2     79       O  
ATOM   2162  CB  MET A 285       1.009   7.960  58.126  1.00 26.33           C  
ANISOU 2162  CB  MET A 285     3690   3144   3172   -759     23     99       C  
ATOM   2163  CG  MET A 285       2.036   7.348  57.195  1.00 26.71           C  
ANISOU 2163  CG  MET A 285     3826   3063   3259   -718      9     73       C  
ATOM   2164  SD  MET A 285       3.530   6.808  58.029  1.00 46.76           S  
ANISOU 2164  SD  MET A 285     6436   5515   5818   -643     11    116       S  
ATOM   2165  CE  MET A 285       4.226   8.400  58.476  1.00 43.81           C  
ANISOU 2165  CE  MET A 285     5981   5234   5431   -540     21     93       C  
ATOM   2166  N   HIS A 286      -0.208   8.037  55.095  1.00 16.38           N  
ANISOU 2166  N   HIS A 286     2418   1875   1930   -831     -8     -8       N  
ATOM   2167  CA  HIS A 286      -0.740   7.271  53.976  1.00 20.26           C  
ANISOU 2167  CA  HIS A 286     2952   2320   2426   -908    -28    -33       C  
ATOM   2168  C   HIS A 286       0.362   6.558  53.206  1.00 23.63           C  
ANISOU 2168  C   HIS A 286     3485   2610   2884   -869    -36    -64       C  
ATOM   2169  O   HIS A 286       1.498   7.032  53.133  1.00 21.46           O  
ANISOU 2169  O   HIS A 286     3222   2304   2629   -765    -28    -81       O  
ATOM   2170  CB  HIS A 286      -1.519   8.184  53.040  1.00 19.59           C  
ANISOU 2170  CB  HIS A 286     2785   2331   2326   -913    -35    -73       C  
ATOM   2171  CG  HIS A 286      -2.632   8.918  53.722  1.00 21.11           C  
ANISOU 2171  CG  HIS A 286     2869   2664   2489   -940    -23    -46       C  
ATOM   2172  ND1 HIS A 286      -3.891   8.380  53.869  1.00 23.52           N  
ANISOU 2172  ND1 HIS A 286     3140   3029   2766  -1055    -29    -16       N  
ATOM   2173  CD2 HIS A 286      -2.669  10.146  54.288  1.00 18.55           C  
ANISOU 2173  CD2 HIS A 286     2463   2431   2156   -866     -4    -45       C  
ATOM   2174  CE1 HIS A 286      -4.661   9.244  54.517  1.00 27.31           C  
ANISOU 2174  CE1 HIS A 286     3515   3639   3221  -1043    -11      3       C  
ATOM   2175  NE2 HIS A 286      -3.943  10.324  54.779  1.00 25.57           N  
ANISOU 2175  NE2 HIS A 286     3269   3435   3013   -927      5    -17       N  
ATOM   2176  N   TYR A 287       0.023   5.407  52.639  1.00 19.20           N  
ANISOU 2176  N   TYR A 287     3001   1968   2326   -954    -51    -71       N  
ATOM   2177  CA  TYR A 287       0.958   4.679  51.800  1.00 19.82           C  
ANISOU 2177  CA  TYR A 287     3184   1915   2431   -918    -56   -109       C  
ATOM   2178  C   TYR A 287       0.487   4.733  50.353  1.00 20.61           C  
ANISOU 2178  C   TYR A 287     3286   2025   2520   -958    -73   -172       C  
ATOM   2179  O   TYR A 287      -0.682   4.453  50.057  1.00 19.14           O  
ANISOU 2179  O   TYR A 287     3080   1884   2310  -1069    -89   -172       O  
ATOM   2180  CB  TYR A 287       1.093   3.245  52.308  1.00 17.86           C  
ANISOU 2180  CB  TYR A 287     3043   1544   2197   -975    -59    -72       C  
ATOM   2181  CG  TYR A 287       1.976   2.310  51.503  1.00 27.12           C  
ANISOU 2181  CG  TYR A 287     4339   2566   3399   -942    -61   -110       C  
ATOM   2182  CD1 TYR A 287       1.447   1.538  50.479  1.00 29.61           C  
ANISOU 2182  CD1 TYR A 287     4722   2820   3708  -1027    -78   -155       C  
ATOM   2183  CD2 TYR A 287       3.326   2.151  51.810  1.00 25.27           C  
ANISOU 2183  CD2 TYR A 287     4154   2252   3194   -829    -47    -99       C  
ATOM   2184  CE1 TYR A 287       2.236   0.661  49.758  1.00 26.67           C  
ANISOU 2184  CE1 TYR A 287     4467   2308   3359   -993    -76   -196       C  
ATOM   2185  CE2 TYR A 287       4.124   1.268  51.099  1.00 20.66           C  
ANISOU 2185  CE2 TYR A 287     3683   1533   2636   -790    -44   -134       C  
ATOM   2186  CZ  TYR A 287       3.570   0.529  50.069  1.00 24.37           C  
ANISOU 2186  CZ  TYR A 287     4223   1937   3099   -871    -57   -185       C  
ATOM   2187  OH  TYR A 287       4.339  -0.353  49.344  1.00 25.19           O  
ANISOU 2187  OH  TYR A 287     4408   1936   3226   -807    -49   -222       O  
ATOM   2188  N   VAL A 288       1.382   5.128  49.450  1.00 20.31           N  
ANISOU 2188  N   VAL A 288     3267   1957   2494   -870    -70   -222       N  
ATOM   2189  CA  VAL A 288       1.069   5.108  48.021  1.00 16.70           C  
ANISOU 2189  CA  VAL A 288     2823   1502   2022   -903    -86   -284       C  
ATOM   2190  C   VAL A 288       1.807   3.952  47.349  1.00 17.34           C  
ANISOU 2190  C   VAL A 288     3034   1435   2118   -898    -85   -322       C  
ATOM   2191  O   VAL A 288       3.032   3.898  47.377  1.00 17.65           O  
ANISOU 2191  O   VAL A 288     3118   1406   2182   -794    -68   -330       O  
ATOM   2192  CB  VAL A 288       1.446   6.430  47.328  1.00 18.78           C  
ANISOU 2192  CB  VAL A 288     3009   1847   2279   -815    -82   -316       C  
ATOM   2193  CG1 VAL A 288       1.108   6.376  45.836  1.00 19.12           C  
ANISOU 2193  CG1 VAL A 288     3065   1898   2299   -853   -100   -375       C  
ATOM   2194  CG2 VAL A 288       0.730   7.593  47.988  1.00 15.25           C  
ANISOU 2194  CG2 VAL A 288     2441   1534   1821   -810    -80   -281       C  
ATOM   2195  N   LYS A 289       1.060   3.022  46.763  1.00 18.27           N  
ANISOU 2195  N   LYS A 289     3215   1507   2220  -1009   -104   -347       N  
ATOM   2196  CA  LYS A 289       1.668   1.878  46.078  1.00 24.24           C  
ANISOU 2196  CA  LYS A 289     4079   2141   2992   -983   -100   -383       C  
ATOM   2197  C   LYS A 289       2.240   2.328  44.742  1.00 25.46           C  
ANISOU 2197  C   LYS A 289     4230   2310   3135   -913    -97   -450       C  
ATOM   2198  O   LYS A 289       1.627   3.120  44.021  1.00 21.51           O  
ANISOU 2198  O   LYS A 289     3659   1910   2603   -945   -111   -476       O  
ATOM   2199  CB  LYS A 289       0.655   0.739  45.863  1.00 22.42           C  
ANISOU 2199  CB  LYS A 289     3883   1887   2748  -1094   -118   -377       C  
ATOM   2200  N   VAL A 290       3.430   1.826  44.437  1.00 23.84           N  
ANISOU 2200  N   VAL A 290     4093   2010   2953   -815    -77   -474       N  
ATOM   2201  CA  VAL A 290       4.124   2.154  43.204  1.00 24.76           C  
ANISOU 2201  CA  VAL A 290     4210   2137   3059   -740    -69   -534       C  
ATOM   2202  C   VAL A 290       4.210   0.931  42.307  1.00 26.12           C  
ANISOU 2202  C   VAL A 290     4462   2231   3231   -749    -69   -577       C  
ATOM   2203  O   VAL A 290       4.784  -0.083  42.707  1.00 22.76           O  
ANISOU 2203  O   VAL A 290     4112   1699   2838   -715    -55   -565       O  
ATOM   2204  CB  VAL A 290       5.543   2.666  43.472  1.00 21.87           C  
ANISOU 2204  CB  VAL A 290     3846   1744   2718   -605    -42   -530       C  
ATOM   2205  CG1 VAL A 290       6.268   2.947  42.134  1.00 17.82           C  
ANISOU 2205  CG1 VAL A 290     3331   1251   2191   -531    -31   -590       C  
ATOM   2206  CG2 VAL A 290       5.513   3.885  44.383  1.00 19.43           C  
ANISOU 2206  CG2 VAL A 290     3462   1509   2410   -591    -42   -490       C  
ATOM   2207  N   ASN A 291       3.653   1.024  41.099  1.00 25.65           N  
ANISOU 2207  N   ASN A 291     4386   2224   3135   -794    -84   -627       N  
ATOM   2208  CA  ASN A 291       3.700  -0.081  40.147  1.00 24.93           C  
ANISOU 2208  CA  ASN A 291     4370   2064   3037   -808    -85   -677       C  
ATOM   2209  C   ASN A 291       5.009  -0.113  39.365  1.00 25.10           C  
ANISOU 2209  C   ASN A 291     4424   2047   3067   -688    -58   -725       C  
ATOM   2210  O   ASN A 291       5.545  -1.183  39.109  1.00 24.34           O  
ANISOU 2210  O   ASN A 291     4408   1853   2988   -655    -44   -750       O  
ATOM   2211  CB  ASN A 291       2.531  -0.009  39.158  1.00 23.64           C  
ANISOU 2211  CB  ASN A 291     4177   1979   2825   -913   -114   -710       C  
ATOM   2212  CG  ASN A 291       1.192  -0.362  39.790  1.00 30.74           C  
ANISOU 2212  CG  ASN A 291     5060   2905   3716  -1043   -140   -667       C  
ATOM   2213  OD1 ASN A 291       1.129  -1.100  40.770  1.00 29.38           O  
ANISOU 2213  OD1 ASN A 291     4931   2660   3572  -1067   -136   -626       O  
ATOM   2214  ND2 ASN A 291       0.108   0.164  39.216  1.00 31.59           N  
ANISOU 2214  ND2 ASN A 291     5099   3125   3781  -1126   -167   -672       N  
ATOM   2215  N   LYS A 292       5.530   1.051  38.990  1.00 21.48           N  
ANISOU 2215  N   LYS A 292     3901   1667   2594   -621    -50   -735       N  
ATOM   2216  CA  LYS A 292       6.694   1.081  38.100  1.00 28.01           C  
ANISOU 2216  CA  LYS A 292     4745   2479   3418   -515    -26   -781       C  
ATOM   2217  C   LYS A 292       7.908   1.842  38.630  1.00 26.07           C  
ANISOU 2217  C   LYS A 292     4464   2243   3197   -396      1   -754       C  
ATOM   2218  O   LYS A 292       8.979   1.258  38.754  1.00 19.61           O  
ANISOU 2218  O   LYS A 292     3690   1355   2408   -307     28   -756       O  
ATOM   2219  CB  LYS A 292       6.318   1.659  36.719  1.00 26.41           C  
ANISOU 2219  CB  LYS A 292     4505   2366   3163   -542    -39   -833       C  
ATOM   2220  CG  LYS A 292       5.605   0.692  35.760  1.00 33.88           C  
ANISOU 2220  CG  LYS A 292     5506   3287   4080   -623    -57   -884       C  
ATOM   2221  CD  LYS A 292       4.115   0.548  36.051  1.00 41.62           C  
ANISOU 2221  CD  LYS A 292     6467   4302   5043   -759    -92   -859       C  
ATOM   2222  CE  LYS A 292       3.449  -0.459  35.100  1.00 49.99           C  
ANISOU 2222  CE  LYS A 292     7587   5334   6074   -841   -110   -909       C  
ATOM   2223  NZ  LYS A 292       2.047  -0.838  35.507  1.00 48.93           N  
ANISOU 2223  NZ  LYS A 292     7443   5219   5927   -976   -142   -877       N  
ATOM   2224  N   GLU A 293       7.758   3.140  38.898  1.00 18.18           N  
ANISOU 2224  N   GLU A 293     3386   1335   2186   -393     -6   -730       N  
ATOM   2225  CA  GLU A 293       8.908   3.976  39.251  1.00 17.33           C  
ANISOU 2225  CA  GLU A 293     3240   1250   2095   -283     17   -709       C  
ATOM   2226  C   GLU A 293       8.562   5.061  40.245  1.00 19.42           C  
ANISOU 2226  C   GLU A 293     3442   1571   2365   -300      7   -661       C  
ATOM   2227  O   GLU A 293       7.451   5.588  40.239  1.00 16.10           O  
ANISOU 2227  O   GLU A 293     2980   1216   1922   -388    -18   -658       O  
ATOM   2228  CB  GLU A 293       9.499   4.661  38.015  1.00 17.08           C  
ANISOU 2228  CB  GLU A 293     3174   1284   2031   -227     27   -753       C  
ATOM   2229  CG  GLU A 293      10.049   3.743  36.936  1.00 19.67           C  
ANISOU 2229  CG  GLU A 293     3557   1568   2348   -192     44   -808       C  
ATOM   2230  CD  GLU A 293      10.893   4.499  35.918  1.00 24.66           C  
ANISOU 2230  CD  GLU A 293     4149   2269   2951   -119     62   -838       C  
ATOM   2231  OE1 GLU A 293      11.335   5.630  36.228  1.00 27.08           O  
ANISOU 2231  OE1 GLU A 293     4393   2638   3259    -73     67   -808       O  
ATOM   2232  OE2 GLU A 293      11.096   3.976  34.803  1.00 31.25           O  
ANISOU 2232  OE2 GLU A 293     5015   3098   3760   -110     70   -893       O  
ATOM   2233  N   VAL A 294       9.543   5.435  41.059  1.00 18.21           N  
ANISOU 2233  N   VAL A 294     3277   1403   2240   -212     26   -625       N  
ATOM   2234  CA  VAL A 294       9.432   6.627  41.872  1.00 14.86           C  
ANISOU 2234  CA  VAL A 294     2766   1058   1821   -202     18   -578       C  
ATOM   2235  C   VAL A 294      10.368   7.679  41.282  1.00 14.21           C  
ANISOU 2235  C   VAL A 294     2621   1048   1732   -114     30   -584       C  
ATOM   2236  O   VAL A 294      11.489   7.370  40.893  1.00 14.43           O  
ANISOU 2236  O   VAL A 294     2684   1034   1764    -31     54   -602       O  
ATOM   2237  CB  VAL A 294       9.798   6.354  43.354  1.00 14.95           C  
ANISOU 2237  CB  VAL A 294     2782   1028   1871   -173     24   -514       C  
ATOM   2238  CG1 VAL A 294       9.681   7.634  44.169  1.00 13.83           C  
ANISOU 2238  CG1 VAL A 294     2532    990   1735   -160     16   -465       C  
ATOM   2239  CG2 VAL A 294       8.914   5.265  43.913  1.00 15.49           C  
ANISOU 2239  CG2 VAL A 294     2918   1023   1946   -264     14   -503       C  
ATOM   2240  N   VAL A 295       9.906   8.914  41.179  1.00 13.51           N  
ANISOU 2240  N   VAL A 295     2439   1065   1631   -130     15   -567       N  
ATOM   2241  CA  VAL A 295      10.795   9.983  40.738  1.00 15.15           C  
ANISOU 2241  CA  VAL A 295     2584   1338   1835    -53     24   -562       C  
ATOM   2242  C   VAL A 295      10.872  11.072  41.798  1.00 17.26           C  
ANISOU 2242  C   VAL A 295     2769   1666   2124    -31     17   -506       C  
ATOM   2243  O   VAL A 295       9.853  11.621  42.215  1.00 18.59           O  
ANISOU 2243  O   VAL A 295     2888   1884   2290    -87     -2   -487       O  
ATOM   2244  CB  VAL A 295      10.351  10.589  39.383  1.00 12.89           C  
ANISOU 2244  CB  VAL A 295     2265   1123   1508    -82     13   -600       C  
ATOM   2245  CG1 VAL A 295      11.353  11.629  38.931  1.00 12.37           C  
ANISOU 2245  CG1 VAL A 295     2143   1118   1439     -4     23   -589       C  
ATOM   2246  CG2 VAL A 295      10.200   9.491  38.354  1.00 13.75           C  
ANISOU 2246  CG2 VAL A 295     2461   1175   1588   -114     18   -663       C  
ATOM   2247  N   VAL A 296      12.083  11.373  42.248  1.00 16.01           N  
ANISOU 2247  N   VAL A 296     2594   1504   1984     51     32   -480       N  
ATOM   2248  CA  VAL A 296      12.233  12.349  43.318  1.00 15.83           C  
ANISOU 2248  CA  VAL A 296     2504   1531   1980     69     25   -431       C  
ATOM   2249  C   VAL A 296      12.586  13.697  42.724  1.00 18.68           C  
ANISOU 2249  C   VAL A 296     2794   1972   2332     98     20   -429       C  
ATOM   2250  O   VAL A 296      13.565  13.820  41.992  1.00 16.15           O  
ANISOU 2250  O   VAL A 296     2473   1658   2004    152     33   -440       O  
ATOM   2251  CB  VAL A 296      13.294  11.933  44.357  1.00 14.13           C  
ANISOU 2251  CB  VAL A 296     2307   1273   1790    129     38   -394       C  
ATOM   2252  CG1 VAL A 296      13.174  12.831  45.596  1.00 10.73           C  
ANISOU 2252  CG1 VAL A 296     1815    892   1371    124     26   -349       C  
ATOM   2253  CG2 VAL A 296      13.136  10.448  44.741  1.00 11.99           C  
ANISOU 2253  CG2 VAL A 296     2121    906   1530    113     45   -396       C  
ATOM   2254  N   THR A 297      11.756  14.697  43.009  1.00 17.70           N  
ANISOU 2254  N   THR A 297     2611   1907   2207     62      3   -413       N  
ATOM   2255  CA  THR A 297      11.966  16.043  42.487  1.00  9.78           C  
ANISOU 2255  CA  THR A 297     1546    973   1199     84     -4   -406       C  
ATOM   2256  C   THR A 297      11.681  17.066  43.599  1.00  9.32           C  
ANISOU 2256  C   THR A 297     1433    949   1157     82    -14   -371       C  
ATOM   2257  O   THR A 297      10.899  18.003  43.428  1.00 10.91           O  
ANISOU 2257  O   THR A 297     1589   1200   1356     60    -27   -367       O  
ATOM   2258  CB  THR A 297      11.082  16.313  41.231  1.00  9.92           C  
ANISOU 2258  CB  THR A 297     1548   1031   1188     42    -17   -433       C  
ATOM   2259  OG1 THR A 297       9.697  16.055  41.518  1.00 12.58           O  
ANISOU 2259  OG1 THR A 297     1882   1377   1521    -26    -31   -435       O  
ATOM   2260  CG2 THR A 297      11.522  15.436  40.047  1.00 10.41           C  
ANISOU 2260  CG2 THR A 297     1664   1066   1227     50     -5   -474       C  
ATOM   2261  N   SER A 298      12.314  16.871  44.754  1.00 13.17           N  
ANISOU 2261  N   SER A 298     1929   1413   1662    107     -8   -346       N  
ATOM   2262  CA  SER A 298      12.034  17.704  45.928  1.00 11.35           C  
ANISOU 2262  CA  SER A 298     1658   1211   1441    101    -15   -320       C  
ATOM   2263  C   SER A 298      13.056  18.821  46.162  1.00 16.42           C  
ANISOU 2263  C   SER A 298     2263   1883   2093    145    -18   -302       C  
ATOM   2264  O   SER A 298      13.056  19.448  47.242  1.00  8.79           O  
ANISOU 2264  O   SER A 298     1274    933   1133    146    -22   -283       O  
ATOM   2265  CB  SER A 298      11.945  16.817  47.174  1.00  9.13           C  
ANISOU 2265  CB  SER A 298     1409    894   1167     88     -9   -301       C  
ATOM   2266  OG  SER A 298      10.827  15.936  47.092  1.00 11.60           O  
ANISOU 2266  OG  SER A 298     1751   1185   1472     31    -10   -313       O  
ATOM   2267  N   GLY A 299      13.909  19.070  45.163  1.00  8.53           N  
ANISOU 2267  N   GLY A 299     1259    894   1090    178    -15   -307       N  
ATOM   2268  CA  GLY A 299      14.859  20.172  45.223  1.00  8.27           C  
ANISOU 2268  CA  GLY A 299     1187    892   1062    208    -20   -287       C  
ATOM   2269  C   GLY A 299      16.220  19.756  45.768  1.00  9.61           C  
ANISOU 2269  C   GLY A 299     1364   1051   1236    250    -13   -265       C  
ATOM   2270  O   GLY A 299      16.340  18.738  46.441  1.00  9.90           O  
ANISOU 2270  O   GLY A 299     1433   1052   1277    257     -5   -259       O  
ATOM   2271  N   ALA A 300      17.246  20.552  45.486  1.00  9.07           N  
ANISOU 2271  N   ALA A 300     1262   1015   1167    275    -16   -249       N  
ATOM   2272  CA  ALA A 300      18.618  20.201  45.844  1.00  8.47           C  
ANISOU 2272  CA  ALA A 300     1181    945   1093    318     -9   -223       C  
ATOM   2273  C   ALA A 300      18.831  19.892  47.343  1.00  9.44           C  
ANISOU 2273  C   ALA A 300     1308   1055   1221    319    -15   -199       C  
ATOM   2274  O   ALA A 300      19.649  19.038  47.681  1.00  8.83           O  
ANISOU 2274  O   ALA A 300     1244    965   1145    356     -7   -180       O  
ATOM   2275  CB  ALA A 300      19.555  21.311  45.420  1.00  8.37           C  
ANISOU 2275  CB  ALA A 300     1122    982   1077    328    -17   -204       C  
ATOM   2276  N   PHE A 301      18.143  20.608  48.228  1.00  8.80           N  
ANISOU 2276  N   PHE A 301     1217    983   1143    282    -29   -198       N  
ATOM   2277  CA  PHE A 301      18.310  20.367  49.660  1.00 13.27           C  
ANISOU 2277  CA  PHE A 301     1788   1548   1708    278    -35   -176       C  
ATOM   2278  C   PHE A 301      17.617  19.075  50.114  1.00 15.99           C  
ANISOU 2278  C   PHE A 301     2175   1848   2051    271    -25   -177       C  
ATOM   2279  O   PHE A 301      18.089  18.419  51.039  1.00 11.79           O  
ANISOU 2279  O   PHE A 301     1655   1307   1517    284    -25   -148       O  
ATOM   2280  CB  PHE A 301      17.743  21.521  50.494  1.00  9.82           C  
ANISOU 2280  CB  PHE A 301     1330   1135   1267    243    -49   -181       C  
ATOM   2281  CG  PHE A 301      18.557  22.768  50.457  1.00  8.29           C  
ANISOU 2281  CG  PHE A 301     1102    976   1073    242    -64   -173       C  
ATOM   2282  CD1 PHE A 301      19.853  22.768  49.961  1.00  9.25           C  
ANISOU 2282  CD1 PHE A 301     1202   1118   1192    270    -66   -150       C  
ATOM   2283  CD2 PHE A 301      18.023  23.953  50.928  1.00  9.94           C  
ANISOU 2283  CD2 PHE A 301     1301   1196   1282    214    -75   -187       C  
ATOM   2284  CE1 PHE A 301      20.608  23.939  49.943  1.00  9.18           C  
ANISOU 2284  CE1 PHE A 301     1161   1144   1182    258    -83   -139       C  
ATOM   2285  CE2 PHE A 301      18.771  25.139  50.903  1.00 17.61           C  
ANISOU 2285  CE2 PHE A 301     2248   2188   2253    206    -91   -180       C  
ATOM   2286  CZ  PHE A 301      20.062  25.132  50.412  1.00 12.28           C  
ANISOU 2286  CZ  PHE A 301     1552   1538   1578    222    -97   -154       C  
ATOM   2287  N   TYR A 302      16.478  18.735  49.502  1.00 13.17           N  
ANISOU 2287  N   TYR A 302     1840   1467   1696    243    -18   -205       N  
ATOM   2288  CA  TYR A 302      15.581  17.749  50.132  1.00  8.82           C  
ANISOU 2288  CA  TYR A 302     1326    881   1143    214    -13   -203       C  
ATOM   2289  C   TYR A 302      15.536  16.411  49.416  1.00 10.22           C  
ANISOU 2289  C   TYR A 302     1555   1003   1326    222      0   -214       C  
ATOM   2290  O   TYR A 302      15.367  15.368  50.062  1.00 13.31           O  
ANISOU 2290  O   TYR A 302     1986   1352   1720    214      4   -197       O  
ATOM   2291  CB  TYR A 302      14.174  18.344  50.274  1.00  8.63           C  
ANISOU 2291  CB  TYR A 302     1285    879   1114    164    -17   -223       C  
ATOM   2292  CG  TYR A 302      14.246  19.553  51.158  1.00  9.79           C  
ANISOU 2292  CG  TYR A 302     1394   1068   1256    162    -26   -216       C  
ATOM   2293  CD1 TYR A 302      14.668  19.423  52.491  1.00 13.21           C  
ANISOU 2293  CD1 TYR A 302     1829   1510   1680    163    -29   -190       C  
ATOM   2294  CD2 TYR A 302      13.979  20.828  50.666  1.00  8.14           C  
ANISOU 2294  CD2 TYR A 302     1153    890   1051    160    -33   -233       C  
ATOM   2295  CE1 TYR A 302      14.795  20.533  53.328  1.00 10.22           C  
ANISOU 2295  CE1 TYR A 302     1421   1170   1291    158    -38   -190       C  
ATOM   2296  CE2 TYR A 302      14.093  21.955  51.502  1.00 10.43           C  
ANISOU 2296  CE2 TYR A 302     1417   1208   1336    158    -40   -232       C  
ATOM   2297  CZ  TYR A 302      14.503  21.790  52.835  1.00 10.57           C  
ANISOU 2297  CZ  TYR A 302     1440   1235   1342    156    -43   -214       C  
ATOM   2298  OH  TYR A 302      14.639  22.880  53.673  1.00  8.38           O  
ANISOU 2298  OH  TYR A 302     1146    985   1055    150    -50   -219       O  
ATOM   2299  N   THR A 303      15.718  16.421  48.100  1.00 10.91           N  
ANISOU 2299  N   THR A 303     1646   1087   1412    238      6   -241       N  
ATOM   2300  CA  THR A 303      15.835  15.160  47.375  1.00  9.71           C  
ANISOU 2300  CA  THR A 303     1551    877   1261    253     20   -258       C  
ATOM   2301  C   THR A 303      16.880  14.229  48.025  1.00 14.18           C  
ANISOU 2301  C   THR A 303     2147   1404   1838    305     30   -227       C  
ATOM   2302  O   THR A 303      16.575  13.063  48.270  1.00 12.52           O  
ANISOU 2302  O   THR A 303     1995   1130   1635    297     37   -225       O  
ATOM   2303  CB  THR A 303      16.145  15.398  45.878  1.00  9.72           C  
ANISOU 2303  CB  THR A 303     1547    893   1253    273     28   -291       C  
ATOM   2304  OG1 THR A 303      14.961  15.891  45.244  1.00  9.53           O  
ANISOU 2304  OG1 THR A 303     1511    893   1218    219     18   -318       O  
ATOM   2305  CG2 THR A 303      16.588  14.092  45.189  1.00 10.33           C  
ANISOU 2305  CG2 THR A 303     1686    909   1328    307     48   -313       C  
ATOM   2306  N   PRO A 304      18.101  14.732  48.339  1.00 14.98           N  
ANISOU 2306  N   PRO A 304     2208   1542   1941    356     29   -198       N  
ATOM   2307  CA  PRO A 304      19.028  13.817  49.018  1.00 10.50           C  
ANISOU 2307  CA  PRO A 304     1664    944   1383    409     36   -160       C  
ATOM   2308  C   PRO A 304      18.561  13.362  50.411  1.00 10.63           C  
ANISOU 2308  C   PRO A 304     1699    939   1402    379     26   -125       C  
ATOM   2309  O   PRO A 304      18.912  12.257  50.829  1.00 12.69           O  
ANISOU 2309  O   PRO A 304     2003   1146   1672    410     34    -98       O  
ATOM   2310  CB  PRO A 304      20.325  14.645  49.132  1.00 10.36           C  
ANISOU 2310  CB  PRO A 304     1583    992   1360    455     32   -132       C  
ATOM   2311  CG  PRO A 304      19.917  16.056  49.004  1.00 10.29           C  
ANISOU 2311  CG  PRO A 304     1526   1042   1343    410     16   -146       C  
ATOM   2312  CD  PRO A 304      18.751  16.023  48.036  1.00 15.64           C  
ANISOU 2312  CD  PRO A 304     2229   1695   2018    370     21   -193       C  
ATOM   2313  N   THR A 305      17.785  14.186  51.115  1.00 10.22           N  
ANISOU 2313  N   THR A 305     1616    927   1340    323     11   -123       N  
ATOM   2314  CA  THR A 305      17.325  13.796  52.449  1.00 10.38           C  
ANISOU 2314  CA  THR A 305     1650    940   1355    292      4    -89       C  
ATOM   2315  C   THR A 305      16.257  12.696  52.381  1.00 12.15           C  
ANISOU 2315  C   THR A 305     1934   1097   1584    249     11    -98       C  
ATOM   2316  O   THR A 305      16.175  11.859  53.265  1.00 11.22           O  
ANISOU 2316  O   THR A 305     1850    946   1468    241     11    -61       O  
ATOM   2317  CB  THR A 305      16.773  15.006  53.260  1.00  9.93           C  
ANISOU 2317  CB  THR A 305     1543    949   1280    248    -10    -90       C  
ATOM   2318  OG1 THR A 305      15.577  15.526  52.667  1.00  9.63           O  
ANISOU 2318  OG1 THR A 305     1498    921   1240    201     -9   -131       O  
ATOM   2319  CG2 THR A 305      17.831  16.095  53.398  1.00  9.65           C  
ANISOU 2319  CG2 THR A 305     1455    973   1239    278    -21    -81       C  
ATOM   2320  N   ILE A 306      15.458  12.681  51.315  1.00 13.60           N  
ANISOU 2320  N   ILE A 306     2133   1264   1769    218     16   -145       N  
ATOM   2321  CA  ILE A 306      14.484  11.618  51.124  1.00 14.94           C  
ANISOU 2321  CA  ILE A 306     2363   1371   1942    169     21   -157       C  
ATOM   2322  C   ILE A 306      15.212  10.297  50.840  1.00 22.94           C  
ANISOU 2322  C   ILE A 306     3448   2298   2972    215     33   -148       C  
ATOM   2323  O   ILE A 306      14.883   9.242  51.416  1.00 12.36           O  
ANISOU 2323  O   ILE A 306     2163    894   1639    192     34   -123       O  
ATOM   2324  CB  ILE A 306      13.501  11.980  49.981  1.00 15.60           C  
ANISOU 2324  CB  ILE A 306     2440   1470   2018    122     20   -209       C  
ATOM   2325  CG1 ILE A 306      12.560  13.105  50.453  1.00 19.29           C  
ANISOU 2325  CG1 ILE A 306     2845   2013   2472     75      9   -209       C  
ATOM   2326  CG2 ILE A 306      12.705  10.764  49.512  1.00 13.82           C  
ANISOU 2326  CG2 ILE A 306     2284   1173   1793     73     23   -228       C  
ATOM   2327  CD1 ILE A 306      11.764  13.767  49.338  1.00 19.10           C  
ANISOU 2327  CD1 ILE A 306     2794   2024   2439     45      5   -251       C  
ATOM   2328  N   LEU A 307      16.218  10.361  49.971  1.00 19.37           N  
ANISOU 2328  N   LEU A 307     2994   1842   2526    283     44   -166       N  
ATOM   2329  CA  LEU A 307      16.998   9.175  49.640  1.00 17.02           C  
ANISOU 2329  CA  LEU A 307     2760   1463   2243    344     61   -162       C  
ATOM   2330  C   LEU A 307      17.699   8.633  50.905  1.00 15.23           C  
ANISOU 2330  C   LEU A 307     2542   1216   2029    385     58    -95       C  
ATOM   2331  O   LEU A 307      17.665   7.435  51.182  1.00 15.32           O  
ANISOU 2331  O   LEU A 307     2625   1141   2056    393     65    -75       O  
ATOM   2332  CB  LEU A 307      18.012   9.493  48.533  1.00 14.13           C  
ANISOU 2332  CB  LEU A 307     2374   1119   1875    416     77   -191       C  
ATOM   2333  CG  LEU A 307      17.415   9.843  47.159  1.00 14.78           C  
ANISOU 2333  CG  LEU A 307     2459   1214   1941    384     81   -256       C  
ATOM   2334  CD1 LEU A 307      18.507  10.121  46.135  1.00 20.01           C  
ANISOU 2334  CD1 LEU A 307     3100   1906   2597    458     99   -277       C  
ATOM   2335  CD2 LEU A 307      16.466   8.756  46.668  1.00 14.11           C  
ANISOU 2335  CD2 LEU A 307     2460   1045   1857    332     85   -294       C  
ATOM   2336  N   GLN A 308      18.305   9.526  51.677  1.00 15.33           N  
ANISOU 2336  N   GLN A 308     2484   1309   2033    405     47    -58       N  
ATOM   2337  CA  GLN A 308      18.992   9.133  52.914  1.00 18.69           C  
ANISOU 2337  CA  GLN A 308     2906   1735   2461    440     39     10       C  
ATOM   2338  C   GLN A 308      18.068   8.475  53.928  1.00 16.42           C  
ANISOU 2338  C   GLN A 308     2659   1409   2172    377     31     43       C  
ATOM   2339  O   GLN A 308      18.374   7.400  54.409  1.00 15.73           O  
ANISOU 2339  O   GLN A 308     2623   1255   2099    405     34     86       O  
ATOM   2340  CB  GLN A 308      19.686  10.348  53.541  1.00 12.32           C  
ANISOU 2340  CB  GLN A 308     2013   1032   1637    453     24     36       C  
ATOM   2341  CG  GLN A 308      20.975  10.734  52.782  1.00 12.31           C  
ANISOU 2341  CG  GLN A 308     1971   1067   1639    530     32     31       C  
ATOM   2342  CD  GLN A 308      21.425  12.160  53.056  1.00 15.59           C  
ANISOU 2342  CD  GLN A 308     2303   1585   2035    518     15     36       C  
ATOM   2343  OE1 GLN A 308      20.770  12.894  53.789  1.00 13.20           O  
ANISOU 2343  OE1 GLN A 308     1976   1322   1717    457     -2     36       O  
ATOM   2344  NE2 GLN A 308      22.557  12.558  52.462  1.00 14.89           N  
ANISOU 2344  NE2 GLN A 308     2171   1540   1946    575     19     40       N  
ATOM   2345  N   ARG A 309      16.932   9.089  54.241  1.00 17.00           N  
ANISOU 2345  N   ARG A 309     2709   1524   2228    294     21     26       N  
ATOM   2346  CA  ARG A 309      15.997   8.466  55.188  1.00 20.85           C  
ANISOU 2346  CA  ARG A 309     3228   1984   2708    228     15     59       C  
ATOM   2347  C   ARG A 309      15.510   7.123  54.671  1.00 21.20           C  
ANISOU 2347  C   ARG A 309     3364   1918   2773    208     25     51       C  
ATOM   2348  O   ARG A 309      15.198   6.219  55.456  1.00 19.33           O  
ANISOU 2348  O   ARG A 309     3174   1630   2540    180     22     98       O  
ATOM   2349  CB  ARG A 309      14.784   9.358  55.455  1.00 22.20           C  
ANISOU 2349  CB  ARG A 309     3355   2225   2856    147      9     35       C  
ATOM   2350  CG  ARG A 309      14.948  10.320  56.598  1.00 22.77           C  
ANISOU 2350  CG  ARG A 309     3363   2387   2902    142     -2     63       C  
ATOM   2351  CD  ARG A 309      13.606  10.875  57.025  1.00 19.04           C  
ANISOU 2351  CD  ARG A 309     2861   1966   2406     64     -3     47       C  
ATOM   2352  NE  ARG A 309      12.858  11.397  55.893  1.00 14.05           N  
ANISOU 2352  NE  ARG A 309     2216   1342   1781     38      2    -13       N  
ATOM   2353  CZ  ARG A 309      13.101  12.566  55.310  1.00 18.74           C  
ANISOU 2353  CZ  ARG A 309     2761   1985   2373     63      0    -50       C  
ATOM   2354  NH1 ARG A 309      14.089  13.336  55.737  1.00 16.45           N  
ANISOU 2354  NH1 ARG A 309     2433   1738   2077    108     -7    -38       N  
ATOM   2355  NH2 ARG A 309      12.364  12.958  54.278  1.00 20.57           N  
ANISOU 2355  NH2 ARG A 309     2982   2225   2610     38      2    -97       N  
ATOM   2356  N   SER A 310      15.437   7.007  53.347  1.00 19.86           N  
ANISOU 2356  N   SER A 310     3220   1711   2614    217     36     -9       N  
ATOM   2357  CA  SER A 310      14.999   5.777  52.683  1.00 14.47           C  
ANISOU 2357  CA  SER A 310     2632    918   1948    195     45    -32       C  
ATOM   2358  C   SER A 310      16.082   4.704  52.662  1.00 22.19           C  
ANISOU 2358  C   SER A 310     3675   1803   2952    283     58     -5       C  
ATOM   2359  O   SER A 310      15.833   3.605  52.205  1.00 21.84           O  
ANISOU 2359  O   SER A 310     3722   1651   2925    273     67    -22       O  
ATOM   2360  CB  SER A 310      14.551   6.057  51.242  1.00 14.25           C  
ANISOU 2360  CB  SER A 310     2610    890   1914    173     51   -111       C  
ATOM   2361  OG  SER A 310      13.365   6.829  51.208  1.00 23.68           O  
ANISOU 2361  OG  SER A 310     3756   2155   3088     87     39   -132       O  
ATOM   2362  N   GLY A 311      17.287   5.016  53.126  1.00 15.17           N  
ANISOU 2362  N   GLY A 311     2743    954   2067    370     59     35       N  
ATOM   2363  CA  GLY A 311      18.316   3.992  53.198  1.00 16.01           C  
ANISOU 2363  CA  GLY A 311     2905    980   2199    463     73     71       C  
ATOM   2364  C   GLY A 311      19.322   3.992  52.063  1.00 18.13           C  
ANISOU 2364  C   GLY A 311     3174   1238   2477    559     95     29       C  
ATOM   2365  O   GLY A 311      20.053   3.017  51.879  1.00 22.45           O  
ANISOU 2365  O   GLY A 311     3781   1702   3047    640    113     43       O  
ATOM   2366  N   ILE A 312      19.362   5.092  51.315  1.00 17.40           N  
ANISOU 2366  N   ILE A 312     3014   1232   2365    552     96    -19       N  
ATOM   2367  CA  ILE A 312      20.302   5.256  50.214  1.00 24.19           C  
ANISOU 2367  CA  ILE A 312     3859   2106   3225    636    118    -58       C  
ATOM   2368  C   ILE A 312      21.261   6.404  50.519  1.00 14.85           C  
ANISOU 2368  C   ILE A 312     2569   1044   2029    681    110    -27       C  
ATOM   2369  O   ILE A 312      20.864   7.569  50.575  1.00 14.03           O  
ANISOU 2369  O   ILE A 312     2399   1026   1905    624     94    -39       O  
ATOM   2370  CB  ILE A 312      19.561   5.508  48.884  1.00 15.19           C  
ANISOU 2370  CB  ILE A 312     2739    962   2071    586    126   -143       C  
ATOM   2371  CG1 ILE A 312      18.637   4.320  48.600  1.00 17.24           C  
ANISOU 2371  CG1 ILE A 312     3108   1101   2342    533    130   -174       C  
ATOM   2372  CG2 ILE A 312      20.549   5.716  47.758  1.00 15.29           C  
ANISOU 2372  CG2 ILE A 312     2727   1006   2077    668    150   -179       C  
ATOM   2373  CD1 ILE A 312      17.605   4.578  47.559  1.00 20.93           C  
ANISOU 2373  CD1 ILE A 312     3590   1574   2788    452    128   -247       C  
ATOM   2374  N   GLY A 313      22.522   6.062  50.745  1.00 15.95           N  
ANISOU 2374  N   GLY A 313     2693   1189   2179    782    121     17       N  
ATOM   2375  CA  GLY A 313      23.503   7.044  51.160  1.00 20.34           C  
ANISOU 2375  CA  GLY A 313     3147   1859   2721    819    109     57       C  
ATOM   2376  C   GLY A 313      24.658   6.407  51.900  1.00 18.29           C  
ANISOU 2376  C   GLY A 313     2879   1598   2475    913    112    131       C  
ATOM   2377  O   GLY A 313      24.954   5.229  51.714  1.00 21.38           O  
ANISOU 2377  O   GLY A 313     3326   1909   2888    963    130    137       O  
ATOM   2378  N   ASP A 314      25.312   7.187  52.751  1.00 15.39           N  
ANISOU 2378  N   ASP A 314     2426   1332   2091    917     89    186       N  
ATOM   2379  CA  ASP A 314      26.438   6.686  53.532  1.00 22.43           C  
ANISOU 2379  CA  ASP A 314     3291   2242   2989   1003     85    266       C  
ATOM   2380  C   ASP A 314      25.955   5.796  54.685  1.00 19.72           C  
ANISOU 2380  C   ASP A 314     3007   1831   2657    983     71    323       C  
ATOM   2381  O   ASP A 314      25.527   6.308  55.722  1.00 22.44           O  
ANISOU 2381  O   ASP A 314     3320   2226   2980    912     42    355       O  
ATOM   2382  CB  ASP A 314      27.262   7.872  54.057  1.00 22.44           C  
ANISOU 2382  CB  ASP A 314     3179   2385   2962    999     61    303       C  
ATOM   2383  CG  ASP A 314      28.532   7.447  54.765  1.00 30.58           C  
ANISOU 2383  CG  ASP A 314     4166   3459   3994   1090     55    389       C  
ATOM   2384  OD1 ASP A 314      28.475   6.556  55.626  1.00 31.67           O  
ANISOU 2384  OD1 ASP A 314     4344   3546   4144   1105     47    443       O  
ATOM   2385  OD2 ASP A 314      29.603   8.009  54.466  1.00 43.93           O  
ANISOU 2385  OD2 ASP A 314     5773   5246   5673   1128     55    401       O  
ATOM   2386  N   PHE A 315      26.068   4.474  54.514  1.00 17.52           N  
ANISOU 2386  N   PHE A 315     2800   1450   2408   1030     89    331       N  
ATOM   2387  CA  PHE A 315      25.569   3.515  55.507  1.00 18.12           C  
ANISOU 2387  CA  PHE A 315     2942   1445   2497   1008     77    387       C  
ATOM   2388  C   PHE A 315      26.094   3.771  56.924  1.00 31.04           C  
ANISOU 2388  C   PHE A 315     4524   3156   4114   1023     47    485       C  
ATOM   2389  O   PHE A 315      25.331   3.710  57.895  1.00 29.62           O  
ANISOU 2389  O   PHE A 315     4367   2967   3922    952     27    521       O  
ATOM   2390  CB  PHE A 315      25.917   2.085  55.098  1.00 19.29           C  
ANISOU 2390  CB  PHE A 315     3149   1497   2682   1054     96    382       C  
ATOM   2391  CG  PHE A 315      24.909   1.449  54.176  1.00 25.50           C  
ANISOU 2391  CG  PHE A 315     4028   2174   3486   1002    114    304       C  
ATOM   2392  CD1 PHE A 315      23.981   2.218  53.501  1.00 26.98           C  
ANISOU 2392  CD1 PHE A 315     4226   2371   3656    932    117    235       C  
ATOM   2393  CD2 PHE A 315      24.889   0.073  53.995  1.00 28.86           C  
ANISOU 2393  CD2 PHE A 315     4530   2490   3946   1020    126    302       C  
ATOM   2394  CE1 PHE A 315      23.056   1.636  52.661  1.00 22.30           C  
ANISOU 2394  CE1 PHE A 315     3711   1690   3074    875    130    166       C  
ATOM   2395  CE2 PHE A 315      23.964  -0.520  53.148  1.00 27.41           C  
ANISOU 2395  CE2 PHE A 315     4428   2212   3774    963    139    231       C  
ATOM   2396  CZ  PHE A 315      23.049   0.263  52.477  1.00 22.91           C  
ANISOU 2396  CZ  PHE A 315     3861   1663   3181    888    140    163       C  
ATOM   2397  N   THR A 316      27.388   4.065  57.039  1.00 24.95           N  
ANISOU 2397  N   THR A 316     3665   2480   3335   1090     42    521       N  
ATOM   2398  CA  THR A 316      28.001   4.277  58.339  1.00 26.94           C  
ANISOU 2398  CA  THR A 316     3856   2816   3564   1101     11    613       C  
ATOM   2399  C   THR A 316      27.384   5.474  59.054  1.00 23.64           C  
ANISOU 2399  C   THR A 316     3391   2487   3103   1007    -18    612       C  
ATOM   2400  O   THR A 316      27.091   5.399  60.246  1.00 28.29           O  
ANISOU 2400  O   THR A 316     3979   3099   3670    960    -43    669       O  
ATOM   2401  CB  THR A 316      29.522   4.502  58.227  1.00 31.51           C  
ANISOU 2401  CB  THR A 316     4338   3498   4137   1173      8    640       C  
ATOM   2402  OG1 THR A 316      30.129   3.375  57.584  1.00 33.37           O  
ANISOU 2402  OG1 THR A 316     4605   3664   4408   1244     35    627       O  
ATOM   2403  CG2 THR A 316      30.134   4.680  59.612  1.00 27.26           C  
ANISOU 2403  CG2 THR A 316     3736   3051   3569   1174    -29    734       C  
ATOM   2404  N   TYR A 317      27.168   6.564  58.321  1.00 18.30           N  
ANISOU 2404  N   TYR A 317     2674   1866   2415    960    -15    538       N  
ATOM   2405  CA  TYR A 317      26.542   7.739  58.903  1.00 17.98           C  
ANISOU 2405  CA  TYR A 317     2588   1908   2337    854    -40    515       C  
ATOM   2406  C   TYR A 317      25.069   7.489  59.200  1.00 27.34           C  
ANISOU 2406  C   TYR A 317     3840   3025   3522    763    -39    487       C  
ATOM   2407  O   TYR A 317      24.585   7.836  60.277  1.00 30.07           O  
ANISOU 2407  O   TYR A 317     4171   3418   3837    696    -61    513       O  
ATOM   2408  CB  TYR A 317      26.664   8.958  57.998  1.00 15.22           C  
ANISOU 2408  CB  TYR A 317     2182   1623   1978    830    -36    447       C  
ATOM   2409  CG  TYR A 317      25.910  10.153  58.567  1.00 18.08           C  
ANISOU 2409  CG  TYR A 317     2511   2052   2307    724    -59    417       C  
ATOM   2410  CD1 TYR A 317      26.442  10.888  59.631  1.00 20.00           C  
ANISOU 2410  CD1 TYR A 317     2689   2398   2513    698    -91    459       C  
ATOM   2411  CD2 TYR A 317      24.659  10.513  58.084  1.00 13.80           C  
ANISOU 2411  CD2 TYR A 317     2004   1469   1768    652    -49    347       C  
ATOM   2412  CE1 TYR A 317      25.763  11.970  60.179  1.00 13.78           C  
ANISOU 2412  CE1 TYR A 317     1879   1664   1694    608   -109    426       C  
ATOM   2413  CE2 TYR A 317      23.966  11.592  58.627  1.00 13.17           C  
ANISOU 2413  CE2 TYR A 317     1896   1449   1660    567    -66    320       C  
ATOM   2414  CZ  TYR A 317      24.529  12.313  59.683  1.00 15.34           C  
ANISOU 2414  CZ  TYR A 317     2113   1817   1899    548    -94    358       C  
ATOM   2415  OH  TYR A 317      23.865  13.396  60.221  1.00 17.67           O  
ANISOU 2415  OH  TYR A 317     2386   2165   2164    469   -108    324       O  
ATOM   2416  N   LEU A 318      24.347   6.937  58.236  1.00 15.72           N  
ANISOU 2416  N   LEU A 318     2439   1455   2079    756    -14    431       N  
ATOM   2417  CA  LEU A 318      22.921   6.684  58.427  1.00 18.90           C  
ANISOU 2417  CA  LEU A 318     2901   1800   2481    664    -13    404       C  
ATOM   2418  C   LEU A 318      22.677   5.773  59.633  1.00 21.17           C  
ANISOU 2418  C   LEU A 318     3230   2049   2764    649    -25    482       C  
ATOM   2419  O   LEU A 318      21.777   6.014  60.445  1.00 18.13           O  
ANISOU 2419  O   LEU A 318     2845   1691   2354    564    -38    492       O  
ATOM   2420  CB  LEU A 318      22.310   6.067  57.168  1.00 19.05           C  
ANISOU 2420  CB  LEU A 318     2993   1713   2530    663     14    338       C  
ATOM   2421  CG  LEU A 318      22.356   6.952  55.922  1.00 23.20           C  
ANISOU 2421  CG  LEU A 318     3484   2277   3055    664     26    260       C  
ATOM   2422  CD1 LEU A 318      21.872   6.195  54.688  1.00 24.12           C  
ANISOU 2422  CD1 LEU A 318     3679   2290   3197    671     52    199       C  
ATOM   2423  CD2 LEU A 318      21.525   8.207  56.152  1.00 17.12           C  
ANISOU 2423  CD2 LEU A 318     2662   1587   2257    572     10    225       C  
ATOM   2424  N   SER A 319      23.486   4.730  59.756  1.00 17.13           N  
ANISOU 2424  N   SER A 319     2754   1478   2277    736    -20    542       N  
ATOM   2425  CA  SER A 319      23.337   3.827  60.890  1.00 26.27           C  
ANISOU 2425  CA  SER A 319     3953   2596   3432    729    -33    628       C  
ATOM   2426  C   SER A 319      23.587   4.578  62.185  1.00 22.54           C  
ANISOU 2426  C   SER A 319     3403   2250   2911    694    -63    683       C  
ATOM   2427  O   SER A 319      22.868   4.384  63.158  1.00 20.89           O  
ANISOU 2427  O   SER A 319     3212   2047   2678    625    -76    722       O  
ATOM   2428  CB  SER A 319      24.295   2.643  60.783  1.00 27.36           C  
ANISOU 2428  CB  SER A 319     4137   2652   3608    845    -22    688       C  
ATOM   2429  OG  SER A 319      23.736   1.607  59.995  1.00 33.62           O  
ANISOU 2429  OG  SER A 319     5037   3296   4442    851      3    653       O  
ATOM   2430  N   SER A 320      24.569   5.478  62.164  1.00 20.70           N  
ANISOU 2430  N   SER A 320     3084   2122   2659    734    -75    683       N  
ATOM   2431  CA  SER A 320      25.001   6.163  63.373  1.00 20.79           C  
ANISOU 2431  CA  SER A 320     3022   2257   2621    709   -107    736       C  
ATOM   2432  C   SER A 320      23.915   7.068  63.933  1.00 22.33           C  
ANISOU 2432  C   SER A 320     3200   2510   2775    593   -116    694       C  
ATOM   2433  O   SER A 320      23.935   7.397  65.115  1.00 19.38           O  
ANISOU 2433  O   SER A 320     2793   2217   2354    554   -140    739       O  
ATOM   2434  CB  SER A 320      26.272   6.977  63.113  1.00 17.17           C  
ANISOU 2434  CB  SER A 320     2475   1899   2151    765   -118    737       C  
ATOM   2435  OG  SER A 320      25.977   8.199  62.462  1.00 23.05           O  
ANISOU 2435  OG  SER A 320     3181   2693   2885    714   -115    651       O  
ATOM   2436  N   ILE A 321      22.959   7.462  63.100  1.00 15.94           N  
ANISOU 2436  N   ILE A 321     2415   1663   1980    542    -98    608       N  
ATOM   2437  CA  ILE A 321      21.877   8.302  63.588  1.00 15.34           C  
ANISOU 2437  CA  ILE A 321     2322   1640   1868    443   -102    567       C  
ATOM   2438  C   ILE A 321      20.576   7.531  63.650  1.00 27.71           C  
ANISOU 2438  C   ILE A 321     3958   3126   3444    382    -88    563       C  
ATOM   2439  O   ILE A 321      19.503   8.109  63.845  1.00 25.01           O  
ANISOU 2439  O   ILE A 321     3608   2816   3079    303    -84    521       O  
ATOM   2440  CB  ILE A 321      21.680   9.529  62.724  1.00 18.85           C  
ANISOU 2440  CB  ILE A 321     2726   2123   2312    420    -96    479       C  
ATOM   2441  CG1 ILE A 321      21.264   9.117  61.306  1.00 16.37           C  
ANISOU 2441  CG1 ILE A 321     2459   1715   2044    438    -70    421       C  
ATOM   2442  CG2 ILE A 321      22.951  10.384  62.743  1.00 14.31           C  
ANISOU 2442  CG2 ILE A 321     2079   1637   1722    464   -113    487       C  
ATOM   2443  CD1 ILE A 321      20.681  10.238  60.508  1.00 13.43           C  
ANISOU 2443  CD1 ILE A 321     2059   1373   1670    396    -63    337       C  
ATOM   2444  N   GLY A 322      20.668   6.220  63.483  1.00 16.27           N  
ANISOU 2444  N   GLY A 322     2578   1575   2030    420    -79    607       N  
ATOM   2445  CA  GLY A 322      19.513   5.374  63.706  1.00 20.83           C  
ANISOU 2445  CA  GLY A 322     3224   2076   2613    354    -70    620       C  
ATOM   2446  C   GLY A 322      18.619   5.096  62.515  1.00 23.01           C  
ANISOU 2446  C   GLY A 322     3554   2266   2924    321    -49    546       C  
ATOM   2447  O   GLY A 322      17.470   4.703  62.710  1.00 20.06           O  
ANISOU 2447  O   GLY A 322     3218   1858   2545    241    -44    544       O  
ATOM   2448  N   VAL A 323      19.104   5.300  61.286  1.00 20.87           N  
ANISOU 2448  N   VAL A 323     3281   1964   2682    376    -36    488       N  
ATOM   2449  CA  VAL A 323      18.328   4.841  60.136  1.00 21.98           C  
ANISOU 2449  CA  VAL A 323     3483   2013   2853    348    -18    424       C  
ATOM   2450  C   VAL A 323      18.414   3.321  60.121  1.00 25.71           C  
ANISOU 2450  C   VAL A 323     4053   2355   3360    376    -11    470       C  
ATOM   2451  O   VAL A 323      19.509   2.763  60.060  1.00 25.26           O  
ANISOU 2451  O   VAL A 323     4014   2257   3326    472     -7    508       O  
ATOM   2452  CB  VAL A 323      18.835   5.402  58.782  1.00 26.15           C  
ANISOU 2452  CB  VAL A 323     3990   2545   3400    401     -4    350       C  
ATOM   2453  CG1 VAL A 323      18.087   4.746  57.614  1.00 15.78           C  
ANISOU 2453  CG1 VAL A 323     2751   1130   2113    374     13    289       C  
ATOM   2454  CG2 VAL A 323      18.685   6.907  58.733  1.00 14.63           C  
ANISOU 2454  CG2 VAL A 323     2445   1201   1911    369    -12    305       C  
ATOM   2455  N   LYS A 324      17.269   2.652  60.229  1.00 27.10           N  
ANISOU 2455  N   LYS A 324     4291   2465   3539    290     -8    471       N  
ATOM   2456  CA  LYS A 324      17.258   1.200  60.403  1.00 29.32           C  
ANISOU 2456  CA  LYS A 324     4672   2616   3851    300     -5    525       C  
ATOM   2457  C   LYS A 324      17.286   0.434  59.073  1.00 30.28           C  
ANISOU 2457  C   LYS A 324     4880   2610   4015    332     14    465       C  
ATOM   2458  O   LYS A 324      18.061  -0.508  58.923  1.00 32.82           O  
ANISOU 2458  O   LYS A 324     5266   2832   4371    416     22    496       O  
ATOM   2459  CB  LYS A 324      16.046   0.765  61.229  1.00 25.67           C  
ANISOU 2459  CB  LYS A 324     4241   2144   3370    185    -14    565       C  
ATOM   2460  N   ASN A 325      16.469   0.834  58.102  1.00 28.15           N  
ANISOU 2460  N   ASN A 325     4611   2342   3742    271     22    378       N  
ATOM   2461  CA  ASN A 325      16.389   0.067  56.860  1.00 27.28           C  
ANISOU 2461  CA  ASN A 325     4589   2112   3664    287     38    317       C  
ATOM   2462  C   ASN A 325      17.300   0.647  55.783  1.00 30.21           C  
ANISOU 2462  C   ASN A 325     4924   2513   4041    381     54    254       C  
ATOM   2463  O   ASN A 325      17.004   1.675  55.171  1.00 29.08           O  
ANISOU 2463  O   ASN A 325     4717   2455   3878    353     54    193       O  
ATOM   2464  CB  ASN A 325      14.945   0.005  56.366  1.00 27.32           C  
ANISOU 2464  CB  ASN A 325     4624   2098   3658    160     35    262       C  
ATOM   2465  CG  ASN A 325      14.019  -0.659  57.372  1.00 32.89           C  
ANISOU 2465  CG  ASN A 325     5368   2773   4357     60     22    327       C  
ATOM   2466  OD1 ASN A 325      14.308  -1.741  57.872  1.00 34.35           O  
ANISOU 2466  OD1 ASN A 325     5631   2856   4565     80     21    389       O  
ATOM   2467  ND2 ASN A 325      12.910  -0.001  57.687  1.00 33.58           N  
ANISOU 2467  ND2 ASN A 325     5397   2951   4410    -44     13    317       N  
ATOM   2468  N   LEU A 326      18.417  -0.035  55.563  1.00 26.21           N  
ANISOU 2468  N   LEU A 326     4458   1937   3563    495     69    274       N  
ATOM   2469  CA  LEU A 326      19.436   0.419  54.635  1.00 23.74           C  
ANISOU 2469  CA  LEU A 326     4092   1672   3254    589     85    226       C  
ATOM   2470  C   LEU A 326      19.278  -0.299  53.288  1.00 28.05           C  
ANISOU 2470  C   LEU A 326     4685   2153   3820    584    104    142       C  
ATOM   2471  O   LEU A 326      19.079  -1.517  53.241  1.00 20.55           O  
ANISOU 2471  O   LEU A 326     3805   1108   2896    570    107    146       O  
ATOM   2472  CB  LEU A 326      20.823   0.180  55.236  1.00 25.09           C  
ANISOU 2472  CB  LEU A 326     4219   1876   3440    700     85    296       C  
ATOM   2473  CG  LEU A 326      21.078   0.858  56.590  1.00 24.70           C  
ANISOU 2473  CG  LEU A 326     4114   1907   3365    706     63    383       C  
ATOM   2474  CD1 LEU A 326      22.447   0.478  57.137  1.00 26.66           C  
ANISOU 2474  CD1 LEU A 326     4317   2185   3625    812     60    454       C  
ATOM   2475  CD2 LEU A 326      20.963   2.359  56.475  1.00 26.91           C  
ANISOU 2475  CD2 LEU A 326     4286   2330   3609    664     53    343       C  
ATOM   2476  N   VAL A 327      19.344   0.449  52.192  1.00 18.90           N  
ANISOU 2476  N   VAL A 327     3490   1047   2645    592    115     67       N  
ATOM   2477  CA  VAL A 327      19.050  -0.144  50.885  1.00 22.40           C  
ANISOU 2477  CA  VAL A 327     3977   1440   3095    573    131    -15       C  
ATOM   2478  C   VAL A 327      20.276  -0.200  49.989  1.00 21.73           C  
ANISOU 2478  C   VAL A 327     3858   1384   3016    678    154    -46       C  
ATOM   2479  O   VAL A 327      20.621  -1.258  49.472  1.00 21.91           O  
ANISOU 2479  O   VAL A 327     3929   1336   3060    714    170    -67       O  
ATOM   2480  CB  VAL A 327      17.931   0.617  50.151  1.00 18.60           C  
ANISOU 2480  CB  VAL A 327     3491    993   2584    478    124    -83       C  
ATOM   2481  CG1 VAL A 327      17.829   0.162  48.700  1.00 19.06           C  
ANISOU 2481  CG1 VAL A 327     3578   1024   2640    472    140   -168       C  
ATOM   2482  CG2 VAL A 327      16.595   0.462  50.894  1.00 19.36           C  
ANISOU 2482  CG2 VAL A 327     3631   1052   2674    359    103    -60       C  
ATOM   2483  N   TYR A 328      20.929   0.935  49.800  1.00 18.87           N  
ANISOU 2483  N   TYR A 328     3411   1125   2633    725    158    -49       N  
ATOM   2484  CA  TYR A 328      22.131   0.960  48.984  1.00 21.08           C  
ANISOU 2484  CA  TYR A 328     3648   1448   2914    819    181    -71       C  
ATOM   2485  C   TYR A 328      23.128   1.979  49.514  1.00 18.55           C  
ANISOU 2485  C   TYR A 328     3230   1237   2580    883    177    -20       C  
ATOM   2486  O   TYR A 328      22.783   3.138  49.755  1.00 17.54           O  
ANISOU 2486  O   TYR A 328     3054   1180   2430    846    162    -18       O  
ATOM   2487  CB  TYR A 328      21.787   1.266  47.519  1.00 23.86           C  
ANISOU 2487  CB  TYR A 328     4002   1819   3244    791    196   -162       C  
ATOM   2488  CG  TYR A 328      22.985   1.252  46.599  1.00 23.06           C  
ANISOU 2488  CG  TYR A 328     3861   1761   3139    882    223   -186       C  
ATOM   2489  CD1 TYR A 328      23.564   0.051  46.199  1.00 20.58           C  
ANISOU 2489  CD1 TYR A 328     3597   1377   2847    942    244   -199       C  
ATOM   2490  CD2 TYR A 328      23.535   2.438  46.123  1.00 23.44           C  
ANISOU 2490  CD2 TYR A 328     3824   1921   3160    908    228   -196       C  
ATOM   2491  CE1 TYR A 328      24.674   0.033  45.357  1.00 24.97           C  
ANISOU 2491  CE1 TYR A 328     4116   1977   3396   1028    273   -221       C  
ATOM   2492  CE2 TYR A 328      24.634   2.430  45.277  1.00 23.20           C  
ANISOU 2492  CE2 TYR A 328     3755   1937   3122    987    255   -215       C  
ATOM   2493  CZ  TYR A 328      25.198   1.226  44.900  1.00 23.76           C  
ANISOU 2493  CZ  TYR A 328     3874   1941   3212   1047    278   -228       C  
ATOM   2494  OH  TYR A 328      26.288   1.220  44.069  1.00 25.06           O  
ANISOU 2494  OH  TYR A 328     4000   2155   3366   1127    307   -246       O  
ATOM   2495  N   ASN A 329      24.362   1.528  49.699  1.00 19.24           N  
ANISOU 2495  N   ASN A 329     3289   1339   2683    978    188     20       N  
ATOM   2496  CA  ASN A 329      25.445   2.376  50.183  1.00 22.24           C  
ANISOU 2496  CA  ASN A 329     3571   1829   3050   1040    182     73       C  
ATOM   2497  C   ASN A 329      26.041   3.230  49.067  1.00 21.43           C  
ANISOU 2497  C   ASN A 329     3401   1816   2924   1068    200     25       C  
ATOM   2498  O   ASN A 329      26.713   2.721  48.178  1.00 19.43           O  
ANISOU 2498  O   ASN A 329     3151   1556   2674   1123    226     -6       O  
ATOM   2499  CB  ASN A 329      26.551   1.524  50.816  1.00 19.90           C  
ANISOU 2499  CB  ASN A 329     3264   1521   2776   1128    185    140       C  
ATOM   2500  CG  ASN A 329      27.638   2.358  51.478  1.00 22.51           C  
ANISOU 2500  CG  ASN A 329     3489   1973   3090   1180    173    205       C  
ATOM   2501  OD1 ASN A 329      27.357   3.228  52.293  1.00 18.82           O  
ANISOU 2501  OD1 ASN A 329     2982   1564   2605   1141    148    242       O  
ATOM   2502  ND2 ASN A 329      28.888   2.099  51.116  1.00 27.15           N  
ANISOU 2502  ND2 ASN A 329     4030   2604   3681   1266    191    218       N  
ATOM   2503  N   ASN A 330      25.756   4.520  49.097  1.00 20.36           N  
ANISOU 2503  N   ASN A 330     3210   1761   2763   1027    186     19       N  
ATOM   2504  CA  ASN A 330      26.407   5.470  48.207  1.00 23.49           C  
ANISOU 2504  CA  ASN A 330     3532   2256   3137   1051    197     -9       C  
ATOM   2505  C   ASN A 330      26.711   6.747  48.965  1.00 16.16           C  
ANISOU 2505  C   ASN A 330     2518   1430   2191   1044    173     38       C  
ATOM   2506  O   ASN A 330      25.841   7.607  49.113  1.00 15.31           O  
ANISOU 2506  O   ASN A 330     2409   1338   2071    980    156     21       O  
ATOM   2507  CB  ASN A 330      25.542   5.775  46.977  1.00 19.20           C  
ANISOU 2507  CB  ASN A 330     3020   1698   2578    993    208    -93       C  
ATOM   2508  CG  ASN A 330      26.226   6.722  46.000  1.00 20.95           C  
ANISOU 2508  CG  ASN A 330     3167   2020   2773   1017    221   -117       C  
ATOM   2509  OD1 ASN A 330      27.330   7.210  46.257  1.00 19.06           O  
ANISOU 2509  OD1 ASN A 330     2849   1865   2526   1071    221    -71       O  
ATOM   2510  ND2 ASN A 330      25.576   6.977  44.865  1.00 15.98           N  
ANISOU 2510  ND2 ASN A 330     2559   1387   2125    974    231   -186       N  
ATOM   2511  N   PRO A 331      27.957   6.883  49.433  1.00 20.44           N  
ANISOU 2511  N   PRO A 331     2988   2047   2731   1107    170     98       N  
ATOM   2512  CA  PRO A 331      28.360   8.035  50.252  1.00 18.45           C  
ANISOU 2512  CA  PRO A 331     2650   1899   2460   1099    143    150       C  
ATOM   2513  C   PRO A 331      28.335   9.367  49.494  1.00 21.85           C  
ANISOU 2513  C   PRO A 331     3021   2412   2867   1068    141    113       C  
ATOM   2514  O   PRO A 331      28.530  10.406  50.126  1.00 22.43           O  
ANISOU 2514  O   PRO A 331     3026   2571   2925   1033    113    145       O  
ATOM   2515  CB  PRO A 331      29.789   7.680  50.670  1.00 20.54           C  
ANISOU 2515  CB  PRO A 331     2854   2224   2727   1173    144    214       C  
ATOM   2516  CG  PRO A 331      29.835   6.184  50.588  1.00 30.96           C  
ANISOU 2516  CG  PRO A 331     4249   3441   4074   1217    165    212       C  
ATOM   2517  CD  PRO A 331      29.004   5.850  49.389  1.00 17.60           C  
ANISOU 2517  CD  PRO A 331     2628   1671   2386   1188    189    126       C  
ATOM   2518  N   LEU A 332      28.108   9.345  48.177  1.00 15.07           N  
ANISOU 2518  N   LEU A 332     2186   1538   2003   1061    166     46       N  
ATOM   2519  CA  LEU A 332      28.061  10.592  47.405  1.00 14.53           C  
ANISOU 2519  CA  LEU A 332     2063   1546   1912   1031    164     15       C  
ATOM   2520  C   LEU A 332      26.688  11.267  47.495  1.00 16.20           C  
ANISOU 2520  C   LEU A 332     2299   1736   2118    923    141    -23       C  
ATOM   2521  O   LEU A 332      26.541  12.441  47.130  1.00 14.25           O  
ANISOU 2521  O   LEU A 332     2001   1558   1856    869    127    -38       O  
ATOM   2522  CB  LEU A 332      28.420  10.343  45.927  1.00 14.77           C  
ANISOU 2522  CB  LEU A 332     2098   1585   1930   1055    198    -36       C  
ATOM   2523  CG  LEU A 332      29.747   9.625  45.638  1.00 18.05           C  
ANISOU 2523  CG  LEU A 332     2484   2028   2346   1136    223    -10       C  
ATOM   2524  CD1 LEU A 332      30.022   9.485  44.119  1.00 16.11           C  
ANISOU 2524  CD1 LEU A 332     2243   1796   2081   1157    258    -66       C  
ATOM   2525  CD2 LEU A 332      30.920  10.296  46.357  1.00 21.68           C  
ANISOU 2525  CD2 LEU A 332     2844   2597   2797   1165    207     63       C  
ATOM   2526  N   VAL A 333      25.680  10.527  47.957  1.00 13.59           N  
ANISOU 2526  N   VAL A 333     2046   1315   1804    885    135    -36       N  
ATOM   2527  CA  VAL A 333      24.328  11.073  48.021  1.00 12.91           C  
ANISOU 2527  CA  VAL A 333     1978   1214   1712    781    115    -71       C  
ATOM   2528  C   VAL A 333      24.331  12.334  48.873  1.00 15.63           C  
ANISOU 2528  C   VAL A 333     2250   1643   2047    726     83    -39       C  
ATOM   2529  O   VAL A 333      24.765  12.304  50.026  1.00 15.33           O  
ANISOU 2529  O   VAL A 333     2189   1627   2010    735     67     15       O  
ATOM   2530  CB  VAL A 333      23.313  10.055  48.598  1.00 15.75           C  
ANISOU 2530  CB  VAL A 333     2422   1473   2087    745    112    -74       C  
ATOM   2531  CG1 VAL A 333      21.953  10.711  48.787  1.00 12.49           C  
ANISOU 2531  CG1 VAL A 333     2011   1068   1667    639     91   -101       C  
ATOM   2532  CG2 VAL A 333      23.194   8.840  47.694  1.00 13.88           C  
ANISOU 2532  CG2 VAL A 333     2271   1140   1861    786    142   -117       C  
ATOM   2533  N   GLY A 334      23.897  13.448  48.284  1.00 15.12           N  
ANISOU 2533  N   GLY A 334     2151   1626   1968    673     74    -71       N  
ATOM   2534  CA  GLY A 334      23.824  14.716  48.993  1.00 16.33           C  
ANISOU 2534  CA  GLY A 334     2245   1847   2112    618     45    -51       C  
ATOM   2535  C   GLY A 334      25.102  15.535  48.916  1.00 15.52           C  
ANISOU 2535  C   GLY A 334     2067   1833   1999    648     39    -19       C  
ATOM   2536  O   GLY A 334      25.146  16.659  49.391  1.00 12.59           O  
ANISOU 2536  O   GLY A 334     1649   1516   1618    601     15     -7       O  
ATOM   2537  N   THR A 335      26.155  14.981  48.329  1.00 11.62           N  
ANISOU 2537  N   THR A 335     1558   1353   1504    725     61     -5       N  
ATOM   2538  CA  THR A 335      27.390  15.731  48.196  1.00 11.81           C  
ANISOU 2538  CA  THR A 335     1502   1471   1515    750     56     30       C  
ATOM   2539  C   THR A 335      27.411  16.505  46.862  1.00 12.82           C  
ANISOU 2539  C   THR A 335     1605   1636   1629    735     68     -5       C  
ATOM   2540  O   THR A 335      26.535  16.328  46.024  1.00 12.25           O  
ANISOU 2540  O   THR A 335     1579   1517   1558    716     81    -55       O  
ATOM   2541  CB  THR A 335      28.607  14.807  48.278  1.00 14.50           C  
ANISOU 2541  CB  THR A 335     1825   1827   1857    848     76     72       C  
ATOM   2542  OG1 THR A 335      28.632  13.954  47.121  1.00 15.93           O  
ANISOU 2542  OG1 THR A 335     2048   1962   2042    910    116     33       O  
ATOM   2543  CG2 THR A 335      28.547  13.954  49.547  1.00 17.15           C  
ANISOU 2543  CG2 THR A 335     2192   2119   2206    867     65    112       C  
ATOM   2544  N   GLY A 336      28.391  17.385  46.683  1.00 14.02           N  
ANISOU 2544  N   GLY A 336     1682   1878   1767    735     60     26       N  
ATOM   2545  CA  GLY A 336      28.510  18.122  45.432  1.00 13.13           C  
ANISOU 2545  CA  GLY A 336     1541   1808   1640    720     70      4       C  
ATOM   2546  C   GLY A 336      27.527  19.265  45.284  1.00 14.82           C  
ANISOU 2546  C   GLY A 336     1762   2016   1855    633     46    -21       C  
ATOM   2547  O   GLY A 336      27.270  19.745  44.176  1.00 18.01           O  
ANISOU 2547  O   GLY A 336     2161   2433   2247    616     55    -46       O  
ATOM   2548  N   LEU A 337      26.982  19.708  46.414  1.00 11.69           N  
ANISOU 2548  N   LEU A 337     1373   1600   1467    581     17    -14       N  
ATOM   2549  CA  LEU A 337      26.089  20.862  46.464  1.00  9.82           C  
ANISOU 2549  CA  LEU A 337     1140   1357   1234    505     -6    -34       C  
ATOM   2550  C   LEU A 337      26.780  22.096  45.886  1.00 10.48           C  
ANISOU 2550  C   LEU A 337     1167   1509   1307    477    -18    -14       C  
ATOM   2551  O   LEU A 337      27.910  22.416  46.271  1.00 11.14           O  
ANISOU 2551  O   LEU A 337     1199   1654   1382    482    -28     28       O  
ATOM   2552  CB  LEU A 337      25.651  21.131  47.907  1.00  9.60           C  
ANISOU 2552  CB  LEU A 337     1123   1313   1213    464    -32    -24       C  
ATOM   2553  CG  LEU A 337      24.840  22.404  48.168  1.00 11.63           C  
ANISOU 2553  CG  LEU A 337     1381   1565   1473    394    -56    -43       C  
ATOM   2554  CD1 LEU A 337      23.502  22.339  47.418  1.00  9.40           C  
ANISOU 2554  CD1 LEU A 337     1140   1233   1199    378    -45    -88       C  
ATOM   2555  CD2 LEU A 337      24.624  22.641  49.679  1.00  9.08           C  
ANISOU 2555  CD2 LEU A 337     1064   1238   1148    361    -78    -33       C  
ATOM   2556  N   LYS A 338      26.101  22.773  44.967  1.00 11.56           N  
ANISOU 2556  N   LYS A 338     1312   1636   1442    444    -18    -40       N  
ATOM   2557  CA  LYS A 338      26.627  23.958  44.300  1.00  9.54           C  
ANISOU 2557  CA  LYS A 338     1012   1436   1178    411    -28    -19       C  
ATOM   2558  C   LYS A 338      25.612  25.077  44.375  1.00 15.81           C  
ANISOU 2558  C   LYS A 338     1825   2199   1984    348    -52    -37       C  
ATOM   2559  O   LYS A 338      24.432  24.827  44.597  1.00 14.52           O  
ANISOU 2559  O   LYS A 338     1705   1980   1832    339    -51    -70       O  
ATOM   2560  CB  LYS A 338      26.957  23.667  42.820  1.00  9.81           C  
ANISOU 2560  CB  LYS A 338     1032   1501   1192    446      0    -26       C  
ATOM   2561  CG  LYS A 338      27.916  22.500  42.595  1.00 14.25           C  
ANISOU 2561  CG  LYS A 338     1581   2091   1742    523     31    -16       C  
ATOM   2562  CD  LYS A 338      29.307  22.844  43.082  1.00 21.13           C  
ANISOU 2562  CD  LYS A 338     2383   3041   2606    532     23     39       C  
ATOM   2563  CE  LYS A 338      29.993  23.826  42.133  1.00 21.18           C  
ANISOU 2563  CE  LYS A 338     2332   3124   2592    505     22     67       C  
ATOM   2564  NZ  LYS A 338      31.341  24.232  42.630  1.00 15.46           N  
ANISOU 2564  NZ  LYS A 338     1533   2485   1857    501      9    125       N  
ATOM   2565  N   ASN A 339      26.055  26.309  44.153  1.00  9.16           N  
ANISOU 2565  N   ASN A 339      949   1391   1139    306    -71    -12       N  
ATOM   2566  CA  ASN A 339      25.126  27.430  44.098  1.00  8.86           C  
ANISOU 2566  CA  ASN A 339      932   1319   1116    255    -90    -26       C  
ATOM   2567  C   ASN A 339      25.794  28.529  43.283  1.00  9.08           C  
ANISOU 2567  C   ASN A 339      924   1390   1138    222   -101      8       C  
ATOM   2568  O   ASN A 339      26.950  28.379  42.881  1.00  9.44           O  
ANISOU 2568  O   ASN A 339      924   1499   1165    236    -93     40       O  
ATOM   2569  CB  ASN A 339      24.778  27.924  45.516  1.00  8.71           C  
ANISOU 2569  CB  ASN A 339      932   1267   1111    221   -114    -34       C  
ATOM   2570  CG  ASN A 339      23.372  28.526  45.615  1.00 11.88           C  
ANISOU 2570  CG  ASN A 339     1373   1611   1530    198   -122    -67       C  
ATOM   2571  OD1 ASN A 339      22.862  29.106  44.666  1.00 14.44           O  
ANISOU 2571  OD1 ASN A 339     1700   1928   1860    188   -121    -70       O  
ATOM   2572  ND2 ASN A 339      22.743  28.384  46.786  1.00 10.94           N  
ANISOU 2572  ND2 ASN A 339     1281   1460   1417    191   -127    -89       N  
ATOM   2573  N   HIS A 340      25.081  29.617  43.025  1.00  8.94           N  
ANISOU 2573  N   HIS A 340      923   1341   1133    182   -118      4       N  
ATOM   2574  CA  HIS A 340      25.725  30.822  42.500  1.00 12.42           C  
ANISOU 2574  CA  HIS A 340     1336   1812   1573    137   -136     43       C  
ATOM   2575  C   HIS A 340      25.867  31.819  43.661  1.00 15.50           C  
ANISOU 2575  C   HIS A 340     1737   2174   1979     86   -168     48       C  
ATOM   2576  O   HIS A 340      25.331  31.590  44.735  1.00 11.08           O  
ANISOU 2576  O   HIS A 340     1206   1574   1428     89   -172     17       O  
ATOM   2577  CB  HIS A 340      24.919  31.425  41.351  1.00 12.81           C  
ANISOU 2577  CB  HIS A 340     1398   1844   1625    128   -135     43       C  
ATOM   2578  CG  HIS A 340      24.740  30.512  40.178  1.00 11.84           C  
ANISOU 2578  CG  HIS A 340     1268   1751   1479    170   -107     33       C  
ATOM   2579  ND1 HIS A 340      25.743  29.696  39.690  1.00 12.77           N  
ANISOU 2579  ND1 HIS A 340     1351   1931   1569    204    -83     46       N  
ATOM   2580  CD2 HIS A 340      23.669  30.297  39.377  1.00  9.01           C  
ANISOU 2580  CD2 HIS A 340      933   1373   1117    184    -98      9       C  
ATOM   2581  CE1 HIS A 340      25.305  29.036  38.636  1.00 11.83           C  
ANISOU 2581  CE1 HIS A 340     1241   1823   1429    235    -60     25       C  
ATOM   2582  NE2 HIS A 340      24.037  29.378  38.426  1.00 15.07           N  
ANISOU 2582  NE2 HIS A 340     1687   2187   1854    219    -71      4       N  
ATOM   2583  N   TYR A 341      26.567  32.929  43.452  1.00 16.39           N  
ANISOU 2583  N   TYR A 341     1830   2306   2092     33   -189     84       N  
ATOM   2584  CA  TYR A 341      26.785  33.863  44.541  1.00 15.39           C  
ANISOU 2584  CA  TYR A 341     1720   2151   1976    -22   -220     84       C  
ATOM   2585  C   TYR A 341      26.959  35.294  44.049  1.00 18.74           C  
ANISOU 2585  C   TYR A 341     2150   2556   2412    -83   -244    113       C  
ATOM   2586  O   TYR A 341      27.729  35.552  43.117  1.00 13.24           O  
ANISOU 2586  O   TYR A 341     1415   1913   1703   -103   -244    159       O  
ATOM   2587  CB  TYR A 341      28.004  33.447  45.359  1.00 13.34           C  
ANISOU 2587  CB  TYR A 341     1420   1953   1696    -34   -229    106       C  
ATOM   2588  CG  TYR A 341      28.076  34.152  46.691  1.00 10.26           C  
ANISOU 2588  CG  TYR A 341     1055   1533   1309    -86   -260     91       C  
ATOM   2589  CD1 TYR A 341      28.625  35.431  46.794  1.00 10.97           C  
ANISOU 2589  CD1 TYR A 341     1147   1618   1402   -163   -291    113       C  
ATOM   2590  CD2 TYR A 341      27.577  33.551  47.848  1.00 16.73           C  
ANISOU 2590  CD2 TYR A 341     1902   2328   2127    -64   -258     54       C  
ATOM   2591  CE1 TYR A 341      28.691  36.085  48.007  1.00 13.96           C  
ANISOU 2591  CE1 TYR A 341     1556   1967   1779   -216   -320     92       C  
ATOM   2592  CE2 TYR A 341      27.642  34.202  49.081  1.00 17.22           C  
ANISOU 2592  CE2 TYR A 341     1989   2369   2185   -114   -285     36       C  
ATOM   2593  CZ  TYR A 341      28.200  35.459  49.150  1.00 15.69           C  
ANISOU 2593  CZ  TYR A 341     1800   2170   1992   -189   -316     51       C  
ATOM   2594  OH  TYR A 341      28.252  36.112  50.351  1.00 13.47           O  
ANISOU 2594  OH  TYR A 341     1551   1864   1703   -241   -343     26       O  
ATOM   2595  N   SER A 342      26.258  36.213  44.711  1.00 11.17           N  
ANISOU 2595  N   SER A 342     1244   1522   1478   -113   -263     87       N  
ATOM   2596  CA  SER A 342      26.107  37.581  44.245  1.00 12.45           C  
ANISOU 2596  CA  SER A 342     1432   1637   1660   -161   -284    108       C  
ATOM   2597  C   SER A 342      26.630  38.655  45.191  1.00 15.29           C  
ANISOU 2597  C   SER A 342     1819   1962   2027   -234   -318    108       C  
ATOM   2598  O   SER A 342      25.879  39.180  46.012  1.00 20.33           O  
ANISOU 2598  O   SER A 342     2513   2526   2685   -238   -327     64       O  
ATOM   2599  CB  SER A 342      24.620  37.847  43.970  1.00 17.85           C  
ANISOU 2599  CB  SER A 342     2164   2247   2372   -123   -275     76       C  
ATOM   2600  OG  SER A 342      24.146  36.994  42.946  1.00 18.25           O  
ANISOU 2600  OG  SER A 342     2191   2331   2412    -70   -249     81       O  
ATOM   2601  N   PRO A 343      27.917  39.012  45.068  1.00 16.87           N  
ANISOU 2601  N   PRO A 343     1980   2219   2210   -294   -337    155       N  
ATOM   2602  CA  PRO A 343      28.372  40.232  45.737  1.00 12.09           C  
ANISOU 2602  CA  PRO A 343     1409   1573   1614   -380   -374    159       C  
ATOM   2603  C   PRO A 343      27.711  41.458  45.134  1.00 17.55           C  
ANISOU 2603  C   PRO A 343     2156   2174   2340   -403   -386    167       C  
ATOM   2604  O   PRO A 343      27.458  41.489  43.930  1.00 17.24           O  
ANISOU 2604  O   PRO A 343     2100   2144   2307   -379   -373    201       O  
ATOM   2605  CB  PRO A 343      29.877  40.252  45.461  1.00 15.12           C  
ANISOU 2605  CB  PRO A 343     1724   2053   1968   -439   -390    220       C  
ATOM   2606  CG  PRO A 343      30.215  38.851  45.052  1.00 16.72           C  
ANISOU 2606  CG  PRO A 343     1858   2348   2145   -369   -357    232       C  
ATOM   2607  CD  PRO A 343      29.005  38.338  44.349  1.00 17.28           C  
ANISOU 2607  CD  PRO A 343     1955   2377   2232   -290   -326    205       C  
ATOM   2608  N   VAL A 344      27.475  42.472  45.951  1.00 12.78           N  
ANISOU 2608  N   VAL A 344     1617   1484   1754   -449   -410    136       N  
ATOM   2609  CA  VAL A 344      26.776  43.673  45.511  1.00 13.14           C  
ANISOU 2609  CA  VAL A 344     1727   1427   1839   -462   -421    140       C  
ATOM   2610  C   VAL A 344      27.721  44.882  45.448  1.00 14.02           C  
ANISOU 2610  C   VAL A 344     1859   1514   1955   -568   -458    182       C  
ATOM   2611  O   VAL A 344      28.593  45.034  46.303  1.00 18.48           O  
ANISOU 2611  O   VAL A 344     2419   2103   2498   -637   -482    174       O  
ATOM   2612  CB  VAL A 344      25.613  43.985  46.473  1.00 16.02           C  
ANISOU 2612  CB  VAL A 344     2166   1695   2227   -423   -415     66       C  
ATOM   2613  CG1 VAL A 344      24.865  45.219  46.038  1.00 18.19           C  
ANISOU 2613  CG1 VAL A 344     2509   1859   2545   -423   -423     70       C  
ATOM   2614  CG2 VAL A 344      24.673  42.770  46.591  1.00 12.24           C  
ANISOU 2614  CG2 VAL A 344     1665   1246   1741   -328   -379     28       C  
ATOM   2615  N   THR A 345      27.573  45.718  44.423  1.00 14.40           N  
ANISOU 2615  N   THR A 345     1925   1518   2028   -587   -466    230       N  
ATOM   2616  CA  THR A 345      28.250  47.009  44.406  1.00 15.34           C  
ANISOU 2616  CA  THR A 345     2084   1583   2161   -690   -504    266       C  
ATOM   2617  C   THR A 345      27.260  48.150  44.280  1.00 15.76           C  
ANISOU 2617  C   THR A 345     2231   1493   2263   -677   -511    252       C  
ATOM   2618  O   THR A 345      26.216  48.006  43.673  1.00 17.36           O  
ANISOU 2618  O   THR A 345     2442   1665   2488   -594   -488    251       O  
ATOM   2619  CB  THR A 345      29.281  47.111  43.274  1.00 17.95           C  
ANISOU 2619  CB  THR A 345     2348   1999   2472   -748   -512    357       C  
ATOM   2620  OG1 THR A 345      28.614  47.304  42.010  1.00 19.68           O  
ANISOU 2620  OG1 THR A 345     2569   2199   2711   -702   -497    400       O  
ATOM   2621  CG2 THR A 345      30.160  45.854  43.246  1.00 15.28           C  
ANISOU 2621  CG2 THR A 345     1908   1810   2085   -733   -495    373       C  
ATOM   2622  N   ILE A 346      27.610  49.295  44.846  1.00 16.73           N  
ANISOU 2622  N   ILE A 346     2425   1527   2403   -761   -544    244       N  
ATOM   2623  CA  ILE A 346      26.759  50.479  44.791  1.00 17.21           C  
ANISOU 2623  CA  ILE A 346     2586   1438   2515   -750   -553    231       C  
ATOM   2624  C   ILE A 346      27.487  51.645  44.128  1.00 19.01           C  
ANISOU 2624  C   ILE A 346     2844   1617   2761   -853   -588    305       C  
ATOM   2625  O   ILE A 346      28.661  51.916  44.417  1.00 21.12           O  
ANISOU 2625  O   ILE A 346     3097   1923   3005   -964   -618    329       O  
ATOM   2626  CB  ILE A 346      26.307  50.910  46.201  1.00 21.26           C  
ANISOU 2626  CB  ILE A 346     3184   1854   3038   -749   -558    138       C  
ATOM   2627  CG1 ILE A 346      25.645  49.740  46.941  1.00 17.85           C  
ANISOU 2627  CG1 ILE A 346     2720   1478   2583   -658   -524     69       C  
ATOM   2628  CG2 ILE A 346      25.372  52.107  46.132  1.00 21.39           C  
ANISOU 2628  CG2 ILE A 346     3307   1710   3111   -720   -561    120       C  
ATOM   2629  CD1 ILE A 346      24.346  49.242  46.294  1.00 15.91           C  
ANISOU 2629  CD1 ILE A 346     2458   1226   2359   -536   -487     66       C  
ATOM   2630  N   THR A 347      26.796  52.351  43.239  1.00 20.63           N  
ANISOU 2630  N   THR A 347     3090   1741   3008   -820   -587    347       N  
ATOM   2631  CA  THR A 347      27.421  53.495  42.573  1.00 19.57           C  
ANISOU 2631  CA  THR A 347     2992   1550   2894   -917   -621    425       C  
ATOM   2632  C   THR A 347      26.691  54.785  42.918  1.00 25.20           C  
ANISOU 2632  C   THR A 347     3834   2077   3665   -914   -636    398       C  
ATOM   2633  O   THR A 347      25.459  54.803  42.987  1.00 20.28           O  
ANISOU 2633  O   THR A 347     3249   1383   3072   -804   -612    357       O  
ATOM   2634  CB  THR A 347      27.436  53.309  41.049  1.00 19.42           C  
ANISOU 2634  CB  THR A 347     2907   1602   2870   -897   -611    522       C  
ATOM   2635  OG1 THR A 347      28.297  52.214  40.716  1.00 18.83           O  
ANISOU 2635  OG1 THR A 347     2717   1697   2739   -912   -598    549       O  
ATOM   2636  CG2 THR A 347      27.921  54.586  40.333  1.00 20.59           C  
ANISOU 2636  CG2 THR A 347     3102   1676   3044   -993   -646    610       C  
ATOM   2637  N   ARG A 348      27.442  55.860  43.143  1.00 21.57           N  
ANISOU 2637  N   ARG A 348     3431   1552   3212  -1020   -667    415       N  
ATOM   2638  CA  ARG A 348      26.822  57.173  43.291  1.00 26.97           C  
ANISOU 2638  CA  ARG A 348     4219   2088   3939   -991   -661    390       C  
ATOM   2639  C   ARG A 348      26.964  57.981  42.005  1.00 27.63           C  
ANISOU 2639  C   ARG A 348     4306   2146   4045  -1016   -671    493       C  
ATOM   2640  O   ARG A 348      28.040  58.042  41.403  1.00 30.47           O  
ANISOU 2640  O   ARG A 348     4612   2588   4376  -1112   -692    568       O  
ATOM   2641  CB  ARG A 348      27.409  57.958  44.478  1.00 23.54           C  
ANISOU 2641  CB  ARG A 348     3848   1603   3493  -1061   -671    320       C  
ATOM   2642  CG  ARG A 348      26.760  59.335  44.648  1.00 24.73           C  
ANISOU 2642  CG  ARG A 348     4109   1595   3693  -1029   -660    291       C  
ATOM   2643  CD  ARG A 348      27.155  60.063  45.925  1.00 33.66           C  
ANISOU 2643  CD  ARG A 348     5309   2667   4815  -1084   -664    206       C  
ATOM   2644  NE  ARG A 348      26.519  59.467  47.103  1.00 37.39           N  
ANISOU 2644  NE  ARG A 348     5795   3139   5273  -1016   -639    100       N  
ATOM   2645  CZ  ARG A 348      27.161  58.921  48.131  1.00 35.04           C  
ANISOU 2645  CZ  ARG A 348     5471   2917   4926  -1069   -649     44       C  
ATOM   2646  NH1 ARG A 348      28.486  58.892  48.158  1.00 34.55           N  
ANISOU 2646  NH1 ARG A 348     5365   2939   4824  -1190   -683     84       N  
ATOM   2647  NH2 ARG A 348      26.469  58.410  49.140  1.00 36.23           N  
ANISOU 2647  NH2 ARG A 348     5636   3065   5065   -998   -624    -48       N  
ATOM   2648  N   VAL A 349      25.861  58.583  41.583  1.00 26.27           N  
ANISOU 2648  N   VAL A 349     4191   1869   3921   -925   -655    499       N  
ATOM   2649  CA  VAL A 349      25.864  59.424  40.398  1.00 26.65           C  
ANISOU 2649  CA  VAL A 349     4251   1882   3994   -939   -663    596       C  
ATOM   2650  C   VAL A 349      25.918  60.893  40.821  1.00 32.12           C  
ANISOU 2650  C   VAL A 349     5047   2438   4720   -971   -666    572       C  
ATOM   2651  O   VAL A 349      25.026  61.395  41.508  1.00 31.59           O  
ANISOU 2651  O   VAL A 349     5056   2258   4689   -894   -644    499       O  
ATOM   2652  CB  VAL A 349      24.642  59.143  39.504  1.00 27.59           C  
ANISOU 2652  CB  VAL A 349     4354   1987   4141   -818   -645    636       C  
ATOM   2653  CG1 VAL A 349      24.659  60.034  38.272  1.00 29.84           C  
ANISOU 2653  CG1 VAL A 349     4650   2243   4446   -833   -654    740       C  
ATOM   2654  CG2 VAL A 349      24.620  57.675  39.086  1.00 22.54           C  
ANISOU 2654  CG2 VAL A 349     3615   1482   3469   -792   -642    659       C  
ATOM   2655  N   HIS A 350      27.006  61.556  40.439  1.00 34.20           N  
ANISOU 2655  N   HIS A 350     5307   2717   4968  -1087   -693    632       N  
ATOM   2656  CA  HIS A 350      27.229  62.959  40.749  1.00 29.00           C  
ANISOU 2656  CA  HIS A 350     4743   1933   4340  -1137   -701    621       C  
ATOM   2657  C   HIS A 350      26.753  63.859  39.609  1.00 31.25           C  
ANISOU 2657  C   HIS A 350     5064   2142   4668  -1106   -699    708       C  
ATOM   2658  O   HIS A 350      26.732  63.446  38.452  1.00 30.29           O  
ANISOU 2658  O   HIS A 350     4876   2100   4534  -1094   -703    798       O  
ATOM   2659  CB  HIS A 350      28.714  63.225  41.008  1.00 35.74           C  
ANISOU 2659  CB  HIS A 350     5577   2849   5153  -1288   -734    640       C  
ATOM   2660  CG  HIS A 350      29.290  62.459  42.151  1.00 40.57           C  
ANISOU 2660  CG  HIS A 350     6155   3540   5720  -1328   -739    562       C  
ATOM   2661  ND1 HIS A 350      29.040  62.783  43.475  1.00 40.69           N  
ANISOU 2661  ND1 HIS A 350     6242   3474   5743  -1316   -731    452       N  
ATOM   2662  CD2 HIS A 350      30.144  61.410  42.188  1.00 39.30           C  
ANISOU 2662  CD2 HIS A 350     5894   3536   5503  -1381   -752    579       C  
ATOM   2663  CE1 HIS A 350      29.695  61.958  44.260  1.00 37.83           C  
ANISOU 2663  CE1 HIS A 350     5826   3217   5330  -1361   -740    409       C  
ATOM   2664  NE2 HIS A 350      30.380  61.109  43.504  1.00 37.87           N  
ANISOU 2664  NE2 HIS A 350     5726   3367   5298  -1399   -752    486       N  
ATOM   2665  N   GLY A 351      26.412  65.100  39.941  1.00 30.60           N  
ANISOU 2665  N   GLY A 351     5085   1908   4633  -1097   -692    682       N  
ATOM   2666  CA  GLY A 351      25.954  66.075  38.965  1.00 38.26           C  
ANISOU 2666  CA  GLY A 351     6100   2788   5648  -1067   -689    762       C  
ATOM   2667  C   GLY A 351      24.782  66.864  39.515  1.00 40.17           C  
ANISOU 2667  C   GLY A 351     6442   2870   5953   -958   -656    698       C  
ATOM   2668  O   GLY A 351      24.409  66.693  40.679  1.00 37.65           O  
ANISOU 2668  O   GLY A 351     6155   2513   5638   -917   -636    590       O  
ATOM   2669  N   GLU A 352      24.216  67.745  38.696  1.00 42.53           N  
ANISOU 2669  N   GLU A 352     6785   3077   6297   -910   -647    767       N  
ATOM   2670  CA  GLU A 352      22.998  68.460  39.072  1.00 45.40           C  
ANISOU 2670  CA  GLU A 352     7231   3297   6723   -788   -609    721       C  
ATOM   2671  C   GLU A 352      21.860  67.464  39.285  1.00 40.45           C  
ANISOU 2671  C   GLU A 352     6556   2720   6091   -649   -578    673       C  
ATOM   2672  O   GLU A 352      21.755  66.490  38.548  1.00 41.50           O  
ANISOU 2672  O   GLU A 352     6602   2976   6192   -626   -586    725       O  
ATOM   2673  CB  GLU A 352      22.610  69.483  37.999  1.00 48.23           C  
ANISOU 2673  CB  GLU A 352     7631   3566   7127   -757   -607    822       C  
ATOM   2674  CG  GLU A 352      23.676  70.528  37.702  1.00 55.10           C  
ANISOU 2674  CG  GLU A 352     8551   4378   8005   -892   -637    878       C  
ATOM   2675  CD  GLU A 352      23.904  71.499  38.853  1.00 61.60           C  
ANISOU 2675  CD  GLU A 352     9479   5060   8865   -935   -632    789       C  
ATOM   2676  OE1 GLU A 352      23.054  71.567  39.769  1.00 57.42           O  
ANISOU 2676  OE1 GLU A 352     8995   4454   8367   -839   -598    692       O  
ATOM   2677  OE2 GLU A 352      24.933  72.209  38.833  1.00 71.41           O  
ANISOU 2677  OE2 GLU A 352    10757   6272  10103  -1066   -663    816       O  
ATOM   2678  N   PRO A 353      21.016  67.702  40.304  1.00 42.14           N  
ANISOU 2678  N   PRO A 353     6826   2847   6339   -560   -542    574       N  
ATOM   2679  CA  PRO A 353      19.896  66.826  40.674  1.00 41.14           C  
ANISOU 2679  CA  PRO A 353     6658   2764   6209   -428   -509    517       C  
ATOM   2680  C   PRO A 353      19.002  66.454  39.494  1.00 42.93           C  
ANISOU 2680  C   PRO A 353     6830   3040   6443   -326   -500    605       C  
ATOM   2681  O   PRO A 353      18.688  65.280  39.328  1.00 42.98           O  
ANISOU 2681  O   PRO A 353     6756   3161   6414   -283   -500    601       O  
ATOM   2682  CB  PRO A 353      19.125  67.662  41.698  1.00 36.89           C  
ANISOU 2682  CB  PRO A 353     6206   2089   5721   -352   -469    425       C  
ATOM   2683  CG  PRO A 353      20.170  68.487  42.339  1.00 39.83           C  
ANISOU 2683  CG  PRO A 353     6648   2389   6097   -477   -490    388       C  
ATOM   2684  CD  PRO A 353      21.147  68.833  41.240  1.00 42.88           C  
ANISOU 2684  CD  PRO A 353     7022   2798   6472   -589   -532    503       C  
ATOM   2685  N   SER A 354      18.590  67.440  38.703  1.00 37.93           N  
ANISOU 2685  N   SER A 354     6239   2320   5854   -287   -494    682       N  
ATOM   2686  CA  SER A 354      17.731  67.182  37.554  1.00 40.95           C  
ANISOU 2686  CA  SER A 354     6571   2751   6239   -190   -488    772       C  
ATOM   2687  C   SER A 354      18.408  66.264  36.543  1.00 43.92           C  
ANISOU 2687  C   SER A 354     6852   3277   6558   -261   -526    854       C  
ATOM   2688  O   SER A 354      17.753  65.468  35.859  1.00 45.27           O  
ANISOU 2688  O   SER A 354     6949   3543   6708   -187   -525    894       O  
ATOM   2689  CB  SER A 354      17.357  68.493  36.870  1.00 41.86           C  
ANISOU 2689  CB  SER A 354     6752   2745   6406   -155   -479    850       C  
ATOM   2690  OG  SER A 354      18.490  69.053  36.229  1.00 44.34           O  
ANISOU 2690  OG  SER A 354     7085   3052   6711   -287   -516    926       O  
ATOM   2691  N   GLU A 355      19.730  66.383  36.462  1.00 37.07           N  
ANISOU 2691  N   GLU A 355     5983   2437   5664   -406   -560    877       N  
ATOM   2692  CA  GLU A 355      20.527  65.611  35.519  1.00 32.36           C  
ANISOU 2692  CA  GLU A 355     5296   1985   5014   -487   -593    957       C  
ATOM   2693  C   GLU A 355      20.766  64.197  36.047  1.00 34.21           C  
ANISOU 2693  C   GLU A 355     5453   2343   5203   -498   -596    896       C  
ATOM   2694  O   GLU A 355      20.717  63.229  35.292  1.00 32.52           O  
ANISOU 2694  O   GLU A 355     5149   2254   4953   -484   -606    945       O  
ATOM   2695  CB  GLU A 355      21.853  66.319  35.256  1.00 34.54           C  
ANISOU 2695  CB  GLU A 355     5594   2250   5279   -636   -624   1008       C  
ATOM   2696  CG  GLU A 355      22.623  65.810  34.055  1.00 40.69           C  
ANISOU 2696  CG  GLU A 355     6282   3170   6008   -714   -653   1114       C  
ATOM   2697  CD  GLU A 355      22.013  66.209  32.708  1.00 39.61           C  
ANISOU 2697  CD  GLU A 355     6131   3039   5881   -657   -653   1225       C  
ATOM   2698  OE1 GLU A 355      20.937  66.853  32.664  1.00 35.53           O  
ANISOU 2698  OE1 GLU A 355     5672   2416   5410   -549   -631   1227       O  
ATOM   2699  OE2 GLU A 355      22.636  65.875  31.678  1.00 35.84           O  
ANISOU 2699  OE2 GLU A 355     5579   2679   5359   -721   -674   1314       O  
ATOM   2700  N   VAL A 356      21.033  64.089  37.347  1.00 31.61           N  
ANISOU 2700  N   VAL A 356     5160   1979   4873   -523   -588    789       N  
ATOM   2701  CA  VAL A 356      21.117  62.788  38.001  1.00 29.11           C  
ANISOU 2701  CA  VAL A 356     4781   1761   4517   -517   -587    720       C  
ATOM   2702  C   VAL A 356      19.788  62.066  37.867  1.00 27.35           C  
ANISOU 2702  C   VAL A 356     4522   1567   4304   -374   -561    703       C  
ATOM   2703  O   VAL A 356      19.736  60.880  37.548  1.00 30.45           O  
ANISOU 2703  O   VAL A 356     4831   2076   4663   -359   -567    715       O  
ATOM   2704  CB  VAL A 356      21.470  62.919  39.495  1.00 30.31           C  
ANISOU 2704  CB  VAL A 356     4987   1861   4668   -554   -578    603       C  
ATOM   2705  CG1 VAL A 356      21.380  61.556  40.193  1.00 25.91           C  
ANISOU 2705  CG1 VAL A 356     4369   1401   4073   -530   -572    532       C  
ATOM   2706  CG2 VAL A 356      22.841  63.549  39.671  1.00 28.23           C  
ANISOU 2706  CG2 VAL A 356     4750   1587   4388   -704   -608    619       C  
ATOM   2707  N   SER A 357      18.709  62.795  38.109  1.00 29.58           N  
ANISOU 2707  N   SER A 357     4862   1744   4631   -268   -531    676       N  
ATOM   2708  CA  SER A 357      17.374  62.222  38.033  1.00 32.07           C  
ANISOU 2708  CA  SER A 357     5142   2087   4956   -127   -504    658       C  
ATOM   2709  C   SER A 357      17.069  61.682  36.641  1.00 32.03           C  
ANISOU 2709  C   SER A 357     5056   2182   4933    -96   -520    763       C  
ATOM   2710  O   SER A 357      16.568  60.566  36.490  1.00 28.87           O  
ANISOU 2710  O   SER A 357     4581   1880   4508    -42   -518    754       O  
ATOM   2711  CB  SER A 357      16.332  63.278  38.413  1.00 36.86           C  
ANISOU 2711  CB  SER A 357     5823   2565   5616    -22   -465    629       C  
ATOM   2712  OG  SER A 357      15.030  62.725  38.412  1.00 44.32           O  
ANISOU 2712  OG  SER A 357     6725   3547   6566    115   -437    609       O  
ATOM   2713  N   ARG A 358      17.382  62.482  35.625  1.00 28.36           N  
ANISOU 2713  N   ARG A 358     4606   1694   4476   -135   -537    863       N  
ATOM   2714  CA  ARG A 358      17.155  62.100  34.239  1.00 26.58           C  
ANISOU 2714  CA  ARG A 358     4306   1567   4227   -116   -554    969       C  
ATOM   2715  C   ARG A 358      17.964  60.851  33.907  1.00 26.81           C  
ANISOU 2715  C   ARG A 358     4242   1743   4201   -193   -576    987       C  
ATOM   2716  O   ARG A 358      17.484  59.930  33.243  1.00 24.49           O  
ANISOU 2716  O   ARG A 358     3866   1558   3880   -144   -578   1019       O  
ATOM   2717  CB  ARG A 358      17.516  63.269  33.304  1.00 36.33           C  
ANISOU 2717  CB  ARG A 358     5581   2747   5476   -162   -568   1070       C  
ATOM   2718  CG  ARG A 358      17.169  63.057  31.839  1.00 35.73           C  
ANISOU 2718  CG  ARG A 358     5436   2767   5374   -134   -582   1183       C  
ATOM   2719  CD  ARG A 358      17.236  64.376  31.064  1.00 41.53           C  
ANISOU 2719  CD  ARG A 358     6228   3419   6133   -150   -589   1273       C  
ATOM   2720  NE  ARG A 358      18.600  64.894  31.018  1.00 39.61           N  
ANISOU 2720  NE  ARG A 358     6012   3157   5881   -294   -611   1301       N  
ATOM   2721  CZ  ARG A 358      19.474  64.611  30.062  1.00 35.72           C  
ANISOU 2721  CZ  ARG A 358     5455   2776   5342   -388   -637   1383       C  
ATOM   2722  NH1 ARG A 358      19.128  63.815  29.054  1.00 32.24           N  
ANISOU 2722  NH1 ARG A 358     4921   2470   4858   -354   -642   1443       N  
ATOM   2723  NH2 ARG A 358      20.697  65.123  30.114  1.00 35.46           N  
ANISOU 2723  NH2 ARG A 358     5445   2727   5301   -518   -655   1403       N  
ATOM   2724  N   PHE A 359      19.193  60.819  34.403  1.00 26.53           N  
ANISOU 2724  N   PHE A 359     4218   1714   4148   -312   -591    963       N  
ATOM   2725  CA  PHE A 359      20.103  59.720  34.120  1.00 24.27           C  
ANISOU 2725  CA  PHE A 359     3847   1566   3809   -393   -608    984       C  
ATOM   2726  C   PHE A 359      19.637  58.414  34.777  1.00 29.30           C  
ANISOU 2726  C   PHE A 359     4435   2265   4431   -334   -596    908       C  
ATOM   2727  O   PHE A 359      19.858  57.321  34.239  1.00 31.59           O  
ANISOU 2727  O   PHE A 359     4638   2685   4680   -345   -599    938       O  
ATOM   2728  CB  PHE A 359      21.521  60.074  34.587  1.00 27.30           C  
ANISOU 2728  CB  PHE A 359     4254   1943   4177   -533   -626    975       C  
ATOM   2729  CG  PHE A 359      22.525  58.982  34.348  1.00 25.55           C  
ANISOU 2729  CG  PHE A 359     3941   1869   3898   -615   -638    998       C  
ATOM   2730  CD1 PHE A 359      22.982  58.715  33.068  1.00 24.48           C  
ANISOU 2730  CD1 PHE A 359     3729   1848   3722   -656   -647   1102       C  
ATOM   2731  CD2 PHE A 359      22.984  58.206  35.394  1.00 24.43           C  
ANISOU 2731  CD2 PHE A 359     3785   1757   3739   -647   -636    918       C  
ATOM   2732  CE1 PHE A 359      23.896  57.708  32.838  1.00 24.93           C  
ANISOU 2732  CE1 PHE A 359     3699   2049   3725   -723   -649   1124       C  
ATOM   2733  CE2 PHE A 359      23.895  57.195  35.171  1.00 28.75           C  
ANISOU 2733  CE2 PHE A 359     4245   2445   4234   -715   -641    942       C  
ATOM   2734  CZ  PHE A 359      24.353  56.945  33.885  1.00 22.27           C  
ANISOU 2734  CZ  PHE A 359     3346   1743   3372   -748   -642   1041       C  
ATOM   2735  N   LEU A 360      18.985  58.525  35.931  1.00 26.75           N  
ANISOU 2735  N   LEU A 360     4167   1858   4138   -269   -576    807       N  
ATOM   2736  CA  LEU A 360      18.525  57.344  36.655  1.00 28.17           C  
ANISOU 2736  CA  LEU A 360     4308   2089   4306   -213   -563    728       C  
ATOM   2737  C   LEU A 360      17.045  57.058  36.413  1.00 27.22           C  
ANISOU 2737  C   LEU A 360     4161   1978   4202    -71   -540    718       C  
ATOM   2738  O   LEU A 360      16.441  56.272  37.130  1.00 24.85           O  
ANISOU 2738  O   LEU A 360     3832   1722   3887     -6   -511    633       O  
ATOM   2739  CB  LEU A 360      18.776  57.501  38.161  1.00 27.11           C  
ANISOU 2739  CB  LEU A 360     4237   1885   4179   -234   -551    613       C  
ATOM   2740  CG  LEU A 360      20.236  57.600  38.604  1.00 26.65           C  
ANISOU 2740  CG  LEU A 360     4191   1842   4095   -375   -572    605       C  
ATOM   2741  CD1 LEU A 360      20.328  57.759  40.111  1.00 28.30           C  
ANISOU 2741  CD1 LEU A 360     4459   1989   4305   -384   -559    487       C  
ATOM   2742  CD2 LEU A 360      20.995  56.368  38.146  1.00 28.30           C  
ANISOU 2742  CD2 LEU A 360     4291   2220   4244   -424   -573    631       C  
ATOM   2743  N   SER A 361      16.457  57.693  35.406  1.00 29.34           N  
ANISOU 2743  N   SER A 361     4429   2234   4487    -24   -542    800       N  
ATOM   2744  CA  SER A 361      15.032  57.516  35.166  1.00 25.51           C  
ANISOU 2744  CA  SER A 361     3914   1762   4015    108   -522    797       C  
ATOM   2745  C   SER A 361      14.730  56.162  34.523  1.00 24.54           C  
ANISOU 2745  C   SER A 361     3679   1802   3842    134   -517    812       C  
ATOM   2746  O   SER A 361      15.626  55.489  33.990  1.00 21.37           O  
ANISOU 2746  O   SER A 361     3219   1513   3388     54   -522    837       O  
ATOM   2747  CB  SER A 361      14.482  58.654  34.300  1.00 30.43           C  
ANISOU 2747  CB  SER A 361     4568   2331   4662    153   -520    878       C  
ATOM   2748  OG  SER A 361      15.173  58.764  33.066  1.00 41.07           O  
ANISOU 2748  OG  SER A 361     5881   3741   5983     79   -547    986       O  
ATOM   2749  N   ASN A 362      13.464  55.762  34.627  1.00 22.76           N  
ANISOU 2749  N   ASN A 362     3420   1605   3622    246   -496    780       N  
ATOM   2750  CA  ASN A 362      12.942  54.559  33.988  1.00 21.70           C  
ANISOU 2750  CA  ASN A 362     3180   1632   3433    281   -482    783       C  
ATOM   2751  C   ASN A 362      13.596  53.253  34.445  1.00 21.76           C  
ANISOU 2751  C   ASN A 362     3133   1750   3383    227   -463    709       C  
ATOM   2752  O   ASN A 362      13.704  52.319  33.664  1.00 25.49           O  
ANISOU 2752  O   ASN A 362     3529   2356   3802    210   -460    730       O  
ATOM   2753  CB  ASN A 362      13.038  54.694  32.458  1.00 20.09           C  
ANISOU 2753  CB  ASN A 362     2930   1499   3204    259   -506    902       C  
ATOM   2754  CG  ASN A 362      12.125  55.776  31.920  1.00 28.67           C  
ANISOU 2754  CG  ASN A 362     4051   2501   4342    336   -523    982       C  
ATOM   2755  OD1 ASN A 362      10.997  55.929  32.384  1.00 27.84           O  
ANISOU 2755  OD1 ASN A 362     3953   2364   4263    438   -503    942       O  
ATOM   2756  ND2 ASN A 362      12.609  56.544  30.948  1.00 35.27           N  
ANISOU 2756  ND2 ASN A 362     4903   3327   5170    287   -543   1077       N  
ATOM   2757  N   MET A 363      14.003  53.181  35.714  1.00 21.73           N  
ANISOU 2757  N   MET A 363     3173   1693   3391    204   -450    620       N  
ATOM   2758  CA  MET A 363      14.632  51.980  36.262  1.00 17.49           C  
ANISOU 2758  CA  MET A 363     2591   1252   2805    159   -433    551       C  
ATOM   2759  C   MET A 363      13.723  51.181  37.195  1.00 17.92           C  
ANISOU 2759  C   MET A 363     2624   1332   2852    231   -402    459       C  
ATOM   2760  O   MET A 363      14.075  50.087  37.595  1.00 15.86           O  
ANISOU 2760  O   MET A 363     2321   1154   2550    206   -387    407       O  
ATOM   2761  CB  MET A 363      15.910  52.338  37.027  1.00 17.47           C  
ANISOU 2761  CB  MET A 363     2639   1193   2804     64   -444    523       C  
ATOM   2762  CG  MET A 363      17.009  52.947  36.176  1.00 24.24           C  
ANISOU 2762  CG  MET A 363     3505   2049   3657    -30   -473    612       C  
ATOM   2763  SD  MET A 363      18.498  53.303  37.142  1.00 22.45           S  
ANISOU 2763  SD  MET A 363     3329   1774   3428   -150   -489    577       S  
ATOM   2764  CE  MET A 363      19.250  51.689  37.295  1.00 17.03           C  
ANISOU 2764  CE  MET A 363     2546   1255   2671   -183   -468    534       C  
ATOM   2765  N   ALA A 364      12.572  51.735  37.553  1.00 21.18           N  
ANISOU 2765  N   ALA A 364     3066   1674   3306    321   -393    442       N  
ATOM   2766  CA  ALA A 364      11.691  51.093  38.530  1.00 24.80           C  
ANISOU 2766  CA  ALA A 364     3508   2153   3760    388   -362    356       C  
ATOM   2767  C   ALA A 364      11.256  49.681  38.133  1.00 23.25           C  
ANISOU 2767  C   ALA A 364     3219   2102   3512    402   -346    344       C  
ATOM   2768  O   ALA A 364      10.961  49.406  36.968  1.00 26.44           O  
ANISOU 2768  O   ALA A 364     3569   2581   3896    410   -357    408       O  
ATOM   2769  CB  ALA A 364      10.472  51.958  38.774  1.00 24.31           C  
ANISOU 2769  CB  ALA A 364     3481   2006   3748    491   -352    355       C  
ATOM   2770  N   ALA A 365      11.202  48.796  39.123  1.00 17.25           N  
ANISOU 2770  N   ALA A 365     2444   1380   2729    402   -323    262       N  
ATOM   2771  CA  ALA A 365      10.792  47.416  38.900  1.00 16.90           C  
ANISOU 2771  CA  ALA A 365     2323   1460   2638    410   -307    242       C  
ATOM   2772  C   ALA A 365       9.327  47.342  38.481  1.00 18.02           C  
ANISOU 2772  C   ALA A 365     2421   1638   2786    495   -299    260       C  
ATOM   2773  O   ALA A 365       8.481  48.066  39.011  1.00 16.36           O  
ANISOU 2773  O   ALA A 365     2238   1363   2615    566   -289    245       O  
ATOM   2774  CB  ALA A 365      11.036  46.573  40.165  1.00 18.35           C  
ANISOU 2774  CB  ALA A 365     2510   1662   2801    393   -284    154       C  
ATOM   2775  N   ASN A 366       9.048  46.522  37.472  1.00 17.07           N  
ANISOU 2775  N   ASN A 366     2233   1625   2627    489   -304    296       N  
ATOM   2776  CA  ASN A 366       7.676  46.159  37.141  1.00 16.20           C  
ANISOU 2776  CA  ASN A 366     2066   1579   2510    555   -297    305       C  
ATOM   2777  C   ASN A 366       7.726  44.691  36.701  1.00 13.50           C  
ANISOU 2777  C   ASN A 366     1662   1357   2108    513   -292    287       C  
ATOM   2778  O   ASN A 366       8.818  44.127  36.624  1.00 18.14           O  
ANISOU 2778  O   ASN A 366     2258   1966   2669    447   -293    273       O  
ATOM   2779  CB  ASN A 366       7.052  47.136  36.094  1.00 22.86           C  
ANISOU 2779  CB  ASN A 366     2901   2408   3379    603   -320    393       C  
ATOM   2780  CG  ASN A 366       7.622  46.990  34.680  1.00 20.20           C  
ANISOU 2780  CG  ASN A 366     2534   2134   3006    550   -346    468       C  
ATOM   2781  OD1 ASN A 366       7.575  45.916  34.077  1.00 16.91           O  
ANISOU 2781  OD1 ASN A 366     2062   1826   2536    520   -346    465       O  
ATOM   2782  ND2 ASN A 366       8.095  48.109  34.119  1.00 15.78           N  
ANISOU 2782  ND2 ASN A 366     2014   1505   2475    541   -369    538       N  
ATOM   2783  N   PRO A 367       6.561  44.045  36.491  1.00 14.15           N  
ANISOU 2783  N   PRO A 367     1687   1518   2171    551   -285    282       N  
ATOM   2784  CA  PRO A 367       6.574  42.620  36.147  1.00 12.79           C  
ANISOU 2784  CA  PRO A 367     1468   1448   1944    508   -280    256       C  
ATOM   2785  C   PRO A 367       7.444  42.235  34.930  1.00 20.64           C  
ANISOU 2785  C   PRO A 367     2448   2496   2896    448   -298    297       C  
ATOM   2786  O   PRO A 367       8.001  41.132  34.910  1.00 16.09           O  
ANISOU 2786  O   PRO A 367     1863   1970   2281    401   -289    260       O  
ATOM   2787  CB  PRO A 367       5.095  42.329  35.831  1.00 13.75           C  
ANISOU 2787  CB  PRO A 367     1529   1643   2055    557   -280    269       C  
ATOM   2788  CG  PRO A 367       4.338  43.311  36.644  1.00 16.62           C  
ANISOU 2788  CG  PRO A 367     1909   1937   2469    633   -269    265       C  
ATOM   2789  CD  PRO A 367       5.180  44.556  36.651  1.00 14.04           C  
ANISOU 2789  CD  PRO A 367     1649   1502   2184    635   -280    295       C  
ATOM   2790  N   THR A 368       7.576  43.116  33.942  1.00 18.91           N  
ANISOU 2790  N   THR A 368     2231   2270   2686    452   -322    372       N  
ATOM   2791  CA  THR A 368       8.251  42.708  32.708  1.00 16.65           C  
ANISOU 2791  CA  THR A 368     1923   2054   2350    399   -336    413       C  
ATOM   2792  C   THR A 368       9.768  42.674  32.864  1.00 19.49           C  
ANISOU 2792  C   THR A 368     2318   2384   2704    340   -331    403       C  
ATOM   2793  O   THR A 368      10.478  42.226  31.954  1.00 19.54           O  
ANISOU 2793  O   THR A 368     2306   2453   2665    295   -336    426       O  
ATOM   2794  CB  THR A 368       7.897  43.634  31.528  1.00 13.85           C  
ANISOU 2794  CB  THR A 368     1552   1713   1997    418   -364    507       C  
ATOM   2795  OG1 THR A 368       8.494  44.921  31.723  1.00 14.33           O  
ANISOU 2795  OG1 THR A 368     1666   1671   2108    422   -374    549       O  
ATOM   2796  CG2 THR A 368       6.383  43.774  31.395  1.00 14.28           C  
ANISOU 2796  CG2 THR A 368     1564   1800   2061    483   -371    527       C  
ATOM   2797  N   ASN A 369      10.277  43.179  33.987  1.00 12.72           N  
ANISOU 2797  N   ASN A 369     1509   1436   1887    339   -323    370       N  
ATOM   2798  CA  ASN A 369      11.722  43.189  34.170  1.00 12.51           C  
ANISOU 2798  CA  ASN A 369     1510   1389   1855    279   -321    365       C  
ATOM   2799  C   ASN A 369      12.181  42.737  35.560  1.00 17.71           C  
ANISOU 2799  C   ASN A 369     2195   2009   2524    268   -302    289       C  
ATOM   2800  O   ASN A 369      13.358  42.440  35.751  1.00 14.88           O  
ANISOU 2800  O   ASN A 369     1846   1658   2151    219   -298    277       O  
ATOM   2801  CB  ASN A 369      12.300  44.578  33.840  1.00 15.47           C  
ANISOU 2801  CB  ASN A 369     1923   1692   2263    262   -343    432       C  
ATOM   2802  CG  ASN A 369      11.692  45.702  34.669  1.00 15.58           C  
ANISOU 2802  CG  ASN A 369     1988   1593   2340    308   -347    427       C  
ATOM   2803  OD1 ASN A 369      11.564  45.608  35.892  1.00 15.90           O  
ANISOU 2803  OD1 ASN A 369     2056   1585   2402    325   -331    360       O  
ATOM   2804  ND2 ASN A 369      11.341  46.793  33.997  1.00 15.72           N  
ANISOU 2804  ND2 ASN A 369     2020   1566   2385    332   -368    500       N  
ATOM   2805  N   MET A 370      11.246  42.666  36.505  1.00 17.49           N  
ANISOU 2805  N   MET A 370     2175   1950   2519    314   -289    240       N  
ATOM   2806  CA  MET A 370      11.535  42.333  37.908  1.00 18.06           C  
ANISOU 2806  CA  MET A 370     2276   1985   2602    308   -271    170       C  
ATOM   2807  C   MET A 370      12.760  43.098  38.455  1.00 11.77           C  
ANISOU 2807  C   MET A 370     1528   1118   1825    263   -280    172       C  
ATOM   2808  O   MET A 370      13.560  42.555  39.217  1.00 15.65           O  
ANISOU 2808  O   MET A 370     2029   1616   2303    228   -271    131       O  
ATOM   2809  CB  MET A 370      11.719  40.819  38.078  1.00 14.74           C  
ANISOU 2809  CB  MET A 370     1823   1639   2138    287   -253    125       C  
ATOM   2810  CG  MET A 370      10.472  39.991  37.687  1.00 17.35           C  
ANISOU 2810  CG  MET A 370     2110   2036   2447    320   -245    115       C  
ATOM   2811  SD  MET A 370       8.990  40.373  38.659  1.00 14.95           S  
ANISOU 2811  SD  MET A 370     1805   1699   2175    385   -232     83       S  
ATOM   2812  CE  MET A 370       9.388  39.448  40.145  1.00 10.46           C  
ANISOU 2812  CE  MET A 370     1255   1121   1596    365   -208      6       C  
ATOM   2813  N   GLY A 371      12.897  44.354  38.043  1.00 14.47           N  
ANISOU 2813  N   GLY A 371     1902   1396   2199    261   -299    223       N  
ATOM   2814  CA  GLY A 371      13.948  45.213  38.542  1.00 12.76           C  
ANISOU 2814  CA  GLY A 371     1738   1106   2005    212   -312    228       C  
ATOM   2815  C   GLY A 371      15.221  45.220  37.726  1.00 21.16           C  
ANISOU 2815  C   GLY A 371     2787   2209   3044    142   -328    281       C  
ATOM   2816  O   GLY A 371      16.090  46.060  37.956  1.00 18.98           O  
ANISOU 2816  O   GLY A 371     2552   1875   2787     92   -344    301       O  
ATOM   2817  N   PHE A 372      15.355  44.277  36.794  1.00 19.51           N  
ANISOU 2817  N   PHE A 372     2522   2100   2791    135   -322    302       N  
ATOM   2818  CA  PHE A 372      16.597  44.144  36.030  1.00 22.32           C  
ANISOU 2818  CA  PHE A 372     2855   2512   3115     73   -330    347       C  
ATOM   2819  C   PHE A 372      16.620  45.016  34.778  1.00 18.24           C  
ANISOU 2819  C   PHE A 372     2334   1996   2600     59   -351    435       C  
ATOM   2820  O   PHE A 372      15.770  44.870  33.903  1.00 18.01           O  
ANISOU 2820  O   PHE A 372     2278   2008   2559     96   -352    463       O  
ATOM   2821  CB  PHE A 372      16.823  42.683  35.639  1.00 17.10           C  
ANISOU 2821  CB  PHE A 372     2139   1958   2400     73   -309    322       C  
ATOM   2822  CG  PHE A 372      16.925  41.757  36.813  1.00 15.73           C  
ANISOU 2822  CG  PHE A 372     1968   1788   2221     82   -290    246       C  
ATOM   2823  CD1 PHE A 372      17.979  41.858  37.700  1.00 17.71           C  
ANISOU 2823  CD1 PHE A 372     2236   2017   2477     40   -292    227       C  
ATOM   2824  CD2 PHE A 372      15.956  40.783  37.032  1.00 19.78           C  
ANISOU 2824  CD2 PHE A 372     2463   2329   2721    126   -272    199       C  
ATOM   2825  CE1 PHE A 372      18.071  41.007  38.800  1.00 16.66           C  
ANISOU 2825  CE1 PHE A 372     2104   1889   2335     49   -276    164       C  
ATOM   2826  CE2 PHE A 372      16.043  39.918  38.124  1.00 17.89           C  
ANISOU 2826  CE2 PHE A 372     2228   2092   2477    132   -255    136       C  
ATOM   2827  CZ  PHE A 372      17.099  40.027  39.006  1.00 14.21           C  
ANISOU 2827  CZ  PHE A 372     1780   1604   2015     96   -257    120       C  
ATOM   2828  N   LYS A 373      17.622  45.887  34.671  1.00 15.00           N  
ANISOU 2828  N   LYS A 373     1948   1549   2202     -1   -369    482       N  
ATOM   2829  CA  LYS A 373      17.728  46.783  33.522  1.00 15.47           C  
ANISOU 2829  CA  LYS A 373     2009   1605   2264    -23   -390    574       C  
ATOM   2830  C   LYS A 373      18.932  46.430  32.632  1.00 14.31           C  
ANISOU 2830  C   LYS A 373     1817   1556   2066    -88   -390    623       C  
ATOM   2831  O   LYS A 373      19.558  47.314  32.050  1.00 15.43           O  
ANISOU 2831  O   LYS A 373     1969   1682   2213   -140   -410    697       O  
ATOM   2832  CB  LYS A 373      17.837  48.247  33.996  1.00 15.06           C  
ANISOU 2832  CB  LYS A 373     2030   1422   2271    -45   -414    603       C  
ATOM   2833  CG  LYS A 373      16.763  48.652  35.008  1.00 17.59           C  
ANISOU 2833  CG  LYS A 373     2401   1640   2642     21   -409    546       C  
ATOM   2834  CD  LYS A 373      15.341  48.495  34.451  1.00 16.36           C  
ANISOU 2834  CD  LYS A 373     2221   1506   2491    107   -403    558       C  
ATOM   2835  CE  LYS A 373      15.111  49.301  33.150  1.00 19.07           C  
ANISOU 2835  CE  LYS A 373     2559   1848   2839    110   -426    662       C  
ATOM   2836  NZ  LYS A 373      13.699  49.173  32.647  1.00 15.95           N  
ANISOU 2836  NZ  LYS A 373     2134   1480   2446    195   -424    677       N  
ATOM   2837  N   GLY A 374      19.255  45.141  32.543  1.00 20.14           N  
ANISOU 2837  N   GLY A 374     2505   2393   2756    -83   -366    581       N  
ATOM   2838  CA  GLY A 374      20.482  44.679  31.902  1.00 18.21           C  
ANISOU 2838  CA  GLY A 374     2215   2246   2460   -134   -357    611       C  
ATOM   2839  C   GLY A 374      21.237  43.789  32.879  1.00 21.06           C  
ANISOU 2839  C   GLY A 374     2561   2631   2808   -144   -338    544       C  
ATOM   2840  O   GLY A 374      20.786  43.619  34.022  1.00 16.46           O  
ANISOU 2840  O   GLY A 374     2010   1987   2256   -117   -335    480       O  
ATOM   2841  N   LEU A 375      22.412  43.285  32.492  1.00 13.19           N  
ANISOU 2841  N   LEU A 375     1519   1724   1768   -182   -326    563       N  
ATOM   2842  CA  LEU A 375      23.160  43.789  31.345  1.00 16.06           C  
ANISOU 2842  CA  LEU A 375     1852   2149   2100   -231   -333    647       C  
ATOM   2843  C   LEU A 375      23.871  42.700  30.533  1.00 19.07           C  
ANISOU 2843  C   LEU A 375     2168   2665   2413   -226   -304    648       C  
ATOM   2844  O   LEU A 375      23.975  42.804  29.314  1.00 24.04           O  
ANISOU 2844  O   LEU A 375     2768   3365   3002   -238   -301    703       O  
ATOM   2845  CB  LEU A 375      24.204  44.811  31.822  1.00 15.58           C  
ANISOU 2845  CB  LEU A 375     1809   2047   2064   -311   -357    691       C  
ATOM   2846  CG  LEU A 375      23.765  46.240  32.160  1.00 19.77           C  
ANISOU 2846  CG  LEU A 375     2409   2448   2655   -338   -390    724       C  
ATOM   2847  CD1 LEU A 375      24.858  46.947  32.955  1.00 15.37           C  
ANISOU 2847  CD1 LEU A 375     1874   1850   2118   -420   -411    737       C  
ATOM   2848  CD2 LEU A 375      23.394  47.026  30.879  1.00 20.94           C  
ANISOU 2848  CD2 LEU A 375     2559   2599   2799   -347   -406    813       C  
ATOM   2849  N   ALA A 376      24.387  41.671  31.193  1.00 16.36           N  
ANISOU 2849  N   ALA A 376     1803   2359   2054   -208   -280    588       N  
ATOM   2850  CA  ALA A 376      25.276  40.757  30.481  1.00 16.13           C  
ANISOU 2850  CA  ALA A 376     1714   2453   1963   -204   -250    593       C  
ATOM   2851  C   ALA A 376      25.484  39.378  31.110  1.00 14.73           C  
ANISOU 2851  C   ALA A 376     1520   2307   1768   -155   -220    516       C  
ATOM   2852  O   ALA A 376      25.252  39.165  32.307  1.00 16.70           O  
ANISOU 2852  O   ALA A 376     1799   2492   2055   -140   -225    465       O  
ATOM   2853  CB  ALA A 376      26.649  41.436  30.302  1.00 13.89           C  
ANISOU 2853  CB  ALA A 376     1395   2218   1665   -277   -258    663       C  
ATOM   2854  N   GLU A 377      25.915  38.449  30.264  1.00 15.23           N  
ANISOU 2854  N   GLU A 377     1540   2472   1774   -129   -188    511       N  
ATOM   2855  CA  GLU A 377      26.618  37.250  30.693  1.00 12.53           C  
ANISOU 2855  CA  GLU A 377     1170   2180   1409    -93   -156    462       C  
ATOM   2856  C   GLU A 377      28.091  37.443  30.305  1.00 13.12           C  
ANISOU 2856  C   GLU A 377     1184   2351   1448   -130   -145    519       C  
ATOM   2857  O   GLU A 377      28.425  37.591  29.112  1.00 13.61           O  
ANISOU 2857  O   GLU A 377     1212   2496   1463   -143   -133    565       O  
ATOM   2858  CB  GLU A 377      26.050  35.989  30.047  1.00 12.29           C  
ANISOU 2858  CB  GLU A 377     1140   2190   1338    -30   -124    407       C  
ATOM   2859  CG  GLU A 377      24.563  35.702  30.337  1.00 11.78           C  
ANISOU 2859  CG  GLU A 377     1127   2047   1301      2   -134    354       C  
ATOM   2860  CD  GLU A 377      24.284  35.411  31.811  1.00 14.79           C  
ANISOU 2860  CD  GLU A 377     1540   2347   1731     18   -141    303       C  
ATOM   2861  OE1 GLU A 377      25.244  35.269  32.608  1.00 12.94           O  
ANISOU 2861  OE1 GLU A 377     1290   2119   1506     11   -137    302       O  
ATOM   2862  OE2 GLU A 377      23.085  35.322  32.173  1.00 10.96           O  
ANISOU 2862  OE2 GLU A 377     1094   1799   1273     38   -151    267       O  
ATOM   2863  N   LEU A 378      28.962  37.489  31.309  1.00 20.35           N  
ANISOU 2863  N   LEU A 378     2084   3264   2384   -151   -151    520       N  
ATOM   2864  CA  LEU A 378      30.373  37.800  31.086  1.00 14.89           C  
ANISOU 2864  CA  LEU A 378     1329   2665   1664   -196   -146    581       C  
ATOM   2865  C   LEU A 378      31.260  36.573  31.240  1.00 17.47           C  
ANISOU 2865  C   LEU A 378     1603   3079   1956   -142   -108    552       C  
ATOM   2866  O   LEU A 378      30.849  35.570  31.835  1.00 13.28           O  
ANISOU 2866  O   LEU A 378     1097   2515   1436    -79    -92    484       O  
ATOM   2867  CB  LEU A 378      30.827  38.903  32.036  1.00 13.99           C  
ANISOU 2867  CB  LEU A 378     1226   2495   1593   -274   -187    616       C  
ATOM   2868  CG  LEU A 378      30.074  40.221  31.888  1.00 17.44           C  
ANISOU 2868  CG  LEU A 378     1719   2838   2068   -328   -225    652       C  
ATOM   2869  CD1 LEU A 378      30.611  41.221  32.882  1.00 16.77           C  
ANISOU 2869  CD1 LEU A 378     1653   2695   2022   -406   -263    676       C  
ATOM   2870  CD2 LEU A 378      30.212  40.752  30.466  1.00 16.29           C  
ANISOU 2870  CD2 LEU A 378     1547   2757   1886   -358   -222    724       C  
ATOM   2871  N   GLY A 379      32.465  36.653  30.679  1.00 18.90           N  
ANISOU 2871  N   GLY A 379     1712   3375   2094   -165    -91    607       N  
ATOM   2872  CA  GLY A 379      33.440  35.586  30.789  1.00 15.97           C  
ANISOU 2872  CA  GLY A 379     1282   3098   1689   -110    -52    591       C  
ATOM   2873  C   GLY A 379      34.426  35.785  31.928  1.00 16.49           C  
ANISOU 2873  C   GLY A 379     1310   3180   1775   -144    -71    614       C  
ATOM   2874  O   GLY A 379      34.245  36.637  32.806  1.00 14.70           O  
ANISOU 2874  O   GLY A 379     1117   2875   1593   -208   -115    625       O  
ATOM   2875  N   PHE A 380      35.473  34.975  31.920  1.00 17.35           N  
ANISOU 2875  N   PHE A 380     1349   3394   1849    -99    -38    621       N  
ATOM   2876  CA  PHE A 380      36.552  35.105  32.882  1.00 15.56           C  
ANISOU 2876  CA  PHE A 380     1068   3213   1630   -130    -54    653       C  
ATOM   2877  C   PHE A 380      37.302  36.418  32.708  1.00 16.23           C  
ANISOU 2877  C   PHE A 380     1111   3347   1710   -245    -87    739       C  
ATOM   2878  O   PHE A 380      37.586  36.847  31.575  1.00 16.76           O  
ANISOU 2878  O   PHE A 380     1142   3487   1739   -275    -74    791       O  
ATOM   2879  CB  PHE A 380      37.533  33.941  32.752  1.00 18.68           C  
ANISOU 2879  CB  PHE A 380     1388   3724   1985    -46     -6    650       C  
ATOM   2880  CG  PHE A 380      36.986  32.627  33.249  1.00 22.48           C  
ANISOU 2880  CG  PHE A 380     1914   4148   2481     59     20    570       C  
ATOM   2881  CD1 PHE A 380      37.004  32.320  34.606  1.00 23.75           C  
ANISOU 2881  CD1 PHE A 380     2092   4254   2679     69     -3    547       C  
ATOM   2882  CD2 PHE A 380      36.491  31.686  32.363  1.00 23.35           C  
ANISOU 2882  CD2 PHE A 380     2048   4262   2564    144     65    521       C  
ATOM   2883  CE1 PHE A 380      36.501  31.109  35.075  1.00 18.73           C  
ANISOU 2883  CE1 PHE A 380     1499   3562   2057    162     20    481       C  
ATOM   2884  CE2 PHE A 380      35.981  30.475  32.832  1.00 17.37           C  
ANISOU 2884  CE2 PHE A 380     1338   3441   1822    233     87    449       C  
ATOM   2885  CZ  PHE A 380      36.000  30.190  34.184  1.00 18.63           C  
ANISOU 2885  CZ  PHE A 380     1513   3543   2021    242     64    433       C  
ATOM   2886  N   HIS A 381      37.617  37.050  33.838  1.00 16.27           N  
ANISOU 2886  N   HIS A 381     1123   3312   1749   -315   -131    755       N  
ATOM   2887  CA  HIS A 381      38.566  38.157  33.880  1.00 17.06           C  
ANISOU 2887  CA  HIS A 381     1172   3468   1840   -430   -164    836       C  
ATOM   2888  C   HIS A 381      39.933  37.625  33.463  1.00 29.68           C  
ANISOU 2888  C   HIS A 381     2651   5242   3383   -410   -130    887       C  
ATOM   2889  O   HIS A 381      40.295  36.494  33.814  1.00 17.73           O  
ANISOU 2889  O   HIS A 381     1101   3781   1857   -319    -99    855       O  
ATOM   2890  CB  HIS A 381      38.604  38.751  35.289  1.00 16.96           C  
ANISOU 2890  CB  HIS A 381     1196   3376   1870   -499   -216    825       C  
ATOM   2891  CG  HIS A 381      39.346  40.043  35.406  1.00 17.75           C  
ANISOU 2891  CG  HIS A 381     1274   3498   1971   -635   -260    899       C  
ATOM   2892  ND1 HIS A 381      40.710  40.140  35.239  1.00 18.63           N  
ANISOU 2892  ND1 HIS A 381     1280   3757   2042   -686   -259    971       N  
ATOM   2893  CD2 HIS A 381      38.918  41.281  35.752  1.00 17.85           C  
ANISOU 2893  CD2 HIS A 381     1360   3400   2023   -734   -309    910       C  
ATOM   2894  CE1 HIS A 381      41.088  41.390  35.442  1.00 19.25           C  
ANISOU 2894  CE1 HIS A 381     1379   3806   2129   -813   -306   1021       C  
ATOM   2895  NE2 HIS A 381      40.019  42.103  35.758  1.00 19.55           N  
ANISOU 2895  NE2 HIS A 381     1519   3691   2220   -849   -338    987       N  
ATOM   2896  N   ARG A 382      40.687  38.410  32.692  1.00 26.21           N  
ANISOU 2896  N   ARG A 382     2152   4897   2912   -491   -135    970       N  
ATOM   2897  CA  ARG A 382      41.988  37.932  32.226  1.00 24.90           C  
ANISOU 2897  CA  ARG A 382     1916   4865   2681   -453   -101   1004       C  
ATOM   2898  C   ARG A 382      42.899  37.524  33.392  1.00 24.35           C  
ANISOU 2898  C   ARG A 382     1819   4822   2610   -440   -112    998       C  
ATOM   2899  O   ARG A 382      43.736  36.633  33.240  1.00 20.94           O  
ANISOU 2899  O   ARG A 382     1337   4483   2136   -359    -74    998       O  
ATOM   2900  CB  ARG A 382      42.689  38.983  31.345  1.00 23.26           C  
ANISOU 2900  CB  ARG A 382     1684   4720   2435   -546   -117   1087       C  
ATOM   2901  CG  ARG A 382      42.714  40.389  31.905  1.00 22.81           C  
ANISOU 2901  CG  ARG A 382     1665   4589   2414   -687   -182   1132       C  
ATOM   2902  CD  ARG A 382      43.498  41.332  30.958  1.00 27.25           C  
ANISOU 2902  CD  ARG A 382     2199   5222   2931   -769   -196   1216       C  
ATOM   2903  NE  ARG A 382      44.930  41.091  31.083  1.00 22.68           N  
ANISOU 2903  NE  ARG A 382     1551   4768   2300   -765   -191   1252       N  
ATOM   2904  CZ  ARG A 382      45.704  41.644  32.015  1.00 34.85           C  
ANISOU 2904  CZ  ARG A 382     3087   6309   3846   -844   -232   1278       C  
ATOM   2905  NH1 ARG A 382      45.191  42.493  32.899  1.00 28.89           N  
ANISOU 2905  NH1 ARG A 382     2399   5431   3146   -932   -283   1267       N  
ATOM   2906  NH2 ARG A 382      46.999  41.352  32.063  1.00 34.09           N  
ANISOU 2906  NH2 ARG A 382     2919   6337   3697   -833   -223   1314       N  
ATOM   2907  N   LEU A 383      42.740  38.152  34.555  1.00 19.53           N  
ANISOU 2907  N   LEU A 383     1244   4132   2043   -517   -164    993       N  
ATOM   2908  CA  LEU A 383      43.636  37.851  35.664  1.00 19.86           C  
ANISOU 2908  CA  LEU A 383     1260   4209   2077   -516   -178    995       C  
ATOM   2909  C   LEU A 383      43.097  36.796  36.639  1.00 21.40           C  
ANISOU 2909  C   LEU A 383     1477   4352   2304   -424   -169    925       C  
ATOM   2910  O   LEU A 383      43.634  36.637  37.741  1.00 19.70           O  
ANISOU 2910  O   LEU A 383     1252   4142   2091   -434   -189    923       O  
ATOM   2911  CB  LEU A 383      43.984  39.129  36.429  1.00 35.96           C  
ANISOU 2911  CB  LEU A 383     3324   6207   4133   -656   -241   1032       C  
ATOM   2912  CG  LEU A 383      44.807  40.146  35.630  1.00 34.01           C  
ANISOU 2912  CG  LEU A 383     3050   6024   3847   -751   -257   1111       C  
ATOM   2913  CD1 LEU A 383      45.128  41.367  36.472  1.00 30.08           C  
ANISOU 2913  CD1 LEU A 383     2590   5473   3367   -888   -321   1137       C  
ATOM   2914  CD2 LEU A 383      46.090  39.511  35.114  1.00 28.09           C  
ANISOU 2914  CD2 LEU A 383     2214   5428   3030   -696   -219   1153       C  
ATOM   2915  N   ASP A 384      42.054  36.069  36.238  1.00 20.43           N  
ANISOU 2915  N   ASP A 384     1382   4180   2201   -337   -139    870       N  
ATOM   2916  CA  ASP A 384      41.605  34.917  37.020  1.00 19.55           C  
ANISOU 2916  CA  ASP A 384     1290   4028   2112   -235   -123    807       C  
ATOM   2917  C   ASP A 384      42.466  33.693  36.686  1.00 20.05           C  
ANISOU 2917  C   ASP A 384     1305   4182   2132   -121    -68    806       C  
ATOM   2918  O   ASP A 384      42.458  33.201  35.551  1.00 18.31           O  
ANISOU 2918  O   ASP A 384     1070   4005   1880    -55    -21    800       O  
ATOM   2919  CB  ASP A 384      40.122  34.614  36.768  1.00 16.93           C  
ANISOU 2919  CB  ASP A 384     1041   3578   1814   -185   -114    738       C  
ATOM   2920  CG  ASP A 384      39.514  33.743  37.870  1.00 16.06           C  
ANISOU 2920  CG  ASP A 384      987   3380   1735   -115   -116    670       C  
ATOM   2921  OD1 ASP A 384      40.263  32.923  38.444  1.00 18.30           O  
ANISOU 2921  OD1 ASP A 384     1214   3733   2006    -58   -104    679       O  
ATOM   2922  OD2 ASP A 384      38.303  33.862  38.149  1.00 15.32           O  
ANISOU 2922  OD2 ASP A 384      989   3155   1677   -115   -130    614       O  
ATOM   2923  N   PRO A 385      43.216  33.196  37.674  1.00 19.27           N  
ANISOU 2923  N   PRO A 385     1184   4111   2028    -96    -74    811       N  
ATOM   2924  CA  PRO A 385      44.119  32.073  37.410  1.00 21.19           C  
ANISOU 2924  CA  PRO A 385     1382   4437   2232     11    -25    817       C  
ATOM   2925  C   PRO A 385      43.398  30.733  37.259  1.00 20.18           C  
ANISOU 2925  C   PRO A 385     1292   4256   2119    146     18    749       C  
ATOM   2926  O   PRO A 385      44.034  29.770  36.847  1.00 19.48           O  
ANISOU 2926  O   PRO A 385     1179   4222   2000    242     63    747       O  
ATOM   2927  CB  PRO A 385      45.024  32.060  38.647  1.00 20.46           C  
ANISOU 2927  CB  PRO A 385     1260   4378   2136    -16    -54    848       C  
ATOM   2928  CG  PRO A 385      44.188  32.641  39.723  1.00 18.79           C  
ANISOU 2928  CG  PRO A 385     1101   4067   1972    -88   -106    821       C  
ATOM   2929  CD  PRO A 385      43.316  33.672  39.068  1.00 18.36           C  
ANISOU 2929  CD  PRO A 385     1084   3955   1938   -168   -127    815       C  
ATOM   2930  N   ASN A 386      42.102  30.672  37.557  1.00 17.55           N  
ANISOU 2930  N   ASN A 386     1021   3816   1831    152      5    695       N  
ATOM   2931  CA  ASN A 386      41.404  29.388  37.570  1.00 23.23           C  
ANISOU 2931  CA  ASN A 386     1785   4475   2566    273     42    630       C  
ATOM   2932  C   ASN A 386      40.458  29.182  36.392  1.00 22.09           C  
ANISOU 2932  C   ASN A 386     1676   4300   2418    313     75    587       C  
ATOM   2933  O   ASN A 386      39.310  28.828  36.577  1.00 27.11           O  
ANISOU 2933  O   ASN A 386     2385   4831   3085    341     74    528       O  
ATOM   2934  CB  ASN A 386      40.626  29.239  38.886  1.00 16.36           C  
ANISOU 2934  CB  ASN A 386      962   3510   1744    268      4    596       C  
ATOM   2935  CG  ASN A 386      41.541  29.165  40.086  1.00 22.00           C  
ANISOU 2935  CG  ASN A 386     1646   4256   2455    249    -21    631       C  
ATOM   2936  OD1 ASN A 386      42.493  28.375  40.113  1.00 18.66           O  
ANISOU 2936  OD1 ASN A 386     1189   3893   2006    317      8    650       O  
ATOM   2937  ND2 ASN A 386      41.284  30.012  41.072  1.00 17.60           N  
ANISOU 2937  ND2 ASN A 386     1102   3662   1921    155    -78    639       N  
ATOM   2938  N   LYS A 387      40.946  29.392  35.176  1.00 24.66           N  
ANISOU 2938  N   LYS A 387     1967   4703   2698    310    105    612       N  
ATOM   2939  CA  LYS A 387      40.143  29.133  33.986  1.00 19.37           C  
ANISOU 2939  CA  LYS A 387     1329   4018   2013    350    142    571       C  
ATOM   2940  C   LYS A 387      40.266  27.656  33.612  1.00 23.81           C  
ANISOU 2940  C   LYS A 387     1918   4574   2554    482    197    516       C  
ATOM   2941  O   LYS A 387      41.312  27.040  33.865  1.00 22.44           O  
ANISOU 2941  O   LYS A 387     1714   4448   2362    534    213    534       O  
ATOM   2942  CB  LYS A 387      40.607  30.012  32.821  1.00 21.69           C  
ANISOU 2942  CB  LYS A 387     1579   4400   2261    286    147    623       C  
ATOM   2943  CG  LYS A 387      40.830  31.483  33.186  1.00 27.10           C  
ANISOU 2943  CG  LYS A 387     2238   5098   2963    148     91    691       C  
ATOM   2944  CD  LYS A 387      41.304  32.297  31.980  1.00 26.63           C  
ANISOU 2944  CD  LYS A 387     2140   5122   2855     86     98    748       C  
ATOM   2945  CE  LYS A 387      41.701  33.733  32.350  1.00 22.35           C  
ANISOU 2945  CE  LYS A 387     1578   4588   2326    -54     42    820       C  
ATOM   2946  NZ  LYS A 387      43.076  33.771  32.938  1.00 23.97           N  
ANISOU 2946  NZ  LYS A 387     1731   4868   2508    -73     30    866       N  
ATOM   2947  N   PRO A 388      39.208  27.075  33.009  1.00 19.65           N  
ANISOU 2947  N   PRO A 388     1452   3985   2029    535    225    449       N  
ATOM   2948  CA  PRO A 388      39.323  25.731  32.427  1.00 23.28           C  
ANISOU 2948  CA  PRO A 388     1949   4433   2463    649    278    393       C  
ATOM   2949  C   PRO A 388      40.468  25.637  31.413  1.00 25.92           C  
ANISOU 2949  C   PRO A 388     2231   4880   2738    673    310    425       C  
ATOM   2950  O   PRO A 388      40.859  26.644  30.822  1.00 21.43           O  
ANISOU 2950  O   PRO A 388     1609   4392   2139    598    298    480       O  
ATOM   2951  CB  PRO A 388      37.979  25.531  31.728  1.00 16.70           C  
ANISOU 2951  CB  PRO A 388     1184   3533   1628    662    295    327       C  
ATOM   2952  CG  PRO A 388      37.021  26.413  32.498  1.00 18.50           C  
ANISOU 2952  CG  PRO A 388     1462   3660   1906    566    234    329       C  
ATOM   2953  CD  PRO A 388      37.834  27.605  32.922  1.00 22.06           C  
ANISOU 2953  CD  PRO A 388     1837   4184   2362    477    197    413       C  
ATOM   2954  N   ALA A 389      40.966  24.427  31.195  1.00 21.99           N  
ANISOU 2954  N   ALA A 389     1752   4380   2225    775    349    391       N  
ATOM   2955  CA  ALA A 389      42.120  24.218  30.335  1.00 23.04           C  
ANISOU 2955  CA  ALA A 389     1831   4618   2303    811    380    418       C  
ATOM   2956  C   ALA A 389      41.863  24.703  28.914  1.00 28.68           C  
ANISOU 2956  C   ALA A 389     2539   5389   2967    781    398    413       C  
ATOM   2957  O   ALA A 389      42.775  25.193  28.250  1.00 21.04           O  
ANISOU 2957  O   ALA A 389     1506   4534   1955    756    404    465       O  
ATOM   2958  CB  ALA A 389      42.500  22.747  30.325  1.00 27.99           C  
ANISOU 2958  CB  ALA A 389     2494   5211   2929    933    421    370       C  
ATOM   2959  N   ASN A 390      40.626  24.573  28.443  1.00 19.63           N  
ANISOU 2959  N   ASN A 390     1462   4171   1826    779    406    351       N  
ATOM   2960  CA  ASN A 390      40.331  24.943  27.071  1.00 22.20           C  
ANISOU 2960  CA  ASN A 390     1787   4550   2098    754    425    343       C  
ATOM   2961  C   ASN A 390      39.590  26.275  26.973  1.00 24.25           C  
ANISOU 2961  C   ASN A 390     2035   4816   2364    642    388    383       C  
ATOM   2962  O   ASN A 390      38.915  26.546  25.980  1.00 24.96           O  
ANISOU 2962  O   ASN A 390     2146   4917   2419    616    398    365       O  
ATOM   2963  CB  ASN A 390      39.499  23.853  26.403  1.00 23.09           C  
ANISOU 2963  CB  ASN A 390     1986   4589   2197    825    461    246       C  
ATOM   2964  CG  ASN A 390      38.087  23.757  26.976  1.00 22.29           C  
ANISOU 2964  CG  ASN A 390     1962   4369   2139    808    443    194       C  
ATOM   2965  OD1 ASN A 390      37.809  24.237  28.079  1.00 24.33           O  
ANISOU 2965  OD1 ASN A 390     2212   4584   2448    769    408    221       O  
ATOM   2966  ND2 ASN A 390      37.188  23.132  26.221  1.00 18.74           N  
ANISOU 2966  ND2 ASN A 390     1587   3867   1668    835    465    118       N  
ATOM   2967  N   ALA A 391      39.723  27.111  27.995  1.00 18.80           N  
ANISOU 2967  N   ALA A 391     1309   4116   1716    572    345    440       N  
ATOM   2968  CA  ALA A 391      38.977  28.367  28.033  1.00 23.46           C  
ANISOU 2968  CA  ALA A 391     1895   4693   2325    465    308    478       C  
ATOM   2969  C   ALA A 391      39.358  29.322  26.898  1.00 25.41           C  
ANISOU 2969  C   ALA A 391     2097   5038   2521    393    305    541       C  
ATOM   2970  O   ALA A 391      38.599  30.236  26.578  1.00 18.40           O  
ANISOU 2970  O   ALA A 391     1218   4136   1638    314    283    566       O  
ATOM   2971  CB  ALA A 391      39.172  29.061  29.380  1.00 21.87           C  
ANISOU 2971  CB  ALA A 391     1668   4460   2182    400    258    525       C  
ATOM   2972  N   ASN A 392      40.529  29.122  26.299  1.00 23.51           N  
ANISOU 2972  N   ASN A 392     1806   4895   2232    420    325    569       N  
ATOM   2973  CA  ASN A 392      40.964  29.990  25.200  1.00 22.87           C  
ANISOU 2973  CA  ASN A 392     1680   4912   2099    354    321    631       C  
ATOM   2974  C   ASN A 392      40.409  29.574  23.833  1.00 22.86           C  
ANISOU 2974  C   ASN A 392     1711   4933   2043    392    357    584       C  
ATOM   2975  O   ASN A 392      40.558  30.298  22.846  1.00 31.45           O  
ANISOU 2975  O   ASN A 392     2770   6093   3086    336    351    632       O  
ATOM   2976  CB  ASN A 392      42.493  30.046  25.154  1.00 31.37           C  
ANISOU 2976  CB  ASN A 392     2680   6096   3144    359    323    688       C  
ATOM   2977  CG  ASN A 392      43.123  28.674  25.026  1.00 43.53           C  
ANISOU 2977  CG  ASN A 392     4220   7658   4661    485    370    635       C  
ATOM   2978  OD1 ASN A 392      42.603  27.683  25.542  1.00 48.05           O  
ANISOU 2978  OD1 ASN A 392     4849   8143   5265    563    389    563       O  
ATOM   2979  ND2 ASN A 392      44.259  28.610  24.344  1.00 49.84           N  
ANISOU 2979  ND2 ASN A 392     4958   8572   5408    506    389    671       N  
ATOM   2980  N   THR A 393      39.780  28.405  23.771  1.00 23.42           N  
ANISOU 2980  N   THR A 393     1845   4939   2116    483    390    491       N  
ATOM   2981  CA  THR A 393      39.269  27.873  22.512  1.00 23.58           C  
ANISOU 2981  CA  THR A 393     1905   4973   2081    521    423    435       C  
ATOM   2982  C   THR A 393      37.742  27.772  22.514  1.00 23.48           C  
ANISOU 2982  C   THR A 393     1973   4866   2085    510    417    376       C  
ATOM   2983  O   THR A 393      37.134  27.557  21.474  1.00 24.76           O  
ANISOU 2983  O   THR A 393     2171   5037   2199    515    434    337       O  
ATOM   2984  CB  THR A 393      39.872  26.494  22.199  1.00 30.87           C  
ANISOU 2984  CB  THR A 393     2844   5903   2981    637    471    368       C  
ATOM   2985  OG1 THR A 393      39.624  25.604  23.291  1.00 38.94           O  
ANISOU 2985  OG1 THR A 393     3915   6823   4058    701    475    315       O  
ATOM   2986  CG2 THR A 393      41.374  26.616  21.996  1.00 39.78           C  
ANISOU 2986  CG2 THR A 393     3888   7146   4080    650    481    428       C  
ATOM   2987  N   VAL A 394      37.130  27.910  23.687  1.00 21.97           N  
ANISOU 2987  N   VAL A 394     1806   4586   1956    493    393    370       N  
ATOM   2988  CA  VAL A 394      35.669  27.964  23.794  1.00 18.09           C  
ANISOU 2988  CA  VAL A 394     1391   3995   1486    469    374    325       C  
ATOM   2989  C   VAL A 394      35.324  28.962  24.897  1.00 19.63           C  
ANISOU 2989  C   VAL A 394     1598   4100   1760    386    307    373       C  
ATOM   2990  O   VAL A 394      36.072  29.094  25.862  1.00 21.74           O  
ANISOU 2990  O   VAL A 394     1823   4371   2064    384    296    407       O  
ATOM   2991  CB  VAL A 394      35.049  26.572  24.093  1.00 23.70           C  
ANISOU 2991  CB  VAL A 394     2183   4611   2211    559    399    218       C  
ATOM   2992  CG1 VAL A 394      35.371  26.119  25.526  1.00 17.42           C  
ANISOU 2992  CG1 VAL A 394     1392   3744   1485    598    387    210       C  
ATOM   2993  CG2 VAL A 394      33.523  26.580  23.838  1.00 20.09           C  
ANISOU 2993  CG2 VAL A 394     1819   4050   1765    523    367    166       C  
ATOM   2994  N   THR A 395      34.213  29.678  24.753  1.00 18.29           N  
ANISOU 2994  N   THR A 395     1483   3854   1612    319    263    377       N  
ATOM   2995  CA  THR A 395      33.931  30.780  25.670  1.00 19.85           C  
ANISOU 2995  CA  THR A 395     1691   3974   1878    237    203    427       C  
ATOM   2996  C   THR A 395      33.027  30.405  26.852  1.00 17.82           C  
ANISOU 2996  C   THR A 395     1507   3574   1691    253    174    369       C  
ATOM   2997  O   THR A 395      31.836  30.139  26.667  1.00 19.90           O  
ANISOU 2997  O   THR A 395     1838   3760   1963    260    164    318       O  
ATOM   2998  CB  THR A 395      33.281  31.952  24.939  1.00 16.26           C  
ANISOU 2998  CB  THR A 395     1249   3515   1415    154    167    480       C  
ATOM   2999  OG1 THR A 395      34.168  32.442  23.920  1.00 17.12           O  
ANISOU 2999  OG1 THR A 395     1285   3760   1460    124    189    549       O  
ATOM   3000  CG2 THR A 395      32.978  33.067  25.934  1.00 15.78           C  
ANISOU 3000  CG2 THR A 395     1209   3359   1428     78    108    523       C  
ATOM   3001  N   TYR A 396      33.600  30.409  28.056  1.00 19.57           N  
ANISOU 3001  N   TYR A 396     1709   3768   1958    254    160    382       N  
ATOM   3002  CA  TYR A 396      32.859  30.104  29.289  1.00 18.79           C  
ANISOU 3002  CA  TYR A 396     1672   3544   1923    265    133    335       C  
ATOM   3003  C   TYR A 396      32.181  31.331  29.879  1.00 15.92           C  
ANISOU 3003  C   TYR A 396     1340   3098   1611    180     75    367       C  
ATOM   3004  O   TYR A 396      32.746  32.432  29.872  1.00 14.34           O  
ANISOU 3004  O   TYR A 396     1100   2933   1415    110     51    437       O  
ATOM   3005  CB  TYR A 396      33.786  29.513  30.350  1.00 14.53           C  
ANISOU 3005  CB  TYR A 396     1099   3019   1405    307    143    335       C  
ATOM   3006  CG  TYR A 396      34.236  28.108  30.075  1.00 17.88           C  
ANISOU 3006  CG  TYR A 396     1515   3483   1796    412    198    287       C  
ATOM   3007  CD1 TYR A 396      35.366  27.854  29.309  1.00 15.76           C  
ANISOU 3007  CD1 TYR A 396     1172   3343   1472    451    242    316       C  
ATOM   3008  CD2 TYR A 396      33.526  27.030  30.573  1.00 14.51           C  
ANISOU 3008  CD2 TYR A 396     1156   2963   1393    473    208    214       C  
ATOM   3009  CE1 TYR A 396      35.783  26.560  29.066  1.00 16.77           C  
ANISOU 3009  CE1 TYR A 396     1298   3501   1572    558    296    268       C  
ATOM   3010  CE2 TYR A 396      33.922  25.742  30.327  1.00 14.94           C  
ANISOU 3010  CE2 TYR A 396     1215   3040   1422    571    258    169       C  
ATOM   3011  CZ  TYR A 396      35.050  25.503  29.586  1.00 15.84           C  
ANISOU 3011  CZ  TYR A 396     1258   3275   1483    618    303    193       C  
ATOM   3012  OH  TYR A 396      35.427  24.203  29.353  1.00 19.19           O  
ANISOU 3012  OH  TYR A 396     1694   3713   1885    725    356    143       O  
ATOM   3013  N   ARG A 397      30.967  31.130  30.383  1.00 13.29           N  
ANISOU 3013  N   ARG A 397     1079   2655   1317    187     56    315       N  
ATOM   3014  CA  ARG A 397      30.283  32.109  31.214  1.00 17.29           C  
ANISOU 3014  CA  ARG A 397     1622   3067   1879    127      7    329       C  
ATOM   3015  C   ARG A 397      30.796  32.037  32.646  1.00 18.15           C  
ANISOU 3015  C   ARG A 397     1726   3142   2028    125     -8    326       C  
ATOM   3016  O   ARG A 397      30.916  30.939  33.205  1.00 12.47           O  
ANISOU 3016  O   ARG A 397     1014   2413   1312    186     13    282       O  
ATOM   3017  CB  ARG A 397      28.773  31.878  31.193  1.00 15.32           C  
ANISOU 3017  CB  ARG A 397     1443   2727   1650    141     -4    275       C  
ATOM   3018  CG  ARG A 397      28.108  32.240  29.874  1.00 13.09           C  
ANISOU 3018  CG  ARG A 397     1169   2471   1333    125     -4    288       C  
ATOM   3019  CD  ARG A 397      26.600  32.109  30.018  1.00 11.95           C  
ANISOU 3019  CD  ARG A 397     1086   2239   1214    132    -22    242       C  
ATOM   3020  NE  ARG A 397      25.905  32.524  28.815  1.00 21.38           N  
ANISOU 3020  NE  ARG A 397     2285   3461   2377    113    -28    261       N  
ATOM   3021  CZ  ARG A 397      24.586  32.471  28.654  1.00 15.06           C  
ANISOU 3021  CZ  ARG A 397     1526   2611   1587    115    -44    232       C  
ATOM   3022  NH1 ARG A 397      23.810  32.000  29.623  1.00 11.35           N  
ANISOU 3022  NH1 ARG A 397     1096   2060   1158    135    -52    181       N  
ATOM   3023  NH2 ARG A 397      24.047  32.880  27.513  1.00 12.18           N  
ANISOU 3023  NH2 ARG A 397     1158   2285   1187     97    -52    259       N  
ATOM   3024  N   LYS A 398      31.100  33.206  33.219  1.00 12.70           N  
ANISOU 3024  N   LYS A 398     1026   2434   1366     52    -47    375       N  
ATOM   3025  CA  LYS A 398      31.642  33.313  34.576  1.00 12.62           C  
ANISOU 3025  CA  LYS A 398     1007   2400   1387     33    -68    378       C  
ATOM   3026  C   LYS A 398      30.825  34.233  35.489  1.00 12.22           C  
ANISOU 3026  C   LYS A 398     1015   2241   1388    -20   -112    369       C  
ATOM   3027  O   LYS A 398      30.694  33.969  36.705  1.00 12.83           O  
ANISOU 3027  O   LYS A 398     1116   2267   1493    -12   -124    337       O  
ATOM   3028  CB  LYS A 398      33.097  33.805  34.516  1.00 13.31           C  
ANISOU 3028  CB  LYS A 398     1017   2590   1452    -11    -71    447       C  
ATOM   3029  CG  LYS A 398      33.777  34.027  35.863  1.00 13.38           C  
ANISOU 3029  CG  LYS A 398     1007   2592   1484    -45    -99    461       C  
ATOM   3030  CD  LYS A 398      33.697  32.791  36.773  1.00 17.34           C  
ANISOU 3030  CD  LYS A 398     1521   3072   1995     32    -82    408       C  
ATOM   3031  CE  LYS A 398      34.410  33.022  38.115  1.00 13.17           C  
ANISOU 3031  CE  LYS A 398      970   2550   1482     -5   -113    427       C  
ATOM   3032  NZ  LYS A 398      34.260  31.826  38.995  1.00 14.21           N  
ANISOU 3032  NZ  LYS A 398     1119   2657   1624     70    -98    382       N  
ATOM   3033  N   TYR A 399      30.283  35.311  34.925  1.00 13.59           N  
ANISOU 3033  N   TYR A 399     1213   2379   1573    -71   -134    397       N  
ATOM   3034  CA  TYR A 399      29.448  36.228  35.714  1.00 12.03           C  
ANISOU 3034  CA  TYR A 399     1076   2072   1424   -112   -171    385       C  
ATOM   3035  C   TYR A 399      28.153  36.565  35.003  1.00 13.79           C  
ANISOU 3035  C   TYR A 399     1345   2237   1659   -100   -175    373       C  
ATOM   3036  O   TYR A 399      28.128  36.742  33.781  1.00 17.49           O  
ANISOU 3036  O   TYR A 399     1794   2753   2098   -103   -166    407       O  
ATOM   3037  CB  TYR A 399      30.162  37.547  36.027  1.00 12.54           C  
ANISOU 3037  CB  TYR A 399     1131   2131   1504   -201   -207    442       C  
ATOM   3038  CG  TYR A 399      31.551  37.454  36.630  1.00 16.03           C  
ANISOU 3038  CG  TYR A 399     1515   2646   1929   -234   -212    471       C  
ATOM   3039  CD1 TYR A 399      31.728  37.380  38.005  1.00 15.06           C  
ANISOU 3039  CD1 TYR A 399     1407   2487   1827   -246   -231    442       C  
ATOM   3040  CD2 TYR A 399      32.688  37.470  35.820  1.00 16.64           C  
ANISOU 3040  CD2 TYR A 399     1518   2839   1965   -256   -198    531       C  
ATOM   3041  CE1 TYR A 399      33.002  37.318  38.570  1.00 17.47           C  
ANISOU 3041  CE1 TYR A 399     1654   2869   2113   -280   -239    474       C  
ATOM   3042  CE2 TYR A 399      33.970  37.415  36.374  1.00 15.56           C  
ANISOU 3042  CE2 TYR A 399     1318   2781   1811   -287   -204    564       C  
ATOM   3043  CZ  TYR A 399      34.111  37.331  37.762  1.00 16.22           C  
ANISOU 3043  CZ  TYR A 399     1418   2826   1918   -300   -226    535       C  
ATOM   3044  OH  TYR A 399      35.359  37.262  38.337  1.00 16.95           O  
ANISOU 3044  OH  TYR A 399     1445   3005   1991   -332   -236    571       O  
ATOM   3045  N   GLN A 400      27.084  36.706  35.776  1.00 11.37           N  
ANISOU 3045  N   GLN A 400     1095   1835   1391    -88   -190    329       N  
ATOM   3046  CA  GLN A 400      25.869  37.297  35.254  1.00 11.28           C  
ANISOU 3046  CA  GLN A 400     1123   1764   1398    -85   -202    329       C  
ATOM   3047  C   GLN A 400      25.809  38.720  35.790  1.00 11.56           C  
ANISOU 3047  C   GLN A 400     1193   1725   1475   -143   -238    359       C  
ATOM   3048  O   GLN A 400      25.731  38.932  36.995  1.00 14.83           O  
ANISOU 3048  O   GLN A 400     1637   2078   1919   -154   -252    327       O  
ATOM   3049  CB  GLN A 400      24.635  36.467  35.639  1.00 10.70           C  
ANISOU 3049  CB  GLN A 400     1086   1644   1337    -28   -190    262       C  
ATOM   3050  CG  GLN A 400      23.302  37.095  35.247  1.00 10.64           C  
ANISOU 3050  CG  GLN A 400     1114   1578   1352    -21   -204    262       C  
ATOM   3051  CD  GLN A 400      22.145  36.103  35.300  1.00 15.66           C  
ANISOU 3051  CD  GLN A 400     1767   2199   1984     32   -188    205       C  
ATOM   3052  OE1 GLN A 400      22.152  35.097  34.597  1.00 17.46           O  
ANISOU 3052  OE1 GLN A 400     1976   2482   2174     60   -165    187       O  
ATOM   3053  NE2 GLN A 400      21.152  36.379  36.137  1.00 12.73           N  
ANISOU 3053  NE2 GLN A 400     1433   1754   1650     44   -200    174       N  
ATOM   3054  N   LEU A 401      25.910  39.702  34.894  1.00 12.06           N  
ANISOU 3054  N   LEU A 401     1253   1792   1537   -184   -254    421       N  
ATOM   3055  CA  LEU A 401      25.969  41.100  35.310  1.00 14.20           C  
ANISOU 3055  CA  LEU A 401     1563   1985   1848   -244   -289    455       C  
ATOM   3056  C   LEU A 401      24.588  41.718  35.321  1.00 12.40           C  
ANISOU 3056  C   LEU A 401     1392   1661   1659   -217   -302    441       C  
ATOM   3057  O   LEU A 401      23.960  41.855  34.270  1.00 13.96           O  
ANISOU 3057  O   LEU A 401     1586   1872   1847   -197   -300    470       O  
ATOM   3058  CB  LEU A 401      26.880  41.917  34.376  1.00 13.21           C  
ANISOU 3058  CB  LEU A 401     1407   1910   1703   -311   -301    540       C  
ATOM   3059  CG  LEU A 401      27.003  43.402  34.707  1.00 13.81           C  
ANISOU 3059  CG  LEU A 401     1529   1898   1820   -383   -339    582       C  
ATOM   3060  CD1 LEU A 401      27.668  43.627  36.077  1.00 15.07           C  
ANISOU 3060  CD1 LEU A 401     1707   2021   1999   -428   -357    553       C  
ATOM   3061  CD2 LEU A 401      27.776  44.130  33.611  1.00 14.56           C  
ANISOU 3061  CD2 LEU A 401     1592   2048   1892   -448   -350    675       C  
ATOM   3062  N   MET A 402      24.140  42.137  36.498  1.00 12.29           N  
ANISOU 3062  N   MET A 402     1429   1555   1686   -217   -316    399       N  
ATOM   3063  CA  MET A 402      22.806  42.717  36.646  1.00 16.30           C  
ANISOU 3063  CA  MET A 402     1990   1971   2234   -180   -324    380       C  
ATOM   3064  C   MET A 402      22.851  44.153  37.155  1.00 14.79           C  
ANISOU 3064  C   MET A 402     1856   1676   2086   -226   -354    401       C  
ATOM   3065  O   MET A 402      23.642  44.498  38.035  1.00 16.81           O  
ANISOU 3065  O   MET A 402     2130   1908   2351   -278   -368    389       O  
ATOM   3066  CB  MET A 402      21.946  41.863  37.589  1.00 11.64           C  
ANISOU 3066  CB  MET A 402     1414   1358   1651   -121   -307    301       C  
ATOM   3067  CG  MET A 402      21.606  40.492  37.023  1.00 11.94           C  
ANISOU 3067  CG  MET A 402     1410   1475   1652    -71   -279    277       C  
ATOM   3068  SD  MET A 402      21.252  39.210  38.259  1.00 18.26           S  
ANISOU 3068  SD  MET A 402     2214   2275   2448    -29   -257    194       S  
ATOM   3069  CE  MET A 402      22.865  38.925  38.967  1.00 12.60           C  
ANISOU 3069  CE  MET A 402     1473   1602   1713    -74   -258    198       C  
ATOM   3070  N   MET A 403      21.988  44.981  36.585  1.00 15.60           N  
ANISOU 3070  N   MET A 403     1992   1719   2218   -206   -366    432       N  
ATOM   3071  CA  MET A 403      21.826  46.367  37.005  1.00 16.93           C  
ANISOU 3071  CA  MET A 403     2228   1769   2435   -235   -392    449       C  
ATOM   3072  C   MET A 403      20.429  46.584  37.544  1.00 19.72           C  
ANISOU 3072  C   MET A 403     2627   2039   2826   -161   -386    401       C  
ATOM   3073  O   MET A 403      19.458  46.237  36.884  1.00 19.60           O  
ANISOU 3073  O   MET A 403     2591   2049   2807   -100   -375    408       O  
ATOM   3074  CB  MET A 403      22.097  47.326  35.839  1.00 14.62           C  
ANISOU 3074  CB  MET A 403     1939   1469   2148   -276   -413    543       C  
ATOM   3075  CG  MET A 403      21.843  48.791  36.167  1.00 20.08           C  
ANISOU 3075  CG  MET A 403     2712   2023   2895   -300   -440    565       C  
ATOM   3076  SD  MET A 403      22.739  49.942  35.091  1.00 19.02           S  
ANISOU 3076  SD  MET A 403     2585   1880   2763   -391   -471    682       S  
ATOM   3077  CE  MET A 403      22.037  49.498  33.500  1.00 16.30           C  
ANISOU 3077  CE  MET A 403     2182   1626   2386   -334   -459    744       C  
ATOM   3078  N   THR A 404      20.320  47.130  38.752  1.00 18.91           N  
ANISOU 3078  N   THR A 404     2584   1846   2756   -167   -393    350       N  
ATOM   3079  CA  THR A 404      19.007  47.481  39.286  1.00 15.66           C  
ANISOU 3079  CA  THR A 404     2217   1351   2381    -94   -385    307       C  
ATOM   3080  C   THR A 404      19.026  48.847  39.913  1.00 14.87           C  
ANISOU 3080  C   THR A 404     2202   1120   2328   -118   -405    302       C  
ATOM   3081  O   THR A 404      20.084  49.366  40.251  1.00 15.28           O  
ANISOU 3081  O   THR A 404     2281   1145   2379   -200   -425    313       O  
ATOM   3082  CB  THR A 404      18.521  46.491  40.351  1.00 16.47           C  
ANISOU 3082  CB  THR A 404     2308   1480   2469    -50   -360    222       C  
ATOM   3083  OG1 THR A 404      19.258  46.700  41.567  1.00 17.09           O  
ANISOU 3083  OG1 THR A 404     2424   1522   2549    -99   -367    176       O  
ATOM   3084  CG2 THR A 404      18.694  45.058  39.858  1.00 15.56           C  
ANISOU 3084  CG2 THR A 404     2118   1487   2307    -38   -341    220       C  
ATOM   3085  N   ALA A 405      17.847  49.434  40.059  1.00 15.19           N  
ANISOU 3085  N   ALA A 405     2285   1080   2408    -46   -399    287       N  
ATOM   3086  CA  ALA A 405      17.695  50.618  40.870  1.00 15.99           C  
ANISOU 3086  CA  ALA A 405     2477   1045   2553    -50   -410    259       C  
ATOM   3087  C   ALA A 405      17.947  50.265  42.333  1.00 22.34           C  
ANISOU 3087  C   ALA A 405     3305   1838   3344    -66   -399    167       C  
ATOM   3088  O   ALA A 405      17.983  49.087  42.703  1.00 17.72           O  
ANISOU 3088  O   ALA A 405     2666   1347   2721    -54   -380    128       O  
ATOM   3089  CB  ALA A 405      16.308  51.199  40.698  1.00 22.85           C  
ANISOU 3089  CB  ALA A 405     3375   1841   3464     49   -400    261       C  
ATOM   3090  N   GLY A 406      18.120  51.288  43.159  1.00 22.89           N  
ANISOU 3090  N   GLY A 406     3462   1793   3442    -94   -412    132       N  
ATOM   3091  CA  GLY A 406      18.216  51.099  44.592  1.00 23.05           C  
ANISOU 3091  CA  GLY A 406     3516   1795   3448   -103   -402     41       C  
ATOM   3092  C   GLY A 406      19.563  50.644  45.112  1.00 25.64           C  
ANISOU 3092  C   GLY A 406     3822   2186   3735   -203   -418     30       C  
ATOM   3093  O   GLY A 406      20.579  50.700  44.417  1.00 25.11           O  
ANISOU 3093  O   GLY A 406     3725   2160   3655   -279   -441     94       O  
ATOM   3094  N   VAL A 407      19.552  50.176  46.355  1.00 23.21           N  
ANISOU 3094  N   VAL A 407     3524   1894   3402   -201   -406    -49       N  
ATOM   3095  CA  VAL A 407      20.758  49.876  47.104  1.00 22.48           C  
ANISOU 3095  CA  VAL A 407     3422   1849   3271   -293   -424    -69       C  
ATOM   3096  C   VAL A 407      20.635  48.452  47.620  1.00 26.37           C  
ANISOU 3096  C   VAL A 407     3845   2453   3721   -256   -399   -105       C  
ATOM   3097  O   VAL A 407      20.101  48.219  48.709  1.00 28.12           O  
ANISOU 3097  O   VAL A 407     4091   2663   3931   -222   -382   -177       O  
ATOM   3098  CB  VAL A 407      20.955  50.885  48.270  1.00 21.77           C  
ANISOU 3098  CB  VAL A 407     3430   1652   3189   -340   -440   -133       C  
ATOM   3099  CG1 VAL A 407      22.227  50.600  49.035  1.00 18.22           C  
ANISOU 3099  CG1 VAL A 407     2966   1263   2695   -443   -465   -148       C  
ATOM   3100  CG2 VAL A 407      20.960  52.330  47.734  1.00 17.82           C  
ANISOU 3100  CG2 VAL A 407     3011   1019   2739   -370   -463    -98       C  
ATOM   3101  N   GLY A 408      21.140  47.501  46.835  1.00 14.30           N  
ANISOU 3101  N   GLY A 408     2234   1033   2167   -263   -397    -53       N  
ATOM   3102  CA  GLY A 408      20.841  46.092  47.048  1.00 13.42           C  
ANISOU 3102  CA  GLY A 408     2058   1017   2024   -213   -370    -76       C  
ATOM   3103  C   GLY A 408      21.658  45.388  48.118  1.00 21.15           C  
ANISOU 3103  C   GLY A 408     3016   2058   2960   -256   -374   -111       C  
ATOM   3104  O   GLY A 408      21.606  44.176  48.218  1.00 25.97           O  
ANISOU 3104  O   GLY A 408     3572   2751   3545   -223   -355   -117       O  
ATOM   3105  N   ILE A 409      22.418  46.141  48.911  1.00 16.13           N  
ANISOU 3105  N   ILE A 409     2427   1385   2319   -331   -401   -130       N  
ATOM   3106  CA  ILE A 409      23.168  45.562  50.024  1.00 16.70           C  
ANISOU 3106  CA  ILE A 409     2481   1517   2347   -375   -409   -162       C  
ATOM   3107  C   ILE A 409      22.283  45.381  51.259  1.00 18.79           C  
ANISOU 3107  C   ILE A 409     2786   1752   2601   -328   -389   -244       C  
ATOM   3108  O   ILE A 409      21.280  46.084  51.418  1.00 14.79           O  
ANISOU 3108  O   ILE A 409     2338   1157   2122   -283   -375   -282       O  
ATOM   3109  CB  ILE A 409      24.394  46.428  50.413  1.00 14.55           C  
ANISOU 3109  CB  ILE A 409     2238   1228   2064   -488   -450   -150       C  
ATOM   3110  CG1 ILE A 409      24.025  47.911  50.432  1.00 15.42           C  
ANISOU 3110  CG1 ILE A 409     2444   1203   2213   -514   -466   -169       C  
ATOM   3111  CG2 ILE A 409      25.550  46.167  49.474  1.00 24.32           C  
ANISOU 3111  CG2 ILE A 409     3404   2549   3289   -542   -468    -69       C  
ATOM   3112  CD1 ILE A 409      25.122  48.813  50.960  1.00 16.33           C  
ANISOU 3112  CD1 ILE A 409     2602   1287   2315   -634   -508   -170       C  
ATOM   3113  N   PRO A 410      22.653  44.433  52.133  1.00 17.87           N  
ANISOU 3113  N   PRO A 410     2635   1715   2442   -336   -385   -266       N  
ATOM   3114  CA  PRO A 410      21.920  44.190  53.386  1.00 15.93           C  
ANISOU 3114  CA  PRO A 410     2420   1457   2174   -301   -366   -339       C  
ATOM   3115  C   PRO A 410      21.814  45.419  54.267  1.00 14.20           C  
ANISOU 3115  C   PRO A 410     2292   1146   1957   -339   -380   -399       C  
ATOM   3116  O   PRO A 410      22.654  46.310  54.190  1.00 17.67           O  
ANISOU 3116  O   PRO A 410     2765   1547   2402   -419   -413   -385       O  
ATOM   3117  CB  PRO A 410      22.751  43.109  54.067  1.00 15.11           C  
ANISOU 3117  CB  PRO A 410     2262   1458   2021   -331   -373   -331       C  
ATOM   3118  CG  PRO A 410      23.337  42.335  52.915  1.00 17.86           C  
ANISOU 3118  CG  PRO A 410     2534   1877   2374   -323   -373   -258       C  
ATOM   3119  CD  PRO A 410      23.667  43.391  51.878  1.00 14.88           C  
ANISOU 3119  CD  PRO A 410     2176   1447   2032   -360   -392   -217       C  
ATOM   3120  N   ALA A 411      20.772  45.472  55.084  1.00 18.86           N  
ANISOU 3120  N   ALA A 411     2922   1702   2543   -283   -352   -466       N  
ATOM   3121  CA  ALA A 411      20.524  46.632  55.937  1.00 19.01           C  
ANISOU 3121  CA  ALA A 411     3035   1626   2563   -303   -357   -536       C  
ATOM   3122  C   ALA A 411      21.703  46.989  56.839  1.00 19.37           C  
ANISOU 3122  C   ALA A 411     3110   1686   2566   -411   -395   -558       C  
ATOM   3123  O   ALA A 411      21.945  48.172  57.091  1.00 17.17           O  
ANISOU 3123  O   ALA A 411     2911   1315   2298   -464   -417   -589       O  
ATOM   3124  CB  ALA A 411      19.278  46.417  56.777  1.00 15.16           C  
ANISOU 3124  CB  ALA A 411     2570   1128   2063   -222   -316   -605       C  
ATOM   3125  N   GLU A 412      22.422  45.993  57.349  1.00 17.94           N  
ANISOU 3125  N   GLU A 412     2866   1615   2335   -445   -406   -541       N  
ATOM   3126  CA  GLU A 412      23.540  46.315  58.232  1.00 24.63           C  
ANISOU 3126  CA  GLU A 412     3733   2489   3136   -550   -446   -558       C  
ATOM   3127  C   GLU A 412      24.627  47.035  57.440  1.00 16.48           C  
ANISOU 3127  C   GLU A 412     2701   1437   2125   -639   -487   -501       C  
ATOM   3128  O   GLU A 412      25.301  47.928  57.958  1.00 21.07           O  
ANISOU 3128  O   GLU A 412     3337   1978   2689   -733   -523   -526       O  
ATOM   3129  CB  GLU A 412      24.111  45.062  58.919  1.00 24.97           C  
ANISOU 3129  CB  GLU A 412     3702   2663   3122   -562   -450   -541       C  
ATOM   3130  CG  GLU A 412      25.210  45.379  59.951  1.00 16.32           C  
ANISOU 3130  CG  GLU A 412     2623   1609   1970   -671   -493   -560       C  
ATOM   3131  CD  GLU A 412      25.764  44.140  60.660  1.00 22.88           C  
ANISOU 3131  CD  GLU A 412     3379   2572   2744   -676   -499   -536       C  
ATOM   3132  OE1 GLU A 412      25.216  43.040  60.453  1.00 18.39           O  
ANISOU 3132  OE1 GLU A 412     2758   2051   2180   -594   -466   -513       O  
ATOM   3133  OE2 GLU A 412      26.751  44.273  61.428  1.00 21.13           O  
ANISOU 3133  OE2 GLU A 412     3152   2406   2471   -765   -538   -537       O  
ATOM   3134  N   GLN A 413      24.794  46.631  56.186  1.00 15.92           N  
ANISOU 3134  N   GLN A 413     2566   1397   2086   -613   -482   -424       N  
ATOM   3135  CA  GLN A 413      25.795  47.247  55.320  1.00 16.32           C  
ANISOU 3135  CA  GLN A 413     2604   1441   2156   -694   -517   -359       C  
ATOM   3136  C   GLN A 413      25.365  48.641  54.866  1.00 20.29           C  
ANISOU 3136  C   GLN A 413     3199   1803   2709   -707   -525   -373       C  
ATOM   3137  O   GLN A 413      26.203  49.512  54.657  1.00 17.81           O  
ANISOU 3137  O   GLN A 413     2914   1453   2400   -805   -562   -347       O  
ATOM   3138  CB  GLN A 413      26.087  46.343  54.128  1.00 16.70           C  
ANISOU 3138  CB  GLN A 413     2556   1574   2216   -657   -506   -277       C  
ATOM   3139  CG  GLN A 413      26.832  45.072  54.544  1.00 17.99           C  
ANISOU 3139  CG  GLN A 413     2632   1874   2331   -660   -507   -252       C  
ATOM   3140  CD  GLN A 413      28.153  45.377  55.231  1.00 19.80           C  
ANISOU 3140  CD  GLN A 413     2849   2157   2517   -774   -553   -240       C  
ATOM   3141  OE1 GLN A 413      28.979  46.097  54.697  1.00 19.32           O  
ANISOU 3141  OE1 GLN A 413     2786   2090   2465   -855   -584   -196       O  
ATOM   3142  NE2 GLN A 413      28.338  44.852  56.447  1.00 18.97           N  
ANISOU 3142  NE2 GLN A 413     2736   2108   2362   -786   -559   -278       N  
ATOM   3143  N   GLN A 414      24.066  48.858  54.700  1.00 17.71           N  
ANISOU 3143  N   GLN A 414     3051   1454   2223   -360   -331    -15       N  
ATOM   3144  CA  GLN A 414      23.574  50.209  54.443  1.00 17.65           C  
ANISOU 3144  CA  GLN A 414     3150   1306   2250   -344   -304    -24       C  
ATOM   3145  C   GLN A 414      23.950  51.108  55.615  1.00 21.97           C  
ANISOU 3145  C   GLN A 414     3813   1776   2759   -440   -285    -87       C  
ATOM   3146  O   GLN A 414      24.401  52.241  55.434  1.00 24.50           O  
ANISOU 3146  O   GLN A 414     4226   2007   3077   -508   -284    -82       O  
ATOM   3147  CB  GLN A 414      22.059  50.202  54.216  1.00 18.53           C  
ANISOU 3147  CB  GLN A 414     3259   1361   2420   -204   -263    -37       C  
ATOM   3148  CG  GLN A 414      21.635  49.409  52.966  1.00 14.77           C  
ANISOU 3148  CG  GLN A 414     2677    959   1974   -121   -281     27       C  
ATOM   3149  CD  GLN A 414      20.127  49.248  52.851  1.00 24.11           C  
ANISOU 3149  CD  GLN A 414     3841   2116   3204      9   -245     17       C  
ATOM   3150  OE1 GLN A 414      19.387  49.603  53.758  1.00 25.50           O  
ANISOU 3150  OE1 GLN A 414     4071   2227   3391     48   -203    -40       O  
ATOM   3151  NE2 GLN A 414      19.673  48.692  51.740  1.00 27.09           N  
ANISOU 3151  NE2 GLN A 414     4137   2552   3603     72   -258     73       N  
ATOM   3152  N   TYR A 415      23.787  50.598  56.828  1.00 16.51           N  
ANISOU 3152  N   TYR A 415     3119   1121   2032   -457   -270   -147       N  
ATOM   3153  CA  TYR A 415      24.124  51.411  57.987  1.00 17.47           C  
ANISOU 3153  CA  TYR A 415     3352   1178   2107   -560   -249   -213       C  
ATOM   3154  C   TYR A 415      25.625  51.693  58.070  1.00 20.39           C  
ANISOU 3154  C   TYR A 415     3734   1600   2413   -719   -296   -185       C  
ATOM   3155  O   TYR A 415      26.046  52.851  58.196  1.00 23.02           O  
ANISOU 3155  O   TYR A 415     4180   1840   2728   -809   -287   -203       O  
ATOM   3156  CB  TYR A 415      23.678  50.759  59.288  1.00 20.89           C  
ANISOU 3156  CB  TYR A 415     3774   1656   2505   -557   -226   -280       C  
ATOM   3157  CG  TYR A 415      24.231  51.518  60.464  1.00 20.56           C  
ANISOU 3157  CG  TYR A 415     3841   1573   2398   -693   -212   -345       C  
ATOM   3158  CD1 TYR A 415      23.786  52.803  60.743  1.00 21.30           C  
ANISOU 3158  CD1 TYR A 415     4042   1542   2510   -684   -152   -393       C  
ATOM   3159  CD2 TYR A 415      25.241  50.983  61.259  1.00 22.00           C  
ANISOU 3159  CD2 TYR A 415     3986   1873   2501   -817   -252   -342       C  
ATOM   3160  CE1 TYR A 415      24.294  53.518  61.809  1.00 25.58           C  
ANISOU 3160  CE1 TYR A 415     4642   2086   2992   -788   -129   -441       C  
ATOM   3161  CE2 TYR A 415      25.754  51.693  62.324  1.00 19.30           C  
ANISOU 3161  CE2 TYR A 415     3705   1534   2095   -926   -233   -384       C  
ATOM   3162  CZ  TYR A 415      25.279  52.957  62.594  1.00 24.88           C  
ANISOU 3162  CZ  TYR A 415     4513   2122   2819   -911   -170   -436       C  
ATOM   3163  OH  TYR A 415      25.801  53.668  63.652  1.00 25.59           O  
ANISOU 3163  OH  TYR A 415     4660   2222   2843  -1019   -148   -475       O  
ATOM   3164  N   LEU A 416      26.424  50.632  58.020  1.00 18.15           N  
ANISOU 3164  N   LEU A 416     3336   1465   2096   -754   -344   -139       N  
ATOM   3165  CA  LEU A 416      27.875  50.767  58.115  1.00 19.71           C  
ANISOU 3165  CA  LEU A 416     3519   1740   2229   -900   -391   -101       C  
ATOM   3166  C   LEU A 416      28.454  51.666  57.014  1.00 20.28           C  
ANISOU 3166  C   LEU A 416     3629   1761   2316   -944   -409    -50       C  
ATOM   3167  O   LEU A 416      29.385  52.434  57.262  1.00 25.23           O  
ANISOU 3167  O   LEU A 416     4317   2379   2889  -1083   -428    -47       O  
ATOM   3168  CB  LEU A 416      28.529  49.379  58.086  1.00 16.62           C  
ANISOU 3168  CB  LEU A 416     2982   1517   1818   -896   -433    -48       C  
ATOM   3169  CG  LEU A 416      28.321  48.594  59.399  1.00 17.47           C  
ANISOU 3169  CG  LEU A 416     3062   1688   1886   -905   -428    -89       C  
ATOM   3170  CD1 LEU A 416      28.874  47.189  59.282  1.00 17.48           C  
ANISOU 3170  CD1 LEU A 416     2921   1839   1883   -879   -463    -28       C  
ATOM   3171  CD2 LEU A 416      28.961  49.322  60.593  1.00 18.95           C  
ANISOU 3171  CD2 LEU A 416     3334   1872   1994  -1061   -433   -131       C  
ATOM   3172  N   SER A 417      27.895  51.577  55.807  1.00 20.37           N  
ANISOU 3172  N   SER A 417     3604   1745   2393   -834   -404     -8       N  
ATOM   3173  CA  SER A 417      28.392  52.342  54.652  1.00 21.79           C  
ANISOU 3173  CA  SER A 417     3806   1886   2587   -869   -424     51       C  
ATOM   3174  C   SER A 417      27.831  53.770  54.556  1.00 27.31           C  
ANISOU 3174  C   SER A 417     4653   2406   3317   -869   -388     24       C  
ATOM   3175  O   SER A 417      28.386  54.619  53.844  1.00 27.43           O  
ANISOU 3175  O   SER A 417     4718   2374   3331   -935   -406     66       O  
ATOM   3176  CB  SER A 417      28.073  51.600  53.352  1.00 18.50           C  
ANISOU 3176  CB  SER A 417     3282   1527   2219   -761   -436    113       C  
ATOM   3177  OG  SER A 417      26.674  51.652  53.086  1.00 20.77           O  
ANISOU 3177  OG  SER A 417     3590   1731   2571   -625   -398     94       O  
ATOM   3178  N   GLY A 418      26.722  54.024  55.247  1.00 26.11           N  
ANISOU 3178  N   GLY A 418     4570   2154   3197   -792   -336    -44       N  
ATOM   3179  CA  GLY A 418      26.035  55.300  55.149  1.00 21.42           C  
ANISOU 3179  CA  GLY A 418     4081   1409   2647   -745   -284    -67       C  
ATOM   3180  C   GLY A 418      25.303  55.450  53.822  1.00 22.65           C  
ANISOU 3180  C   GLY A 418     4218   1507   2880   -630   -284     -2       C  
ATOM   3181  O   GLY A 418      24.923  56.557  53.430  1.00 27.20           O  
ANISOU 3181  O   GLY A 418     4855   1980   3498   -592   -251      8       O  
ATOM   3182  N   LEU A 419      25.083  54.332  53.135  1.00 20.21           N  
ANISOU 3182  N   LEU A 419     3789   1302   2588   -558   -313     44       N  
ATOM   3183  CA  LEU A 419      24.400  54.356  51.840  1.00 22.49           C  
ANISOU 3183  CA  LEU A 419     4032   1574   2938   -451   -316    112       C  
ATOM   3184  C   LEU A 419      22.928  53.982  51.997  1.00 24.98           C  
ANISOU 3184  C   LEU A 419     4322   1862   3308   -299   -274     86       C  
ATOM   3185  O   LEU A 419      22.588  52.821  52.217  1.00 25.69           O  
ANISOU 3185  O   LEU A 419     4315   2057   3388   -248   -277     71       O  
ATOM   3186  CB  LEU A 419      25.096  53.412  50.866  1.00 17.58           C  
ANISOU 3186  CB  LEU A 419     3282   1103   2295   -470   -367    179       C  
ATOM   3187  CG  LEU A 419      26.574  53.759  50.691  1.00 18.32           C  
ANISOU 3187  CG  LEU A 419     3388   1241   2333   -620   -409    209       C  
ATOM   3188  CD1 LEU A 419      27.300  52.680  49.899  1.00 18.83           C  
ANISOU 3188  CD1 LEU A 419     3315   1466   2372   -634   -449    264       C  
ATOM   3189  CD2 LEU A 419      26.700  55.119  50.014  1.00 20.33           C  
ANISOU 3189  CD2 LEU A 419     3744   1372   2607   -661   -410    250       C  
ATOM   3190  N   SER A 420      22.062  54.979  51.878  1.00 26.14           N  
ANISOU 3190  N   SER A 420     4554   1867   3511   -226   -233     86       N  
ATOM   3191  CA  SER A 420      20.651  54.810  52.195  1.00 27.42           C  
ANISOU 3191  CA  SER A 420     4704   1991   3723    -85   -184     57       C  
ATOM   3192  C   SER A 420      19.823  54.390  50.995  1.00 31.65           C  
ANISOU 3192  C   SER A 420     5142   2578   4307     29   -197    135       C  
ATOM   3193  O   SER A 420      20.019  54.895  49.886  1.00 25.75           O  
ANISOU 3193  O   SER A 420     4395   1808   3581     26   -223    214       O  
ATOM   3194  CB  SER A 420      20.082  56.106  52.770  1.00 30.93           C  
ANISOU 3194  CB  SER A 420     5230   2313   4208    -51   -115     13       C  
ATOM   3195  OG  SER A 420      18.686  55.987  52.968  1.00 34.26           O  
ANISOU 3195  OG  SER A 420     5614   2718   4684     89    -66     -3       O  
ATOM   3196  N   PRO A 421      18.883  53.463  51.217  1.00 35.20           N  
ANISOU 3196  N   PRO A 421     5507   3101   4766    124   -181    116       N  
ATOM   3197  CA  PRO A 421      17.967  53.042  50.149  1.00 33.76           C  
ANISOU 3197  CA  PRO A 421     5232   2974   4622    229   -190    187       C  
ATOM   3198  C   PRO A 421      17.067  54.181  49.678  1.00 35.22           C  
ANISOU 3198  C   PRO A 421     5466   3039   4878    323   -157    233       C  
ATOM   3199  O   PRO A 421      16.443  54.069  48.625  1.00 40.40           O  
ANISOU 3199  O   PRO A 421     6051   3738   5564    392   -173    312       O  
ATOM   3200  CB  PRO A 421      17.146  51.925  50.805  1.00 31.59           C  
ANISOU 3200  CB  PRO A 421     4880   2787   4336    295   -170    138       C  
ATOM   3201  CG  PRO A 421      17.258  52.183  52.296  1.00 37.01           C  
ANISOU 3201  CG  PRO A 421     5649   3411   5002    260   -130     40       C  
ATOM   3202  CD  PRO A 421      18.627  52.767  52.495  1.00 38.62           C  
ANISOU 3202  CD  PRO A 421     5931   3575   5169    126   -154     29       C  
ATOM   3203  N   SER A 422      17.014  55.269  50.440  1.00 31.52           N  
ANISOU 3203  N   SER A 422     5080   2462   4433    312   -105    183       N  
ATOM   3204  CA  SER A 422      16.169  56.403  50.093  1.00 38.57           C  
ANISOU 3204  CA  SER A 422     5983   3269   5404    394    -65    220       C  
ATOM   3205  C   SER A 422      16.947  57.491  49.364  1.00 43.90           C  
ANISOU 3205  C   SER A 422     6719   3868   6093    327    -83    277       C  
ATOM   3206  O   SER A 422      16.420  58.573  49.109  1.00 47.93           O  
ANISOU 3206  O   SER A 422     7254   4288   6670    379    -54    308       O  
ATOM   3207  CB  SER A 422      15.524  56.991  51.347  1.00 41.46           C  
ANISOU 3207  CB  SER A 422     6400   3557   5796    433      4    131       C  
ATOM   3208  OG  SER A 422      16.494  57.647  52.151  1.00 44.86           O  
ANISOU 3208  OG  SER A 422     6938   3916   6191    321     17     65       O  
ATOM   3209  N   SER A 423      18.201  57.205  49.028  1.00 48.10           N  
ANISOU 3209  N   SER A 423     7271   4441   6564    209   -135    292       N  
ATOM   3210  CA  SER A 423      19.019  58.155  48.275  1.00 45.76           C  
ANISOU 3210  CA  SER A 423     7024   4093   6270    131   -157    349       C  
ATOM   3211  C   SER A 423      18.838  57.924  46.780  1.00 42.74           C  
ANISOU 3211  C   SER A 423     6563   3776   5902    167   -200    462       C  
ATOM   3212  O   SER A 423      19.218  56.873  46.251  1.00 40.05           O  
ANISOU 3212  O   SER A 423     6154   3549   5515    136   -253    489       O  
ATOM   3213  CB  SER A 423      20.498  58.030  48.652  1.00 45.50           C  
ANISOU 3213  CB  SER A 423     7042   4087   6158    -27   -194    312       C  
ATOM   3214  OG  SER A 423      20.730  58.512  49.961  1.00 48.87           O  
ANISOU 3214  OG  SER A 423     7553   4449   6567    -77   -152    216       O  
ATOM   3215  N   ASN A 424      18.270  58.909  46.095  1.00 37.66           N  
ANISOU 3215  N   ASN A 424     5924   3062   5323    227   -180    531       N  
ATOM   3216  CA  ASN A 424      17.909  58.725  44.697  1.00 39.60           C  
ANISOU 3216  CA  ASN A 424     6088   3377   5581    271   -213    644       C  
ATOM   3217  C   ASN A 424      19.054  59.003  43.728  1.00 40.09           C  
ANISOU 3217  C   ASN A 424     6166   3468   5598    159   -263    704       C  
ATOM   3218  O   ASN A 424      18.822  59.260  42.547  1.00 44.20           O  
ANISOU 3218  O   ASN A 424     6645   4019   6129    184   -281    800       O  
ATOM   3219  CB  ASN A 424      16.698  59.592  44.350  1.00 47.61           C  
ANISOU 3219  CB  ASN A 424     7081   4318   6690    391   -173    706       C  
ATOM   3220  CG  ASN A 424      16.903  61.043  44.708  1.00 56.96           C  
ANISOU 3220  CG  ASN A 424     8366   5348   7930    370   -139    693       C  
ATOM   3221  OD1 ASN A 424      17.493  61.804  43.944  1.00 62.99           O  
ANISOU 3221  OD1 ASN A 424     9166   6072   8694    317   -153    758       O  
ATOM   3222  ND2 ASN A 424      16.423  61.437  45.882  1.00 61.45           N  
ANISOU 3222  ND2 ASN A 424     8983   5829   8534    409    -95    604       N  
ATOM   3223  N   ASN A 425      20.287  58.974  44.224  1.00 22.28           N  
ANISOU 3223  N   ASN A 425     3967   1212   3285     32   -286    650       N  
ATOM   3224  CA  ASN A 425      21.444  59.104  43.341  1.00 24.23           C  
ANISOU 3224  CA  ASN A 425     4212   1513   3482    -86   -340    702       C  
ATOM   3225  C   ASN A 425      22.318  57.848  43.384  1.00 23.18           C  
ANISOU 3225  C   ASN A 425     4021   1511   3277   -171   -393    678       C  
ATOM   3226  O   ASN A 425      23.488  57.874  43.006  1.00 30.05           O  
ANISOU 3226  O   ASN A 425     4891   2431   4095   -290   -432    696       O  
ATOM   3227  CB  ASN A 425      22.274  60.345  43.699  1.00 23.39           C  
ANISOU 3227  CB  ASN A 425     4215   1301   3372   -180   -324    681       C  
ATOM   3228  CG  ASN A 425      22.850  60.294  45.108  1.00 24.06           C  
ANISOU 3228  CG  ASN A 425     4368   1353   3421   -251   -305    572       C  
ATOM   3229  OD1 ASN A 425      22.472  59.454  45.926  1.00 22.57           O  
ANISOU 3229  OD1 ASN A 425     4155   1197   3225   -212   -293    510       O  
ATOM   3230  ND2 ASN A 425      23.766  61.204  45.398  1.00 24.23           N  
ANISOU 3230  ND2 ASN A 425     4474   1317   3416   -360   -303    551       N  
ATOM   3231  N   LEU A 426      21.741  56.750  43.860  1.00 21.46           N  
ANISOU 3231  N   LEU A 426     3747   1350   3058   -108   -390    640       N  
ATOM   3232  CA  LEU A 426      22.470  55.492  44.004  1.00 18.80           C  
ANISOU 3232  CA  LEU A 426     3343   1136   2662   -172   -428    614       C  
ATOM   3233  C   LEU A 426      21.809  54.398  43.188  1.00 24.09           C  
ANISOU 3233  C   LEU A 426     3883   1939   3331   -100   -439    648       C  
ATOM   3234  O   LEU A 426      20.588  54.393  43.043  1.00 18.04           O  
ANISOU 3234  O   LEU A 426     3096   1149   2609     12   -419    668       O  
ATOM   3235  CB  LEU A 426      22.523  55.060  45.472  1.00 19.80           C  
ANISOU 3235  CB  LEU A 426     3494   1255   2773   -176   -397    509       C  
ATOM   3236  CG  LEU A 426      23.146  56.001  46.489  1.00 21.95           C  
ANISOU 3236  CG  LEU A 426     3897   1410   3034   -260   -379    454       C  
ATOM   3237  CD1 LEU A 426      23.139  55.353  47.872  1.00 18.83           C  
ANISOU 3237  CD1 LEU A 426     3501   1043   2612   -265   -353    355       C  
ATOM   3238  CD2 LEU A 426      24.565  56.327  46.068  1.00 19.52           C  
ANISOU 3238  CD2 LEU A 426     3604   1141   2673   -406   -421    486       C  
ATOM   3239  N   PHE A 427      22.612  53.471  42.662  1.00 20.78           N  
ANISOU 3239  N   PHE A 427     3377   1660   2859   -165   -468    654       N  
ATOM   3240  CA  PHE A 427      22.072  52.275  42.028  1.00 17.70           C  
ANISOU 3240  CA  PHE A 427     2871   1398   2456   -111   -471    666       C  
ATOM   3241  C   PHE A 427      23.032  51.105  42.178  1.00 18.47           C  
ANISOU 3241  C   PHE A 427     2896   1621   2499   -175   -478    624       C  
ATOM   3242  O   PHE A 427      24.187  51.270  42.599  1.00 19.78           O  
ANISOU 3242  O   PHE A 427     3090   1791   2635   -266   -490    603       O  
ATOM   3243  CB  PHE A 427      21.734  52.522  40.539  1.00 21.42           C  
ANISOU 3243  CB  PHE A 427     3300   1908   2932   -101   -496    765       C  
ATOM   3244  CG  PHE A 427      22.933  52.656  39.640  1.00 20.75           C  
ANISOU 3244  CG  PHE A 427     3199   1883   2801   -214   -531    811       C  
ATOM   3245  CD1 PHE A 427      23.560  53.882  39.472  1.00 20.56           C  
ANISOU 3245  CD1 PHE A 427     3260   1768   2782   -282   -549    853       C  
ATOM   3246  CD2 PHE A 427      23.433  51.556  38.966  1.00 20.29           C  
ANISOU 3246  CD2 PHE A 427     3044   1972   2693   -252   -540    809       C  
ATOM   3247  CE1 PHE A 427      24.659  54.007  38.640  1.00 22.44           C  
ANISOU 3247  CE1 PHE A 427     3480   2072   2974   -391   -581    898       C  
ATOM   3248  CE2 PHE A 427      24.533  51.670  38.136  1.00 21.48           C  
ANISOU 3248  CE2 PHE A 427     3175   2186   2800   -353   -566    850       C  
ATOM   3249  CZ  PHE A 427      25.149  52.898  37.973  1.00 21.49           C  
ANISOU 3249  CZ  PHE A 427     3254   2107   2804   -424   -589    896       C  
ATOM   3250  N   THR A 428      22.540  49.921  41.824  1.00 14.62           N  
ANISOU 3250  N   THR A 428     2316   1238   1999   -127   -471    615       N  
ATOM   3251  CA  THR A 428      23.218  48.668  42.125  1.00 18.21           C  
ANISOU 3251  CA  THR A 428     2705   1799   2416   -158   -465    567       C  
ATOM   3252  C   THR A 428      23.717  47.960  40.872  1.00 13.47           C  
ANISOU 3252  C   THR A 428     2023   1317   1779   -197   -477    606       C  
ATOM   3253  O   THR A 428      23.008  47.892  39.880  1.00 16.01           O  
ANISOU 3253  O   THR A 428     2311   1671   2103   -166   -481    651       O  
ATOM   3254  CB  THR A 428      22.277  47.701  42.895  1.00 19.24           C  
ANISOU 3254  CB  THR A 428     2802   1950   2558    -75   -436    509       C  
ATOM   3255  OG1 THR A 428      21.912  48.283  44.147  1.00 16.87           O  
ANISOU 3255  OG1 THR A 428     2575   1550   2285    -47   -419    462       O  
ATOM   3256  CG2 THR A 428      22.941  46.365  43.148  1.00 12.39           C  
ANISOU 3256  CG2 THR A 428     1866   1184   1656   -100   -429    468       C  
ATOM   3257  N   LEU A 429      24.938  47.440  40.930  1.00 15.12           N  
ANISOU 3257  N   LEU A 429     2198   1595   1952   -266   -481    589       N  
ATOM   3258  CA  LEU A 429      25.433  46.513  39.920  1.00 17.67           C  
ANISOU 3258  CA  LEU A 429     2437   2037   2239   -293   -477    605       C  
ATOM   3259  C   LEU A 429      25.937  45.271  40.641  1.00 17.76           C  
ANISOU 3259  C   LEU A 429     2399   2112   2237   -284   -453    547       C  
ATOM   3260  O   LEU A 429      26.615  45.376  41.665  1.00 18.83           O  
ANISOU 3260  O   LEU A 429     2556   2226   2371   -311   -457    519       O  
ATOM   3261  CB  LEU A 429      26.549  47.135  39.070  1.00 15.64           C  
ANISOU 3261  CB  LEU A 429     2178   1812   1951   -387   -501    658       C  
ATOM   3262  CG  LEU A 429      26.181  48.220  38.062  1.00 15.82           C  
ANISOU 3262  CG  LEU A 429     2236   1795   1979   -407   -526    732       C  
ATOM   3263  CD1 LEU A 429      27.442  49.014  37.648  1.00 14.66           C  
ANISOU 3263  CD1 LEU A 429     2110   1658   1803   -516   -553    775       C  
ATOM   3264  CD2 LEU A 429      25.502  47.607  36.857  1.00 13.87           C  
ANISOU 3264  CD2 LEU A 429     1926   1629   1716   -381   -520    762       C  
ATOM   3265  N   ILE A 430      25.593  44.108  40.103  1.00 16.85           N  
ANISOU 3265  N   ILE A 430     2219   2074   2110   -250   -429    532       N  
ATOM   3266  CA  ILE A 430      25.972  42.820  40.666  1.00 13.48           C  
ANISOU 3266  CA  ILE A 430     1744   1703   1676   -231   -400    483       C  
ATOM   3267  C   ILE A 430      26.647  41.928  39.630  1.00 12.27           C  
ANISOU 3267  C   ILE A 430     1521   1650   1491   -258   -377    491       C  
ATOM   3268  O   ILE A 430      26.051  41.603  38.620  1.00 12.95           O  
ANISOU 3268  O   ILE A 430     1585   1774   1563   -249   -365    502       O  
ATOM   3269  CB  ILE A 430      24.725  42.091  41.217  1.00 16.21           C  
ANISOU 3269  CB  ILE A 430     2088   2029   2040   -151   -379    440       C  
ATOM   3270  CG1 ILE A 430      24.130  42.871  42.390  1.00 15.81           C  
ANISOU 3270  CG1 ILE A 430     2103   1884   2019   -121   -391    421       C  
ATOM   3271  CG2 ILE A 430      25.057  40.658  41.630  1.00 16.52           C  
ANISOU 3271  CG2 ILE A 430     2079   2126   2072   -131   -347    397       C  
ATOM   3272  CD1 ILE A 430      22.798  42.341  42.837  1.00 13.49           C  
ANISOU 3272  CD1 ILE A 430     1808   1574   1742    -45   -372    389       C  
ATOM   3273  N   ALA A 431      27.886  41.528  39.883  1.00 16.03           N  
ANISOU 3273  N   ALA A 431     1962   2175   1955   -292   -369    486       N  
ATOM   3274  CA  ALA A 431      28.528  40.487  39.086  1.00 17.00           C  
ANISOU 3274  CA  ALA A 431     2015   2388   2054   -300   -331    480       C  
ATOM   3275  C   ALA A 431      28.391  39.149  39.813  1.00 17.36           C  
ANISOU 3275  C   ALA A 431     2032   2447   2116   -240   -293    430       C  
ATOM   3276  O   ALA A 431      29.227  38.805  40.646  1.00 14.20           O  
ANISOU 3276  O   ALA A 431     1610   2061   1725   -239   -290    424       O  
ATOM   3277  CB  ALA A 431      30.004  40.810  38.841  1.00 17.63           C  
ANISOU 3277  CB  ALA A 431     2062   2524   2113   -368   -339    513       C  
ATOM   3278  N   ASP A 432      27.333  38.414  39.484  1.00 15.05           N  
ANISOU 3278  N   ASP A 432     1741   2153   1825   -195   -268    401       N  
ATOM   3279  CA  ASP A 432      27.005  37.134  40.106  1.00 15.32           C  
ANISOU 3279  CA  ASP A 432     1759   2189   1873   -139   -231    355       C  
ATOM   3280  C   ASP A 432      27.989  36.092  39.623  1.00 15.79           C  
ANISOU 3280  C   ASP A 432     1763   2313   1923   -142   -182    345       C  
ATOM   3281  O   ASP A 432      28.120  35.916  38.420  1.00 18.70           O  
ANISOU 3281  O   ASP A 432     2112   2730   2265   -169   -158    350       O  
ATOM   3282  CB  ASP A 432      25.572  36.745  39.731  1.00  9.54           C  
ANISOU 3282  CB  ASP A 432     1046   1445   1135   -107   -218    332       C  
ATOM   3283  CG  ASP A 432      25.024  35.570  40.533  1.00 16.37           C  
ANISOU 3283  CG  ASP A 432     1910   2295   2015    -54   -188    284       C  
ATOM   3284  OD1 ASP A 432      25.787  34.768  41.089  1.00 10.91           O  
ANISOU 3284  OD1 ASP A 432     1195   1615   1336    -37   -163    268       O  
ATOM   3285  OD2 ASP A 432      23.781  35.442  40.577  1.00 20.20           O  
ANISOU 3285  OD2 ASP A 432     2416   2763   2498    -29   -190    268       O  
ATOM   3286  N   ASP A 433      28.719  35.440  40.531  1.00 12.34           N  
ANISOU 3286  N   ASP A 433     1301   1881   1507   -115   -167    336       N  
ATOM   3287  CA  ASP A 433      29.631  34.363  40.113  1.00 12.52           C  
ANISOU 3287  CA  ASP A 433     1267   1959   1529   -100   -112    329       C  
ATOM   3288  C   ASP A 433      28.791  33.113  39.795  1.00 12.75           C  
ANISOU 3288  C   ASP A 433     1306   1977   1560    -56    -58    280       C  
ATOM   3289  O   ASP A 433      28.232  32.466  40.696  1.00  9.53           O  
ANISOU 3289  O   ASP A 433      917   1530   1175    -11    -52    255       O  
ATOM   3290  CB  ASP A 433      30.694  34.077  41.191  1.00 10.24           C  
ANISOU 3290  CB  ASP A 433      941   1685   1266    -82   -115    348       C  
ATOM   3291  CG  ASP A 433      31.768  33.108  40.720  1.00 14.54           C  
ANISOU 3291  CG  ASP A 433     1418   2289   1816    -61    -56    354       C  
ATOM   3292  OD1 ASP A 433      31.621  32.487  39.648  1.00 16.75           O  
ANISOU 3292  OD1 ASP A 433     1691   2589   2083    -54     -2    328       O  
ATOM   3293  OD2 ASP A 433      32.772  32.939  41.433  1.00 12.38           O  
ANISOU 3293  OD2 ASP A 433     1099   2047   1560    -50    -59    386       O  
ATOM   3294  N   ILE A 434      28.691  32.779  38.508  1.00 11.36           N  
ANISOU 3294  N   ILE A 434     1122   1839   1355    -79    -18    265       N  
ATOM   3295  CA  ILE A 434      27.870  31.650  38.095  1.00  9.95           C  
ANISOU 3295  CA  ILE A 434      961   1653   1167    -56     35    215       C  
ATOM   3296  C   ILE A 434      28.694  30.407  37.740  1.00 10.32           C  
ANISOU 3296  C   ILE A 434      976   1723   1221    -30    115    188       C  
ATOM   3297  O   ILE A 434      28.139  29.412  37.254  1.00 17.07           O  
ANISOU 3297  O   ILE A 434     1852   2571   2063    -21    171    141       O  
ATOM   3298  CB  ILE A 434      26.961  32.023  36.907  1.00 14.21           C  
ANISOU 3298  CB  ILE A 434     1522   2217   1659   -106     30    211       C  
ATOM   3299  CG1 ILE A 434      27.753  32.755  35.824  1.00 10.47           C  
ANISOU 3299  CG1 ILE A 434     1021   1802   1155   -165     25    244       C  
ATOM   3300  CG2 ILE A 434      25.800  32.886  37.397  1.00 16.84           C  
ANISOU 3300  CG2 ILE A 434     1892   2511   1996   -104    -33    228       C  
ATOM   3301  CD1 ILE A 434      26.924  33.056  34.585  1.00 22.42           C  
ANISOU 3301  CD1 ILE A 434     2550   3353   2617   -220     21    248       C  
ATOM   3302  N   ARG A 435      30.005  30.483  37.973  1.00 10.65           N  
ANISOU 3302  N   ARG A 435      969   1795   1284    -19    123    219       N  
ATOM   3303  CA  ARG A 435      30.872  29.303  38.109  1.00 11.04           C  
ANISOU 3303  CA  ARG A 435      980   1852   1363     35    194    206       C  
ATOM   3304  C   ARG A 435      31.489  29.319  39.497  1.00 13.15           C  
ANISOU 3304  C   ARG A 435     1219   2104   1674     78    161    245       C  
ATOM   3305  O   ARG A 435      32.721  29.226  39.642  1.00 14.46           O  
ANISOU 3305  O   ARG A 435     1323   2313   1858     95    177    282       O  
ATOM   3306  CB  ARG A 435      32.008  29.271  37.087  1.00 23.56           C  
ANISOU 3306  CB  ARG A 435     2513   3506   2932     15    243    217       C  
ATOM   3307  CG  ARG A 435      31.662  28.736  35.739  1.00 20.38           C  
ANISOU 3307  CG  ARG A 435     2130   3124   2490    -14    310    167       C  
ATOM   3308  CD  ARG A 435      32.895  28.666  34.801  1.00 12.76           C  
ANISOU 3308  CD  ARG A 435     1105   2233   1509    -30    366    175       C  
ATOM   3309  NE  ARG A 435      33.553  27.358  34.794  1.00 13.31           N  
ANISOU 3309  NE  ARG A 435     1150   2293   1613     40    465    145       N  
ATOM   3310  CZ  ARG A 435      33.078  26.268  34.188  1.00 19.87           C  
ANISOU 3310  CZ  ARG A 435     2023   3093   2435     54    550     77       C  
ATOM   3311  NH1 ARG A 435      31.910  26.297  33.552  1.00 19.44           N  
ANISOU 3311  NH1 ARG A 435     2032   3025   2331     -5    543     34       N  
ATOM   3312  NH2 ARG A 435      33.762  25.131  34.228  1.00 18.19           N  
ANISOU 3312  NH2 ARG A 435     1790   2861   2262    125    643     55       N  
ATOM   3313  N   PHE A 436      30.633  29.448  40.503  1.00 11.39           N  
ANISOU 3313  N   PHE A 436     1037   1828   1463     92    116    240       N  
ATOM   3314  CA  PHE A 436      31.056  29.590  41.912  1.00 14.86           C  
ANISOU 3314  CA  PHE A 436     1458   2255   1933    116     73    277       C  
ATOM   3315  C   PHE A 436      31.746  28.328  42.434  1.00 10.72           C  
ANISOU 3315  C   PHE A 436      894   1730   1450    185    127    286       C  
ATOM   3316  O   PHE A 436      31.132  27.276  42.516  1.00 10.63           O  
ANISOU 3316  O   PHE A 436      913   1672   1454    228    172    249       O  
ATOM   3317  CB  PHE A 436      29.827  29.942  42.750  1.00  9.79           C  
ANISOU 3317  CB  PHE A 436      874   1557   1288    113     24    258       C  
ATOM   3318  CG  PHE A 436      30.128  30.474  44.113  1.00 15.92           C  
ANISOU 3318  CG  PHE A 436     1645   2326   2078    111    -33    291       C  
ATOM   3319  CD1 PHE A 436      31.076  31.471  44.305  1.00 13.68           C  
ANISOU 3319  CD1 PHE A 436     1332   2082   1785     66    -76    337       C  
ATOM   3320  CD2 PHE A 436      29.421  29.998  45.212  1.00 11.90           C  
ANISOU 3320  CD2 PHE A 436     1165   1773   1584    142    -44    276       C  
ATOM   3321  CE1 PHE A 436      31.336  31.967  45.575  1.00 14.89           C  
ANISOU 3321  CE1 PHE A 436     1486   2232   1941     49   -127    364       C  
ATOM   3322  CE2 PHE A 436      29.670  30.493  46.482  1.00  9.94           C  
ANISOU 3322  CE2 PHE A 436      914   1523   1339    129    -96    303       C  
ATOM   3323  CZ  PHE A 436      30.631  31.472  46.667  1.00 12.73           C  
ANISOU 3323  CZ  PHE A 436     1240   1916   1680     81   -136    345       C  
ATOM   3324  N   ALA A 437      33.025  28.436  42.785  1.00 11.20           N  
ANISOU 3324  N   ALA A 437      886   1843   1527    195    122    341       N  
ATOM   3325  CA  ALA A 437      33.831  27.267  43.106  1.00 11.73           C  
ANISOU 3325  CA  ALA A 437      901   1919   1638    268    179    363       C  
ATOM   3326  C   ALA A 437      33.421  26.431  44.344  1.00 11.57           C  
ANISOU 3326  C   ALA A 437      898   1846   1652    322    175    370       C  
ATOM   3327  O   ALA A 437      33.618  25.209  44.323  1.00 11.95           O  
ANISOU 3327  O   ALA A 437      936   1867   1738    391    243    365       O  
ATOM   3328  CB  ALA A 437      35.302  27.680  43.252  1.00 12.36           C  
ANISOU 3328  CB  ALA A 437      890   2084   1723    261    166    434       C  
ATOM   3329  N   PRO A 438      32.917  27.063  45.434  1.00 12.22           N  
ANISOU 3329  N   PRO A 438     1006   1912   1723    292    100    382       N  
ATOM   3330  CA  PRO A 438      32.607  26.228  46.612  1.00 11.05           C  
ANISOU 3330  CA  PRO A 438      869   1725   1604    339     97    394       C  
ATOM   3331  C   PRO A 438      31.687  25.053  46.344  1.00 17.13           C  
ANISOU 3331  C   PRO A 438     1694   2424   2392    385    158    340       C  
ATOM   3332  O   PRO A 438      30.831  25.074  45.448  1.00 19.46           O  
ANISOU 3332  O   PRO A 438     2041   2691   2662    362    182    280       O  
ATOM   3333  CB  PRO A 438      31.918  27.215  47.576  1.00 10.52           C  
ANISOU 3333  CB  PRO A 438      841   1646   1508    285     15    391       C  
ATOM   3334  CG  PRO A 438      32.598  28.508  47.279  1.00 14.60           C  
ANISOU 3334  CG  PRO A 438     1332   2218   1996    220    -30    418       C  
ATOM   3335  CD  PRO A 438      32.746  28.495  45.750  1.00 14.42           C  
ANISOU 3335  CD  PRO A 438     1304   2209   1966    218     20    393       C  
ATOM   3336  N   GLU A 439      31.916  24.013  47.124  1.00 13.39           N  
ANISOU 3336  N   GLU A 439     1205   1925   1957    445    182    368       N  
ATOM   3337  CA  GLU A 439      31.145  22.786  47.090  1.00 13.16           C  
ANISOU 3337  CA  GLU A 439     1230   1823   1949    488    240    326       C  
ATOM   3338  C   GLU A 439      30.756  22.405  48.510  1.00 11.05           C  
ANISOU 3338  C   GLU A 439      976   1528   1695    504    200    355       C  
ATOM   3339  O   GLU A 439      31.567  22.512  49.427  1.00 15.64           O  
ANISOU 3339  O   GLU A 439     1500   2150   2294    518    163    425       O  
ATOM   3340  CB  GLU A 439      31.961  21.687  46.445  1.00 19.02           C  
ANISOU 3340  CB  GLU A 439     1942   2550   2734    558    333    335       C  
ATOM   3341  CG  GLU A 439      31.211  20.439  46.136  1.00 28.54           C  
ANISOU 3341  CG  GLU A 439     3217   3670   3955    592    407    280       C  
ATOM   3342  CD  GLU A 439      32.067  19.479  45.335  1.00 34.47           C  
ANISOU 3342  CD  GLU A 439     3946   4403   4748    659    511    279       C  
ATOM   3343  OE1 GLU A 439      32.693  19.935  44.353  1.00 35.35           O  
ANISOU 3343  OE1 GLU A 439     4021   4565   4846    645    538    269       O  
ATOM   3344  OE2 GLU A 439      32.134  18.287  45.703  1.00 39.97           O  
ANISOU 3344  OE2 GLU A 439     4664   5034   5491    722    566    287       O  
ATOM   3345  N   GLY A 440      29.517  21.984  48.708  1.00 13.25           N  
ANISOU 3345  N   GLY A 440     1326   1749   1959    493    203    304       N  
ATOM   3346  CA  GLY A 440      29.094  21.597  50.038  1.00 10.51           C  
ANISOU 3346  CA  GLY A 440      994   1380   1619    502    167    329       C  
ATOM   3347  C   GLY A 440      28.436  20.237  50.023  1.00 18.26           C  
ANISOU 3347  C   GLY A 440     2030   2286   2621    539    227    299       C  
ATOM   3348  O   GLY A 440      28.604  19.487  49.060  1.00 12.19           O  
ANISOU 3348  O   GLY A 440     1277   1482   1871    570    305    271       O  
ATOM   3349  N   TYR A 441      27.691  19.930  51.088  1.00 16.68           N  
ANISOU 3349  N   TYR A 441     1862   2062   2414    529    194    303       N  
ATOM   3350  CA  TYR A 441      26.975  18.665  51.201  1.00 14.04           C  
ANISOU 3350  CA  TYR A 441     1586   1655   2092    552    243    278       C  
ATOM   3351  C   TYR A 441      25.849  18.747  52.216  1.00 18.68           C  
ANISOU 3351  C   TYR A 441     2215   2236   2646    511    190    263       C  
ATOM   3352  O   TYR A 441      25.834  19.626  53.091  1.00 15.33           O  
ANISOU 3352  O   TYR A 441     1765   1860   2200    480    119    288       O  
ATOM   3353  CB  TYR A 441      27.913  17.515  51.569  1.00 12.15           C  
ANISOU 3353  CB  TYR A 441     1319   1380   1916    629    291    341       C  
ATOM   3354  CG  TYR A 441      28.671  17.678  52.874  1.00 19.60           C  
ANISOU 3354  CG  TYR A 441     2197   2369   2880    648    232    434       C  
ATOM   3355  CD1 TYR A 441      29.851  18.427  52.935  1.00 17.49           C  
ANISOU 3355  CD1 TYR A 441     1845   2178   2621    655    201    492       C  
ATOM   3356  CD2 TYR A 441      28.230  17.050  54.035  1.00 17.45           C  
ANISOU 3356  CD2 TYR A 441     1947   2072   2612    651    207    467       C  
ATOM   3357  CE1 TYR A 441      30.553  18.561  54.118  1.00 16.63           C  
ANISOU 3357  CE1 TYR A 441     1686   2123   2509    640    142    565       C  
ATOM   3358  CE2 TYR A 441      28.927  17.181  55.234  1.00 12.93           C  
ANISOU 3358  CE2 TYR A 441     1317   1553   2044    648    149    547       C  
ATOM   3359  CZ  TYR A 441      30.083  17.937  55.264  1.00 17.82           C  
ANISOU 3359  CZ  TYR A 441     1862   2251   2659    636    117    591       C  
ATOM   3360  OH  TYR A 441      30.767  18.059  56.448  1.00 25.76           O  
ANISOU 3360  OH  TYR A 441     2817   3316   3656    615     61    664       O  
ATOM   3361  N   ILE A 442      24.908  17.816  52.070  1.00 17.39           N  
ANISOU 3361  N   ILE A 442     2118   2014   2474    505    231    220       N  
ATOM   3362  CA  ILE A 442      23.680  17.762  52.862  1.00 14.51           C  
ANISOU 3362  CA  ILE A 442     1797   1644   2071    461    194    196       C  
ATOM   3363  C   ILE A 442      23.553  16.402  53.542  1.00 15.09           C  
ANISOU 3363  C   ILE A 442     1905   1656   2172    489    225    222       C  
ATOM   3364  O   ILE A 442      23.739  15.358  52.886  1.00 14.79           O  
ANISOU 3364  O   ILE A 442     1903   1554   2164    521    300    210       O  
ATOM   3365  CB  ILE A 442      22.436  17.987  51.983  1.00 17.34           C  
ANISOU 3365  CB  ILE A 442     2207   2001   2379    409    207    116       C  
ATOM   3366  CG1 ILE A 442      22.482  19.362  51.319  1.00 15.91           C  
ANISOU 3366  CG1 ILE A 442     1996   1876   2173    382    173     98       C  
ATOM   3367  CG2 ILE A 442      21.149  17.805  52.798  1.00  9.09           C  
ANISOU 3367  CG2 ILE A 442     1203    956   1295    367    177     94       C  
ATOM   3368  CD1 ILE A 442      22.149  19.353  49.828  1.00  9.94           C  
ANISOU 3368  CD1 ILE A 442     1264   1117   1394    360    220     44       C  
ATOM   3369  N   LYS A 443      23.249  16.409  54.841  1.00 11.36           N  
ANISOU 3369  N   LYS A 443     1427   1201   1687    473    172    257       N  
ATOM   3370  CA  LYS A 443      23.032  15.175  55.619  1.00 15.18           C  
ANISOU 3370  CA  LYS A 443     1946   1632   2191    489    191    290       C  
ATOM   3371  C   LYS A 443      21.859  15.319  56.578  1.00 12.75           C  
ANISOU 3371  C   LYS A 443     1667   1347   1829    429    140    271       C  
ATOM   3372  O   LYS A 443      21.843  16.254  57.371  1.00 18.46           O  
ANISOU 3372  O   LYS A 443     2354   2135   2527    403     75    286       O  
ATOM   3373  CB  LYS A 443      24.280  14.815  56.425  1.00 22.12           C  
ANISOU 3373  CB  LYS A 443     2766   2515   3123    547    179    390       C  
ATOM   3374  CG  LYS A 443      25.456  14.356  55.584  1.00 33.72           C  
ANISOU 3374  CG  LYS A 443     4205   3952   4655    622    244    420       C  
ATOM   3375  CD  LYS A 443      26.785  14.531  56.296  1.00 39.78           C  
ANISOU 3375  CD  LYS A 443     4882   4769   5463    670    211    524       C  
ATOM   3376  CE  LYS A 443      27.034  13.455  57.337  1.00 40.40           C  
ANISOU 3376  CE  LYS A 443     4962   4821   5565    688    206    590       C  
ATOM   3377  NZ  LYS A 443      28.394  13.580  57.968  1.00 35.45           N  
ANISOU 3377  NZ  LYS A 443     4249   4265   4957    703    172    671       N  
ATOM   3378  N   ILE A 444      20.892  14.393  56.534  1.00 13.99           N  
ANISOU 3378  N   ILE A 444     1892   1454   1968    404    173    236       N  
ATOM   3379  CA  ILE A 444      19.820  14.406  57.525  1.00 19.13           C  
ANISOU 3379  CA  ILE A 444     2566   2134   2570    349    129    226       C  
ATOM   3380  C   ILE A 444      20.458  14.324  58.905  1.00 10.33           C  
ANISOU 3380  C   ILE A 444     1411   1042   1472    364     81    309       C  
ATOM   3381  O   ILE A 444      21.464  13.633  59.087  1.00 12.43           O  
ANISOU 3381  O   ILE A 444     1657   1272   1794    419    102    378       O  
ATOM   3382  CB  ILE A 444      18.810  13.234  57.354  1.00 16.39           C  
ANISOU 3382  CB  ILE A 444     2298   1728   2203    315    174    191       C  
ATOM   3383  CG1 ILE A 444      19.536  11.882  57.347  1.00 11.14           C  
ANISOU 3383  CG1 ILE A 444     1665    969   1598    367    232    239       C  
ATOM   3384  CG2 ILE A 444      17.982  13.426  56.087  1.00 15.03           C  
ANISOU 3384  CG2 ILE A 444     2162   1557   1992    276    209    107       C  
ATOM   3385  CD1 ILE A 444      18.610  10.671  57.306  1.00 11.82           C  
ANISOU 3385  CD1 ILE A 444     1840    987   1665    326    276    211       C  
ATOM   3386  N   GLY A 445      19.899  15.054  59.863  1.00  9.96           N  
ANISOU 3386  N   GLY A 445     1347   1060   1376    316     20    304       N  
ATOM   3387  CA  GLY A 445      20.412  15.002  61.224  1.00 10.28           C  
ANISOU 3387  CA  GLY A 445     1352   1136   1418    312    -29    380       C  
ATOM   3388  C   GLY A 445      19.758  13.903  62.049  1.00 10.65           C  
ANISOU 3388  C   GLY A 445     1441   1154   1450    287    -27    404       C  
ATOM   3389  O   GLY A 445      20.348  13.418  63.012  1.00 11.18           O  
ANISOU 3389  O   GLY A 445     1485   1226   1535    298    -51    486       O  
ATOM   3390  N   THR A 446      18.527  13.543  61.675  1.00 10.85           N  
ANISOU 3390  N   THR A 446     1527   1157   1439    247     -1    337       N  
ATOM   3391  CA  THR A 446      17.717  12.553  62.378  1.00 10.73           C  
ANISOU 3391  CA  THR A 446     1561   1119   1399    207      2    347       C  
ATOM   3392  C   THR A 446      16.957  11.679  61.377  1.00 10.84           C  
ANISOU 3392  C   THR A 446     1648   1062   1409    194     66    292       C  
ATOM   3393  O   THR A 446      16.740  12.084  60.239  1.00 13.77           O  
ANISOU 3393  O   THR A 446     2027   1430   1775    196     95    230       O  
ATOM   3394  CB  THR A 446      16.679  13.221  63.314  1.00 12.35           C  
ANISOU 3394  CB  THR A 446     1758   1406   1528    137    -50    315       C  
ATOM   3395  OG1 THR A 446      15.953  14.206  62.572  1.00 13.81           O  
ANISOU 3395  OG1 THR A 446     1939   1629   1678    118    -48    233       O  
ATOM   3396  CG2 THR A 446      17.341  13.851  64.530  1.00 10.43           C  
ANISOU 3396  CG2 THR A 446     1459   1228   1276    130   -111    373       C  
ATOM   3397  N   PRO A 447      16.516  10.485  61.802  1.00 16.42           N  
ANISOU 3397  N   PRO A 447     2411   1716   2112    169     86    314       N  
ATOM   3398  CA  PRO A 447      15.920   9.550  60.842  1.00 11.65           C  
ANISOU 3398  CA  PRO A 447     1887   1035   1505    149    154    265       C  
ATOM   3399  C   PRO A 447      14.383   9.620  60.675  1.00 20.55           C  
ANISOU 3399  C   PRO A 447     3052   2207   2550     60    150    190       C  
ATOM   3400  O   PRO A 447      13.868   9.068  59.698  1.00 16.10           O  
ANISOU 3400  O   PRO A 447     2547   1599   1972     30    203    137       O  
ATOM   3401  CB  PRO A 447      16.315   8.195  61.427  1.00 12.55           C  
ANISOU 3401  CB  PRO A 447     2048   1060   1663    170    180    337       C  
ATOM   3402  CG  PRO A 447      16.253   8.418  62.895  1.00 18.17           C  
ANISOU 3402  CG  PRO A 447     2717   1837   2348    145    109    399       C  
ATOM   3403  CD  PRO A 447      16.747   9.841  63.110  1.00 15.38           C  
ANISOU 3403  CD  PRO A 447     2277   1581   1987    164     55    398       C  
ATOM   3404  N   ASN A 448      13.669  10.264  61.594  1.00 13.11           N  
ANISOU 3404  N   ASN A 448     2074   1354   1551     14     92    185       N  
ATOM   3405  CA  ASN A 448      12.211  10.066  61.689  1.00 14.36           C  
ANISOU 3405  CA  ASN A 448     2266   1558   1633    -71     90    135       C  
ATOM   3406  C   ASN A 448      11.366  10.652  60.566  1.00 16.67           C  
ANISOU 3406  C   ASN A 448     2557   1894   1883   -102    107     56       C  
ATOM   3407  O   ASN A 448      10.481   9.982  60.033  1.00 17.99           O  
ANISOU 3407  O   ASN A 448     2777   2050   2008   -163    140     17       O  
ATOM   3408  CB  ASN A 448      11.687  10.645  63.004  1.00 13.22           C  
ANISOU 3408  CB  ASN A 448     2079   1505   1439   -107     28    150       C  
ATOM   3409  CG  ASN A 448      12.367  10.048  64.197  1.00 16.02           C  
ANISOU 3409  CG  ASN A 448     2433   1835   1818    -96      3    233       C  
ATOM   3410  OD1 ASN A 448      13.597  10.114  64.305  1.00 18.13           O  
ANISOU 3410  OD1 ASN A 448     2673   2069   2148    -32     -2    290       O  
ATOM   3411  ND2 ASN A 448      11.583   9.477  65.119  1.00 13.19           N  
ANISOU 3411  ND2 ASN A 448     2099   1504   1410   -162    -15    249       N  
ATOM   3412  N   ILE A 449      11.610  11.923  60.255  1.00 16.88           N  
ANISOU 3412  N   ILE A 449     2523   1975   1915    -66     82     36       N  
ATOM   3413  CA  ILE A 449      10.720  12.717  59.423  1.00 12.50           C  
ANISOU 3413  CA  ILE A 449     1949   1487   1316    -93     83    -26       C  
ATOM   3414  C   ILE A 449      11.493  13.726  58.585  1.00 12.74           C  
ANISOU 3414  C   ILE A 449     1937   1518   1385    -35     82    -36       C  
ATOM   3415  O   ILE A 449      12.636  14.084  58.928  1.00 13.98           O  
ANISOU 3415  O   ILE A 449     2066   1653   1594     21     66      4       O  
ATOM   3416  CB  ILE A 449       9.707  13.501  60.289  1.00 13.43           C  
ANISOU 3416  CB  ILE A 449     2024   1705   1375   -127     37    -42       C  
ATOM   3417  CG1 ILE A 449      10.467  14.271  61.372  1.00 16.84           C  
ANISOU 3417  CG1 ILE A 449     2411   2157   1833    -85     -7     -6       C  
ATOM   3418  CG2 ILE A 449       8.682  12.566  60.938  1.00 17.08           C  
ANISOU 3418  CG2 ILE A 449     2523   2187   1781   -201     39    -43       C  
ATOM   3419  CD1 ILE A 449       9.698  15.467  61.932  1.00 25.71           C  
ANISOU 3419  CD1 ILE A 449     3485   3372   2911    -96    -42    -36       C  
ATOM   3420  N   PRO A 450      10.878  14.205  57.486  1.00 16.22           N  
ANISOU 3420  N   PRO A 450     2372   1995   1797    -54     96    -83       N  
ATOM   3421  CA  PRO A 450      11.501  15.338  56.796  1.00 15.57           C  
ANISOU 3421  CA  PRO A 450     2245   1928   1744     -6     86    -89       C  
ATOM   3422  C   PRO A 450      11.628  16.526  57.746  1.00 19.30           C  
ANISOU 3422  C   PRO A 450     2663   2451   2218     22     33    -74       C  
ATOM   3423  O   PRO A 450      10.704  16.750  58.528  1.00 12.67           O  
ANISOU 3423  O   PRO A 450     1812   1667   1336     -8      9    -85       O  
ATOM   3424  CB  PRO A 450      10.519  15.653  55.661  1.00  8.31           C  
ANISOU 3424  CB  PRO A 450     1324   1058    777    -46    100   -135       C  
ATOM   3425  CG  PRO A 450       9.239  14.972  56.027  1.00 17.17           C  
ANISOU 3425  CG  PRO A 450     2470   2218   1835   -116    103   -153       C  
ATOM   3426  CD  PRO A 450       9.622  13.781  56.837  1.00 16.27           C  
ANISOU 3426  CD  PRO A 450     2406   2036   1739   -125    118   -126       C  
ATOM   3427  N   ARG A 451      12.741  17.253  57.668  1.00 13.91           N  
ANISOU 3427  N   ARG A 451     1950   1752   1582     73     19    -52       N  
ATOM   3428  CA  ARG A 451      12.963  18.464  58.453  1.00  7.65           C  
ANISOU 3428  CA  ARG A 451     1115   1000    791     92    -27    -44       C  
ATOM   3429  C   ARG A 451      13.413  19.601  57.524  1.00  7.38           C  
ANISOU 3429  C   ARG A 451     1053    972    778    123    -31    -55       C  
ATOM   3430  O   ARG A 451      14.077  19.361  56.514  1.00 10.35           O  
ANISOU 3430  O   ARG A 451     1435   1315   1185    141     -4    -51       O  
ATOM   3431  CB  ARG A 451      13.996  18.214  59.550  1.00 11.20           C  
ANISOU 3431  CB  ARG A 451     1556   1428   1270    109    -49      9       C  
ATOM   3432  CG  ARG A 451      13.498  17.266  60.645  1.00 13.04           C  
ANISOU 3432  CG  ARG A 451     1812   1665   1477     73    -55     27       C  
ATOM   3433  CD  ARG A 451      14.572  16.974  61.651  1.00 17.77           C  
ANISOU 3433  CD  ARG A 451     2397   2249   2105     89    -78     91       C  
ATOM   3434  NE  ARG A 451      15.010  18.163  62.377  1.00 15.53           N  
ANISOU 3434  NE  ARG A 451     2074   2013   1814     90   -122     98       N  
ATOM   3435  CZ  ARG A 451      16.057  18.177  63.197  1.00 12.79           C  
ANISOU 3435  CZ  ARG A 451     1702   1672   1486     97   -150    157       C  
ATOM   3436  NH1 ARG A 451      16.770  17.074  63.360  1.00  9.92           N  
ANISOU 3436  NH1 ARG A 451     1343   1267   1158    117   -139    220       N  
ATOM   3437  NH2 ARG A 451      16.405  19.291  63.840  1.00  9.12           N  
ANISOU 3437  NH2 ARG A 451     1209   1253   1004     83   -188    155       N  
ATOM   3438  N   ASP A 452      13.003  20.821  57.848  1.00  8.35           N  
ANISOU 3438  N   ASP A 452     1149   1138    884    127    -61    -72       N  
ATOM   3439  CA  ASP A 452      13.514  22.025  57.192  1.00 11.44           C  
ANISOU 3439  CA  ASP A 452     1518   1531   1298    155    -72    -75       C  
ATOM   3440  C   ASP A 452      15.025  22.040  57.204  1.00 13.87           C  
ANISOU 3440  C   ASP A 452     1816   1803   1651    179    -78    -36       C  
ATOM   3441  O   ASP A 452      15.658  22.529  56.274  1.00 10.45           O  
ANISOU 3441  O   ASP A 452     1370   1358   1242    197    -72    -32       O  
ATOM   3442  CB  ASP A 452      13.033  23.300  57.907  1.00 11.85           C  
ANISOU 3442  CB  ASP A 452     1554   1616   1333    158   -102    -93       C  
ATOM   3443  CG  ASP A 452      11.569  23.597  57.675  1.00 21.59           C  
ANISOU 3443  CG  ASP A 452     2781   2894   2528    150    -95   -127       C  
ATOM   3444  OD1 ASP A 452      11.237  24.266  56.665  1.00 15.95           O  
ANISOU 3444  OD1 ASP A 452     2053   2190   1817    166    -90   -135       O  
ATOM   3445  OD2 ASP A 452      10.756  23.187  58.533  1.00 32.39           O  
ANISOU 3445  OD2 ASP A 452     4152   4292   3862    128    -95   -139       O  
ATOM   3446  N   VAL A 453      15.596  21.538  58.298  1.00  9.81           N  
ANISOU 3446  N   VAL A 453     1301   1281   1145    176    -92     -3       N  
ATOM   3447  CA  VAL A 453      17.010  21.730  58.564  1.00  7.58           C  
ANISOU 3447  CA  VAL A 453      995    987    899    195   -108     43       C  
ATOM   3448  C   VAL A 453      17.749  20.405  58.694  1.00  7.77           C  
ANISOU 3448  C   VAL A 453     1022    975    954    212    -86     90       C  
ATOM   3449  O   VAL A 453      18.054  19.962  59.806  1.00 11.86           O  
ANISOU 3449  O   VAL A 453     1534   1500   1472    204   -106    130       O  
ATOM   3450  CB  VAL A 453      17.226  22.555  59.855  1.00 10.90           C  
ANISOU 3450  CB  VAL A 453     1401   1440   1300    173   -153     54       C  
ATOM   3451  CG1 VAL A 453      18.694  22.952  59.989  1.00  9.72           C  
ANISOU 3451  CG1 VAL A 453     1220   1293   1180    183   -174    103       C  
ATOM   3452  CG2 VAL A 453      16.357  23.800  59.844  1.00  7.25           C  
ANISOU 3452  CG2 VAL A 453      945   1000    808    162   -165      3       C  
ATOM   3453  N   PRO A 454      18.064  19.777  57.560  1.00  7.86           N  
ANISOU 3453  N   PRO A 454     1044    948    995    237    -42     88       N  
ATOM   3454  CA  PRO A 454      19.111  18.761  57.582  1.00  9.09           C  
ANISOU 3454  CA  PRO A 454     1194   1063   1197    272    -16    141       C  
ATOM   3455  C   PRO A 454      20.433  19.480  57.856  1.00 11.28           C  
ANISOU 3455  C   PRO A 454     1418   1366   1503    295    -46    191       C  
ATOM   3456  O   PRO A 454      20.435  20.708  57.941  1.00 13.06           O  
ANISOU 3456  O   PRO A 454     1625   1630   1707    275    -82    175       O  
ATOM   3457  CB  PRO A 454      19.076  18.189  56.154  1.00  8.41           C  
ANISOU 3457  CB  PRO A 454     1134    934   1127    288     44    110       C  
ATOM   3458  CG  PRO A 454      18.717  19.348  55.329  1.00  7.98           C  
ANISOU 3458  CG  PRO A 454     1068    915   1049    272     32     68       C  
ATOM   3459  CD  PRO A 454      17.704  20.145  56.174  1.00  7.64           C  
ANISOU 3459  CD  PRO A 454     1025    917    962    238    -15     45       C  
ATOM   3460  N   LYS A 455      21.537  18.763  57.977  1.00  8.97           N  
ANISOU 3460  N   LYS A 455     1100   1052   1255    335    -30    253       N  
ATOM   3461  CA  LYS A 455      22.834  19.445  57.985  1.00  9.13           C  
ANISOU 3461  CA  LYS A 455     1062   1108   1300    353    -53    302       C  
ATOM   3462  C   LYS A 455      23.165  19.942  56.579  1.00 10.46           C  
ANISOU 3462  C   LYS A 455     1223   1269   1483    370    -22    270       C  
ATOM   3463  O   LYS A 455      23.266  19.142  55.665  1.00 11.63           O  
ANISOU 3463  O   LYS A 455     1389   1374   1658    402     37    258       O  
ATOM   3464  CB  LYS A 455      23.952  18.519  58.468  1.00  9.83           C  
ANISOU 3464  CB  LYS A 455     1112   1186   1436    399    -42    389       C  
ATOM   3465  CG  LYS A 455      23.691  17.885  59.837  1.00 10.34           C  
ANISOU 3465  CG  LYS A 455     1182   1257   1489    383    -72    435       C  
ATOM   3466  CD  LYS A 455      24.866  17.009  60.287  1.00 13.83           C  
ANISOU 3466  CD  LYS A 455     1578   1694   1984    436    -64    536       C  
ATOM   3467  CE  LYS A 455      24.543  16.361  61.650  1.00 18.77           C  
ANISOU 3467  CE  LYS A 455     2211   2328   2593    413    -97    588       C  
ATOM   3468  NZ  LYS A 455      25.699  15.602  62.168  1.00 20.83           N  
ANISOU 3468  NZ  LYS A 455     2417   2594   2905    465    -98    702       N  
ATOM   3469  N   ILE A 456      23.345  21.244  56.409  1.00 14.04           N  
ANISOU 3469  N   ILE A 456     1655   1764   1916    343    -58    256       N  
ATOM   3470  CA  ILE A 456      23.776  21.787  55.111  1.00 10.57           C  
ANISOU 3470  CA  ILE A 456     1203   1327   1487    353    -34    237       C  
ATOM   3471  C   ILE A 456      25.090  22.509  55.323  1.00 11.46           C  
ANISOU 3471  C   ILE A 456     1256   1485   1613    353    -66    291       C  
ATOM   3472  O   ILE A 456      25.140  23.575  55.941  1.00  8.73           O  
ANISOU 3472  O   ILE A 456      902   1176   1240    312   -118    294       O  
ATOM   3473  CB  ILE A 456      22.745  22.751  54.492  1.00  8.08           C  
ANISOU 3473  CB  ILE A 456      919   1017   1134    318    -46    172       C  
ATOM   3474  CG1 ILE A 456      21.370  22.075  54.408  1.00  7.87           C  
ANISOU 3474  CG1 ILE A 456      942    964   1083    307    -23    124       C  
ATOM   3475  CG2 ILE A 456      23.223  23.256  53.060  1.00  8.07           C  
ANISOU 3475  CG2 ILE A 456      903   1020   1141    323    -22    159       C  
ATOM   3476  CD1 ILE A 456      20.236  23.032  54.149  1.00 10.78           C  
ANISOU 3476  CD1 ILE A 456     1331   1351   1413    276    -44     75       C  
ATOM   3477  N   PHE A 457      26.164  21.893  54.867  1.00  9.35           N  
ANISOU 3477  N   PHE A 457      949   1217   1388    398    -30    337       N  
ATOM   3478  CA  PHE A 457      27.466  22.519  54.948  1.00  9.70           C  
ANISOU 3478  CA  PHE A 457      927   1316   1443    397    -56    394       C  
ATOM   3479  C   PHE A 457      27.809  23.176  53.610  1.00 16.38           C  
ANISOU 3479  C   PHE A 457     1763   2171   2289    393    -34    367       C  
ATOM   3480  O   PHE A 457      27.828  22.506  52.584  1.00 16.29           O  
ANISOU 3480  O   PHE A 457     1761   2128   2300    429     28    345       O  
ATOM   3481  CB  PHE A 457      28.515  21.497  55.325  1.00 10.42           C  
ANISOU 3481  CB  PHE A 457      965   1414   1582    453    -33    474       C  
ATOM   3482  CG  PHE A 457      28.401  21.004  56.746  1.00 17.43           C  
ANISOU 3482  CG  PHE A 457     1847   2311   2465    448    -69    523       C  
ATOM   3483  CD1 PHE A 457      28.900  21.762  57.798  1.00 14.91           C  
ANISOU 3483  CD1 PHE A 457     1488   2061   2116    399   -137    571       C  
ATOM   3484  CD2 PHE A 457      27.820  19.782  57.021  1.00 10.78           C  
ANISOU 3484  CD2 PHE A 457     1043   1410   1645    483    -34    522       C  
ATOM   3485  CE1 PHE A 457      28.806  21.312  59.098  1.00 16.77           C  
ANISOU 3485  CE1 PHE A 457     1716   2315   2341    385   -172    618       C  
ATOM   3486  CE2 PHE A 457      27.726  19.322  58.332  1.00 15.53           C  
ANISOU 3486  CE2 PHE A 457     1638   2024   2239    473    -70    574       C  
ATOM   3487  CZ  PHE A 457      28.222  20.088  59.364  1.00 13.11           C  
ANISOU 3487  CZ  PHE A 457     1286   1794   1901    424   -139    623       C  
ATOM   3488  N   PHE A 458      28.045  24.484  53.630  1.00 13.46           N  
ANISOU 3488  N   PHE A 458     1381   1842   1890    342    -81    366       N  
ATOM   3489  CA  PHE A 458      28.401  25.229  52.418  1.00 13.76           C  
ANISOU 3489  CA  PHE A 458     1409   1896   1923    328    -69    348       C  
ATOM   3490  C   PHE A 458      29.262  26.432  52.793  1.00 10.38           C  
ANISOU 3490  C   PHE A 458      944   1525   1475    278   -125    387       C  
ATOM   3491  O   PHE A 458      28.757  27.520  53.068  1.00 12.12           O  
ANISOU 3491  O   PHE A 458     1200   1744   1662    226   -167    359       O  
ATOM   3492  CB  PHE A 458      27.154  25.663  51.654  1.00  8.84           C  
ANISOU 3492  CB  PHE A 458      847   1237   1274    307    -61    276       C  
ATOM   3493  CG  PHE A 458      27.420  26.102  50.237  1.00 12.07           C  
ANISOU 3493  CG  PHE A 458     1250   1657   1680    299    -35    259       C  
ATOM   3494  CD1 PHE A 458      27.776  25.179  49.256  1.00 11.13           C  
ANISOU 3494  CD1 PHE A 458     1118   1528   1583    336     31    252       C  
ATOM   3495  CD2 PHE A 458      27.282  27.437  49.874  1.00 14.10           C  
ANISOU 3495  CD2 PHE A 458     1518   1930   1911    251    -74    248       C  
ATOM   3496  CE1 PHE A 458      28.011  25.587  47.933  1.00  9.70           C  
ANISOU 3496  CE1 PHE A 458      930   1365   1390    320     56    235       C  
ATOM   3497  CE2 PHE A 458      27.505  27.851  48.559  1.00 12.49           C  
ANISOU 3497  CE2 PHE A 458     1308   1740   1699    238    -53    238       C  
ATOM   3498  CZ  PHE A 458      27.866  26.921  47.589  1.00  9.85           C  
ANISOU 3498  CZ  PHE A 458      956   1408   1380    269     10    230       C  
ATOM   3499  N   ASN A 459      30.571  26.207  52.814  1.00 10.51           N  
ANISOU 3499  N   ASN A 459      889   1593   1512    294   -120    453       N  
ATOM   3500  CA  ASN A 459      31.542  27.234  53.181  1.00 13.04           C  
ANISOU 3500  CA  ASN A 459     1166   1981   1809    238   -171    499       C  
ATOM   3501  C   ASN A 459      32.082  27.974  51.955  1.00 16.51           C  
ANISOU 3501  C   ASN A 459     1587   2444   2241    216   -160    493       C  
ATOM   3502  O   ASN A 459      32.505  27.352  50.981  1.00 15.09           O  
ANISOU 3502  O   ASN A 459     1377   2268   2089    263   -105    497       O  
ATOM   3503  CB  ASN A 459      32.686  26.592  53.968  1.00 13.16           C  
ANISOU 3503  CB  ASN A 459     1100   2057   1844    261   -180    588       C  
ATOM   3504  CG  ASN A 459      32.195  25.917  55.245  1.00 15.85           C  
ANISOU 3504  CG  ASN A 459     1455   2381   2185    272   -199    605       C  
ATOM   3505  OD1 ASN A 459      31.335  26.455  55.946  1.00 10.76           O  
ANISOU 3505  OD1 ASN A 459      868   1715   1505    223   -236    564       O  
ATOM   3506  ND2 ASN A 459      32.723  24.732  55.538  1.00 11.68           N  
ANISOU 3506  ND2 ASN A 459      877   1860   1699    338   -170    665       N  
ATOM   3507  N   THR A 460      32.070  29.303  51.998  1.00 14.03           N  
ANISOU 3507  N   THR A 460     1298   2144   1889    142   -208    482       N  
ATOM   3508  CA  THR A 460      32.415  30.063  50.791  1.00 16.51           C  
ANISOU 3508  CA  THR A 460     1608   2473   2193    115   -199    472       C  
ATOM   3509  C   THR A 460      33.837  30.630  50.826  1.00 14.74           C  
ANISOU 3509  C   THR A 460     1313   2333   1954     69   -226    538       C  
ATOM   3510  O   THR A 460      34.800  29.931  50.465  1.00 11.60           O  
ANISOU 3510  O   THR A 460      840   1988   1581    109   -192    586       O  
ATOM   3511  CB  THR A 460      31.419  31.219  50.547  1.00 15.41           C  
ANISOU 3511  CB  THR A 460     1547   2283   2024     66   -228    417       C  
ATOM   3512  OG1 THR A 460      31.330  32.041  51.723  1.00 10.97           O  
ANISOU 3512  OG1 THR A 460     1015   1719   1433      9   -283    421       O  
ATOM   3513  CG2 THR A 460      30.019  30.668  50.192  1.00 15.62           C  
ANISOU 3513  CG2 THR A 460     1630   2242   2061    111   -196    356       C  
ATOM   3514  N   PHE A 461      33.962  31.886  51.260  1.00 11.18           N  
ANISOU 3514  N   PHE A 461      890   1896   1463    -16   -282    542       N  
ATOM   3515  CA  PHE A 461      35.221  32.640  51.126  1.00 19.47           C  
ANISOU 3515  CA  PHE A 461     1885   3025   2487    -83   -312    597       C  
ATOM   3516  C   PHE A 461      36.205  32.341  52.228  1.00 21.53           C  
ANISOU 3516  C   PHE A 461     2074   3369   2739   -103   -342    670       C  
ATOM   3517  O   PHE A 461      36.554  33.218  53.025  1.00 22.83           O  
ANISOU 3517  O   PHE A 461     2248   3566   2858   -192   -397    690       O  
ATOM   3518  CB  PHE A 461      34.941  34.137  51.088  1.00 13.71           C  
ANISOU 3518  CB  PHE A 461     1226   2268   1716   -174   -356    569       C  
ATOM   3519  CG  PHE A 461      33.936  34.513  50.066  1.00 15.33           C  
ANISOU 3519  CG  PHE A 461     1498   2397   1928   -157   -334    510       C  
ATOM   3520  CD1 PHE A 461      34.309  34.684  48.732  1.00 18.46           C  
ANISOU 3520  CD1 PHE A 461     1871   2815   2327   -158   -310    517       C  
ATOM   3521  CD2 PHE A 461      32.606  34.654  50.413  1.00 13.89           C  
ANISOU 3521  CD2 PHE A 461     1395   2131   1750   -138   -337    452       C  
ATOM   3522  CE1 PHE A 461      33.379  35.007  47.784  1.00 18.69           C  
ANISOU 3522  CE1 PHE A 461     1957   2786   2360   -146   -293    472       C  
ATOM   3523  CE2 PHE A 461      31.672  34.976  49.464  1.00 13.90           C  
ANISOU 3523  CE2 PHE A 461     1448   2076   1759   -119   -319    409       C  
ATOM   3524  CZ  PHE A 461      32.053  35.147  48.147  1.00 16.95           C  
ANISOU 3524  CZ  PHE A 461     1810   2485   2144   -125   -299    421       C  
ATOM   3525  N   VAL A 462      36.641  31.089  52.268  1.00 12.67           N  
ANISOU 3525  N   VAL A 462      880   2276   1656    -21   -303    712       N  
ATOM   3526  CA  VAL A 462      37.550  30.629  53.292  1.00 16.66           C  
ANISOU 3526  CA  VAL A 462     1316   2855   2159    -24   -321    787       C  
ATOM   3527  C   VAL A 462      38.942  31.228  53.097  1.00 19.88           C  
ANISOU 3527  C   VAL A 462     1665   3353   2534    -86   -331    843       C  
ATOM   3528  O   VAL A 462      39.290  31.693  52.003  1.00 16.85           O  
ANISOU 3528  O   VAL A 462     1262   2993   2148   -100   -318    839       O  
ATOM   3529  CB  VAL A 462      37.620  29.091  53.301  1.00 19.04           C  
ANISOU 3529  CB  VAL A 462     1585   3133   2516     88   -258    804       C  
ATOM   3530  CG1 VAL A 462      36.242  28.501  53.624  1.00 17.70           C  
ANISOU 3530  CG1 VAL A 462     1479   2876   2369    136   -250    752       C  
ATOM   3531  CG2 VAL A 462      38.118  28.582  51.957  1.00 14.48           C  
ANISOU 3531  CG2 VAL A 462      962   2564   1976    154   -191    807       C  
ATOM   3532  N   THR A 463      39.721  31.239  54.173  1.00 21.63           N  
ANISOU 3532  N   THR A 463     1996   3705   2516    172     58    791       N  
ATOM   3533  CA  THR A 463      41.091  31.738  54.131  1.00 21.82           C  
ANISOU 3533  CA  THR A 463     2020   3810   2462    118     11    722       C  
ATOM   3534  C   THR A 463      42.010  30.584  53.774  1.00 23.60           C  
ANISOU 3534  C   THR A 463     2180   4076   2709    120     38    744       C  
ATOM   3535  O   THR A 463      41.663  29.417  53.983  1.00 16.55           O  
ANISOU 3535  O   THR A 463     1243   3168   1878    192     95    817       O  
ATOM   3536  CB  THR A 463      41.554  32.333  55.478  1.00 27.21           C  
ANISOU 3536  CB  THR A 463     2705   4598   3037    186    -10    697       C  
ATOM   3537  OG1 THR A 463      41.456  31.331  56.494  1.00 28.47           O  
ANISOU 3537  OG1 THR A 463     2812   4822   3184    312     50    777       O  
ATOM   3538  CG2 THR A 463      40.713  33.544  55.875  1.00 32.00           C  
ANISOU 3538  CG2 THR A 463     3375   5168   3616    191    -45    659       C  
ATOM   3539  N   TYR A 464      43.185  30.906  53.248  1.00 22.06           N  
ANISOU 3539  N   TYR A 464     1977   3934   2471     43     -3    682       N  
ATOM   3540  CA  TYR A 464      44.217  29.898  53.097  1.00 23.57           C  
ANISOU 3540  CA  TYR A 464     2103   4190   2661     59     17    692       C  
ATOM   3541  C   TYR A 464      45.202  30.014  54.258  1.00 22.39           C  
ANISOU 3541  C   TYR A 464     1926   4170   2411    118      7    678       C  
ATOM   3542  O   TYR A 464      45.774  31.079  54.500  1.00 24.47           O  
ANISOU 3542  O   TYR A 464     2213   4486   2601     71    -46    609       O  
ATOM   3543  CB  TYR A 464      44.954  30.034  51.746  1.00 16.00           C  
ANISOU 3543  CB  TYR A 464     1138   3228   1715    -54    -15    636       C  
ATOM   3544  CG  TYR A 464      46.060  29.009  51.618  1.00 17.80           C  
ANISOU 3544  CG  TYR A 464     1296   3533   1935    -30      3    639       C  
ATOM   3545  CD1 TYR A 464      45.759  27.684  51.319  1.00 16.14           C  
ANISOU 3545  CD1 TYR A 464     1043   3280   1810     25     50    687       C  
ATOM   3546  CD2 TYR A 464      47.399  29.347  51.863  1.00 17.38           C  
ANISOU 3546  CD2 TYR A 464     1214   3595   1794    -57    -28    591       C  
ATOM   3547  CE1 TYR A 464      46.755  26.720  51.232  1.00 16.42           C  
ANISOU 3547  CE1 TYR A 464     1014   3381   1843     58     64    687       C  
ATOM   3548  CE2 TYR A 464      48.410  28.382  51.778  1.00 16.85           C  
ANISOU 3548  CE2 TYR A 464     1079   3606   1717    -25    -12    593       C  
ATOM   3549  CZ  TYR A 464      48.075  27.068  51.459  1.00 18.72           C  
ANISOU 3549  CZ  TYR A 464     1279   3794   2038     35     35    642       C  
ATOM   3550  OH  TYR A 464      49.050  26.087  51.382  1.00 22.96           O  
ANISOU 3550  OH  TYR A 464     1751   4401   2572     76     50    642       O  
ATOM   3551  N   THR A 465      45.401  28.915  54.976  1.00 21.27           N  
ANISOU 3551  N   THR A 465     1730   4080   2270    223     56    742       N  
ATOM   3552  CA  THR A 465      46.351  28.898  56.071  1.00 20.70           C  
ANISOU 3552  CA  THR A 465     1622   4144   2097    294     48    734       C  
ATOM   3553  C   THR A 465      47.648  28.254  55.605  1.00 23.29           C  
ANISOU 3553  C   THR A 465     1895   4543   2413    271     43    711       C  
ATOM   3554  O   THR A 465      47.667  27.069  55.277  1.00 25.19           O  
ANISOU 3554  O   THR A 465     2095   4756   2722    310     87    765       O  
ATOM   3555  CB  THR A 465      45.803  28.130  57.281  1.00 28.35           C  
ANISOU 3555  CB  THR A 465     2565   5148   3060    441    108    832       C  
ATOM   3556  OG1 THR A 465      44.510  28.643  57.628  1.00 35.06           O  
ANISOU 3556  OG1 THR A 465     3460   5931   3928    466    119    860       O  
ATOM   3557  CG2 THR A 465      46.750  28.262  58.469  1.00 32.06           C  
ANISOU 3557  CG2 THR A 465     3000   5776   3406    523     93    815       C  
ATOM   3558  N   PRO A 466      48.741  29.030  55.593  1.00 22.84           N  
ANISOU 3558  N   PRO A 466     1830   4574   2274    209    -12    627       N  
ATOM   3559  CA  PRO A 466      50.019  28.496  55.117  1.00 24.04           C  
ANISOU 3559  CA  PRO A 466     1924   4804   2406    181    -20    599       C  
ATOM   3560  C   PRO A 466      50.476  27.307  55.948  1.00 31.06           C  
ANISOU 3560  C   PRO A 466     2751   5774   3275    312     24    662       C  
ATOM   3561  O   PRO A 466      50.228  27.247  57.156  1.00 26.41           O  
ANISOU 3561  O   PRO A 466     2158   5240   2637    418     42    703       O  
ATOM   3562  CB  PRO A 466      50.987  29.677  55.260  1.00 24.36           C  
ANISOU 3562  CB  PRO A 466     1965   4932   2357    104    -87    504       C  
ATOM   3563  CG  PRO A 466      50.125  30.886  55.374  1.00 26.17           C  
ANISOU 3563  CG  PRO A 466     2266   5087   2590     56   -120    474       C  
ATOM   3564  CD  PRO A 466      48.836  30.444  55.994  1.00 24.40           C  
ANISOU 3564  CD  PRO A 466     2070   4799   2403    158    -72    552       C  
ATOM   3565  N   THR A 467      51.116  26.358  55.275  1.00 30.73           N  
ANISOU 3565  N   THR A 467     2661   5744   3273    310     42    670       N  
ATOM   3566  CA  THR A 467      51.709  25.209  55.920  1.00 22.93           C  
ANISOU 3566  CA  THR A 467     1651   4792   2269    416     79    715       C  
ATOM   3567  C   THR A 467      53.214  25.463  56.006  1.00 24.59           C  
ANISOU 3567  C   THR A 467     1830   5132   2380    389     40    639       C  
ATOM   3568  O   THR A 467      53.677  26.588  55.823  1.00 23.47           O  
ANISOU 3568  O   THR A 467     1679   5057   2180    302    -13    562       O  
ATOM   3569  CB  THR A 467      51.439  23.908  55.143  1.00 22.11           C  
ANISOU 3569  CB  THR A 467     1552   4566   2281    431    120    757       C  
ATOM   3570  OG1 THR A 467      52.136  23.944  53.889  1.00 18.92           O  
ANISOU 3570  OG1 THR A 467     1134   4163   1891    336     89    682       O  
ATOM   3571  CG2 THR A 467      49.942  23.743  54.893  1.00 23.45           C  
ANISOU 3571  CG2 THR A 467     1751   4598   2561    434    152    817       C  
ATOM   3572  N   SER A 468      53.972  24.414  56.284  1.00 24.52           N  
ANISOU 3572  N   SER A 468     1806   5152   2358    461     65    662       N  
ATOM   3573  CA  SER A 468      55.405  24.546  56.439  1.00 26.58           C  
ANISOU 3573  CA  SER A 468     2035   5538   2525    449     35    595       C  
ATOM   3574  C   SER A 468      56.103  24.111  55.153  1.00 20.60           C  
ANISOU 3574  C   SER A 468     1265   4753   1809    376     26    549       C  
ATOM   3575  O   SER A 468      57.327  24.114  55.065  1.00 22.39           O  
ANISOU 3575  O   SER A 468     1465   5072   1970    357      6    494       O  
ATOM   3576  CB  SER A 468      55.894  23.713  57.625  1.00 24.25           C  
ANISOU 3576  CB  SER A 468     1731   5311   2173    581     65    646       C  
ATOM   3577  OG  SER A 468      55.820  22.326  57.333  1.00 28.20           O  
ANISOU 3577  OG  SER A 468     2235   5725   2755    638    107    710       O  
ATOM   3578  N   ALA A 469      55.321  23.715  54.162  1.00 20.03           N  
ANISOU 3578  N   ALA A 469     1211   4557   1843    340     42    569       N  
ATOM   3579  CA  ALA A 469      55.876  23.322  52.868  1.00 19.87           C  
ANISOU 3579  CA  ALA A 469     1181   4510   1859    276     32    519       C  
ATOM   3580  C   ALA A 469      56.467  24.529  52.115  1.00 24.05           C  
ANISOU 3580  C   ALA A 469     1711   5096   2330    145    -13    438       C  
ATOM   3581  O   ALA A 469      56.055  25.670  52.341  1.00 19.54           O  
ANISOU 3581  O   ALA A 469     1156   4535   1734     84    -37    425       O  
ATOM   3582  CB  ALA A 469      54.798  22.634  52.025  1.00 19.38           C  
ANISOU 3582  CB  ALA A 469     1136   4302   1927    276     58    551       C  
ATOM   3583  N   PRO A 470      57.450  24.278  51.230  1.00 21.42           N  
ANISOU 3583  N   PRO A 470     1362   4797   1978    101    -23    386       N  
ATOM   3584  CA  PRO A 470      57.972  25.364  50.392  1.00 23.20           C  
ANISOU 3584  CA  PRO A 470     1598   5056   2161    -27    -55    324       C  
ATOM   3585  C   PRO A 470      56.846  26.148  49.731  1.00 19.22           C  
ANISOU 3585  C   PRO A 470     1134   4458   1711   -108    -64    333       C  
ATOM   3586  O   PRO A 470      55.846  25.566  49.335  1.00 18.79           O  
ANISOU 3586  O   PRO A 470     1094   4306   1739    -78    -44    367       O  
ATOM   3587  CB  PRO A 470      58.808  24.628  49.344  1.00 20.41           C  
ANISOU 3587  CB  PRO A 470     1226   4718   1809    -34    -49    289       C  
ATOM   3588  CG  PRO A 470      59.272  23.395  50.049  1.00 20.94           C  
ANISOU 3588  CG  PRO A 470     1262   4818   1877     87    -28    311       C  
ATOM   3589  CD  PRO A 470      58.178  23.015  51.017  1.00 22.14           C  
ANISOU 3589  CD  PRO A 470     1426   4902   2083    172     -5    384       C  
ATOM   3590  N   ALA A 471      57.019  27.460  49.650  1.00 20.18           N  
ANISOU 3590  N   ALA A 471     1273   4603   1792   -208    -95    302       N  
ATOM   3591  CA  ALA A 471      56.050  28.351  49.032  1.00 18.79           C  
ANISOU 3591  CA  ALA A 471     1140   4342   1658   -293   -110    309       C  
ATOM   3592  C   ALA A 471      55.619  27.827  47.672  1.00 19.28           C  
ANISOU 3592  C   ALA A 471     1221   4327   1777   -314    -94    312       C  
ATOM   3593  O   ALA A 471      54.439  27.771  47.377  1.00 17.91           O  
ANISOU 3593  O   ALA A 471     1072   4063   1670   -311    -87    341       O  
ATOM   3594  CB  ALA A 471      56.634  29.741  48.887  1.00 24.77           C  
ANISOU 3594  CB  ALA A 471     1914   5129   2369   -407   -145    269       C  
ATOM   3595  N   ASP A 472      56.594  27.457  46.844  1.00 20.93           N  
ANISOU 3595  N   ASP A 472     1414   4582   1957   -330    -90    279       N  
ATOM   3596  CA  ASP A 472      56.307  27.040  45.465  1.00 18.48           C  
ANISOU 3596  CA  ASP A 472     1115   4220   1685   -349    -81    267       C  
ATOM   3597  C   ASP A 472      55.343  25.859  45.425  1.00 18.12           C  
ANISOU 3597  C   ASP A 472     1062   4093   1731   -262    -59    289       C  
ATOM   3598  O   ASP A 472      54.581  25.706  44.481  1.00 22.77           O  
ANISOU 3598  O   ASP A 472     1667   4611   2373   -278    -57    284       O  
ATOM   3599  CB  ASP A 472      57.595  26.648  44.732  1.00 18.99           C  
ANISOU 3599  CB  ASP A 472     1151   4369   1695   -355    -78    227       C  
ATOM   3600  CG  ASP A 472      58.519  27.819  44.503  1.00 19.42           C  
ANISOU 3600  CG  ASP A 472     1212   4491   1676   -452    -94    211       C  
ATOM   3601  OD1 ASP A 472      58.079  28.969  44.689  1.00 19.30           O  
ANISOU 3601  OD1 ASP A 472     1230   4440   1664   -524   -110    227       O  
ATOM   3602  OD2 ASP A 472      59.691  27.580  44.141  1.00 19.95           O  
ANISOU 3602  OD2 ASP A 472     1247   4646   1688   -454    -89    184       O  
ATOM   3603  N   GLN A 473      55.389  25.021  46.455  1.00 18.27           N  
ANISOU 3603  N   GLN A 473     1053   4121   1769   -167    -42    315       N  
ATOM   3604  CA  GLN A 473      54.510  23.857  46.521  1.00 18.09           C  
ANISOU 3604  CA  GLN A 473     1018   4007   1849    -80    -15    345       C  
ATOM   3605  C   GLN A 473      53.136  24.282  47.001  1.00 17.63           C  
ANISOU 3605  C   GLN A 473      987   3863   1847    -80     -7    396       C  
ATOM   3606  O   GLN A 473      52.128  23.681  46.640  1.00 30.78           O  
ANISOU 3606  O   GLN A 473     2656   5430   3611    -51     11    415       O  
ATOM   3607  CB  GLN A 473      55.066  22.786  47.463  1.00 23.21           C  
ANISOU 3607  CB  GLN A 473     1630   4686   2503     28      6    369       C  
ATOM   3608  CG  GLN A 473      54.253  21.499  47.456  1.00 24.11           C  
ANISOU 3608  CG  GLN A 473     1729   4692   2741    115     37    403       C  
ATOM   3609  CD  GLN A 473      54.881  20.380  48.263  1.00 30.76           C  
ANISOU 3609  CD  GLN A 473     2538   5555   3594    221     59    431       C  
ATOM   3610  OE1 GLN A 473      55.616  20.622  49.231  1.00 27.54           O  
ANISOU 3610  OE1 GLN A 473     2126   5238   3101    250     57    449       O  
ATOM   3611  NE2 GLN A 473      54.601  19.142  47.863  1.00 31.24           N  
ANISOU 3611  NE2 GLN A 473     2574   5532   3765    282     77    432       N  
ATOM   3612  N   GLN A 474      53.092  25.367  47.766  1.00 23.71           N  
ANISOU 3612  N   GLN A 474     1776   4675   2558   -118    -22    412       N  
ATOM   3613  CA  GLN A 474      51.837  25.817  48.360  1.00 21.39           C  
ANISOU 3613  CA  GLN A 474     1504   4317   2306   -108    -14    463       C  
ATOM   3614  C   GLN A 474      50.976  26.645  47.412  1.00 22.93           C  
ANISOU 3614  C   GLN A 474     1739   4442   2532   -200    -32    451       C  
ATOM   3615  O   GLN A 474      49.746  26.538  47.442  1.00 21.82           O  
ANISOU 3615  O   GLN A 474     1613   4213   2464   -180    -17    489       O  
ATOM   3616  CB  GLN A 474      52.114  26.627  49.637  1.00 17.49           C  
ANISOU 3616  CB  GLN A 474     1005   3904   1735    -98    -28    477       C  
ATOM   3617  CG  GLN A 474      52.696  25.816  50.791  1.00 19.19           C  
ANISOU 3617  CG  GLN A 474     1189   4184   1920     16     -5    506       C  
ATOM   3618  CD  GLN A 474      52.576  26.547  52.122  1.00 25.18           C  
ANISOU 3618  CD  GLN A 474     1942   5010   2613     53    -16    526       C  
ATOM   3619  OE1 GLN A 474      51.477  26.952  52.514  1.00 21.30           O  
ANISOU 3619  OE1 GLN A 474     1484   4458   2152     67     -9    562       O  
ATOM   3620  NE2 GLN A 474      53.699  26.723  52.817  1.00 18.79           N  
ANISOU 3620  NE2 GLN A 474     1108   4318   1712     73    -35    493       N  
ATOM   3621  N   TRP A 475      51.603  27.461  46.566  1.00 22.96           N  
ANISOU 3621  N   TRP A 475     1762   4480   2480   -296    -63    404       N  
ATOM   3622  CA  TRP A 475      50.833  28.372  45.719  1.00 18.10           C  
ANISOU 3622  CA  TRP A 475     1192   3802   1883   -382    -82    401       C  
ATOM   3623  C   TRP A 475      49.703  27.713  44.913  1.00 17.89           C  
ANISOU 3623  C   TRP A 475     1174   3678   1947   -357    -65    410       C  
ATOM   3624  O   TRP A 475      48.612  28.274  44.856  1.00 15.78           O  
ANISOU 3624  O   TRP A 475      937   3342   1716   -384    -70    435       O  
ATOM   3625  CB  TRP A 475      51.769  29.139  44.784  1.00 18.64           C  
ANISOU 3625  CB  TRP A 475     1279   3918   1885   -474   -105    361       C  
ATOM   3626  CG  TRP A 475      52.512  30.205  45.518  1.00 21.38           C  
ANISOU 3626  CG  TRP A 475     1631   4327   2166   -529   -131    353       C  
ATOM   3627  CD1 TRP A 475      53.862  30.388  45.563  1.00 21.10           C  
ANISOU 3627  CD1 TRP A 475     1574   4380   2064   -554   -138    322       C  
ATOM   3628  CD2 TRP A 475      51.937  31.243  46.329  1.00 22.27           C  
ANISOU 3628  CD2 TRP A 475     1767   4416   2278   -564   -157    368       C  
ATOM   3629  NE1 TRP A 475      54.166  31.480  46.346  1.00 20.64           N  
ANISOU 3629  NE1 TRP A 475     1525   4347   1972   -606   -167    313       N  
ATOM   3630  CE2 TRP A 475      53.001  32.018  46.835  1.00 22.42           C  
ANISOU 3630  CE2 TRP A 475     1777   4505   2235   -612   -182    337       C  
ATOM   3631  CE3 TRP A 475      50.624  31.589  46.679  1.00 16.70           C  
ANISOU 3631  CE3 TRP A 475     1086   3638   1622   -559   -163    401       C  
ATOM   3632  CZ2 TRP A 475      52.800  33.122  47.662  1.00 17.85           C  
ANISOU 3632  CZ2 TRP A 475     1217   3923   1644   -653   -222    328       C  
ATOM   3633  CZ3 TRP A 475      50.424  32.682  47.506  1.00 21.05           C  
ANISOU 3633  CZ3 TRP A 475     1678   4170   2152   -586   -195    393       C  
ATOM   3634  CH2 TRP A 475      51.506  33.436  47.988  1.00 21.90           C  
ANISOU 3634  CH2 TRP A 475     1762   4360   2199   -639   -232    355       C  
ATOM   3635  N   PRO A 476      49.943  26.532  44.307  1.00 16.22           N  
ANISOU 3635  N   PRO A 476      931   3458   1775   -305    -48    385       N  
ATOM   3636  CA  PRO A 476      48.797  25.918  43.628  1.00 19.78           C  
ANISOU 3636  CA  PRO A 476     1381   3812   2324   -280    -37    386       C  
ATOM   3637  C   PRO A 476      47.666  25.508  44.569  1.00 21.42           C  
ANISOU 3637  C   PRO A 476     1583   3937   2617   -216    -10    445       C  
ATOM   3638  O   PRO A 476      46.527  25.466  44.116  1.00 15.78           O  
ANISOU 3638  O   PRO A 476      881   3138   1977   -220     -7    454       O  
ATOM   3639  CB  PRO A 476      49.399  24.685  42.942  1.00 20.71           C  
ANISOU 3639  CB  PRO A 476     1454   3945   2472   -229    -29    339       C  
ATOM   3640  CG  PRO A 476      50.842  25.031  42.736  1.00 20.45           C  
ANISOU 3640  CG  PRO A 476     1416   4023   2332   -264    -43    306       C  
ATOM   3641  CD  PRO A 476      51.211  25.861  43.959  1.00 16.65           C  
ANISOU 3641  CD  PRO A 476      950   3587   1788   -283    -46    344       C  
ATOM   3642  N   ILE A 477      47.962  25.212  45.834  1.00 21.40           N  
ANISOU 3642  N   ILE A 477     1563   3964   2603   -152     12    489       N  
ATOM   3643  CA  ILE A 477      46.911  24.908  46.795  1.00 18.03           C  
ANISOU 3643  CA  ILE A 477     1137   3467   2247    -84     45    561       C  
ATOM   3644  C   ILE A 477      46.144  26.184  47.128  1.00 18.27           C  
ANISOU 3644  C   ILE A 477     1236   3462   2244   -132     28    577       C  
ATOM   3645  O   ILE A 477      44.912  26.208  47.102  1.00 17.00           O  
ANISOU 3645  O   ILE A 477     1108   3200   2153   -120     41    604       O  
ATOM   3646  CB  ILE A 477      47.467  24.309  48.105  1.00 23.62           C  
ANISOU 3646  CB  ILE A 477     1821   4220   2934      9     74    608       C  
ATOM   3647  CG1 ILE A 477      48.339  23.092  47.821  1.00 24.99           C  
ANISOU 3647  CG1 ILE A 477     1957   4406   3132     59     84    582       C  
ATOM   3648  CG2 ILE A 477      46.322  23.967  49.070  1.00 16.26           C  
ANISOU 3648  CG2 ILE A 477      897   3208   2074     87    115    694       C  
ATOM   3649  CD1 ILE A 477      47.601  21.979  47.120  1.00 29.82           C  
ANISOU 3649  CD1 ILE A 477     2550   4901   3879     93    101    577       C  
ATOM   3650  N   ALA A 478      46.873  27.248  47.459  1.00 19.55           N  
ANISOU 3650  N   ALA A 478     1421   3703   2303   -186     -2    554       N  
ATOM   3651  CA  ALA A 478      46.222  28.523  47.783  1.00 15.46           C  
ANISOU 3651  CA  ALA A 478      973   3145   1754   -230    -25    557       C  
ATOM   3652  C   ALA A 478      45.368  29.015  46.619  1.00 22.09           C  
ANISOU 3652  C   ALA A 478     1852   3904   2636   -300    -43    541       C  
ATOM   3653  O   ALA A 478      44.284  29.573  46.821  1.00 20.75           O  
ANISOU 3653  O   ALA A 478     1737   3654   2494   -299    -45    561       O  
ATOM   3654  CB  ALA A 478      47.258  29.575  48.162  1.00 15.75           C  
ANISOU 3654  CB  ALA A 478     1021   3276   1690   -289    -64    522       C  
ATOM   3655  N   GLN A 479      45.835  28.761  45.399  1.00 20.82           N  
ANISOU 3655  N   GLN A 479     1661   3773   2477   -350    -55    505       N  
ATOM   3656  CA  GLN A 479      45.122  29.192  44.198  1.00 14.84           C  
ANISOU 3656  CA  GLN A 479      932   2960   1747   -409    -73    488       C  
ATOM   3657  C   GLN A 479      43.710  28.631  44.172  1.00 15.81           C  
ANISOU 3657  C   GLN A 479     1069   2968   1969   -354    -51    511       C  
ATOM   3658  O   GLN A 479      42.763  29.347  43.873  1.00 19.99           O  
ANISOU 3658  O   GLN A 479     1650   3430   2515   -384    -65    517       O  
ATOM   3659  CB  GLN A 479      45.880  28.762  42.945  1.00 15.01           C  
ANISOU 3659  CB  GLN A 479      906   3047   1750   -444    -82    444       C  
ATOM   3660  CG  GLN A 479      45.307  29.295  41.643  1.00 20.13           C  
ANISOU 3660  CG  GLN A 479     1588   3660   2401   -501   -103    424       C  
ATOM   3661  CD  GLN A 479      46.094  28.830  40.430  1.00 25.22           C  
ANISOU 3661  CD  GLN A 479     2211   4359   3012   -506   -107    371       C  
ATOM   3662  OE1 GLN A 479      47.330  28.904  40.403  1.00 24.21           O  
ANISOU 3662  OE1 GLN A 479     2072   4312   2814   -523   -109    354       O  
ATOM   3663  NE2 GLN A 479      45.382  28.305  39.434  1.00 23.06           N  
ANISOU 3663  NE2 GLN A 479     1924   4050   2789   -487   -110    342       N  
ATOM   3664  N   LYS A 480      43.575  27.356  44.515  1.00 18.39           N  
ANISOU 3664  N   LYS A 480     1347   3271   2370   -274    -16    527       N  
ATOM   3665  CA  LYS A 480      42.270  26.707  44.545  1.00 14.52           C  
ANISOU 3665  CA  LYS A 480      855   2669   1991   -221      8    553       C  
ATOM   3666  C   LYS A 480      41.446  27.193  45.735  1.00 17.76           C  
ANISOU 3666  C   LYS A 480     1311   3030   2407   -184     27    612       C  
ATOM   3667  O   LYS A 480      40.258  27.494  45.602  1.00 15.10           O  
ANISOU 3667  O   LYS A 480     1008   2611   2120   -185     28    626       O  
ATOM   3668  CB  LYS A 480      42.423  25.183  44.588  1.00 26.52           C  
ANISOU 3668  CB  LYS A 480     2304   4169   3603   -148     39    557       C  
ATOM   3669  N   THR A 481      42.075  27.251  46.903  1.00 14.65           N  
ANISOU 3669  N   THR A 481      914   2695   1956   -143     41    643       N  
ATOM   3670  CA  THR A 481      41.367  27.652  48.117  1.00 18.43           C  
ANISOU 3670  CA  THR A 481     1427   3149   2426    -91     61    697       C  
ATOM   3671  C   THR A 481      40.773  29.037  47.954  1.00 19.12           C  
ANISOU 3671  C   THR A 481     1587   3208   2471   -150     25    675       C  
ATOM   3672  O   THR A 481      39.619  29.269  48.306  1.00 14.75           O  
ANISOU 3672  O   THR A 481     1064   2587   1956   -120     37    707       O  
ATOM   3673  CB  THR A 481      42.307  27.638  49.362  1.00 18.84           C  
ANISOU 3673  CB  THR A 481     1463   3298   2398    -38     72    720       C  
ATOM   3674  OG1 THR A 481      42.854  26.329  49.537  1.00 15.65           O  
ANISOU 3674  OG1 THR A 481      991   2918   2037     25    107    748       O  
ATOM   3675  CG2 THR A 481      41.561  28.074  50.644  1.00 15.21           C  
ANISOU 3675  CG2 THR A 481     1034   2831   1915     29     91    771       C  
ATOM   3676  N   LEU A 482      41.563  29.942  47.382  1.00 19.26           N  
ANISOU 3676  N   LEU A 482     1629   3275   2413   -234    -20    625       N  
ATOM   3677  CA  LEU A 482      41.175  31.341  47.241  1.00 18.18           C  
ANISOU 3677  CA  LEU A 482     1562   3110   2235   -295    -60    605       C  
ATOM   3678  C   LEU A 482      40.305  31.619  46.016  1.00 15.45           C  
ANISOU 3678  C   LEU A 482     1243   2689   1937   -345    -76    593       C  
ATOM   3679  O   LEU A 482      39.881  32.754  45.822  1.00 15.52           O  
ANISOU 3679  O   LEU A 482     1312   2662   1922   -392   -108    583       O  
ATOM   3680  CB  LEU A 482      42.426  32.228  47.178  1.00 17.44           C  
ANISOU 3680  CB  LEU A 482     1478   3096   2053   -370   -101    565       C  
ATOM   3681  CG  LEU A 482      43.337  32.259  48.407  1.00 18.57           C  
ANISOU 3681  CG  LEU A 482     1601   3325   2130   -330   -101    561       C  
ATOM   3682  CD1 LEU A 482      44.668  32.940  48.040  1.00 21.16           C  
ANISOU 3682  CD1 LEU A 482     1917   3732   2389   -419   -141    515       C  
ATOM   3683  CD2 LEU A 482      42.662  32.966  49.577  1.00 21.30           C  
ANISOU 3683  CD2 LEU A 482     1994   3646   2454   -279   -108    570       C  
ATOM   3684  N   ALA A 483      40.013  30.592  45.217  1.00 17.79           N  
ANISOU 3684  N   ALA A 483     1494   2961   2304   -330    -56    590       N  
ATOM   3685  CA  ALA A 483      39.230  30.772  43.981  1.00 18.52           C  
ANISOU 3685  CA  ALA A 483     1602   2998   2436   -370    -74    569       C  
ATOM   3686  C   ALA A 483      37.978  31.645  44.169  1.00 17.08           C  
ANISOU 3686  C   ALA A 483     1483   2737   2270   -368    -86    587       C  
ATOM   3687  O   ALA A 483      37.746  32.553  43.376  1.00 13.75           O  
ANISOU 3687  O   ALA A 483     1104   2299   1821   -427   -120    571       O  
ATOM   3688  CB  ALA A 483      38.835  29.420  43.391  1.00 13.72           C  
ANISOU 3688  CB  ALA A 483      931   2359   1923   -327    -50    558       C  
ATOM   3689  N   PRO A 484      37.192  31.414  45.231  1.00 14.39           N  
ANISOU 3689  N   PRO A 484     1148   2352   1969   -297    -56    626       N  
ATOM   3690  CA  PRO A 484      36.007  32.279  45.261  1.00 13.65           C  
ANISOU 3690  CA  PRO A 484     1111   2189   1886   -296    -71    635       C  
ATOM   3691  C   PRO A 484      36.309  33.747  45.558  1.00 13.58           C  
ANISOU 3691  C   PRO A 484     1173   2193   1793   -342   -113    621       C  
ATOM   3692  O   PRO A 484      35.655  34.624  44.979  1.00 14.88           O  
ANISOU 3692  O   PRO A 484     1389   2308   1957   -377   -143    612       O  
ATOM   3693  CB  PRO A 484      35.142  31.663  46.373  1.00 16.80           C  
ANISOU 3693  CB  PRO A 484     1490   2553   2341   -205    -25    685       C  
ATOM   3694  CG  PRO A 484      36.016  30.809  47.148  1.00 13.72           C  
ANISOU 3694  CG  PRO A 484     1050   2222   1943   -161      8    709       C  
ATOM   3695  CD  PRO A 484      37.087  30.316  46.212  1.00 13.70           C  
ANISOU 3695  CD  PRO A 484     1010   2264   1932   -211     -6    669       C  
ATOM   3696  N   LEU A 485      37.292  34.010  46.411  1.00 14.47           N  
ANISOU 3696  N   LEU A 485     1287   2369   1844   -340   -118    616       N  
ATOM   3697  CA  LEU A 485      37.705  35.384  46.715  1.00 14.25           C  
ANISOU 3697  CA  LEU A 485     1318   2349   1748   -388   -164    591       C  
ATOM   3698  C   LEU A 485      38.325  36.045  45.490  1.00 14.12           C  
ANISOU 3698  C   LEU A 485     1318   2339   1707   -493   -202    569       C  
ATOM   3699  O   LEU A 485      38.058  37.202  45.190  1.00 16.04           O  
ANISOU 3699  O   LEU A 485     1621   2537   1938   -542   -240    561       O  
ATOM   3700  CB  LEU A 485      38.699  35.395  47.879  1.00 14.38           C  
ANISOU 3700  CB  LEU A 485     1317   2443   1705   -361   -163    580       C  
ATOM   3701  CG  LEU A 485      38.101  35.436  49.287  1.00 23.70           C  
ANISOU 3701  CG  LEU A 485     2507   3625   2871   -264   -146    597       C  
ATOM   3702  CD1 LEU A 485      39.194  35.457  50.332  1.00 21.77           C  
ANISOU 3702  CD1 LEU A 485     2239   3476   2556   -236   -151    577       C  
ATOM   3703  CD2 LEU A 485      37.223  36.671  49.433  1.00 19.90           C  
ANISOU 3703  CD2 LEU A 485     2099   3077   2385   -269   -182    578       C  
ATOM   3704  N   ILE A 486      39.169  35.298  44.797  1.00 14.92           N  
ANISOU 3704  N   ILE A 486     1364   2501   1804   -522   -190    562       N  
ATOM   3705  CA  ILE A 486      39.778  35.787  43.575  1.00 18.48           C  
ANISOU 3705  CA  ILE A 486     1816   2978   2227   -614   -217    551       C  
ATOM   3706  C   ILE A 486      38.718  36.244  42.579  1.00 16.67           C  
ANISOU 3706  C   ILE A 486     1626   2680   2028   -634   -232    561       C  
ATOM   3707  O   ILE A 486      38.772  37.370  42.086  1.00 14.34           O  
ANISOU 3707  O   ILE A 486     1378   2363   1707   -700   -266    568       O  
ATOM   3708  CB  ILE A 486      40.655  34.711  42.940  1.00 18.47           C  
ANISOU 3708  CB  ILE A 486     1740   3058   2220   -619   -195    538       C  
ATOM   3709  CG1 ILE A 486      41.934  34.545  43.770  1.00 16.00           C  
ANISOU 3709  CG1 ILE A 486     1392   2829   1859   -620   -192    527       C  
ATOM   3710  CG2 ILE A 486      40.970  35.060  41.477  1.00 14.35           C  
ANISOU 3710  CG2 ILE A 486     1212   2567   1673   -695   -215    534       C  
ATOM   3711  CD1 ILE A 486      42.673  33.239  43.506  1.00 19.96           C  
ANISOU 3711  CD1 ILE A 486     1814   3404   2365   -589   -162    515       C  
ATOM   3712  N   SER A 487      37.739  35.383  42.320  1.00 14.33           N  
ANISOU 3712  N   SER A 487     1308   2346   1792   -575   -207    564       N  
ATOM   3713  CA  SER A 487      36.710  35.674  41.316  1.00 17.16           C  
ANISOU 3713  CA  SER A 487     1691   2651   2179   -584   -222    567       C  
ATOM   3714  C   SER A 487      35.813  36.826  41.705  1.00 13.75           C  
ANISOU 3714  C   SER A 487     1335   2141   1748   -582   -246    583       C  
ATOM   3715  O   SER A 487      35.417  37.607  40.847  1.00 14.23           O  
ANISOU 3715  O   SER A 487     1435   2173   1799   -621   -274    591       O  
ATOM   3716  CB  SER A 487      35.845  34.444  41.050  1.00 13.45           C  
ANISOU 3716  CB  SER A 487     1170   2154   1785   -519   -193    557       C  
ATOM   3717  OG  SER A 487      36.629  33.388  40.515  1.00 17.15           O  
ANISOU 3717  OG  SER A 487     1568   2688   2260   -519   -178    532       O  
ATOM   3718  N   ALA A 488      35.505  36.943  42.997  1.00 13.73           N  
ANISOU 3718  N   ALA A 488     1353   2110   1753   -529   -236    589       N  
ATOM   3719  CA  ALA A 488      34.613  37.999  43.465  1.00 13.84           C  
ANISOU 3719  CA  ALA A 488     1437   2052   1769   -512   -260    595       C  
ATOM   3720  C   ALA A 488      35.285  39.355  43.365  1.00 14.25           C  
ANISOU 3720  C   ALA A 488     1545   2095   1774   -587   -307    588       C  
ATOM   3721  O   ALA A 488      34.656  40.342  43.006  1.00 21.76           O  
ANISOU 3721  O   ALA A 488     2555   2982   2730   -606   -339    595       O  
ATOM   3722  CB  ALA A 488      34.167  37.731  44.906  1.00 13.82           C  
ANISOU 3722  CB  ALA A 488     1432   2041   1778   -426   -235    600       C  
ATOM   3723  N   LEU A 489      36.568  39.421  43.695  1.00 14.48           N  
ANISOU 3723  N   LEU A 489     1554   2185   1762   -630   -313    575       N  
ATOM   3724  CA  LEU A 489      37.257  40.697  43.597  1.00 14.99           C  
ANISOU 3724  CA  LEU A 489     1664   2235   1798   -711   -360    569       C  
ATOM   3725  C   LEU A 489      37.426  41.108  42.136  1.00 19.67           C  
ANISOU 3725  C   LEU A 489     2263   2825   2385   -791   -375    598       C  
ATOM   3726  O   LEU A 489      37.352  42.295  41.793  1.00 16.56           O  
ANISOU 3726  O   LEU A 489     1924   2374   1992   -846   -413    615       O  
ATOM   3727  CB  LEU A 489      38.604  40.643  44.307  1.00 15.28           C  
ANISOU 3727  CB  LEU A 489     1666   2344   1795   -739   -364    544       C  
ATOM   3728  CG  LEU A 489      38.543  41.216  45.729  1.00 21.57           C  
ANISOU 3728  CG  LEU A 489     2494   3121   2580   -692   -386    508       C  
ATOM   3729  CD1 LEU A 489      37.556  40.432  46.597  1.00 15.20           C  
ANISOU 3729  CD1 LEU A 489     1677   2309   1787   -574   -348    512       C  
ATOM   3730  CD2 LEU A 489      39.929  41.281  46.386  1.00 15.97           C  
ANISOU 3730  CD2 LEU A 489     1750   2490   1830   -725   -400    474       C  
ATOM   3731  N   LEU A 490      37.636  40.127  41.270  1.00 14.90           N  
ANISOU 3731  N   LEU A 490     1600   2284   1776   -792   -346    606       N  
ATOM   3732  CA  LEU A 490      37.742  40.415  39.847  1.00 18.31           C  
ANISOU 3732  CA  LEU A 490     2029   2736   2191   -852   -356    635       C  
ATOM   3733  C   LEU A 490      36.406  40.893  39.307  1.00 16.89           C  
ANISOU 3733  C   LEU A 490     1900   2478   2039   -825   -370    654       C  
ATOM   3734  O   LEU A 490      36.356  41.717  38.397  1.00 20.80           O  
ANISOU 3734  O   LEU A 490     2426   2958   2518   -877   -394    690       O  
ATOM   3735  CB  LEU A 490      38.216  39.181  39.091  1.00 14.90           C  
ANISOU 3735  CB  LEU A 490     1517   2398   1745   -843   -325    623       C  
ATOM   3736  CG  LEU A 490      39.673  38.854  39.408  1.00 20.30           C  
ANISOU 3736  CG  LEU A 490     2150   3172   2391   -881   -315    611       C  
ATOM   3737  CD1 LEU A 490      40.083  37.572  38.743  1.00 19.20           C  
ANISOU 3737  CD1 LEU A 490     1931   3121   2242   -856   -286    590       C  
ATOM   3738  CD2 LEU A 490      40.601  40.011  39.005  1.00 19.66           C  
ANISOU 3738  CD2 LEU A 490     2087   3112   2270   -985   -343    641       C  
ATOM   3739  N   GLY A 491      35.323  40.391  39.893  1.00 14.65           N  
ANISOU 3739  N   GLY A 491     1622   2147   1797   -742   -356    636       N  
ATOM   3740  CA  GLY A 491      33.991  40.886  39.588  1.00 14.63           C  
ANISOU 3740  CA  GLY A 491     1667   2068   1823   -706   -371    648       C  
ATOM   3741  C   GLY A 491      33.864  42.372  39.892  1.00 18.96           C  
ANISOU 3741  C   GLY A 491     2298   2540   2367   -739   -413    665       C  
ATOM   3742  O   GLY A 491      33.293  43.125  39.094  1.00 21.08           O  
ANISOU 3742  O   GLY A 491     2608   2764   2636   -756   -438    695       O  
ATOM   3743  N   TYR A 492      34.394  42.794  41.039  1.00 15.27           N  
ANISOU 3743  N   TYR A 492     1850   2056   1894   -743   -425    644       N  
ATOM   3744  CA  TYR A 492      34.446  44.210  41.405  1.00 15.85           C  
ANISOU 3744  CA  TYR A 492     1997   2053   1973   -779   -472    647       C  
ATOM   3745  C   TYR A 492      35.192  45.031  40.362  1.00 18.27           C  
ANISOU 3745  C   TYR A 492     2319   2359   2266   -882   -497    691       C  
ATOM   3746  O   TYR A 492      34.788  46.143  40.044  1.00 19.85           O  
ANISOU 3746  O   TYR A 492     2580   2476   2485   -907   -533    718       O  
ATOM   3747  CB  TYR A 492      35.133  44.419  42.777  1.00 16.05           C  
ANISOU 3747  CB  TYR A 492     2024   2085   1989   -771   -483    602       C  
ATOM   3748  CG  TYR A 492      34.382  43.854  43.977  1.00 17.35           C  
ANISOU 3748  CG  TYR A 492     2182   2251   2160   -663   -462    568       C  
ATOM   3749  CD1 TYR A 492      32.998  43.760  43.980  1.00 15.45           C  
ANISOU 3749  CD1 TYR A 492     1963   1960   1946   -589   -452    576       C  
ATOM   3750  CD2 TYR A 492      35.064  43.443  45.114  1.00 15.71           C  
ANISOU 3750  CD2 TYR A 492     1942   2101   1929   -633   -450    534       C  
ATOM   3751  CE1 TYR A 492      32.303  43.238  45.078  1.00 18.34           C  
ANISOU 3751  CE1 TYR A 492     2316   2336   2318   -489   -426    557       C  
ATOM   3752  CE2 TYR A 492      34.384  42.933  46.222  1.00 18.82           C  
ANISOU 3752  CE2 TYR A 492     2325   2507   2321   -528   -425    517       C  
ATOM   3753  CZ  TYR A 492      32.995  42.832  46.200  1.00 16.76           C  
ANISOU 3753  CZ  TYR A 492     2082   2196   2089   -458   -411    532       C  
ATOM   3754  OH  TYR A 492      32.314  42.324  47.287  1.00 15.17           O  
ANISOU 3754  OH  TYR A 492     1862   2014   1885   -355   -381    527       O  
ATOM   3755  N   ASP A 493      36.312  44.498  39.871  1.00 19.18           N  
ANISOU 3755  N   ASP A 493     2373   2565   2349   -939   -477    702       N  
ATOM   3756  CA  ASP A 493      37.138  45.223  38.917  1.00 20.59           C  
ANISOU 3756  CA  ASP A 493     2553   2761   2511  -1040   -493    754       C  
ATOM   3757  C   ASP A 493      36.438  45.351  37.568  1.00 21.25           C  
ANISOU 3757  C   ASP A 493     2646   2843   2583  -1039   -490    808       C  
ATOM   3758  O   ASP A 493      36.552  46.378  36.887  1.00 17.88           O  
ANISOU 3758  O   ASP A 493     2257   2378   2159  -1101   -514    868       O  
ATOM   3759  CB  ASP A 493      38.493  44.546  38.731  1.00 20.80           C  
ANISOU 3759  CB  ASP A 493     2502   2904   2498  -1092   -468    750       C  
ATOM   3760  CG  ASP A 493      39.388  45.308  37.752  1.00 24.94           C  
ANISOU 3760  CG  ASP A 493     3017   3456   3002  -1199   -479    814       C  
ATOM   3761  OD1 ASP A 493      39.859  46.410  38.111  1.00 23.52           O  
ANISOU 3761  OD1 ASP A 493     2874   3212   2851  -1267   -513    829       O  
ATOM   3762  OD2 ASP A 493      39.603  44.809  36.622  1.00 19.61           O  
ANISOU 3762  OD2 ASP A 493     2296   2869   2286  -1213   -455    850       O  
ATOM   3763  N   ILE A 494      35.744  44.289  37.175  1.00 21.56           N  
ANISOU 3763  N   ILE A 494     2649   2928   2614   -969   -462    789       N  
ATOM   3764  CA  ILE A 494      34.898  44.314  35.986  1.00 22.60           C  
ANISOU 3764  CA  ILE A 494     2787   3065   2735   -947   -464    823       C  
ATOM   3765  C   ILE A 494      33.927  45.489  36.068  1.00 21.87           C  
ANISOU 3765  C   ILE A 494     2780   2856   2674   -932   -499    851       C  
ATOM   3766  O   ILE A 494      33.796  46.270  35.128  1.00 17.58           O  
ANISOU 3766  O   ILE A 494     2265   2297   2116   -966   -517    914       O  
ATOM   3767  CB  ILE A 494      34.098  42.997  35.823  1.00 26.37           C  
ANISOU 3767  CB  ILE A 494     3213   3584   3222   -861   -436    776       C  
ATOM   3768  CG1 ILE A 494      34.988  41.892  35.247  1.00 23.54           C  
ANISOU 3768  CG1 ILE A 494     2768   3348   2827   -874   -407    756       C  
ATOM   3769  CG2 ILE A 494      32.884  43.210  34.933  1.00 16.06           C  
ANISOU 3769  CG2 ILE A 494     1929   2252   1919   -817   -450    794       C  
ATOM   3770  CD1 ILE A 494      34.255  40.573  35.040  1.00 21.01           C  
ANISOU 3770  CD1 ILE A 494     2392   3058   2534   -795   -385    703       C  
ATOM   3771  N   ILE A 495      33.285  45.626  37.222  1.00 16.73           N  
ANISOU 3771  N   ILE A 495     2167   2127   2063   -878   -510    808       N  
ATOM   3772  CA  ILE A 495      32.295  46.673  37.442  1.00 19.13           C  
ANISOU 3772  CA  ILE A 495     2550   2318   2400   -848   -545    820       C  
ATOM   3773  C   ILE A 495      32.994  48.038  37.485  1.00 20.62           C  
ANISOU 3773  C   ILE A 495     2794   2437   2605   -931   -585    860       C  
ATOM   3774  O   ILE A 495      32.512  49.004  36.894  1.00 18.49           O  
ANISOU 3774  O   ILE A 495     2580   2097   2350   -943   -613    911       O  
ATOM   3775  CB  ILE A 495      31.471  46.412  38.755  1.00 17.84           C  
ANISOU 3775  CB  ILE A 495     2403   2105   2269   -760   -543    759       C  
ATOM   3776  CG1 ILE A 495      30.551  45.198  38.559  1.00 17.95           C  
ANISOU 3776  CG1 ILE A 495     2365   2165   2289   -681   -507    737       C  
ATOM   3777  CG2 ILE A 495      30.656  47.639  39.143  1.00 20.19           C  
ANISOU 3777  CG2 ILE A 495     2786   2287   2600   -733   -587    761       C  
ATOM   3778  CD1 ILE A 495      29.896  44.650  39.823  1.00 15.49           C  
ANISOU 3778  CD1 ILE A 495     2044   1835   2006   -598   -488    690       C  
ATOM   3779  N   TYR A 496      34.151  48.095  38.140  1.00 18.09           N  
ANISOU 3779  N   TYR A 496     2453   2136   2284   -989   -586    838       N  
ATOM   3780  CA  TYR A 496      34.965  49.311  38.168  1.00 19.02           C  
ANISOU 3780  CA  TYR A 496     2608   2190   2429  -1081   -624    871       C  
ATOM   3781  C   TYR A 496      35.305  49.785  36.748  1.00 19.65           C  
ANISOU 3781  C   TYR A 496     2683   2292   2492  -1155   -621    970       C  
ATOM   3782  O   TYR A 496      35.082  50.941  36.404  1.00 20.45           O  
ANISOU 3782  O   TYR A 496     2843   2297   2630  -1189   -654   1025       O  
ATOM   3783  CB  TYR A 496      36.249  49.067  38.948  1.00 19.08           C  
ANISOU 3783  CB  TYR A 496     2571   2249   2430  -1133   -620    829       C  
ATOM   3784  CG  TYR A 496      37.075  50.308  39.217  1.00 20.11           C  
ANISOU 3784  CG  TYR A 496     2732   2301   2606  -1227   -665    841       C  
ATOM   3785  CD1 TYR A 496      36.571  51.347  40.001  1.00 20.62           C  
ANISOU 3785  CD1 TYR A 496     2870   2235   2730  -1207   -718    804       C  
ATOM   3786  CD2 TYR A 496      38.368  50.434  38.712  1.00 27.60           C  
ANISOU 3786  CD2 TYR A 496     3633   3308   3545  -1334   -658    885       C  
ATOM   3787  CE1 TYR A 496      37.337  52.481  40.276  1.00 24.75           C  
ANISOU 3787  CE1 TYR A 496     3418   2674   3312  -1295   -766    805       C  
ATOM   3788  CE2 TYR A 496      39.139  51.572  38.974  1.00 29.41           C  
ANISOU 3788  CE2 TYR A 496     3883   3458   3833  -1428   -701    896       C  
ATOM   3789  CZ  TYR A 496      38.612  52.588  39.757  1.00 29.31           C  
ANISOU 3789  CZ  TYR A 496     3944   3304   3890  -1409   -757    853       C  
ATOM   3790  OH  TYR A 496      39.356  53.717  40.027  1.00 34.47           O  
ANISOU 3790  OH  TYR A 496     4614   3868   4614  -1497   -804    851       O  
ATOM   3791  N   GLN A 497      35.841  48.877  35.939  1.00 19.37           N  
ANISOU 3791  N   GLN A 497     2575   2385   2399  -1172   -581    992       N  
ATOM   3792  CA  GLN A 497      36.091  49.132  34.519  1.00 23.94           C  
ANISOU 3792  CA  GLN A 497     3135   3020   2940  -1221   -569   1086       C  
ATOM   3793  C   GLN A 497      34.857  49.638  33.790  1.00 22.67           C  
ANISOU 3793  C   GLN A 497     3028   2803   2784  -1169   -585   1133       C  
ATOM   3794  O   GLN A 497      34.924  50.623  33.057  1.00 21.05           O  
ANISOU 3794  O   GLN A 497     2853   2559   2585  -1209   -600   1216       O  
ATOM   3795  CB  GLN A 497      36.596  47.869  33.825  1.00 19.48           C  
ANISOU 3795  CB  GLN A 497     2479   2615   2306  -1212   -525   1076       C  
ATOM   3796  CG  GLN A 497      38.057  47.547  34.123  1.00 19.61           C  
ANISOU 3796  CG  GLN A 497     2434   2711   2304  -1285   -508   1064       C  
ATOM   3797  CD  GLN A 497      38.577  46.462  33.221  1.00 21.53           C  
ANISOU 3797  CD  GLN A 497     2590   3114   2475  -1277   -468   1066       C  
ATOM   3798  OE1 GLN A 497      38.489  46.561  31.991  1.00 23.53           O  
ANISOU 3798  OE1 GLN A 497     2826   3434   2682  -1284   -458   1130       O  
ATOM   3799  NE2 GLN A 497      39.092  45.400  33.816  1.00 19.69           N  
ANISOU 3799  NE2 GLN A 497     2301   2949   2230  -1253   -446    993       N  
ATOM   3800  N   THR A 498      33.733  48.958  33.977  1.00 19.39           N  
ANISOU 3800  N   THR A 498     2615   2387   2365  -1069   -579   1076       N  
ATOM   3801  CA  THR A 498      32.499  49.357  33.308  1.00 19.56           C  
ANISOU 3801  CA  THR A 498     2680   2365   2387  -1008   -595   1110       C  
ATOM   3802  C   THR A 498      32.105  50.792  33.654  1.00 20.31           C  
ANISOU 3802  C   THR A 498     2867   2309   2540  -1023   -641   1149       C  
ATOM   3803  O   THR A 498      31.800  51.597  32.767  1.00 22.93           O  
ANISOU 3803  O   THR A 498     3235   2610   2869  -1035   -656   1235       O  
ATOM   3804  CB  THR A 498      31.342  48.416  33.664  1.00 18.66           C  
ANISOU 3804  CB  THR A 498     2551   2262   2278   -901   -585   1032       C  
ATOM   3805  OG1 THR A 498      31.677  47.085  33.264  1.00 18.10           O  
ANISOU 3805  OG1 THR A 498     2393   2318   2166   -886   -548    995       O  
ATOM   3806  CG2 THR A 498      30.063  48.850  32.957  1.00 18.90           C  
ANISOU 3806  CG2 THR A 498     2621   2255   2307   -837   -605   1063       C  
ATOM   3807  N   LEU A 499      32.165  51.127  34.939  1.00 20.21           N  
ANISOU 3807  N   LEU A 499     2890   2207   2581  -1020   -663   1087       N  
ATOM   3808  CA  LEU A 499      31.772  52.460  35.400  1.00 20.96           C  
ANISOU 3808  CA  LEU A 499     3072   2149   2742  -1024   -713   1101       C  
ATOM   3809  C   LEU A 499      32.692  53.541  34.841  1.00 22.13           C  
ANISOU 3809  C   LEU A 499     3235   2254   2917  -1125   -729   1183       C  
ATOM   3810  O   LEU A 499      32.239  54.629  34.477  1.00 23.59           O  
ANISOU 3810  O   LEU A 499     3474   2348   3141  -1111   -754   1223       O  
ATOM   3811  CB  LEU A 499      31.775  52.515  36.930  1.00 29.02           C  
ANISOU 3811  CB  LEU A 499     4115   3108   3805   -995   -734   1001       C  
ATOM   3812  CG  LEU A 499      30.738  51.665  37.673  1.00 19.75           C  
ANISOU 3812  CG  LEU A 499     2930   1957   2618   -880   -718    920       C  
ATOM   3813  CD1 LEU A 499      31.110  51.564  39.157  1.00 21.18           C  
ANISOU 3813  CD1 LEU A 499     3109   2120   2818   -862   -728    830       C  
ATOM   3814  CD2 LEU A 499      29.347  52.256  37.489  1.00 19.94           C  
ANISOU 3814  CD2 LEU A 499     3016   1898   2663   -800   -745    930       C  
ATOM   3815  N   MET A 500      33.985  53.239  34.779  1.00 22.24           N  
ANISOU 3815  N   MET A 500     3187   2350   2912  -1201   -704   1185       N  
ATOM   3816  CA  MET A 500      34.953  54.183  34.244  1.00 23.64           C  
ANISOU 3816  CA  MET A 500     3354   2514   3114  -1276   -705   1240       C  
ATOM   3817  C   MET A 500      34.603  54.533  32.789  1.00 26.11           C  
ANISOU 3817  C   MET A 500     3662   2867   3392  -1260   -685   1337       C  
ATOM   3818  O   MET A 500      34.620  55.704  32.414  1.00 27.33           O  
ANISOU 3818  O   MET A 500     3853   2936   3593  -1281   -701   1395       O  
ATOM   3819  CB  MET A 500      36.371  53.625  34.337  1.00 26.49           C  
ANISOU 3819  CB  MET A 500     3638   2982   3447  -1347   -677   1225       C  
ATOM   3820  CG  MET A 500      36.958  53.645  35.741  1.00 24.58           C  
ANISOU 3820  CG  MET A 500     3399   2689   3250  -1380   -703   1140       C  
ATOM   3821  SD  MET A 500      38.746  53.438  35.674  1.00 43.03           S  
ANISOU 3821  SD  MET A 500     5650   5134   5567  -1471   -676   1139       S  
ATOM   3822  CE  MET A 500      38.857  51.809  34.928  1.00 25.00           C  
ANISOU 3822  CE  MET A 500     3284   3042   3174  -1435   -617   1144       C  
ATOM   3823  N   SER A 501      34.258  53.528  31.988  1.00 23.38           N  
ANISOU 3823  N   SER A 501     3271   2647   2965  -1220   -652   1355       N  
ATOM   3824  CA  SER A 501      33.832  53.772  30.609  1.00 29.37           C  
ANISOU 3824  CA  SER A 501     4022   3458   3677  -1193   -636   1442       C  
ATOM   3825  C   SER A 501      32.475  54.453  30.563  1.00 25.71           C  
ANISOU 3825  C   SER A 501     3636   2886   3247  -1120   -667   1456       C  
ATOM   3826  O   SER A 501      32.196  55.215  29.645  1.00 25.08           O  
ANISOU 3826  O   SER A 501     3575   2793   3162  -1107   -665   1536       O  
ATOM   3827  CB  SER A 501      33.768  52.477  29.801  1.00 31.61           C  
ANISOU 3827  CB  SER A 501     4235   3911   3865  -1163   -601   1445       C  
ATOM   3828  OG  SER A 501      35.055  51.922  29.626  1.00 38.52           O  
ANISOU 3828  OG  SER A 501     5033   4901   4701  -1225   -569   1442       O  
ATOM   3829  N   MET A 502      31.623  54.178  31.545  1.00 23.36           N  
ANISOU 3829  N   MET A 502     3381   2515   2979  -1065   -693   1381       N  
ATOM   3830  CA  MET A 502      30.319  54.840  31.574  1.00 23.57           C  
ANISOU 3830  CA  MET A 502     3480   2439   3038   -987   -725   1385       C  
ATOM   3831  C   MET A 502      30.507  56.329  31.825  1.00 24.78           C  
ANISOU 3831  C   MET A 502     3693   2449   3273  -1018   -756   1413       C  
ATOM   3832  O   MET A 502      29.696  57.141  31.403  1.00 30.45           O  
ANISOU 3832  O   MET A 502     4462   3097   4012   -969   -773   1453       O  
ATOM   3833  CB  MET A 502      29.407  54.225  32.635  1.00 22.54           C  
ANISOU 3833  CB  MET A 502     3376   2264   2924   -918   -746   1298       C  
ATOM   3834  CG  MET A 502      28.652  52.996  32.165  1.00 21.62           C  
ANISOU 3834  CG  MET A 502     3214   2260   2743   -850   -724   1279       C  
ATOM   3835  SD  MET A 502      27.726  52.182  33.487  1.00 22.88           S  
ANISOU 3835  SD  MET A 502     3368   2397   2930   -752   -722   1142       S  
ATOM   3836  CE  MET A 502      26.299  53.261  33.626  1.00 21.02           C  
ANISOU 3836  CE  MET A 502     3221   2028   2736   -667   -770   1152       C  
ATOM   3837  N   ASN A 503      31.591  56.693  32.501  1.00 30.28           N  
ANISOU 3837  N   ASN A 503     4382   3103   4018  -1097   -764   1390       N  
ATOM   3838  CA  ASN A 503      31.867  58.101  32.718  1.00 26.44           C  
ANISOU 3838  CA  ASN A 503     3946   2480   3621  -1135   -795   1414       C  
ATOM   3839  C   ASN A 503      32.060  58.819  31.384  1.00 27.64           C  
ANISOU 3839  C   ASN A 503     4087   2652   3764  -1156   -771   1533       C  
ATOM   3840  O   ASN A 503      31.686  59.979  31.238  1.00 28.85           O  
ANISOU 3840  O   ASN A 503     4295   2687   3980  -1145   -794   1574       O  
ATOM   3841  CB  ASN A 503      33.085  58.278  33.617  1.00 26.69           C  
ANISOU 3841  CB  ASN A 503     3957   2480   3704  -1221   -809   1366       C  
ATOM   3842  CG  ASN A 503      32.725  58.257  35.084  1.00 31.93           C  
ANISOU 3842  CG  ASN A 503     4666   3050   4416  -1192   -856   1255       C  
ATOM   3843  OD1 ASN A 503      31.649  58.710  35.476  1.00 31.27           O  
ANISOU 3843  OD1 ASN A 503     4648   2866   4365  -1118   -892   1226       O  
ATOM   3844  ND2 ASN A 503      33.621  57.729  35.904  1.00 29.82           N  
ANISOU 3844  ND2 ASN A 503     4361   2820   4148  -1243   -856   1193       N  
ATOM   3845  N   GLN A 504      32.606  58.107  30.406  1.00 27.49           N  
ANISOU 3845  N   GLN A 504     3997   2786   3662  -1180   -724   1588       N  
ATOM   3846  CA  GLN A 504      32.754  58.651  29.066  1.00 28.85           C  
ANISOU 3846  CA  GLN A 504     4152   3003   3806  -1189   -695   1707       C  
ATOM   3847  C   GLN A 504      31.443  58.568  28.280  1.00 31.34           C  
ANISOU 3847  C   GLN A 504     4495   3343   4069  -1090   -695   1743       C  
ATOM   3848  O   GLN A 504      31.024  59.558  27.681  1.00 33.67           O  
ANISOU 3848  O   GLN A 504     4831   3573   4390  -1067   -699   1820       O  
ATOM   3849  CB  GLN A 504      33.870  57.925  28.311  1.00 28.61           C  
ANISOU 3849  CB  GLN A 504     4031   3140   3701  -1246   -648   1749       C  
ATOM   3850  CG  GLN A 504      34.257  58.576  26.998  1.00 41.07           C  
ANISOU 3850  CG  GLN A 504     5584   4767   5254  -1267   -616   1879       C  
ATOM   3851  CD  GLN A 504      34.735  60.005  27.168  1.00 43.36           C  
ANISOU 3851  CD  GLN A 504     5912   4911   5651  -1326   -630   1936       C  
ATOM   3852  OE1 GLN A 504      34.241  60.918  26.506  1.00 48.31           O  
ANISOU 3852  OE1 GLN A 504     6578   5476   6301  -1300   -630   2023       O  
ATOM   3853  NE2 GLN A 504      35.709  60.206  28.051  1.00 46.35           N  
ANISOU 3853  NE2 GLN A 504     6278   5234   6097  -1406   -644   1888       N  
ATOM   3854  N   THR A 505      30.778  57.408  28.296  1.00 28.05           N  
ANISOU 3854  N   THR A 505     4057   3018   3583  -1029   -690   1687       N  
ATOM   3855  CA  THR A 505      29.606  57.234  27.433  1.00 27.17           C  
ANISOU 3855  CA  THR A 505     3957   2956   3411   -935   -689   1721       C  
ATOM   3856  C   THR A 505      28.403  58.004  27.947  1.00 27.34           C  
ANISOU 3856  C   THR A 505     4063   2832   3493   -863   -730   1696       C  
ATOM   3857  O   THR A 505      27.519  58.365  27.172  1.00 40.31           O  
ANISOU 3857  O   THR A 505     5730   4479   5108   -792   -733   1748       O  
ATOM   3858  CB  THR A 505      29.211  55.748  27.244  1.00 28.22           C  
ANISOU 3858  CB  THR A 505     4034   3230   3457   -889   -677   1667       C  
ATOM   3859  OG1 THR A 505      28.907  55.143  28.510  1.00 27.82           O  
ANISOU 3859  OG1 THR A 505     4000   3124   3445   -876   -698   1562       O  
ATOM   3860  CG2 THR A 505      30.332  54.985  26.538  1.00 25.86           C  
ANISOU 3860  CG2 THR A 505     3647   3094   3084   -946   -636   1696       C  
ATOM   3861  N   ALA A 506      28.366  58.282  29.241  1.00 27.01           N  
ANISOU 3861  N   ALA A 506     4065   2667   3532   -874   -763   1616       N  
ATOM   3862  CA  ALA A 506      27.300  59.132  29.758  1.00 34.03           C  
ANISOU 3862  CA  ALA A 506     5033   3415   4483   -805   -804   1590       C  
ATOM   3863  C   ALA A 506      27.431  60.545  29.174  1.00 35.22           C  
ANISOU 3863  C   ALA A 506     5224   3471   4686   -823   -809   1683       C  
ATOM   3864  O   ALA A 506      26.439  61.159  28.760  1.00 29.57           O  
ANISOU 3864  O   ALA A 506     4555   2705   3975   -747   -822   1717       O  
ATOM   3865  CB  ALA A 506      27.331  59.175  31.286  1.00 29.32           C  
ANISOU 3865  CB  ALA A 506     4472   2713   3957   -812   -841   1483       C  
ATOM   3866  N   ARG A 507      28.666  61.034  29.103  1.00 31.91           N  
ANISOU 3866  N   ARG A 507     4783   3034   4306   -922   -795   1728       N  
ATOM   3867  CA  ARG A 507      28.913  62.365  28.565  1.00 36.38           C  
ANISOU 3867  CA  ARG A 507     5381   3506   4934   -950   -795   1824       C  
ATOM   3868  C   ARG A 507      28.572  62.409  27.080  1.00 37.15           C  
ANISOU 3868  C   ARG A 507     5461   3703   4953   -909   -757   1941       C  
ATOM   3869  O   ARG A 507      27.910  63.338  26.620  1.00 40.82           O  
ANISOU 3869  O   ARG A 507     5977   4091   5444   -860   -766   2005       O  
ATOM   3870  CB  ARG A 507      30.374  62.779  28.770  1.00 42.06           C  
ANISOU 3870  CB  ARG A 507     6068   4201   5712  -1069   -784   1848       C  
ATOM   3871  CG  ARG A 507      30.740  63.323  30.143  1.00 46.60           C  
ANISOU 3871  CG  ARG A 507     6678   4630   6396  -1112   -832   1756       C  
ATOM   3872  CD  ARG A 507      32.262  63.510  30.207  1.00 59.81           C  
ANISOU 3872  CD  ARG A 507     8299   6317   8108  -1232   -815   1781       C  
ATOM   3873  NE  ARG A 507      32.730  64.224  31.396  1.00 67.60           N  
ANISOU 3873  NE  ARG A 507     9317   7160   9211  -1281   -864   1703       N  
ATOM   3874  CZ  ARG A 507      33.078  63.644  32.543  1.00 73.32           C  
ANISOU 3874  CZ  ARG A 507    10029   7887   9942  -1299   -889   1587       C  
ATOM   3875  NH1 ARG A 507      33.496  64.384  33.566  1.00 73.85           N  
ANISOU 3875  NH1 ARG A 507    10123   7821  10114  -1339   -938   1516       N  
ATOM   3876  NH2 ARG A 507      33.016  62.325  32.673  1.00 76.08           N  
ANISOU 3876  NH2 ARG A 507    10339   8372  10196  -1275   -868   1540       N  
ATOM   3877  N   ASP A 508      29.016  61.390  26.347  1.00 32.64           N  
ANISOU 3877  N   ASP A 508     4815   3306   4280   -923   -718   1965       N  
ATOM   3878  CA  ASP A 508      28.779  61.274  24.909  1.00 33.80           C  
ANISOU 3878  CA  ASP A 508     4932   3579   4332   -880   -683   2067       C  
ATOM   3879  C   ASP A 508      27.282  61.248  24.587  1.00 39.05           C  
ANISOU 3879  C   ASP A 508     5640   4241   4957   -758   -703   2059       C  
ATOM   3880  O   ASP A 508      26.866  61.637  23.496  1.00 42.57           O  
ANISOU 3880  O   ASP A 508     6090   4734   5350   -706   -687   2153       O  
ATOM   3881  CB  ASP A 508      29.458  60.018  24.354  1.00 31.41           C  
ANISOU 3881  CB  ASP A 508     4538   3472   3925   -907   -646   2062       C  
ATOM   3882  CG  ASP A 508      30.959  60.020  24.566  1.00 42.70           C  
ANISOU 3882  CG  ASP A 508     5916   4924   5384  -1021   -623   2075       C  
ATOM   3883  OD1 ASP A 508      31.536  61.099  24.803  1.00 47.99           O  
ANISOU 3883  OD1 ASP A 508     6614   5475   6144  -1083   -628   2122       O  
ATOM   3884  OD2 ASP A 508      31.567  58.934  24.496  1.00 40.98           O  
ANISOU 3884  OD2 ASP A 508     5627   4842   5100  -1047   -602   2037       O  
ATOM   3885  N   SER A 509      26.480  60.764  25.531  1.00 36.47           N  
ANISOU 3885  N   SER A 509     5340   3868   4649   -708   -738   1948       N  
ATOM   3886  CA  SER A 509      25.031  60.699  25.352  1.00 35.45           C  
ANISOU 3886  CA  SER A 509     5246   3735   4488   -590   -761   1926       C  
ATOM   3887  C   SER A 509      24.330  61.926  25.931  1.00 35.20           C  
ANISOU 3887  C   SER A 509     5301   3522   4552   -549   -797   1921       C  
ATOM   3888  O   SER A 509      23.107  61.941  26.084  1.00 30.98           O  
ANISOU 3888  O   SER A 509     4801   2959   4010   -451   -824   1881       O  
ATOM   3889  CB  SER A 509      24.470  59.427  25.992  1.00 35.36           C  
ANISOU 3889  CB  SER A 509     5207   3786   4443   -549   -777   1811       C  
ATOM   3890  OG  SER A 509      25.038  58.270  25.396  1.00 39.19           O  
ANISOU 3890  OG  SER A 509     5610   4441   4839   -576   -746   1813       O  
ATOM   3891  N   GLY A 510      25.115  62.942  26.274  1.00 35.49           N  
ANISOU 3891  N   GLY A 510     5367   3437   4681   -625   -800   1956       N  
ATOM   3892  CA  GLY A 510      24.570  64.209  26.720  1.00 40.52           C  
ANISOU 3892  CA  GLY A 510     6082   3899   5414   -592   -835   1960       C  
ATOM   3893  C   GLY A 510      24.165  64.302  28.180  1.00 42.77           C  
ANISOU 3893  C   GLY A 510     6410   4064   5777   -574   -884   1830       C  
ATOM   3894  O   GLY A 510      23.443  65.222  28.562  1.00 43.84           O  
ANISOU 3894  O   GLY A 510     6610   4069   5979   -519   -919   1815       O  
ATOM   3895  N   PHE A 511      24.639  63.375  29.010  1.00 41.19           N  
ANISOU 3895  N   PHE A 511     6174   3908   5568   -615   -888   1738       N  
ATOM   3896  CA  PHE A 511      24.353  63.451  30.439  1.00 35.62           C  
ANISOU 3896  CA  PHE A 511     5507   3099   4930   -597   -934   1616       C  
ATOM   3897  C   PHE A 511      25.514  64.111  31.181  1.00 32.42           C  
ANISOU 3897  C   PHE A 511     5109   2590   4618   -699   -952   1596       C  
ATOM   3898  O   PHE A 511      26.642  63.638  31.126  1.00 33.46           O  
ANISOU 3898  O   PHE A 511     5189   2790   4735   -790   -927   1609       O  
ATOM   3899  CB  PHE A 511      24.061  62.058  31.021  1.00 32.16           C  
ANISOU 3899  CB  PHE A 511     5030   2761   4429   -568   -930   1522       C  
ATOM   3900  CG  PHE A 511      22.773  61.449  30.516  1.00 33.17           C  
ANISOU 3900  CG  PHE A 511     5152   2968   4485   -458   -925   1517       C  
ATOM   3901  CD1 PHE A 511      21.573  61.702  31.163  1.00 30.67           C  
ANISOU 3901  CD1 PHE A 511     4880   2579   4192   -358   -961   1448       C  
ATOM   3902  CD2 PHE A 511      22.763  60.628  29.394  1.00 32.84           C  
ANISOU 3902  CD2 PHE A 511     5052   3076   4348   -451   -888   1575       C  
ATOM   3903  CE1 PHE A 511      20.386  61.143  30.708  1.00 33.72           C  
ANISOU 3903  CE1 PHE A 511     5254   3042   4517   -257   -958   1440       C  
ATOM   3904  CE2 PHE A 511      21.579  60.070  28.928  1.00 31.14           C  
ANISOU 3904  CE2 PHE A 511     4826   2935   4071   -350   -891   1563       C  
ATOM   3905  CZ  PHE A 511      20.389  60.329  29.583  1.00 32.66           C  
ANISOU 3905  CZ  PHE A 511     5062   3053   4295   -255   -925   1497       C  
ATOM   3906  N   GLN A 512      25.217  65.209  31.876  1.00 32.48           N  
ANISOU 3906  N   GLN A 512     5180   2437   4723   -679  -1000   1558       N  
ATOM   3907  CA  GLN A 512      26.210  65.928  32.670  1.00 35.39           C  
ANISOU 3907  CA  GLN A 512     5561   2692   5194   -765  -1030   1523       C  
ATOM   3908  C   GLN A 512      26.365  65.274  34.035  1.00 35.05           C  
ANISOU 3908  C   GLN A 512     5514   2646   5157   -766  -1064   1386       C  
ATOM   3909  O   GLN A 512      26.045  65.876  35.057  1.00 34.69           O  
ANISOU 3909  O   GLN A 512     5518   2480   5183   -731  -1120   1296       O  
ATOM   3910  CB  GLN A 512      25.799  67.389  32.853  1.00 38.76           C  
ANISOU 3910  CB  GLN A 512     6057   2942   5729   -737  -1073   1531       C  
ATOM   3911  CG  GLN A 512      25.688  68.178  31.558  1.00 51.37           C  
ANISOU 3911  CG  GLN A 512     7665   4521   7332   -737  -1040   1676       C  
ATOM   3912  CD  GLN A 512      27.041  68.551  30.993  1.00 61.05           C  
ANISOU 3912  CD  GLN A 512     8852   5750   8596   -859  -1008   1770       C  
ATOM   3913  OE1 GLN A 512      27.672  67.765  30.282  1.00 65.84           O  
ANISOU 3913  OE1 GLN A 512     9395   6500   9121   -907   -957   1830       O  
ATOM   3914  NE2 GLN A 512      27.494  69.761  31.301  1.00 67.70           N  
ANISOU 3914  NE2 GLN A 512     9726   6433   9563   -908  -1037   1782       N  
ATOM   3915  N   VAL A 513      26.857  64.041  34.055  1.00 32.16           N  
ANISOU 3915  N   VAL A 513     5088   2416   4715   -799  -1031   1369       N  
ATOM   3916  CA  VAL A 513      27.007  63.322  35.313  1.00 29.81           C  
ANISOU 3916  CA  VAL A 513     4784   2128   4413   -795  -1056   1251       C  
ATOM   3917  C   VAL A 513      28.345  62.622  35.385  1.00 30.19           C  
ANISOU 3917  C   VAL A 513     4767   2265   4438   -900  -1027   1254       C  
ATOM   3918  O   VAL A 513      29.021  62.435  34.369  1.00 29.58           O  
ANISOU 3918  O   VAL A 513     4639   2274   4324   -962   -979   1346       O  
ATOM   3919  CB  VAL A 513      25.899  62.252  35.516  1.00 28.38           C  
ANISOU 3919  CB  VAL A 513     4600   2030   4152   -694  -1046   1202       C  
ATOM   3920  CG1 VAL A 513      24.510  62.876  35.504  1.00 28.77           C  
ANISOU 3920  CG1 VAL A 513     4708   2006   4217   -579  -1075   1188       C  
ATOM   3921  CG2 VAL A 513      26.004  61.166  34.455  1.00 27.54           C  
ANISOU 3921  CG2 VAL A 513     4428   2087   3948   -708   -985   1271       C  
ATOM   3922  N   SER A 514      28.727  62.244  36.597  1.00 28.79           N  
ANISOU 3922  N   SER A 514     4589   2071   4279   -915  -1056   1152       N  
ATOM   3923  CA  SER A 514      29.870  61.372  36.797  1.00 28.12           C  
ANISOU 3923  CA  SER A 514     4439   2089   4159   -997  -1027   1139       C  
ATOM   3924  C   SER A 514      29.446  60.253  37.731  1.00 34.68           C  
ANISOU 3924  C   SER A 514     5264   2973   4939   -942  -1033   1051       C  
ATOM   3925  O   SER A 514      28.526  60.414  38.541  1.00 33.13           O  
ANISOU 3925  O   SER A 514     5122   2703   4764   -855  -1074    979       O  
ATOM   3926  CB  SER A 514      31.076  62.133  37.356  1.00 29.17           C  
ANISOU 3926  CB  SER A 514     4563   2144   4376  -1093  -1057   1111       C  
ATOM   3927  OG  SER A 514      30.792  62.676  38.627  1.00 43.94           O  
ANISOU 3927  OG  SER A 514     6488   3892   6316  -1056  -1126    998       O  
ATOM   3928  N   LEU A 515      30.113  59.114  37.601  1.00 31.65           N  
ANISOU 3928  N   LEU A 515     4813   2721   4490   -987   -988   1060       N  
ATOM   3929  CA  LEU A 515      29.769  57.933  38.370  1.00 31.61           C  
ANISOU 3929  CA  LEU A 515     4794   2782   4437   -940   -980    995       C  
ATOM   3930  C   LEU A 515      30.952  57.532  39.247  1.00 33.93           C  
ANISOU 3930  C   LEU A 515     5037   3125   4730  -1001   -975    922       C  
ATOM   3931  O   LEU A 515      32.109  57.572  38.816  1.00 30.06           O  
ANISOU 3931  O   LEU A 515     4508   2667   4247  -1110   -962    973       O  
ATOM   3932  CB  LEU A 515      29.346  56.782  37.444  1.00 23.50           C  
ANISOU 3932  CB  LEU A 515     3710   1900   3319   -905   -917   1044       C  
ATOM   3933  CG  LEU A 515      28.069  56.927  36.590  1.00 23.51           C  
ANISOU 3933  CG  LEU A 515     3740   1895   3299   -821   -914   1094       C  
ATOM   3934  CD1 LEU A 515      28.254  57.824  35.380  1.00 24.59           C  
ANISOU 3934  CD1 LEU A 515     3880   2019   3444   -855   -904   1185       C  
ATOM   3935  CD2 LEU A 515      27.558  55.563  36.132  1.00 26.50           C  
ANISOU 3935  CD2 LEU A 515     4054   2419   3596   -767   -862   1087       C  
ATOM   3936  N   GLU A 516      30.652  57.185  40.496  1.00 30.96           N  
ANISOU 3936  N   GLU A 516     4126   3038   4600   -771   -452   1496       N  
ATOM   3937  CA  GLU A 516      31.670  56.775  41.448  1.00 24.14           C  
ANISOU 3937  CA  GLU A 516     3240   2209   3725   -848   -406   1360       C  
ATOM   3938  C   GLU A 516      31.244  55.507  42.179  1.00 26.02           C  
ANISOU 3938  C   GLU A 516     3448   2531   3907   -812   -452   1227       C  
ATOM   3939  O   GLU A 516      30.196  55.469  42.827  1.00 24.14           O  
ANISOU 3939  O   GLU A 516     3202   2223   3746   -763   -474   1175       O  
ATOM   3940  CB  GLU A 516      31.941  57.896  42.456  1.00 28.51           C  
ANISOU 3940  CB  GLU A 516     3790   2615   4427   -900   -331   1294       C  
ATOM   3941  CG  GLU A 516      32.944  57.523  43.535  1.00 31.24           C  
ANISOU 3941  CG  GLU A 516     4110   2992   4768   -985   -304   1156       C  
ATOM   3942  CD  GLU A 516      32.928  58.482  44.718  1.00 34.05           C  
ANISOU 3942  CD  GLU A 516     4464   3223   5252  -1013   -242   1044       C  
ATOM   3943  OE1 GLU A 516      31.918  59.196  44.893  1.00 38.61           O  
ANISOU 3943  OE1 GLU A 516     5058   3691   5921   -957   -223   1052       O  
ATOM   3944  OE2 GLU A 516      33.915  58.505  45.484  1.00 31.69           O  
ANISOU 3944  OE2 GLU A 516     4144   2940   4956  -1092   -213    941       O  
ATOM   3945  N   MET A 517      32.049  54.461  42.055  1.00 23.07           N  
ANISOU 3945  N   MET A 517     3058   2298   3408   -835   -456   1175       N  
ATOM   3946  CA  MET A 517      31.821  53.240  42.805  1.00 22.44           C  
ANISOU 3946  CA  MET A 517     2955   2293   3278   -806   -480   1050       C  
ATOM   3947  C   MET A 517      32.038  53.553  44.286  1.00 27.05           C  
ANISOU 3947  C   MET A 517     3535   2794   3949   -843   -445    934       C  
ATOM   3948  O   MET A 517      33.134  53.983  44.661  1.00 25.19           O  
ANISOU 3948  O   MET A 517     3291   2553   3726   -917   -407    906       O  
ATOM   3949  CB  MET A 517      32.778  52.144  42.321  1.00 23.91           C  
ANISOU 3949  CB  MET A 517     3124   2637   3323   -826   -478   1030       C  
ATOM   3950  CG  MET A 517      32.527  50.748  42.861  1.00 28.58           C  
ANISOU 3950  CG  MET A 517     3694   3315   3851   -784   -497    924       C  
ATOM   3951  SD  MET A 517      33.411  49.540  41.834  1.00 31.43           S  
ANISOU 3951  SD  MET A 517     4036   3851   4054   -793   -491    938       S  
ATOM   3952  CE  MET A 517      32.927  48.017  42.624  1.00 18.53           C  
ANISOU 3952  CE  MET A 517     2380   2277   2383   -736   -498    813       C  
ATOM   3953  N   VAL A 518      31.012  53.373  45.122  1.00 19.97           N  
ANISOU 3953  N   VAL A 518     2642   1832   3113   -795   -455    864       N  
ATOM   3954  CA  VAL A 518      31.151  53.720  46.543  1.00 19.84           C  
ANISOU 3954  CA  VAL A 518     2637   1734   3168   -830   -418    752       C  
ATOM   3955  C   VAL A 518      30.932  52.545  47.515  1.00 23.06           C  
ANISOU 3955  C   VAL A 518     3047   2198   3516   -794   -423    633       C  
ATOM   3956  O   VAL A 518      31.146  52.683  48.721  1.00 21.79           O  
ANISOU 3956  O   VAL A 518     2905   1996   3380   -821   -396    535       O  
ATOM   3957  CB  VAL A 518      30.192  54.870  46.933  1.00 20.57           C  
ANISOU 3957  CB  VAL A 518     2747   1651   3416   -820   -393    765       C  
ATOM   3958  CG1 VAL A 518      30.598  56.152  46.223  1.00 21.76           C  
ANISOU 3958  CG1 VAL A 518     2903   1725   3642   -866   -366    873       C  
ATOM   3959  CG2 VAL A 518      28.754  54.499  46.609  1.00 20.37           C  
ANISOU 3959  CG2 VAL A 518     2715   1598   3428   -730   -426    792       C  
ATOM   3960  N   TYR A 519      30.517  51.398  46.991  1.00 23.14           N  
ANISOU 3960  N   TYR A 519     3043   2302   3446   -735   -451    640       N  
ATOM   3961  CA  TYR A 519      30.492  50.159  47.763  1.00 24.84           C  
ANISOU 3961  CA  TYR A 519     3261   2584   3594   -701   -442    543       C  
ATOM   3962  C   TYR A 519      30.907  49.020  46.847  1.00 20.69           C  
ANISOU 3962  C   TYR A 519     2709   2203   2951   -680   -463    572       C  
ATOM   3963  O   TYR A 519      30.283  48.808  45.821  1.00 25.67           O  
ANISOU 3963  O   TYR A 519     3325   2861   3570   -647   -490    630       O  
ATOM   3964  CB  TYR A 519      29.113  49.885  48.352  1.00 16.91           C  
ANISOU 3964  CB  TYR A 519     2271   1495   2660   -639   -426    489       C  
ATOM   3965  CG  TYR A 519      29.101  48.748  49.351  1.00 16.14           C  
ANISOU 3965  CG  TYR A 519     2193   1437   2504   -607   -394    387       C  
ATOM   3966  CD1 TYR A 519      29.106  47.423  48.932  1.00 15.49           C  
ANISOU 3966  CD1 TYR A 519     2090   1460   2336   -565   -398    377       C  
ATOM   3967  CD2 TYR A 519      29.080  49.001  50.716  1.00 16.19           C  
ANISOU 3967  CD2 TYR A 519     2243   1370   2539   -618   -354    302       C  
ATOM   3968  CE1 TYR A 519      29.094  46.382  49.850  1.00 16.28           C  
ANISOU 3968  CE1 TYR A 519     2213   1585   2389   -529   -356    296       C  
ATOM   3969  CE2 TYR A 519      29.062  47.977  51.633  1.00 15.65           C  
ANISOU 3969  CE2 TYR A 519     2204   1334   2407   -582   -319    222       C  
ATOM   3970  CZ  TYR A 519      29.064  46.670  51.204  1.00 15.00           C  
ANISOU 3970  CZ  TYR A 519     2102   1349   2249   -534   -318    225       C  
ATOM   3971  OH  TYR A 519      29.040  45.645  52.139  1.00 14.57           O  
ANISOU 3971  OH  TYR A 519     2084   1316   2137   -491   -271    155       O  
ATOM   3972  N   PRO A 520      31.984  48.305  47.189  1.00 20.11           N  
ANISOU 3972  N   PRO A 520     2624   2225   2792   -700   -451    529       N  
ATOM   3973  CA  PRO A 520      32.918  48.559  48.298  1.00 21.51           C  
ANISOU 3973  CA  PRO A 520     2810   2399   2965   -744   -438    464       C  
ATOM   3974  C   PRO A 520      33.618  49.915  48.153  1.00 25.92           C  
ANISOU 3974  C   PRO A 520     3361   2903   3584   -823   -437    502       C  
ATOM   3975  O   PRO A 520      33.531  50.521  47.077  1.00 25.41           O  
ANISOU 3975  O   PRO A 520     3288   2819   3546   -840   -441    595       O  
ATOM   3976  CB  PRO A 520      33.930  47.410  48.176  1.00 18.61           C  
ANISOU 3976  CB  PRO A 520     2411   2169   2489   -737   -438    447       C  
ATOM   3977  CG  PRO A 520      33.205  46.332  47.413  1.00 19.23           C  
ANISOU 3977  CG  PRO A 520     2483   2300   2524   -676   -433    466       C  
ATOM   3978  CD  PRO A 520      32.341  47.088  46.436  1.00 19.81           C  
ANISOU 3978  CD  PRO A 520     2559   2315   2651   -676   -454    540       C  
ATOM   3979  N   LEU A 521      34.270  50.370  49.223  1.00 26.44           N  
ANISOU 3979  N   LEU A 521     3433   2944   3670   -870   -430    428       N  
ATOM   3980  CA  LEU A 521      34.922  51.676  49.270  1.00 27.14           C  
ANISOU 3980  CA  LEU A 521     3511   2967   3835   -954   -418    437       C  
ATOM   3981  C   LEU A 521      35.695  51.993  48.000  1.00 23.22           C  
ANISOU 3981  C   LEU A 521     2977   2514   3331   -997   -412    534       C  
ATOM   3982  O   LEU A 521      36.494  51.185  47.520  1.00 22.50           O  
ANISOU 3982  O   LEU A 521     2850   2542   3155   -997   -420    547       O  
ATOM   3983  CB  LEU A 521      35.864  51.756  50.469  1.00 28.53           C  
ANISOU 3983  CB  LEU A 521     3677   3171   3992  -1002   -427    330       C  
ATOM   3984  CG  LEU A 521      35.192  51.831  51.839  1.00 28.64           C  
ANISOU 3984  CG  LEU A 521     3744   3114   4022   -981   -420    230       C  
ATOM   3985  CD1 LEU A 521      36.249  51.850  52.925  1.00 28.43           C  
ANISOU 3985  CD1 LEU A 521     3707   3146   3949  -1028   -446    127       C  
ATOM   3986  CD2 LEU A 521      34.302  53.055  51.926  1.00 29.73           C  
ANISOU 3986  CD2 LEU A 521     3916   3090   4291  -1005   -382    238       C  
ATOM   3987  N   ASN A 522      35.441  53.173  47.457  1.00 20.50           N  
ANISOU 3987  N   ASN A 522     2645   2066   3079  -1032   -387    604       N  
ATOM   3988  CA  ASN A 522      36.096  53.590  46.231  1.00 21.42           C  
ANISOU 3988  CA  ASN A 522     2742   2206   3191  -1072   -365    709       C  
ATOM   3989  C   ASN A 522      37.618  53.488  46.323  1.00 25.62           C  
ANISOU 3989  C   ASN A 522     3221   2818   3694  -1145   -351    669       C  
ATOM   3990  O   ASN A 522      38.275  52.988  45.402  1.00 20.87           O  
ANISOU 3990  O   ASN A 522     2594   2309   3026  -1152   -340    724       O  
ATOM   3991  CB  ASN A 522      35.693  55.013  45.883  1.00 24.12           C  
ANISOU 3991  CB  ASN A 522     3109   2400   3654  -1102   -328    783       C  
ATOM   3992  CG  ASN A 522      36.241  55.453  44.547  1.00 29.96           C  
ANISOU 3992  CG  ASN A 522     3846   3154   4381  -1133   -295    910       C  
ATOM   3993  OD1 ASN A 522      37.322  56.040  44.467  1.00 32.76           O  
ANISOU 3993  OD1 ASN A 522     4175   3496   4775  -1214   -247    909       O  
ATOM   3994  ND2 ASN A 522      35.509  55.153  43.488  1.00 22.33           N  
ANISOU 3994  ND2 ASN A 522     2909   2218   3359  -1068   -319   1017       N  
ATOM   3995  N   ASP A 523      38.170  53.925  47.451  1.00 22.05           N  
ANISOU 3995  N   ASP A 523     2749   2335   3294  -1199   -350    564       N  
ATOM   3996  CA  ASP A 523      39.617  53.898  47.642  1.00 21.68           C  
ANISOU 3996  CA  ASP A 523     2636   2362   3240  -1271   -346    511       C  
ATOM   3997  C   ASP A 523      40.179  52.483  47.505  1.00 20.91           C  
ANISOU 3997  C   ASP A 523     2501   2421   3024  -1226   -379    496       C  
ATOM   3998  O   ASP A 523      41.230  52.282  46.895  1.00 25.06           O  
ANISOU 3998  O   ASP A 523     2969   3019   3532  -1265   -359    519       O  
ATOM   3999  CB  ASP A 523      39.978  54.490  49.007  1.00 31.08           C  
ANISOU 3999  CB  ASP A 523     3812   3507   4490  -1326   -361    380       C  
ATOM   4000  CG  ASP A 523      41.463  54.391  49.318  1.00 33.53           C  
ANISOU 4000  CG  ASP A 523     4038   3907   4794  -1395   -376    307       C  
ATOM   4001  OD1 ASP A 523      42.257  55.119  48.686  1.00 34.95           O  
ANISOU 4001  OD1 ASP A 523     4172   4058   5049  -1474   -327    339       O  
ATOM   4002  OD2 ASP A 523      41.831  53.594  50.207  1.00 36.00           O  
ANISOU 4002  OD2 ASP A 523     4328   4315   5033  -1367   -435    219       O  
ATOM   4003  N   LEU A 524      39.470  51.501  48.060  1.00 23.84           N  
ANISOU 4003  N   LEU A 524     2902   2834   3322  -1144   -416    458       N  
ATOM   4004  CA  LEU A 524      39.901  50.102  48.006  1.00 19.24           C  
ANISOU 4004  CA  LEU A 524     2288   2385   2636  -1091   -438    443       C  
ATOM   4005  C   LEU A 524      39.863  49.508  46.590  1.00 18.97           C  
ANISOU 4005  C   LEU A 524     2248   2410   2548  -1068   -409    540       C  
ATOM   4006  O   LEU A 524      40.767  48.773  46.189  1.00 25.47           O  
ANISOU 4006  O   LEU A 524     3020   3335   3322  -1072   -399    544       O  
ATOM   4007  CB  LEU A 524      39.026  49.259  48.947  1.00 18.38           C  
ANISOU 4007  CB  LEU A 524     2226   2283   2475  -1008   -465    385       C  
ATOM   4008  CG  LEU A 524      39.192  49.514  50.451  1.00 18.65           C  
ANISOU 4008  CG  LEU A 524     2274   2296   2518  -1018   -496    277       C  
ATOM   4009  CD1 LEU A 524      38.310  48.591  51.272  1.00 18.64           C  
ANISOU 4009  CD1 LEU A 524     2329   2298   2454   -929   -504    235       C  
ATOM   4010  CD2 LEU A 524      40.647  49.350  50.865  1.00 19.23           C  
ANISOU 4010  CD2 LEU A 524     2273   2467   2568  -1061   -529    224       C  
ATOM   4011  N   ILE A 525      38.810  49.809  45.840  1.00 18.87           N  
ANISOU 4011  N   ILE A 525     2286   2337   2545  -1041   -399    615       N  
ATOM   4012  CA  ILE A 525      38.682  49.309  44.464  1.00 22.38           C  
ANISOU 4012  CA  ILE A 525     2737   2843   2925  -1020   -379    703       C  
ATOM   4013  C   ILE A 525      39.729  49.957  43.553  1.00 26.48           C  
ANISOU 4013  C   ILE A 525     3229   3372   3460  -1096   -332    770       C  
ATOM   4014  O   ILE A 525      40.326  49.310  42.686  1.00 19.78           O  
ANISOU 4014  O   ILE A 525     2359   2614   2544  -1102   -303    804       O  
ATOM   4015  CB  ILE A 525      37.281  49.576  43.904  1.00 24.63           C  
ANISOU 4015  CB  ILE A 525     3079   3064   3217   -970   -395    767       C  
ATOM   4016  CG1 ILE A 525      36.217  48.946  44.804  1.00 23.39           C  
ANISOU 4016  CG1 ILE A 525     2943   2883   3062   -899   -426    695       C  
ATOM   4017  CG2 ILE A 525      37.148  49.027  42.485  1.00 20.92           C  
ANISOU 4017  CG2 ILE A 525     2618   2671   2658   -949   -386    849       C  
ATOM   4018  CD1 ILE A 525      36.370  47.435  44.970  1.00 20.31           C  
ANISOU 4018  CD1 ILE A 525     2531   2600   2583   -849   -426    640       C  
ATOM   4019  N   TYR A 526      39.946  51.247  43.765  1.00 30.13           N  
ANISOU 4019  N   TYR A 526     3694   3733   4019  -1159   -312    783       N  
ATOM   4020  CA  TYR A 526      41.010  51.970  43.082  1.00 27.31           C  
ANISOU 4020  CA  TYR A 526     3308   3365   3704  -1242   -251    832       C  
ATOM   4021  C   TYR A 526      42.350  51.259  43.305  1.00 27.83           C  
ANISOU 4021  C   TYR A 526     3291   3537   3747  -1277   -239    765       C  
ATOM   4022  O   TYR A 526      43.103  50.998  42.359  1.00 22.07           O  
ANISOU 4022  O   TYR A 526     2536   2866   2984  -1305   -187    814       O  
ATOM   4023  CB  TYR A 526      41.066  53.416  43.590  1.00 30.48           C  
ANISOU 4023  CB  TYR A 526     3714   3629   4236  -1307   -226    823       C  
ATOM   4024  CG  TYR A 526      42.227  54.222  43.071  1.00 29.07           C  
ANISOU 4024  CG  TYR A 526     3496   3422   4127  -1403   -150    854       C  
ATOM   4025  CD1 TYR A 526      42.229  54.705  41.764  1.00 28.72           C  
ANISOU 4025  CD1 TYR A 526     3494   3346   4074  -1418    -83    986       C  
ATOM   4026  CD2 TYR A 526      43.312  54.515  43.882  1.00 26.96           C  
ANISOU 4026  CD2 TYR A 526     3151   3158   3935  -1479   -142    749       C  
ATOM   4027  CE1 TYR A 526      43.293  55.456  41.272  1.00 30.72           C  
ANISOU 4027  CE1 TYR A 526     3715   3559   4399  -1509      8   1018       C  
ATOM   4028  CE2 TYR A 526      44.384  55.264  43.399  1.00 33.27           C  
ANISOU 4028  CE2 TYR A 526     3903   3922   4817  -1574    -61    768       C  
ATOM   4029  CZ  TYR A 526      44.367  55.725  42.093  1.00 35.42           C  
ANISOU 4029  CZ  TYR A 526     4221   4151   5086  -1589     22    904       C  
ATOM   4030  OH  TYR A 526      45.421  56.463  41.610  1.00 44.49           O  
ANISOU 4030  OH  TYR A 526     5331   5254   6317  -1665    124    912       O  
ATOM   4031  N   LYS A 527      42.625  50.927  44.562  1.00 21.30           N  
ANISOU 4031  N   LYS A 527     2424   2735   2935  -1269   -289    654       N  
ATOM   4032  CA  LYS A 527      43.871  50.269  44.940  1.00 26.57           C  
ANISOU 4032  CA  LYS A 527     3002   3503   3592  -1290   -296    585       C  
ATOM   4033  C   LYS A 527      43.959  48.870  44.323  1.00 23.88           C  
ANISOU 4033  C   LYS A 527     2649   3276   3148  -1228   -287    611       C  
ATOM   4034  O   LYS A 527      45.019  48.467  43.834  1.00 21.12           O  
ANISOU 4034  O   LYS A 527     2232   2997   2795  -1258   -249    614       O  
ATOM   4035  CB  LYS A 527      43.992  50.206  46.471  1.00 21.30           C  
ANISOU 4035  CB  LYS A 527     2309   2842   2942  -1280   -366    468       C  
ATOM   4036  CG  LYS A 527      44.317  51.543  47.118  1.00 22.30           C  
ANISOU 4036  CG  LYS A 527     2418   2876   3179  -1367   -366    412       C  
ATOM   4037  CD  LYS A 527      44.352  51.442  48.635  1.00 38.97           C  
ANISOU 4037  CD  LYS A 527     4520   5005   5282  -1353   -441    290       C  
ATOM   4038  CE  LYS A 527      44.599  52.796  49.291  1.00 39.26           C  
ANISOU 4038  CE  LYS A 527     4543   4945   5429  -1446   -437    217       C  
ATOM   4039  NZ  LYS A 527      46.018  53.192  49.309  1.00 45.01           N  
ANISOU 4039  NZ  LYS A 527     5162   5712   6229  -1538   -431    161       N  
ATOM   4040  N   LEU A 528      42.839  48.150  44.311  1.00 22.77           N  
ANISOU 4040  N   LEU A 528     2570   3146   2937  -1145   -313    624       N  
ATOM   4041  CA  LEU A 528      42.768  46.835  43.675  1.00 19.13           C  
ANISOU 4041  CA  LEU A 528     2105   2779   2384  -1087   -295    642       C  
ATOM   4042  C   LEU A 528      43.117  46.933  42.189  1.00 21.63           C  
ANISOU 4042  C   LEU A 528     2427   3121   2671  -1127   -227    728       C  
ATOM   4043  O   LEU A 528      43.937  46.168  41.665  1.00 20.17           O  
ANISOU 4043  O   LEU A 528     2194   3020   2451  -1133   -183    727       O  
ATOM   4044  CB  LEU A 528      41.361  46.225  43.836  1.00 18.72           C  
ANISOU 4044  CB  LEU A 528     2121   2712   2281  -1003   -325    639       C  
ATOM   4045  CG  LEU A 528      41.060  44.998  42.966  1.00 17.67           C  
ANISOU 4045  CG  LEU A 528     1995   2659   2060   -952   -297    661       C  
ATOM   4046  CD1 LEU A 528      41.949  43.798  43.338  1.00 20.61           C  
ANISOU 4046  CD1 LEU A 528     2303   3123   2405   -924   -278    607       C  
ATOM   4047  CD2 LEU A 528      39.561  44.613  42.977  1.00 16.97           C  
ANISOU 4047  CD2 LEU A 528     1967   2537   1942   -883   -323    658       C  
ATOM   4048  N   HIS A 529      42.484  47.881  41.511  1.00 20.13           N  
ANISOU 4048  N   HIS A 529     2299   2857   2493  -1149   -214    806       N  
ATOM   4049  CA  HIS A 529      42.717  48.049  40.071  1.00 23.61           C  
ANISOU 4049  CA  HIS A 529     2767   3318   2885  -1181   -150    901       C  
ATOM   4050  C   HIS A 529      44.203  48.302  39.803  1.00 29.49           C  
ANISOU 4050  C   HIS A 529     3442   4086   3678  -1262    -78    898       C  
ATOM   4051  O   HIS A 529      44.801  47.719  38.886  1.00 23.34           O  
ANISOU 4051  O   HIS A 529     2649   3377   2842  -1277    -14    926       O  
ATOM   4052  CB  HIS A 529      41.867  49.190  39.509  1.00 21.41           C  
ANISOU 4052  CB  HIS A 529     2566   2944   2623  -1189   -152    995       C  
ATOM   4053  CG  HIS A 529      41.925  49.308  38.017  1.00 22.19           C  
ANISOU 4053  CG  HIS A 529     2716   3072   2644  -1205    -96   1104       C  
ATOM   4054  ND1 HIS A 529      41.501  48.303  37.173  1.00 24.63           N  
ANISOU 4054  ND1 HIS A 529     3054   3476   2828  -1159    -99   1121       N  
ATOM   4055  CD2 HIS A 529      42.360  50.312  37.217  1.00 23.42           C  
ANISOU 4055  CD2 HIS A 529     2903   3173   2821  -1263    -28   1199       C  
ATOM   4056  CE1 HIS A 529      41.663  48.688  35.920  1.00 29.49           C  
ANISOU 4056  CE1 HIS A 529     3723   4103   3378  -1187    -45   1222       C  
ATOM   4057  NE2 HIS A 529      42.184  49.901  35.920  1.00 23.82           N  
ANISOU 4057  NE2 HIS A 529     3011   3293   2747  -1247      3   1278       N  
ATOM   4058  N   ASN A 530      44.800  49.152  40.631  1.00 29.58           N  
ANISOU 4058  N   ASN A 530     3405   4035   3798  -1317    -85    853       N  
ATOM   4059  CA  ASN A 530      46.210  49.480  40.481  1.00 32.20           C  
ANISOU 4059  CA  ASN A 530     3654   4377   4202  -1400    -19    835       C  
ATOM   4060  C   ASN A 530      47.096  48.262  40.726  1.00 28.47           C  
ANISOU 4060  C   ASN A 530     3091   4019   3708  -1380    -19    766       C  
ATOM   4061  O   ASN A 530      48.087  48.052  40.014  1.00 27.90           O  
ANISOU 4061  O   ASN A 530     2965   3987   3647  -1425     60    781       O  
ATOM   4062  CB  ASN A 530      46.589  50.624  41.421  1.00 34.07           C  
ANISOU 4062  CB  ASN A 530     3851   4526   4570  -1465    -37    779       C  
ATOM   4063  CG  ASN A 530      46.000  51.952  40.982  1.00 40.73           C  
ANISOU 4063  CG  ASN A 530     4770   5240   5465  -1502      2    861       C  
ATOM   4064  OD1 ASN A 530      45.706  52.155  39.804  1.00 39.30           O  
ANISOU 4064  OD1 ASN A 530     4655   5042   5234  -1501     61    973       O  
ATOM   4065  ND2 ASN A 530      45.835  52.869  41.929  1.00 41.83           N  
ANISOU 4065  ND2 ASN A 530     4902   5288   5703  -1534    -29    806       N  
ATOM   4066  N   GLY A 531      46.736  47.465  41.731  1.00 21.96           N  
ANISOU 4066  N   GLY A 531     2250   3238   2855  -1309   -100    694       N  
ATOM   4067  CA  GLY A 531      47.461  46.247  42.046  1.00 22.98           C  
ANISOU 4067  CA  GLY A 531     2299   3469   2962  -1270   -106    638       C  
ATOM   4068  C   GLY A 531      47.426  45.223  40.920  1.00 23.69           C  
ANISOU 4068  C   GLY A 531     2408   3627   2967  -1239    -37    684       C  
ATOM   4069  O   GLY A 531      48.421  44.554  40.634  1.00 23.50           O  
ANISOU 4069  O   GLY A 531     2304   3668   2956  -1250     15    666       O  
ATOM   4070  N   LEU A 532      46.273  45.101  40.274  1.00 24.33           N  
ANISOU 4070  N   LEU A 532     2589   3693   2964  -1203    -36    738       N  
ATOM   4071  CA  LEU A 532      46.131  44.181  39.150  1.00 27.91           C  
ANISOU 4071  CA  LEU A 532     3070   4211   3323  -1180     27    773       C  
ATOM   4072  C   LEU A 532      47.129  44.530  38.056  1.00 25.48           C  
ANISOU 4072  C   LEU A 532     2740   3916   3025  -1259    131    822       C  
ATOM   4073  O   LEU A 532      47.759  43.647  37.467  1.00 23.63           O  
ANISOU 4073  O   LEU A 532     2468   3752   2761  -1260    203    810       O  
ATOM   4074  CB  LEU A 532      44.705  44.214  38.604  1.00 25.24           C  
ANISOU 4074  CB  LEU A 532     2839   3852   2898  -1139     -3    820       C  
ATOM   4075  CG  LEU A 532      43.651  43.701  39.597  1.00 29.01           C  
ANISOU 4075  CG  LEU A 532     3339   4316   3369  -1058    -85    766       C  
ATOM   4076  CD1 LEU A 532      42.271  43.796  39.014  1.00 18.89           C  
ANISOU 4076  CD1 LEU A 532     2145   3011   2022  -1022   -115    808       C  
ATOM   4077  CD2 LEU A 532      43.942  42.278  40.020  1.00 24.92           C  
ANISOU 4077  CD2 LEU A 532     2769   3871   2829  -1001    -71    699       C  
ATOM   4078  N   ALA A 533      47.263  45.824  37.795  1.00 22.70           N  
ANISOU 4078  N   ALA A 533     2414   3488   2723  -1325    152    875       N  
ATOM   4079  CA  ALA A 533      48.199  46.312  36.789  1.00 31.15           C  
ANISOU 4079  CA  ALA A 533     3472   4549   3813  -1406    266    929       C  
ATOM   4080  C   ALA A 533      49.638  46.109  37.246  1.00 31.73           C  
ANISOU 4080  C   ALA A 533     3410   4650   3996  -1452    307    859       C  
ATOM   4081  O   ALA A 533      50.506  45.778  36.440  1.00 26.29           O  
ANISOU 4081  O   ALA A 533     2692   3986   3310  -1473    409    860       O  
ATOM   4082  CB  ALA A 533      47.937  47.782  36.486  1.00 24.77           C  
ANISOU 4082  CB  ALA A 533     2729   3636   3046  -1460    284   1007       C  
ATOM   4083  N   THR A 534      49.884  46.300  38.544  1.00 27.81           N  
ANISOU 4083  N   THR A 534     2838   4138   3590  -1445    223    782       N  
ATOM   4084  CA  THR A 534      51.243  46.227  39.080  1.00 27.55           C  
ANISOU 4084  CA  THR A 534     2662   4133   3673  -1487    239    710       C  
ATOM   4085  C   THR A 534      51.754  44.792  39.165  1.00 27.38           C  
ANISOU 4085  C   THR A 534     2565   4212   3627  -1428    246    665       C  
ATOM   4086  O   THR A 534      52.869  44.502  38.731  1.00 26.86           O  
ANISOU 4086  O   THR A 534     2410   4174   3621  -1461    329    647       O  
ATOM   4087  CB  THR A 534      51.341  46.875  40.491  1.00 37.32           C  
ANISOU 4087  CB  THR A 534     3844   5335   5002  -1496    131    632       C  
ATOM   4088  OG1 THR A 534      51.087  48.283  40.400  1.00 25.62           O  
ANISOU 4088  OG1 THR A 534     2410   3745   3577  -1567    149    665       O  
ATOM   4089  CG2 THR A 534      52.731  46.664  41.096  1.00 32.65           C  
ANISOU 4089  CG2 THR A 534     3090   4793   4521  -1528    123    547       C  
ATOM   4090  N   TYR A 535      50.944  43.891  39.711  1.00 23.41           N  
ANISOU 4090  N   TYR A 535     2099   3750   3046  -1333    172    644       N  
ATOM   4091  CA  TYR A 535      51.428  42.542  40.004  1.00 30.51           C  
ANISOU 4091  CA  TYR A 535     2921   4732   3940  -1266    174    598       C  
ATOM   4092  C   TYR A 535      51.026  41.511  38.955  1.00 27.18           C  
ANISOU 4092  C   TYR A 535     2555   4352   3420  -1231    258    632       C  
ATOM   4093  O   TYR A 535      51.567  40.403  38.936  1.00 26.32           O  
ANISOU 4093  O   TYR A 535     2377   4302   3320  -1190    299    602       O  
ATOM   4094  CB  TYR A 535      50.949  42.103  41.399  1.00 28.48           C  
ANISOU 4094  CB  TYR A 535     2657   4492   3673  -1180     51    545       C  
ATOM   4095  CG  TYR A 535      51.437  43.045  42.474  1.00 27.91           C  
ANISOU 4095  CG  TYR A 535     2522   4392   3688  -1218    -36    494       C  
ATOM   4096  CD1 TYR A 535      52.777  43.052  42.849  1.00 27.39           C  
ANISOU 4096  CD1 TYR A 535     2313   4368   3726  -1250    -41    444       C  
ATOM   4097  CD2 TYR A 535      50.576  43.955  43.085  1.00 22.51           C  
ANISOU 4097  CD2 TYR A 535     1918   3642   2994  -1228   -108    489       C  
ATOM   4098  CE1 TYR A 535      53.248  43.919  43.805  1.00 29.07           C  
ANISOU 4098  CE1 TYR A 535     2461   4564   4019  -1293   -124    383       C  
ATOM   4099  CE2 TYR A 535      51.040  44.832  44.043  1.00 23.17           C  
ANISOU 4099  CE2 TYR A 535     1945   3700   3157  -1273   -179    429       C  
ATOM   4100  CZ  TYR A 535      52.382  44.805  44.408  1.00 33.82           C  
ANISOU 4100  CZ  TYR A 535     3151   5099   4599  -1307   -191    372       C  
ATOM   4101  OH  TYR A 535      52.872  45.664  45.372  1.00 25.01           O  
ANISOU 4101  OH  TYR A 535     1972   3969   3563  -1357   -269    296       O  
ATOM   4102  N   GLY A 536      50.102  41.880  38.070  1.00 30.88           N  
ANISOU 4102  N   GLY A 536     3144   4791   3797  -1248    285    692       N  
ATOM   4103  CA  GLY A 536      49.667  40.992  36.999  1.00 26.80           C  
ANISOU 4103  CA  GLY A 536     2689   4320   3174  -1226    361    714       C  
ATOM   4104  C   GLY A 536      49.091  39.681  37.515  1.00 28.76           C  
ANISOU 4104  C   GLY A 536     2935   4613   3380  -1130    326    664       C  
ATOM   4105  O   GLY A 536      48.369  39.675  38.517  1.00 23.59           O  
ANISOU 4105  O   GLY A 536     2300   3935   2727  -1072    228    641       O  
ATOM   4106  N   ALA A 537      49.430  38.577  36.842  1.00 25.62           N  
ANISOU 4106  N   ALA A 537     2514   4270   2952  -1115    420    645       N  
ATOM   4107  CA  ALA A 537      48.839  37.258  37.118  1.00 23.57           C  
ANISOU 4107  CA  ALA A 537     2261   4043   2652  -1029    418    600       C  
ATOM   4108  C   ALA A 537      48.949  36.785  38.570  1.00 22.54           C  
ANISOU 4108  C   ALA A 537     2065   3909   2590   -949    340    558       C  
ATOM   4109  O   ALA A 537      48.012  36.191  39.087  1.00 23.29           O  
ANISOU 4109  O   ALA A 537     2207   3996   2647   -878    298    536       O  
ATOM   4110  CB  ALA A 537      49.455  36.207  36.212  1.00 21.12           C  
ANISOU 4110  CB  ALA A 537     1932   3756   2335  -1012    538    565       C  
ATOM   4111  N   ASN A 538      50.084  37.009  39.224  1.00 23.86           N  
ANISOU 4111  N   ASN A 538     2125   4084   2855   -959    322    546       N  
ATOM   4112  CA  ASN A 538      50.229  36.500  40.591  1.00 23.41           C  
ANISOU 4112  CA  ASN A 538     2012   4038   2845   -874    242    511       C  
ATOM   4113  C   ASN A 538      49.767  37.506  41.645  1.00 25.14           C  
ANISOU 4113  C   ASN A 538     2265   4217   3071   -875    115    507       C  
ATOM   4114  O   ASN A 538      50.095  37.359  42.819  1.00 26.67           O  
ANISOU 4114  O   ASN A 538     2407   4423   3301   -822     38    479       O  
ATOM   4115  CB  ASN A 538      51.682  36.098  40.885  1.00 28.93           C  
ANISOU 4115  CB  ASN A 538     2565   4780   3647   -867    268    492       C  
ATOM   4116  CG  ASN A 538      52.115  34.831  40.150  1.00 28.15           C  
ANISOU 4116  CG  ASN A 538     2422   4716   3557   -838    395    485       C  
ATOM   4117  OD1 ASN A 538      51.301  34.129  39.559  1.00 24.83           O  
ANISOU 4117  OD1 ASN A 538     2080   4293   3062   -814    456    484       O  
ATOM   4118  ND2 ASN A 538      53.407  34.520  40.220  1.00 29.64           N  
ANISOU 4118  ND2 ASN A 538     2476   4937   3849   -838    434    473       N  
ATOM   4119  N   TRP A 539      48.957  38.483  41.241  1.00 19.77           N  
ANISOU 4119  N   TRP A 539     1677   3486   2349   -926     94    535       N  
ATOM   4120  CA  TRP A 539      48.429  39.487  42.177  1.00 26.62           C  
ANISOU 4120  CA  TRP A 539     2585   4302   3229   -933    -11    527       C  
ATOM   4121  C   TRP A 539      47.795  38.873  43.422  1.00 24.87           C  
ANISOU 4121  C   TRP A 539     2389   4078   2984   -836    -85    491       C  
ATOM   4122  O   TRP A 539      47.905  39.420  44.528  1.00 23.14           O  
ANISOU 4122  O   TRP A 539     2156   3842   2792   -829   -171    462       O  
ATOM   4123  CB  TRP A 539      47.380  40.357  41.482  1.00 19.28           C  
ANISOU 4123  CB  TRP A 539     1764   3312   2250   -975    -11    571       C  
ATOM   4124  CG  TRP A 539      46.090  39.627  41.161  1.00 18.39           C  
ANISOU 4124  CG  TRP A 539     1739   3197   2053   -914     -4    576       C  
ATOM   4125  CD1 TRP A 539      45.833  38.870  40.050  1.00 22.74           C  
ANISOU 4125  CD1 TRP A 539     2316   3784   2539   -911     73    590       C  
ATOM   4126  CD2 TRP A 539      44.888  39.602  41.944  1.00 17.57           C  
ANISOU 4126  CD2 TRP A 539     1703   3048   1926   -855    -71    556       C  
ATOM   4127  NE1 TRP A 539      44.551  38.373  40.098  1.00 23.33           N  
ANISOU 4127  NE1 TRP A 539     2462   3844   2559   -854     51    575       N  
ATOM   4128  CE2 TRP A 539      43.946  38.807  41.259  1.00 22.11           C  
ANISOU 4128  CE2 TRP A 539     2332   3635   2433   -818    -33    557       C  
ATOM   4129  CE3 TRP A 539      44.514  40.163  43.174  1.00 21.17           C  
ANISOU 4129  CE3 TRP A 539     2177   3454   2413   -833   -153    530       C  
ATOM   4130  CZ2 TRP A 539      42.662  38.572  41.733  1.00 20.58           C  
ANISOU 4130  CZ2 TRP A 539     2201   3400   2217   -761    -72    535       C  
ATOM   4131  CZ3 TRP A 539      43.245  39.940  43.647  1.00 23.57           C  
ANISOU 4131  CZ3 TRP A 539     2553   3714   2687   -776   -184    514       C  
ATOM   4132  CH2 TRP A 539      42.329  39.146  42.934  1.00 25.09           C  
ANISOU 4132  CH2 TRP A 539     2790   3915   2827   -739   -143    517       C  
ATOM   4133  N   TRP A 540      47.154  37.725  43.228  1.00 18.14           N  
ANISOU 4133  N   TRP A 540     1573   3240   2078   -766    -41    488       N  
ATOM   4134  CA  TRP A 540      46.349  37.089  44.265  1.00 20.25           C  
ANISOU 4134  CA  TRP A 540     1887   3490   2316   -673    -84    462       C  
ATOM   4135  C   TRP A 540      47.218  36.457  45.354  1.00 26.31           C  
ANISOU 4135  C   TRP A 540     2580   4301   3116   -605   -118    440       C  
ATOM   4136  O   TRP A 540      46.714  36.043  46.406  1.00 22.15           O  
ANISOU 4136  O   TRP A 540     2093   3760   2563   -527   -161    424       O  
ATOM   4137  CB  TRP A 540      45.430  36.047  43.637  1.00 17.55           C  
ANISOU 4137  CB  TRP A 540     1601   3145   1924   -626    -11    460       C  
ATOM   4138  CG  TRP A 540      46.171  35.021  42.837  1.00 19.30           C  
ANISOU 4138  CG  TRP A 540     1760   3420   2154   -620     89    459       C  
ATOM   4139  CD1 TRP A 540      46.443  35.060  41.491  1.00 17.51           C  
ANISOU 4139  CD1 TRP A 540     1525   3217   1909   -687    166    475       C  
ATOM   4140  CD2 TRP A 540      46.752  33.809  43.326  1.00 22.40           C  
ANISOU 4140  CD2 TRP A 540     2090   3844   2575   -540    132    444       C  
ATOM   4141  NE1 TRP A 540      47.155  33.944  41.120  1.00 17.84           N  
ANISOU 4141  NE1 TRP A 540     1503   3303   1974   -660    260    461       N  
ATOM   4142  CE2 TRP A 540      47.353  33.150  42.232  1.00 22.71           C  
ANISOU 4142  CE2 TRP A 540     2081   3921   2627   -567    240    445       C  
ATOM   4143  CE3 TRP A 540      46.816  33.199  44.590  1.00 17.17           C  
ANISOU 4143  CE3 TRP A 540     1416   3180   1928   -444     93    435       C  
ATOM   4144  CZ2 TRP A 540      48.015  31.925  42.353  1.00 20.51           C  
ANISOU 4144  CZ2 TRP A 540     1732   3670   2391   -502    315    434       C  
ATOM   4145  CZ3 TRP A 540      47.473  31.979  44.713  1.00 17.52           C  
ANISOU 4145  CZ3 TRP A 540     1395   3256   2007   -372    161    436       C  
ATOM   4146  CH2 TRP A 540      48.063  31.359  43.603  1.00 21.55           C  
ANISOU 4146  CH2 TRP A 540     1847   3795   2545   -401    272    434       C  
ATOM   4147  N   HIS A 541      48.525  36.397  45.108  1.00 22.66           N  
ANISOU 4147  N   HIS A 541     2008   3891   2711   -634   -100    443       N  
ATOM   4148  CA  HIS A 541      49.455  35.926  46.120  1.00 20.02           C  
ANISOU 4148  CA  HIS A 541     1585   3607   2414   -571   -151    426       C  
ATOM   4149  C   HIS A 541      49.334  36.786  47.358  1.00 22.26           C  
ANISOU 4149  C   HIS A 541     1891   3878   2688   -571   -275    398       C  
ATOM   4150  O   HIS A 541      49.507  36.309  48.480  1.00 19.64           O  
ANISOU 4150  O   HIS A 541     1548   3576   2337   -487   -339    385       O  
ATOM   4151  CB  HIS A 541      50.899  35.957  45.609  1.00 21.97           C  
ANISOU 4151  CB  HIS A 541     1695   3906   2747   -618   -119    426       C  
ATOM   4152  CG  HIS A 541      51.250  34.817  44.708  1.00 22.49           C  
ANISOU 4152  CG  HIS A 541     1718   3996   2830   -591      4    444       C  
ATOM   4153  ND1 HIS A 541      52.554  34.466  44.429  1.00 24.44           N  
ANISOU 4153  ND1 HIS A 541     1830   4290   3164   -599     47    442       N  
ATOM   4154  CD2 HIS A 541      50.473  33.938  44.031  1.00 21.16           C  
ANISOU 4154  CD2 HIS A 541     1619   3810   2612   -559     99    454       C  
ATOM   4155  CE1 HIS A 541      52.565  33.427  43.612  1.00 21.30           C  
ANISOU 4155  CE1 HIS A 541     1427   3898   2768   -573    170    453       C  
ATOM   4156  NE2 HIS A 541      51.316  33.085  43.360  1.00 25.17           N  
ANISOU 4156  NE2 HIS A 541     2040   4352   3173   -550    202    457       N  
ATOM   4157  N   TYR A 542      48.990  38.051  47.153  1.00 20.18           N  
ANISOU 4157  N   TYR A 542     1669   3567   2432   -661   -305    390       N  
ATOM   4158  CA  TYR A 542      48.932  38.991  48.257  1.00 19.70           C  
ANISOU 4158  CA  TYR A 542     1625   3487   2372   -680   -412    351       C  
ATOM   4159  C   TYR A 542      47.747  38.730  49.195  1.00 18.93           C  
ANISOU 4159  C   TYR A 542     1644   3350   2200   -603   -448    340       C  
ATOM   4160  O   TYR A 542      47.592  39.436  50.183  1.00 20.62           O  
ANISOU 4160  O   TYR A 542     1889   3546   2401   -612   -530    301       O  
ATOM   4161  CB  TYR A 542      48.933  40.429  47.715  1.00 20.01           C  
ANISOU 4161  CB  TYR A 542     1672   3472   2460   -801   -412    347       C  
ATOM   4162  CG  TYR A 542      50.340  40.853  47.331  1.00 21.16           C  
ANISOU 4162  CG  TYR A 542     1686   3659   2696   -876   -403    333       C  
ATOM   4163  CD1 TYR A 542      50.868  40.542  46.085  1.00 23.52           C  
ANISOU 4163  CD1 TYR A 542     1935   3974   3029   -913   -300    372       C  
ATOM   4164  CD2 TYR A 542      51.159  41.502  48.244  1.00 22.15           C  
ANISOU 4164  CD2 TYR A 542     1730   3811   2874   -910   -494    273       C  
ATOM   4165  CE1 TYR A 542      52.174  40.902  45.743  1.00 27.32           C  
ANISOU 4165  CE1 TYR A 542     2290   4485   3607   -983   -277    355       C  
ATOM   4166  CE2 TYR A 542      52.465  41.863  47.919  1.00 29.11           C  
ANISOU 4166  CE2 TYR A 542     2475   4728   3856   -980   -483    250       C  
ATOM   4167  CZ  TYR A 542      52.964  41.559  46.666  1.00 29.39           C  
ANISOU 4167  CZ  TYR A 542     2462   4769   3936  -1016   -369    293       C  
ATOM   4168  OH  TYR A 542      54.248  41.917  46.336  1.00 29.22           O  
ANISOU 4168  OH  TYR A 542     2301   4773   4027  -1089   -343    267       O  
ATOM   4169  N   PHE A 543      46.918  37.729  48.879  1.00 18.10           N  
ANISOU 4169  N   PHE A 543     1601   3226   2050   -533   -379    366       N  
ATOM   4170  CA  PHE A 543      45.929  37.204  49.834  1.00 19.80           C  
ANISOU 4170  CA  PHE A 543     1913   3407   2205   -444   -393    355       C  
ATOM   4171  C   PHE A 543      46.631  36.463  50.960  1.00 22.26           C  
ANISOU 4171  C   PHE A 543     2187   3780   2491   -352   -442    348       C  
ATOM   4172  O   PHE A 543      46.045  36.223  52.006  1.00 19.51           O  
ANISOU 4172  O   PHE A 543     1916   3411   2085   -283   -471    337       O  
ATOM   4173  CB  PHE A 543      44.945  36.230  49.188  1.00 16.65           C  
ANISOU 4173  CB  PHE A 543     1572   2972   1781   -395   -296    376       C  
ATOM   4174  CG  PHE A 543      43.814  36.877  48.451  1.00 25.29           C  
ANISOU 4174  CG  PHE A 543     2738   3997   2873   -451   -271    378       C  
ATOM   4175  CD1 PHE A 543      42.822  37.566  49.128  1.00 15.67           C  
ANISOU 4175  CD1 PHE A 543     1605   2707   1643   -452   -313    357       C  
ATOM   4176  CD2 PHE A 543      43.715  36.742  47.071  1.00 23.64           C  
ANISOU 4176  CD2 PHE A 543     2514   3796   2673   -496   -205    402       C  
ATOM   4177  CE1 PHE A 543      41.773  38.135  48.436  1.00 15.20           C  
ANISOU 4177  CE1 PHE A 543     1600   2583   1593   -494   -295    364       C  
ATOM   4178  CE2 PHE A 543      42.664  37.302  46.377  1.00 23.77           C  
ANISOU 4178  CE2 PHE A 543     2593   3757   2680   -537   -195    410       C  
ATOM   4179  CZ  PHE A 543      41.693  38.001  47.052  1.00 24.16           C  
ANISOU 4179  CZ  PHE A 543     2715   3734   2730   -533   -243    394       C  
ATOM   4180  N   VAL A 544      47.861  36.021  50.705  1.00 25.70           N  
ANISOU 4180  N   VAL A 544     2505   4291   2969   -344   -441    362       N  
ATOM   4181  CA  VAL A 544      48.629  35.281  51.702  1.00 19.66           C  
ANISOU 4181  CA  VAL A 544     1689   3595   2186   -247   -496    367       C  
ATOM   4182  C   VAL A 544      50.001  35.914  51.924  1.00 22.14           C  
ANISOU 4182  C   VAL A 544     1872   3985   2555   -297   -588    340       C  
ATOM   4183  O   VAL A 544      51.022  35.335  51.552  1.00 22.30           O  
ANISOU 4183  O   VAL A 544     1775   4064   2635   -277   -567    359       O  
ATOM   4184  CB  VAL A 544      48.803  33.783  51.301  1.00 19.78           C  
ANISOU 4184  CB  VAL A 544     1673   3628   2214   -152   -397    413       C  
ATOM   4185  CG1 VAL A 544      49.183  32.942  52.522  1.00 20.25           C  
ANISOU 4185  CG1 VAL A 544     1729   3734   2231    -20   -448    436       C  
ATOM   4186  CG2 VAL A 544      47.511  33.225  50.649  1.00 18.37           C  
ANISOU 4186  CG2 VAL A 544     1598   3372   2012   -139   -282    424       C  
ATOM   4187  N   PRO A 545      50.025  37.102  52.550  1.00 27.31           N  
ANISOU 4187  N   PRO A 545     2541   4634   3202   -365   -685    288       N  
ATOM   4188  CA  PRO A 545      51.246  37.903  52.726  1.00 27.48           C  
ANISOU 4188  CA  PRO A 545     2435   4717   3291   -438   -771    242       C  
ATOM   4189  C   PRO A 545      52.410  37.174  53.402  1.00 25.49           C  
ANISOU 4189  C   PRO A 545     2065   4572   3049   -354   -848    243       C  
ATOM   4190  O   PRO A 545      53.557  37.436  53.028  1.00 30.70           O  
ANISOU 4190  O   PRO A 545     2578   5283   3805   -407   -869    222       O  
ATOM   4191  CB  PRO A 545      50.778  39.083  53.593  1.00 31.68           C  
ANISOU 4191  CB  PRO A 545     3038   5216   3784   -495   -860    178       C  
ATOM   4192  CG  PRO A 545      49.491  38.654  54.208  1.00 29.02           C  
ANISOU 4192  CG  PRO A 545     2858   4824   3345   -416   -840    195       C  
ATOM   4193  CD  PRO A 545      48.861  37.716  53.213  1.00 29.12           C  
ANISOU 4193  CD  PRO A 545     2907   4794   3363   -373   -712    262       C  
ATOM   4194  N   THR A 546      52.149  36.293  54.367  1.00 28.51           N  
ANISOU 4194  N   THR A 546     2504   4985   3342   -224   -887    270       N  
ATOM   4195  CA  THR A 546      53.253  35.624  55.063  1.00 29.21           C  
ANISOU 4195  CA  THR A 546     2482   5182   3436   -131   -974    282       C  
ATOM   4196  C   THR A 546      54.050  34.699  54.127  1.00 29.32           C  
ANISOU 4196  C   THR A 546     2370   5220   3549    -98   -885    333       C  
ATOM   4197  O   THR A 546      55.207  34.399  54.396  1.00 34.19           O  
ANISOU 4197  O   THR A 546     2844   5923   4222    -58   -952    334       O  
ATOM   4198  CB  THR A 546      52.771  34.830  56.303  1.00 31.37           C  
ANISOU 4198  CB  THR A 546     2861   5478   3579     15  -1024    317       C  
ATOM   4199  OG1 THR A 546      51.786  33.865  55.919  1.00 33.91           O  
ANISOU 4199  OG1 THR A 546     3291   5722   3870     87   -887    381       O  
ATOM   4200  CG2 THR A 546      52.157  35.770  57.335  1.00 30.03           C  
ANISOU 4200  CG2 THR A 546     2804   5296   3310    -20  -1120    254       C  
ATOM   4201  N   LEU A 547      53.431  34.258  53.033  1.00 31.71           N  
ANISOU 4201  N   LEU A 547     2722   5450   3878   -117   -734    371       N  
ATOM   4202  CA  LEU A 547      54.122  33.454  52.017  1.00 32.08           C  
ANISOU 4202  CA  LEU A 547     2660   5508   4022   -105   -626    407       C  
ATOM   4203  C   LEU A 547      54.789  34.291  50.925  1.00 33.60           C  
ANISOU 4203  C   LEU A 547     2752   5695   4321   -247   -583    373       C  
ATOM   4204  O   LEU A 547      55.600  33.769  50.147  1.00 29.97           O  
ANISOU 4204  O   LEU A 547     2178   5254   3954   -251   -503    390       O  
ATOM   4205  CB  LEU A 547      53.163  32.474  51.346  1.00 28.66           C  
ANISOU 4205  CB  LEU A 547     2326   5004   3558    -56   -476    454       C  
ATOM   4206  CG  LEU A 547      52.883  31.148  52.035  1.00 27.63           C  
ANISOU 4206  CG  LEU A 547     2243   4875   3381    102   -447    508       C  
ATOM   4207  CD1 LEU A 547      52.003  30.290  51.134  1.00 27.00           C  
ANISOU 4207  CD1 LEU A 547     2239   4718   3302    116   -280    532       C  
ATOM   4208  CD2 LEU A 547      54.197  30.437  52.339  1.00 26.47           C  
ANISOU 4208  CD2 LEU A 547     1944   4809   3306    188   -483    540       C  
ATOM   4209  N   VAL A 548      54.440  35.576  50.851  1.00 34.32           N  
ANISOU 4209  N   VAL A 548     2889   5749   4402   -362   -622    327       N  
ATOM   4210  CA  VAL A 548      54.906  36.424  49.753  1.00 34.20           C  
ANISOU 4210  CA  VAL A 548     2808   5707   4479   -499   -558    305       C  
ATOM   4211  C   VAL A 548      56.305  36.969  49.988  1.00 41.18           C  
ANISOU 4211  C   VAL A 548     3517   6656   5474   -552   -633    255       C  
ATOM   4212  O   VAL A 548      57.148  36.939  49.087  1.00 48.14           O  
ANISOU 4212  O   VAL A 548     4284   7543   6463   -607   -552    257       O  
ATOM   4213  CB  VAL A 548      53.939  37.603  49.510  1.00 30.33           C  
ANISOU 4213  CB  VAL A 548     2439   5137   3948   -599   -554    286       C  
ATOM   4214  CG1 VAL A 548      54.546  38.631  48.548  1.00 30.51           C  
ANISOU 4214  CG1 VAL A 548     2392   5132   4069   -740   -501    267       C  
ATOM   4215  CG2 VAL A 548      52.628  37.088  48.967  1.00 22.44           C  
ANISOU 4215  CG2 VAL A 548     1586   4072   2867   -565   -462    332       C  
ATOM   4216  N   GLY A 549      56.563  37.462  51.191  1.00 42.13           N  
ANISOU 4216  N   GLY A 549     3612   6826   5570   -537   -785    204       N  
ATOM   4217  CA  GLY A 549      57.873  38.009  51.487  1.00 46.61           C  
ANISOU 4217  CA  GLY A 549     4002   7461   6248   -590   -873    140       C  
ATOM   4218  C   GLY A 549      58.167  39.287  50.718  1.00 46.49           C  
ANISOU 4218  C   GLY A 549     3946   7387   6332   -755   -820     90       C  
ATOM   4219  O   GLY A 549      59.229  39.435  50.114  1.00 51.46           O  
ANISOU 4219  O   GLY A 549     4451   8007   7096   -804   -766     64       O  
ATOM   4220  N   ASP A 550      57.192  40.189  50.700  1.00 39.00           N  
ANISOU 4220  N   ASP A 550     3133   6361   5323   -825   -811     78       N  
ATOM   4221  CA  ASP A 550      57.377  41.535  50.177  1.00 36.94           C  
ANISOU 4221  CA  ASP A 550     2856   6030   5149   -973   -772     31       C  
ATOM   4222  C   ASP A 550      57.172  42.513  51.334  1.00 35.81           C  
ANISOU 4222  C   ASP A 550     2760   5869   4977   -999   -898    -56       C  
ATOM   4223  O   ASP A 550      56.066  43.006  51.545  1.00 36.78           O  
ANISOU 4223  O   ASP A 550     3015   5941   5017  -1024   -904    -48       O  
ATOM   4224  CB  ASP A 550      56.394  41.806  49.031  1.00 36.68           C  
ANISOU 4224  CB  ASP A 550     2955   5899   5083  -1027   -634     99       C  
ATOM   4225  CG  ASP A 550      56.504  43.212  48.472  1.00 32.15           C  
ANISOU 4225  CG  ASP A 550     2378   5244   4594  -1174   -583     70       C  
ATOM   4226  OD1 ASP A 550      57.452  43.934  48.824  1.00 34.39           O  
ANISOU 4226  OD1 ASP A 550     2562   5520   4985  -1227   -623    -12       O  
ATOM   4227  OD2 ASP A 550      55.627  43.599  47.675  1.00 33.58           O  
ANISOU 4227  OD2 ASP A 550     2682   5339   4737  -1212   -492    126       O  
ATOM   4228  N   ASP A 551      58.224  42.804  52.087  1.00 35.06           N  
ANISOU 4228  N   ASP A 551     2557   5810   4955   -994   -996   -144       N  
ATOM   4229  CA  ASP A 551      58.043  43.642  53.269  1.00 44.45           C  
ANISOU 4229  CA  ASP A 551     3795   6990   6105  -1010  -1120   -235       C  
ATOM   4230  C   ASP A 551      58.246  45.116  52.938  1.00 45.17           C  
ANISOU 4230  C   ASP A 551     3868   6982   6312  -1156  -1077   -305       C  
ATOM   4231  O   ASP A 551      58.815  45.869  53.722  1.00 52.59           O  
ANISOU 4231  O   ASP A 551     4759   7915   7307  -1193  -1170   -402       O  
ATOM   4232  CB  ASP A 551      58.987  43.220  54.390  1.00 49.64           C  
ANISOU 4232  CB  ASP A 551     4362   7734   6764   -925  -1269   -292       C  
ATOM   4233  CG  ASP A 551      58.518  43.698  55.750  1.00 57.73           C  
ANISOU 4233  CG  ASP A 551     5484   8768   7680   -903  -1401   -359       C  
ATOM   4234  OD1 ASP A 551      57.291  43.870  55.925  1.00 52.40           O  
ANISOU 4234  OD1 ASP A 551     4960   8055   6893   -903  -1376   -339       O  
ATOM   4235  OD2 ASP A 551      59.376  43.933  56.632  1.00 64.39           O  
ANISOU 4235  OD2 ASP A 551     6257   9654   8555   -894  -1528   -430       O  
ATOM   4236  N   THR A 552      57.764  45.519  51.769  1.00 41.00           N  
ANISOU 4236  N   THR A 552     3386   6372   5819  -1236   -935   -247       N  
ATOM   4237  CA  THR A 552      57.795  46.910  51.360  1.00 35.57           C  
ANISOU 4237  CA  THR A 552     2705   5574   5238  -1367   -870   -290       C  
ATOM   4238  C   THR A 552      56.502  47.618  51.741  1.00 36.87           C  
ANISOU 4238  C   THR A 552     3026   5669   5315  -1396   -879   -291       C  
ATOM   4239  O   THR A 552      55.457  46.971  51.884  1.00 34.80           O  
ANISOU 4239  O   THR A 552     2876   5428   4917  -1329   -892   -226       O  
ATOM   4240  CB  THR A 552      58.003  47.030  49.848  1.00 34.40           C  
ANISOU 4240  CB  THR A 552     2534   5361   5174  -1435   -702   -216       C  
ATOM   4241  OG1 THR A 552      56.908  46.398  49.174  1.00 33.57           O  
ANISOU 4241  OG1 THR A 552     2551   5254   4951  -1398   -633   -102       O  
ATOM   4242  CG2 THR A 552      59.325  46.367  49.441  1.00 34.70           C  
ANISOU 4242  CG2 THR A 552     2412   5455   5319  -1413   -677   -222       C  
ATOM   4243  N   PRO A 553      56.561  48.953  51.890  1.00 31.54           N  
ANISOU 4243  N   PRO A 553     2354   4898   4730  -1497   -866   -361       N  
ATOM   4244  CA  PRO A 553      55.328  49.699  52.161  1.00 33.99           C  
ANISOU 4244  CA  PRO A 553     2810   5124   4982  -1531   -854   -360       C  
ATOM   4245  C   PRO A 553      54.250  49.432  51.109  1.00 36.91           C  
ANISOU 4245  C   PRO A 553     3292   5442   5290  -1529   -747   -227       C  
ATOM   4246  O   PRO A 553      53.074  49.328  51.463  1.00 36.52           O  
ANISOU 4246  O   PRO A 553     3368   5370   5138  -1496   -772   -196       O  
ATOM   4247  CB  PRO A 553      55.781  51.159  52.113  1.00 33.65           C  
ANISOU 4247  CB  PRO A 553     2726   4969   5091  -1650   -813   -435       C  
ATOM   4248  CG  PRO A 553      57.244  51.115  52.476  1.00 38.29           C  
ANISOU 4248  CG  PRO A 553     3152   5615   5780  -1658   -881   -510       C  
ATOM   4249  CD  PRO A 553      57.755  49.820  51.902  1.00 33.35           C  
ANISOU 4249  CD  PRO A 553     2456   5088   5129  -1581   -865   -443       C  
ATOM   4250  N   ALA A 554      54.650  49.314  49.843  1.00 33.36           N  
ANISOU 4250  N   ALA A 554     2802   4970   4904  -1562   -631   -151       N  
ATOM   4251  CA  ALA A 554      53.704  49.039  48.764  1.00 29.70           C  
ANISOU 4251  CA  ALA A 554     2444   4463   4379  -1557   -535    -21       C  
ATOM   4252  C   ALA A 554      53.074  47.639  48.896  1.00 26.94           C  
ANISOU 4252  C   ALA A 554     2155   4190   3889  -1424   -571     36       C  
ATOM   4253  O   ALA A 554      51.854  47.472  48.794  1.00 25.35           O  
ANISOU 4253  O   ALA A 554     2091   3942   3600  -1370   -556     92       O  
ATOM   4254  CB  ALA A 554      54.396  49.193  47.405  1.00 29.97           C  
ANISOU 4254  CB  ALA A 554     2426   4461   4499  -1612   -397     39       C  
ATOM   4255  N   GLY A 555      53.919  46.643  49.148  1.00 28.79           N  
ANISOU 4255  N   GLY A 555     2284   4537   4117  -1365   -615     17       N  
ATOM   4256  CA  GLY A 555      53.462  45.282  49.340  1.00 25.83           C  
ANISOU 4256  CA  GLY A 555     1958   4229   3629  -1233   -638     64       C  
ATOM   4257  C   GLY A 555      52.498  45.165  50.508  1.00 25.19           C  
ANISOU 4257  C   GLY A 555     1985   4144   3440  -1160   -731     36       C  
ATOM   4258  O   GLY A 555      51.430  44.572  50.366  1.00 23.95           O  
ANISOU 4258  O   GLY A 555     1947   3960   3194  -1085   -699     94       O  
ATOM   4259  N   ARG A 556      52.863  45.740  51.655  1.00 26.12           N  
ANISOU 4259  N   ARG A 556     2066   4288   3570  -1186   -839    -60       N  
ATOM   4260  CA  ARG A 556      51.992  45.685  52.828  1.00 33.36           C  
ANISOU 4260  CA  ARG A 556     3095   5202   4380  -1123   -920    -95       C  
ATOM   4261  C   ARG A 556      50.657  46.363  52.541  1.00 29.47           C  
ANISOU 4261  C   ARG A 556     2748   4581   3868  -1151   -856    -63       C  
ATOM   4262  O   ARG A 556      49.598  45.848  52.900  1.00 26.16           O  
ANISOU 4262  O   ARG A 556     2448   4139   3354  -1068   -855    -34       O  
ATOM   4263  CB  ARG A 556      52.660  46.329  54.048  1.00 27.11           C  
ANISOU 4263  CB  ARG A 556     2237   4461   3601  -1164  -1045   -217       C  
ATOM   4264  CG  ARG A 556      53.824  45.540  54.613  1.00 31.89           C  
ANISOU 4264  CG  ARG A 556     2721   5193   4202  -1092  -1136   -251       C  
ATOM   4265  CD  ARG A 556      54.265  46.107  55.956  1.00 38.71           C  
ANISOU 4265  CD  ARG A 556     3575   6083   5050  -1088  -1261   -373       C  
ATOM   4266  NE  ARG A 556      54.749  47.481  55.847  1.00 48.50           N  
ANISOU 4266  NE  ARG A 556     4761   7246   6423  -1216  -1245   -462       N  
ATOM   4267  CZ  ARG A 556      56.028  47.813  55.691  1.00 52.27           C  
ANISOU 4267  CZ  ARG A 556     5092   7738   7030  -1261  -1265   -516       C  
ATOM   4268  NH1 ARG A 556      56.955  46.867  55.634  1.00 53.86           N  
ANISOU 4268  NH1 ARG A 556     5184   8032   7247  -1187  -1306   -491       N  
ATOM   4269  NH2 ARG A 556      56.382  49.089  55.593  1.00 51.12           N  
ANISOU 4269  NH2 ARG A 556     4908   7505   7010  -1379  -1239   -589       N  
ATOM   4270  N   GLU A 557      50.704  47.498  51.852  1.00 33.57           N  
ANISOU 4270  N   GLU A 557     3256   5012   4487  -1263   -792    -64       N  
ATOM   4271  CA  GLU A 557      49.477  48.212  51.538  1.00 30.32           C  
ANISOU 4271  CA  GLU A 557     2972   4474   4073  -1287   -734    -25       C  
ATOM   4272  C   GLU A 557      48.578  47.386  50.625  1.00 28.55           C  
ANISOU 4272  C   GLU A 557     2831   4233   3785  -1211   -661     84       C  
ATOM   4273  O   GLU A 557      47.361  47.363  50.815  1.00 22.13           O  
ANISOU 4273  O   GLU A 557     2132   3357   2918  -1165   -653    107       O  
ATOM   4274  CB  GLU A 557      49.779  49.564  50.889  1.00 30.33           C  
ANISOU 4274  CB  GLU A 557     2942   4380   4202  -1416   -668    -30       C  
ATOM   4275  CG  GLU A 557      48.533  50.411  50.622  1.00 33.24           C  
ANISOU 4275  CG  GLU A 557     3436   4611   4584  -1437   -613     12       C  
ATOM   4276  CD  GLU A 557      48.794  51.573  49.670  1.00 39.90           C  
ANISOU 4276  CD  GLU A 557     4259   5353   5549  -1546   -519     51       C  
ATOM   4277  OE1 GLU A 557      49.465  52.543  50.080  1.00 45.68           O  
ANISOU 4277  OE1 GLU A 557     4926   6047   6383  -1643   -523    -32       O  
ATOM   4278  OE2 GLU A 557      48.322  51.514  48.509  1.00 39.02           O  
ANISOU 4278  OE2 GLU A 557     4198   5198   5428  -1533   -438    164       O  
ATOM   4279  N   PHE A 558      49.158  46.682  49.656  1.00 26.82           N  
ANISOU 4279  N   PHE A 558     2549   4067   3572  -1198   -606    143       N  
ATOM   4280  CA  PHE A 558      48.318  45.904  48.749  1.00 24.35           C  
ANISOU 4280  CA  PHE A 558     2312   3743   3196  -1135   -537    233       C  
ATOM   4281  C   PHE A 558      47.747  44.678  49.471  1.00 22.15           C  
ANISOU 4281  C   PHE A 558     2081   3516   2817  -1014   -577    228       C  
ATOM   4282  O   PHE A 558      46.602  44.295  49.236  1.00 19.93           O  
ANISOU 4282  O   PHE A 558     1897   3193   2481   -960   -546    268       O  
ATOM   4283  CB  PHE A 558      49.073  45.487  47.479  1.00 23.39           C  
ANISOU 4283  CB  PHE A 558     2122   3663   3104  -1161   -454    291       C  
ATOM   4284  CG  PHE A 558      48.194  44.805  46.453  1.00 23.90           C  
ANISOU 4284  CG  PHE A 558     2267   3715   3098  -1113   -382    373       C  
ATOM   4285  CD1 PHE A 558      47.046  45.430  45.980  1.00 20.53           C  
ANISOU 4285  CD1 PHE A 558     1947   3202   2653  -1125   -358    420       C  
ATOM   4286  CD2 PHE A 558      48.507  43.542  45.971  1.00 24.15           C  
ANISOU 4286  CD2 PHE A 558     2264   3823   3089  -1054   -341    397       C  
ATOM   4287  CE1 PHE A 558      46.224  44.814  45.042  1.00 19.79           C  
ANISOU 4287  CE1 PHE A 558     1920   3108   2490  -1082   -307    485       C  
ATOM   4288  CE2 PHE A 558      47.683  42.911  45.029  1.00 19.91           C  
ANISOU 4288  CE2 PHE A 558     1799   3280   2484  -1017   -277    455       C  
ATOM   4289  CZ  PHE A 558      46.544  43.559  44.560  1.00 19.48           C  
ANISOU 4289  CZ  PHE A 558     1848   3150   2404  -1033   -266    497       C  
ATOM   4290  N   ALA A 559      48.521  44.096  50.382  1.00 21.41           N  
ANISOU 4290  N   ALA A 559     1921   3509   2705   -968   -646    178       N  
ATOM   4291  CA  ALA A 559      48.011  42.981  51.182  1.00 25.89           C  
ANISOU 4291  CA  ALA A 559     2543   4116   3178   -849   -678    178       C  
ATOM   4292  C   ALA A 559      46.823  43.447  52.015  1.00 25.17           C  
ANISOU 4292  C   ALA A 559     2575   3948   3039   -831   -706    148       C  
ATOM   4293  O   ALA A 559      45.765  42.795  52.071  1.00 19.39           O  
ANISOU 4293  O   ALA A 559     1936   3182   2248   -757   -671    178       O  
ATOM   4294  CB  ALA A 559      49.097  42.426  52.069  1.00 21.70           C  
ANISOU 4294  CB  ALA A 559     1919   3691   2634   -802   -760    135       C  
ATOM   4295  N   ASP A 560      47.013  44.605  52.631  1.00 21.10           N  
ANISOU 4295  N   ASP A 560     2055   3399   2562   -907   -759     83       N  
ATOM   4296  CA  ASP A 560      45.976  45.261  53.412  1.00 25.25           C  
ANISOU 4296  CA  ASP A 560     2691   3840   3064   -911   -776     43       C  
ATOM   4297  C   ASP A 560      44.737  45.538  52.559  1.00 25.45           C  
ANISOU 4297  C   ASP A 560     2801   3758   3111   -917   -695    104       C  
ATOM   4298  O   ASP A 560      43.607  45.362  53.012  1.00 26.89           O  
ANISOU 4298  O   ASP A 560     3083   3882   3252   -864   -682    102       O  
ATOM   4299  CB  ASP A 560      46.519  46.559  54.007  1.00 28.03           C  
ANISOU 4299  CB  ASP A 560     3006   4168   3477  -1013   -829    -44       C  
ATOM   4300  CG  ASP A 560      45.518  47.254  54.914  1.00 40.33           C  
ANISOU 4300  CG  ASP A 560     4675   5636   5013  -1021   -841   -100       C  
ATOM   4301  OD1 ASP A 560      45.060  46.614  55.890  1.00 39.56           O  
ANISOU 4301  OD1 ASP A 560     4649   5564   4816   -939   -875   -125       O  
ATOM   4302  OD2 ASP A 560      45.193  48.437  54.651  1.00 43.80           O  
ANISOU 4302  OD2 ASP A 560     5133   5972   5537  -1109   -807   -116       O  
ATOM   4303  N   THR A 561      44.947  45.968  51.318  1.00 24.48           N  
ANISOU 4303  N   THR A 561     2639   3608   3053   -980   -640    160       N  
ATOM   4304  CA  THR A 561      43.823  46.268  50.449  1.00 19.24           C  
ANISOU 4304  CA  THR A 561     2050   2855   2406   -982   -578    225       C  
ATOM   4305  C   THR A 561      43.004  44.996  50.186  1.00 18.18           C  
ANISOU 4305  C   THR A 561     1965   2744   2197   -882   -547    266       C  
ATOM   4306  O   THR A 561      41.773  45.008  50.305  1.00 21.13           O  
ANISOU 4306  O   THR A 561     2422   3047   2560   -845   -531    273       O  
ATOM   4307  CB  THR A 561      44.281  46.900  49.106  1.00 19.65           C  
ANISOU 4307  CB  THR A 561     2057   2886   2523  -1061   -522    290       C  
ATOM   4308  OG1 THR A 561      44.862  48.191  49.350  1.00 20.68           O  
ANISOU 4308  OG1 THR A 561     2152   2965   2743  -1160   -531    250       O  
ATOM   4309  CG2 THR A 561      43.103  47.059  48.176  1.00 20.23           C  
ANISOU 4309  CG2 THR A 561     2208   2888   2591  -1045   -473    367       C  
ATOM   4310  N   LEU A 562      43.680  43.899  49.854  1.00 18.06           N  
ANISOU 4310  N   LEU A 562     1893   2823   2144   -838   -533    285       N  
ATOM   4311  CA  LEU A 562      42.985  42.626  49.629  1.00 17.17           C  
ANISOU 4311  CA  LEU A 562     1820   2733   1972   -747   -492    312       C  
ATOM   4312  C   LEU A 562      42.334  42.080  50.912  1.00 18.27           C  
ANISOU 4312  C   LEU A 562     2026   2856   2059   -664   -517    268       C  
ATOM   4313  O   LEU A 562      41.234  41.498  50.877  1.00 19.36           O  
ANISOU 4313  O   LEU A 562     2231   2951   2173   -605   -476    277       O  
ATOM   4314  CB  LEU A 562      43.944  41.588  49.046  1.00 17.28           C  
ANISOU 4314  CB  LEU A 562     1754   2843   1971   -721   -460    336       C  
ATOM   4315  CG  LEU A 562      44.533  41.921  47.665  1.00 19.93           C  
ANISOU 4315  CG  LEU A 562     2034   3195   2343   -796   -410    384       C  
ATOM   4316  CD1 LEU A 562      45.223  40.699  47.040  1.00 18.74           C  
ANISOU 4316  CD1 LEU A 562     1820   3127   2173   -758   -354    404       C  
ATOM   4317  CD2 LEU A 562      43.458  42.476  46.712  1.00 17.22           C  
ANISOU 4317  CD2 LEU A 562     1763   2780   1999   -826   -374    430       C  
ATOM   4318  N   SER A 563      43.016  42.261  52.040  1.00 17.50           N  
ANISOU 4318  N   SER A 563     1910   2795   1945   -660   -582    216       N  
ATOM   4319  CA  SER A 563      42.482  41.833  53.323  1.00 17.42           C  
ANISOU 4319  CA  SER A 563     1975   2773   1870   -584   -604    177       C  
ATOM   4320  C   SER A 563      41.163  42.538  53.603  1.00 20.18           C  
ANISOU 4320  C   SER A 563     2424   3006   2238   -599   -583    156       C  
ATOM   4321  O   SER A 563      40.160  41.900  53.921  1.00 18.88           O  
ANISOU 4321  O   SER A 563     2335   2797   2043   -528   -539    157       O  
ATOM   4322  CB  SER A 563      43.476  42.110  54.449  1.00 23.33           C  
ANISOU 4322  CB  SER A 563     2689   3588   2587   -591   -694    120       C  
ATOM   4323  OG  SER A 563      42.950  41.676  55.686  1.00 27.56           O  
ANISOU 4323  OG  SER A 563     3314   4116   3041   -513   -711     88       O  
ATOM   4324  N   LYS A 564      41.171  43.861  53.494  1.00 19.69           N  
ANISOU 4324  N   LYS A 564     2358   2886   2239   -690   -604    135       N  
ATOM   4325  CA  LYS A 564      39.964  44.649  53.716  1.00 23.16           C  
ANISOU 4325  CA  LYS A 564     2880   3204   2717   -708   -580    117       C  
ATOM   4326  C   LYS A 564      38.855  44.340  52.703  1.00 26.88           C  
ANISOU 4326  C   LYS A 564     3378   3616   3218   -681   -518    177       C  
ATOM   4327  O   LYS A 564      37.668  44.333  53.051  1.00 21.39           O  
ANISOU 4327  O   LYS A 564     2754   2837   2535   -644   -487    162       O  
ATOM   4328  CB  LYS A 564      40.305  46.139  53.685  1.00 29.41           C  
ANISOU 4328  CB  LYS A 564     3648   3940   3587   -815   -605     90       C  
ATOM   4329  CG  LYS A 564      41.006  46.629  54.935  1.00 32.86           C  
ANISOU 4329  CG  LYS A 564     4082   4405   4000   -848   -668     -1       C  
ATOM   4330  CD  LYS A 564      41.449  48.077  54.782  1.00 36.63           C  
ANISOU 4330  CD  LYS A 564     4520   4825   4573   -964   -679    -34       C  
ATOM   4331  CE  LYS A 564      41.834  48.677  56.115  1.00 41.31           C  
ANISOU 4331  CE  LYS A 564     5128   5422   5144  -1003   -736   -147       C  
ATOM   4332  NZ  LYS A 564      42.836  47.823  56.805  1.00 46.46           N  
ANISOU 4332  NZ  LYS A 564     5735   6217   5700   -957   -812   -182       N  
ATOM   4333  N   LEU A 565      39.237  44.098  51.449  1.00 16.19           N  
ANISOU 4333  N   LEU A 565     1966   2308   1877   -700   -499    238       N  
ATOM   4334  CA  LEU A 565      38.245  43.843  50.409  1.00 15.58           C  
ANISOU 4334  CA  LEU A 565     1909   2192   1817   -679   -455    289       C  
ATOM   4335  C   LEU A 565      37.583  42.483  50.594  1.00 14.87           C  
ANISOU 4335  C   LEU A 565     1849   2122   1679   -587   -415    278       C  
ATOM   4336  O   LEU A 565      36.437  42.295  50.186  1.00 17.77           O  
ANISOU 4336  O   LEU A 565     2250   2434   2069   -559   -383    288       O  
ATOM   4337  CB  LEU A 565      38.866  43.934  49.002  1.00 15.89           C  
ANISOU 4337  CB  LEU A 565     1890   2284   1865   -727   -441    355       C  
ATOM   4338  CG  LEU A 565      38.831  45.328  48.378  1.00 16.31           C  
ANISOU 4338  CG  LEU A 565     1943   2271   1985   -807   -448    396       C  
ATOM   4339  CD1 LEU A 565      39.601  45.348  47.059  1.00 16.65           C  
ANISOU 4339  CD1 LEU A 565     1935   2373   2019   -852   -424    462       C  
ATOM   4340  CD2 LEU A 565      37.397  45.798  48.168  1.00 16.05           C  
ANISOU 4340  CD2 LEU A 565     1970   2137   1992   -787   -441    417       C  
ATOM   4341  N   SER A 566      38.295  41.539  51.212  1.00 18.60           N  
ANISOU 4341  N   SER A 566     2305   2669   2095   -537   -414    258       N  
ATOM   4342  CA  SER A 566      37.751  40.189  51.411  1.00 14.35           C  
ANISOU 4342  CA  SER A 566     1794   2140   1519   -447   -359    251       C  
ATOM   4343  C   SER A 566      36.493  40.175  52.287  1.00 17.17           C  
ANISOU 4343  C   SER A 566     2238   2400   1886   -402   -329    211       C  
ATOM   4344  O   SER A 566      35.742  39.200  52.297  1.00 18.15           O  
ANISOU 4344  O   SER A 566     2390   2501   2006   -337   -266    203       O  
ATOM   4345  CB  SER A 566      38.812  39.266  52.013  1.00 14.64           C  
ANISOU 4345  CB  SER A 566     1799   2266   1498   -395   -364    248       C  
ATOM   4346  OG  SER A 566      39.994  39.257  51.231  1.00 20.37           O  
ANISOU 4346  OG  SER A 566     2435   3076   2229   -437   -382    279       O  
ATOM   4347  N   TYR A 567      36.283  41.255  53.027  1.00 18.10           N  
ANISOU 4347  N   TYR A 567     2396   2454   2026   -439   -364    180       N  
ATOM   4348  CA  TYR A 567      35.118  41.414  53.883  1.00 18.47           C  
ANISOU 4348  CA  TYR A 567     2526   2397   2093   -408   -329    136       C  
ATOM   4349  C   TYR A 567      33.840  41.504  53.074  1.00 18.93           C  
ANISOU 4349  C   TYR A 567     2590   2376   2229   -406   -288    149       C  
ATOM   4350  O   TYR A 567      32.816  40.948  53.445  1.00 19.66           O  
ANISOU 4350  O   TYR A 567     2726   2403   2341   -352   -228    120       O  
ATOM   4351  CB  TYR A 567      35.277  42.671  54.730  1.00 19.15           C  
ANISOU 4351  CB  TYR A 567     2646   2434   2195   -464   -373     94       C  
ATOM   4352  CG  TYR A 567      34.067  43.070  55.548  1.00 16.27           C  
ANISOU 4352  CG  TYR A 567     2367   1948   1869   -448   -329     45       C  
ATOM   4353  CD1 TYR A 567      33.773  42.419  56.736  1.00 15.66           C  
ANISOU 4353  CD1 TYR A 567     2369   1854   1728   -384   -288      1       C  
ATOM   4354  CD2 TYR A 567      33.255  44.127  55.161  1.00 15.10           C  
ANISOU 4354  CD2 TYR A 567     2221   1694   1821   -497   -322     45       C  
ATOM   4355  CE1 TYR A 567      32.686  42.792  57.513  1.00 17.40           C  
ANISOU 4355  CE1 TYR A 567     2670   1955   1984   -373   -233    -49       C  
ATOM   4356  CE2 TYR A 567      32.166  44.513  55.936  1.00 17.90           C  
ANISOU 4356  CE2 TYR A 567     2648   1929   2226   -483   -273     -5       C  
ATOM   4357  CZ  TYR A 567      31.893  43.828  57.114  1.00 17.51           C  
ANISOU 4357  CZ  TYR A 567     2678   1865   2111   -424   -224    -56       C  
ATOM   4358  OH  TYR A 567      30.823  44.175  57.902  1.00 20.23           O  
ANISOU 4358  OH  TYR A 567     3097   2085   2504   -413   -159   -111       O  
ATOM   4359  N   TYR A 568      33.919  42.206  51.952  1.00 19.04           N  
ANISOU 4359  N   TYR A 568     2553   2394   2287   -464   -321    193       N  
ATOM   4360  CA  TYR A 568      32.732  42.564  51.193  1.00 13.72           C  
ANISOU 4360  CA  TYR A 568     1879   1645   1688   -468   -308    211       C  
ATOM   4361  C   TYR A 568      32.004  41.413  50.503  1.00 13.21           C  
ANISOU 4361  C   TYR A 568     1797   1601   1622   -415   -264    211       C  
ATOM   4362  O   TYR A 568      30.782  41.373  50.545  1.00 13.34           O  
ANISOU 4362  O   TYR A 568     1831   1536   1700   -386   -235    185       O  
ATOM   4363  CB  TYR A 568      33.093  43.650  50.175  1.00 22.55           C  
ANISOU 4363  CB  TYR A 568     2958   2769   2841   -539   -357    272       C  
ATOM   4364  CG  TYR A 568      33.423  44.962  50.852  1.00 21.98           C  
ANISOU 4364  CG  TYR A 568     2907   2634   2812   -596   -384    258       C  
ATOM   4365  CD1 TYR A 568      34.721  45.252  51.259  1.00 15.15           C  
ANISOU 4365  CD1 TYR A 568     2020   1828   1908   -642   -414    246       C  
ATOM   4366  CD2 TYR A 568      32.425  45.895  51.124  1.00 18.36           C  
ANISOU 4366  CD2 TYR A 568     2482   2051   2443   -606   -376    247       C  
ATOM   4367  CE1 TYR A 568      35.028  46.450  51.884  1.00 15.82           C  
ANISOU 4367  CE1 TYR A 568     2118   1854   2038   -703   -434    217       C  
ATOM   4368  CE2 TYR A 568      32.717  47.080  51.749  1.00 19.05           C  
ANISOU 4368  CE2 TYR A 568     2589   2072   2578   -663   -388    225       C  
ATOM   4369  CZ  TYR A 568      34.019  47.352  52.131  1.00 22.50           C  
ANISOU 4369  CZ  TYR A 568     3005   2572   2970   -715   -417    205       C  
ATOM   4370  OH  TYR A 568      34.292  48.541  52.755  1.00 16.77           O  
ANISOU 4370  OH  TYR A 568     2295   1777   2299   -780   -425    167       O  
ATOM   4371  N   PRO A 569      32.726  40.471  49.871  1.00 13.03           N  
ANISOU 4371  N   PRO A 569     1733   1680   1537   -403   -252    231       N  
ATOM   4372  CA  PRO A 569      31.940  39.391  49.274  1.00 12.65           C  
ANISOU 4372  CA  PRO A 569     1670   1640   1498   -358   -201    212       C  
ATOM   4373  C   PRO A 569      31.295  38.502  50.344  1.00 17.49           C  
ANISOU 4373  C   PRO A 569     2329   2195   2123   -289   -125    153       C  
ATOM   4374  O   PRO A 569      30.328  37.784  50.071  1.00 17.48           O  
ANISOU 4374  O   PRO A 569     2321   2157   2162   -254    -71    118       O  
ATOM   4375  CB  PRO A 569      32.979  38.611  48.452  1.00 14.51           C  
ANISOU 4375  CB  PRO A 569     1856   1992   1667   -367   -193    241       C  
ATOM   4376  CG  PRO A 569      34.128  39.525  48.301  1.00 15.03           C  
ANISOU 4376  CG  PRO A 569     1900   2103   1709   -427   -250    287       C  
ATOM   4377  CD  PRO A 569      34.158  40.307  49.572  1.00 15.12           C  
ANISOU 4377  CD  PRO A 569     1955   2049   1740   -431   -275    263       C  
ATOM   4378  N   ARG A 570      31.838  38.560  51.554  1.00 15.29           N  
ANISOU 4378  N   ARG A 570     2096   1906   1806   -269   -120    140       N  
ATOM   4379  CA  ARG A 570      31.322  37.779  52.667  1.00 15.38           C  
ANISOU 4379  CA  ARG A 570     2171   1861   1813   -200    -41     95       C  
ATOM   4380  C   ARG A 570      29.970  38.294  53.170  1.00 14.36           C  
ANISOU 4380  C   ARG A 570     2088   1603   1767   -194     -6     50       C  
ATOM   4381  O   ARG A 570      29.042  37.501  53.385  1.00 12.35           O  
ANISOU 4381  O   ARG A 570     1853   1285   1555   -145     81     10       O  
ATOM   4382  CB  ARG A 570      32.355  37.756  53.803  1.00 17.87           C  
ANISOU 4382  CB  ARG A 570     2528   2219   2044   -179    -60     99       C  
ATOM   4383  CG  ARG A 570      33.548  36.855  53.468  1.00 17.92           C  
ANISOU 4383  CG  ARG A 570     2484   2340   1984   -156    -64    136       C  
ATOM   4384  CD  ARG A 570      34.628  36.884  54.543  1.00 16.71           C  
ANISOU 4384  CD  ARG A 570     2357   2243   1749   -132   -107    144       C  
ATOM   4385  NE  ARG A 570      35.710  35.960  54.224  1.00 13.55           N  
ANISOU 4385  NE  ARG A 570     1899   1945   1304    -98   -105    182       N  
ATOM   4386  CZ  ARG A 570      36.995  36.260  54.342  1.00 18.27           C  
ANISOU 4386  CZ  ARG A 570     2449   2633   1860   -120   -182    204       C  
ATOM   4387  NH1 ARG A 570      37.352  37.448  54.800  1.00 20.03           N  
ANISOU 4387  NH1 ARG A 570     2679   2858   2075   -179   -265    186       N  
ATOM   4388  NH2 ARG A 570      37.918  35.371  54.015  1.00 14.72           N  
ANISOU 4388  NH2 ARG A 570     1938   2267   1388    -84   -170    238       N  
ATOM   4389  N   VAL A 571      29.843  39.610  53.333  1.00 14.55           N  
ANISOU 4389  N   VAL A 571     2124   1577   1827   -245    -62     54       N  
ATOM   4390  CA  VAL A 571      28.630  40.172  53.932  1.00 15.02           C  
ANISOU 4390  CA  VAL A 571     2228   1505   1975   -239    -23      9       C  
ATOM   4391  C   VAL A 571      27.932  41.268  53.107  1.00 17.12           C  
ANISOU 4391  C   VAL A 571     2449   1713   2341   -286    -73     29       C  
ATOM   4392  O   VAL A 571      26.786  41.614  53.396  1.00 15.55           O  
ANISOU 4392  O   VAL A 571     2265   1401   2240   -274    -35     -7       O  
ATOM   4393  CB  VAL A 571      28.925  40.740  55.346  1.00 21.08           C  
ANISOU 4393  CB  VAL A 571     3079   2227   2701   -243    -14    -25       C  
ATOM   4394  CG1 VAL A 571      29.485  39.648  56.261  1.00 17.86           C  
ANISOU 4394  CG1 VAL A 571     2729   1870   2188   -181     36    -36       C  
ATOM   4395  CG2 VAL A 571      29.874  41.936  55.273  1.00 18.40           C  
ANISOU 4395  CG2 VAL A 571     2723   1928   2339   -316   -107      0       C  
ATOM   4396  N   GLY A 572      28.619  41.812  52.099  1.00 23.34           N  
ANISOU 4396  N   GLY A 572     3184   2574   3110   -334   -152     90       N  
ATOM   4397  CA  GLY A 572      28.030  42.775  51.172  1.00 13.43           C  
ANISOU 4397  CA  GLY A 572     1888   1278   1937   -368   -204    130       C  
ATOM   4398  C   GLY A 572      27.491  42.037  49.950  1.00 18.86           C  
ANISOU 4398  C   GLY A 572     2516   2016   2633   -345   -213    147       C  
ATOM   4399  O   GLY A 572      27.878  42.296  48.804  1.00 16.40           O  
ANISOU 4399  O   GLY A 572     2163   1776   2292   -376   -272    208       O  
ATOM   4400  N   ALA A 573      26.587  41.101  50.203  1.00 17.96           N  
ANISOU 4400  N   ALA A 573     2402   1865   2559   -295   -147     86       N  
ATOM   4401  CA  ALA A 573      26.273  40.079  49.225  1.00 14.65           C  
ANISOU 4401  CA  ALA A 573     1927   1512   2126   -274   -139     75       C  
ATOM   4402  C   ALA A 573      25.026  39.297  49.592  1.00 20.00           C  
ANISOU 4402  C   ALA A 573     2598   2110   2893   -225    -60     -6       C  
ATOM   4403  O   ALA A 573      24.493  39.420  50.703  1.00 20.98           O  
ANISOU 4403  O   ALA A 573     2770   2128   3076   -202      5    -50       O  
ATOM   4404  CB  ALA A 573      27.444  39.134  49.091  1.00 12.50           C  
ANISOU 4404  CB  ALA A 573     1655   1352   1741   -272   -118     86       C  
ATOM   4405  N   HIS A 574      24.569  38.481  48.655  1.00 25.21           N  
ANISOU 4405  N   HIS A 574     2918   2950   3709   -710   -233    -78       N  
ATOM   4406  CA  HIS A 574      23.561  37.478  48.965  1.00 24.20           C  
ANISOU 4406  CA  HIS A 574     2852   2846   3496   -634   -224   -108       C  
ATOM   4407  C   HIS A 574      23.986  36.157  48.347  1.00 22.81           C  
ANISOU 4407  C   HIS A 574     2635   2759   3273   -571   -205    -55       C  
ATOM   4408  O   HIS A 574      24.415  36.118  47.182  1.00 12.80           O  
ANISOU 4408  O   HIS A 574     1319   1514   2029   -557   -164     15       O  
ATOM   4409  CB  HIS A 574      22.188  37.895  48.430  1.00 24.33           C  
ANISOU 4409  CB  HIS A 574     2936   2793   3516   -598   -177   -110       C  
ATOM   4410  CG  HIS A 574      21.762  39.267  48.864  1.00 36.33           C  
ANISOU 4410  CG  HIS A 574     4496   4212   5097   -649   -185   -156       C  
ATOM   4411  ND1 HIS A 574      20.886  39.483  49.897  1.00 41.70           N  
ANISOU 4411  ND1 HIS A 574     5244   4851   5749   -643   -201   -239       N  
ATOM   4412  CD2 HIS A 574      22.116  40.485  48.388  1.00 38.75           C  
ANISOU 4412  CD2 HIS A 574     4785   4446   5491   -704   -176   -128       C  
ATOM   4413  CE1 HIS A 574      20.707  40.795  50.048  1.00 39.71           C  
ANISOU 4413  CE1 HIS A 574     5018   4503   5568   -688   -202   -270       C  
ATOM   4414  NE2 HIS A 574      21.439  41.414  49.150  1.00 42.04           N  
ANISOU 4414  NE2 HIS A 574     5265   4773   5937   -727   -189   -202       N  
ATOM   4415  N   LEU A 575      23.868  35.081  49.124  1.00 18.94           N  
ANISOU 4415  N   LEU A 575     2167   2317   2712   -532   -232    -86       N  
ATOM   4416  CA  LEU A 575      23.951  33.732  48.578  1.00 20.13           C  
ANISOU 4416  CA  LEU A 575     2305   2530   2814   -459   -209    -47       C  
ATOM   4417  C   LEU A 575      22.720  33.565  47.681  1.00 20.96           C  
ANISOU 4417  C   LEU A 575     2463   2600   2901   -411   -153    -35       C  
ATOM   4418  O   LEU A 575      21.624  33.939  48.084  1.00 12.91           O  
ANISOU 4418  O   LEU A 575     1506   1529   1872   -414   -150    -77       O  
ATOM   4419  CB  LEU A 575      23.983  32.682  49.701  1.00 15.27           C  
ANISOU 4419  CB  LEU A 575     1714   1957   2132   -430   -252    -81       C  
ATOM   4420  CG  LEU A 575      23.987  31.193  49.334  1.00 18.37           C  
ANISOU 4420  CG  LEU A 575     2109   2397   2474   -351   -232    -50       C  
ATOM   4421  CD1 LEU A 575      25.203  30.826  48.475  1.00 11.69           C  
ANISOU 4421  CD1 LEU A 575     1176   1609   1657   -328   -219      8       C  
ATOM   4422  CD2 LEU A 575      23.938  30.299  50.572  1.00 13.43           C  
ANISOU 4422  CD2 LEU A 575     1519   1797   1787   -330   -277    -78       C  
ATOM   4423  N   ASP A 576      22.901  33.073  46.452  1.00 14.97           N  
ANISOU 4423  N   ASP A 576     1677   1874   2138   -368   -110     20       N  
ATOM   4424  CA  ASP A 576      21.778  32.869  45.539  1.00 18.14           C  
ANISOU 4424  CA  ASP A 576     2124   2253   2516   -323    -66     30       C  
ATOM   4425  C   ASP A 576      20.895  31.718  46.043  1.00 17.12           C  
ANISOU 4425  C   ASP A 576     2050   2129   2324   -277    -72     -9       C  
ATOM   4426  O   ASP A 576      21.359  30.857  46.811  1.00 13.01           O  
ANISOU 4426  O   ASP A 576     1527   1641   1774   -264   -100    -24       O  
ATOM   4427  CB  ASP A 576      22.264  32.545  44.119  1.00 14.25           C  
ANISOU 4427  CB  ASP A 576     1590   1804   2019   -287    -21     93       C  
ATOM   4428  CG  ASP A 576      22.729  33.776  43.335  1.00 19.32           C  
ANISOU 4428  CG  ASP A 576     2193   2430   2720   -329      5    146       C  
ATOM   4429  OD1 ASP A 576      23.087  34.803  43.946  1.00 16.11           O  
ANISOU 4429  OD1 ASP A 576     1770   1982   2370   -395    -20    138       O  
ATOM   4430  OD2 ASP A 576      22.780  33.679  42.085  1.00 16.45           O  
ANISOU 4430  OD2 ASP A 576     1815   2094   2342   -297     50    198       O  
ATOM   4431  N   SER A 577      19.640  31.695  45.597  1.00 13.41           N  
ANISOU 4431  N   SER A 577     1627   1629   1838   -254    -48    -21       N  
ATOM   4432  CA  SER A 577      18.796  30.522  45.813  1.00 12.78           C  
ANISOU 4432  CA  SER A 577     1593   1557   1707   -213    -45    -48       C  
ATOM   4433  C   SER A 577      18.828  29.571  44.610  1.00 14.45           C  
ANISOU 4433  C   SER A 577     1799   1803   1890   -161    -16    -20       C  
ATOM   4434  O   SER A 577      17.793  29.062  44.164  1.00 14.06           O  
ANISOU 4434  O   SER A 577     1784   1743   1814   -134     -2    -35       O  
ATOM   4435  CB  SER A 577      17.367  30.942  46.104  1.00 16.34           C  
ANISOU 4435  CB  SER A 577     2091   1961   2157   -219    -37    -85       C  
ATOM   4436  OG  SER A 577      17.293  31.630  47.336  1.00 16.69           O  
ANISOU 4436  OG  SER A 577     2152   1977   2214   -259    -60   -125       O  
ATOM   4437  N   HIS A 578      20.027  29.308  44.114  1.00 14.29           N  
ANISOU 4437  N   HIS A 578     1729   1825   1874   -145     -9     16       N  
ATOM   4438  CA  HIS A 578      20.202  28.492  42.921  1.00 12.66           C  
ANISOU 4438  CA  HIS A 578     1516   1655   1638    -92     23     38       C  
ATOM   4439  C   HIS A 578      20.863  27.164  43.260  1.00  9.44           C  
ANISOU 4439  C   HIS A 578     1105   1277   1205    -50     15     30       C  
ATOM   4440  O   HIS A 578      21.612  26.598  42.456  1.00  9.45           O  
ANISOU 4440  O   HIS A 578     1077   1318   1195     -6     40     53       O  
ATOM   4441  CB  HIS A 578      21.012  29.277  41.877  1.00 11.17           C  
ANISOU 4441  CB  HIS A 578     1274   1498   1473    -98     54     92       C  
ATOM   4442  CG  HIS A 578      20.288  30.479  41.343  1.00 11.92           C  
ANISOU 4442  CG  HIS A 578     1381   1559   1590   -126     66    112       C  
ATOM   4443  ND1 HIS A 578      20.936  31.640  40.967  1.00 16.40           N  
ANISOU 4443  ND1 HIS A 578     1906   2123   2203   -164     81    161       N  
ATOM   4444  CD2 HIS A 578      18.975  30.689  41.086  1.00 12.94           C  
ANISOU 4444  CD2 HIS A 578     1558   1655   1706   -119     66     94       C  
ATOM   4445  CE1 HIS A 578      20.049  32.526  40.549  1.00 16.58           C  
ANISOU 4445  CE1 HIS A 578     1956   2104   2239   -176     88    174       C  
ATOM   4446  NE2 HIS A 578      18.848  31.970  40.603  1.00 18.55           N  
ANISOU 4446  NE2 HIS A 578     2257   2339   2452   -146     78    133       N  
ATOM   4447  N   GLN A 579      20.571  26.661  44.459  1.00 11.69           N  
ANISOU 4447  N   GLN A 579     1422   1538   1479    -58    -17      0       N  
ATOM   4448  CA  GLN A 579      21.195  25.427  44.927  1.00  9.16           C  
ANISOU 4448  CA  GLN A 579     1105   1236   1140    -17    -30      0       C  
ATOM   4449  C   GLN A 579      20.883  24.244  44.008  1.00 10.40           C  
ANISOU 4449  C   GLN A 579     1292   1390   1268     43      0     -8       C  
ATOM   4450  O   GLN A 579      19.748  24.088  43.528  1.00 14.62           O  
ANISOU 4450  O   GLN A 579     1873   1897   1785     41     14    -33       O  
ATOM   4451  CB  GLN A 579      20.764  25.098  46.369  1.00  9.05           C  
ANISOU 4451  CB  GLN A 579     1133   1195   1110    -37    -67    -25       C  
ATOM   4452  CG  GLN A 579      19.254  24.835  46.581  1.00  8.59           C  
ANISOU 4452  CG  GLN A 579     1143   1091   1030    -49    -56    -59       C  
ATOM   4453  CD  GLN A 579      18.496  26.111  46.936  1.00  8.77           C  
ANISOU 4453  CD  GLN A 579     1172   1091   1068   -102    -59    -79       C  
ATOM   4454  OE1 GLN A 579      18.910  27.213  46.567  1.00  8.54           O  
ANISOU 4454  OE1 GLN A 579     1105   1069   1071   -126    -58    -67       O  
ATOM   4455  NE2 GLN A 579      17.382  25.966  47.662  1.00  9.90           N  
ANISOU 4455  NE2 GLN A 579     1364   1205   1193   -120    -59   -110       N  
ATOM   4456  N   GLY A 580      21.900  23.417  43.764  1.00 11.90           N  
ANISOU 4456  N   GLY A 580     1455   1611   1456     96      7      9       N  
ATOM   4457  CA  GLY A 580      21.768  22.283  42.867  1.00  9.64           C  
ANISOU 4457  CA  GLY A 580     1198   1319   1144    158     37     -6       C  
ATOM   4458  C   GLY A 580      22.907  21.295  42.997  1.00 14.12           C  
ANISOU 4458  C   GLY A 580     1740   1908   1717    223     38      9       C  
ATOM   4459  O   GLY A 580      23.823  21.506  43.795  1.00 11.83           O  
ANISOU 4459  O   GLY A 580     1401   1646   1449    219     10     37       O  
ATOM   4460  N   CYS A 581      22.817  20.210  42.224  1.00 10.42           N  
ANISOU 4460  N   CYS A 581     1306   1425   1227    285     66    -13       N  
ATOM   4461  CA  CYS A 581      23.906  19.238  42.007  1.00 11.10           C  
ANISOU 4461  CA  CYS A 581     1367   1531   1320    367     82     -3       C  
ATOM   4462  C   CYS A 581      24.170  18.270  43.171  1.00 13.03           C  
ANISOU 4462  C   CYS A 581     1637   1738   1578    397     46      6       C  
ATOM   4463  O   CYS A 581      25.179  17.562  43.166  1.00 17.95           O  
ANISOU 4463  O   CYS A 581     2228   2378   2215    468     51     24       O  
ATOM   4464  CB  CYS A 581      25.200  19.976  41.673  1.00 11.57           C  
ANISOU 4464  CB  CYS A 581     1325   1669   1401    378     99     40       C  
ATOM   4465  SG  CYS A 581      25.045  21.205  40.321  1.00 15.14           S  
ANISOU 4465  SG  CYS A 581     1743   2171   1838    342    147     52       S  
ATOM   4466  N   SER A 582      23.265  18.209  44.145  1.00 11.79           N  
ANISOU 4466  N   SER A 582     1536   1530   1414    348     12     -3       N  
ATOM   4467  CA  SER A 582      23.504  17.409  45.339  1.00 14.05           C  
ANISOU 4467  CA  SER A 582     1848   1785   1704    369    -24     19       C  
ATOM   4468  C   SER A 582      23.255  15.911  45.123  1.00 15.65           C  
ANISOU 4468  C   SER A 582     2121   1919   1907    432     -8      2       C  
ATOM   4469  O   SER A 582      23.569  15.101  45.978  1.00 15.12           O  
ANISOU 4469  O   SER A 582     2077   1822   1847    466    -33     29       O  
ATOM   4470  CB  SER A 582      22.624  17.908  46.482  1.00 10.75           C  
ANISOU 4470  CB  SER A 582     1468   1345   1273    293    -57     19       C  
ATOM   4471  OG  SER A 582      21.257  17.742  46.140  1.00 13.35           O  
ANISOU 4471  OG  SER A 582     1863   1621   1589    258    -36    -19       O  
ATOM   4472  N   CYS A 583      22.710  15.547  43.972  1.00 14.57           N  
ANISOU 4472  N   CYS A 583     2018   1756   1761    447     30    -43       N  
ATOM   4473  CA  CYS A 583      22.481  14.142  43.628  1.00 19.84           C  
ANISOU 4473  CA  CYS A 583     2755   2350   2433    504     47    -71       C  
ATOM   4474  C   CYS A 583      22.778  13.919  42.149  1.00 21.42           C  
ANISOU 4474  C   CYS A 583     2946   2571   2622    558     93   -113       C  
ATOM   4475  O   CYS A 583      21.976  13.342  41.414  1.00 15.24           O  
ANISOU 4475  O   CYS A 583     2226   1738   1825    557    110   -167       O  
ATOM   4476  CB  CYS A 583      21.036  13.722  43.945  1.00 24.98           C  
ANISOU 4476  CB  CYS A 583     3490   2922   3078    443     39   -101       C  
ATOM   4477  SG  CYS A 583      20.608  13.673  45.729  1.00 15.86           S  
ANISOU 4477  SG  CYS A 583     2367   1734   1926    390     -2    -52       S  
ATOM   4478  N   SER A 584      23.937  14.391  41.719  1.00 19.08           N  
ANISOU 4478  N   SER A 584     2569   2353   2329    603    112    -88       N  
ATOM   4479  CA  SER A 584      24.140  14.658  40.308  1.00 20.57           C  
ANISOU 4479  CA  SER A 584     2733   2591   2491    631    160   -118       C  
ATOM   4480  C   SER A 584      24.434  13.419  39.445  1.00 20.27           C  
ANISOU 4480  C   SER A 584     2738   2518   2445    726    199   -166       C  
ATOM   4481  O   SER A 584      24.863  12.366  39.933  1.00 19.71           O  
ANISOU 4481  O   SER A 584     2694   2393   2404    789    193   -163       O  
ATOM   4482  CB  SER A 584      25.259  15.685  40.165  1.00 16.79           C  
ANISOU 4482  CB  SER A 584     2146   2212   2022    635    174    -69       C  
ATOM   4483  OG  SER A 584      26.455  15.164  40.693  1.00 15.66           O  
ANISOU 4483  OG  SER A 584     1951   2087   1912    705    169    -34       O  
ATOM   4484  N   ILE A 585      24.168  13.566  38.153  1.00 20.03           N  
ANISOU 4484  N   ILE A 585     2719   2518   2371    735    238   -212       N  
ATOM   4485  CA  ILE A 585      24.526  12.569  37.150  1.00 14.72           C  
ANISOU 4485  CA  ILE A 585     2082   1833   1679    827    283   -268       C  
ATOM   4486  C   ILE A 585      25.990  12.188  37.307  1.00 15.84           C  
ANISOU 4486  C   ILE A 585     2156   2009   1852    925    311   -233       C  
ATOM   4487  O   ILE A 585      26.862  13.060  37.415  1.00 16.03           O  
ANISOU 4487  O   ILE A 585     2080   2123   1887    923    321   -175       O  
ATOM   4488  CB  ILE A 585      24.275  13.120  35.718  1.00 14.81           C  
ANISOU 4488  CB  ILE A 585     2091   1913   1623    823    325   -305       C  
ATOM   4489  CG1 ILE A 585      22.786  13.415  35.511  1.00 14.14           C  
ANISOU 4489  CG1 ILE A 585     2070   1795   1509    735    291   -343       C  
ATOM   4490  CG2 ILE A 585      24.816  12.184  34.636  1.00 15.89           C  
ANISOU 4490  CG2 ILE A 585     2256   2055   1728    927    380   -366       C  
ATOM   4491  CD1 ILE A 585      22.501  14.324  34.332  1.00 14.08           C  
ANISOU 4491  CD1 ILE A 585     2043   1871   1434    713    316   -350       C  
ATOM   4492  N   GLY A 586      26.251  10.885  37.342  1.00 16.33           N  
ANISOU 4492  N   GLY A 586     2271   1998   1937   1010    321   -267       N  
ATOM   4493  CA  GLY A 586      27.601  10.383  37.493  1.00 17.26           C  
ANISOU 4493  CA  GLY A 586     2327   2141   2091   1118    346   -237       C  
ATOM   4494  C   GLY A 586      27.998  10.192  38.951  1.00 27.26           C  
ANISOU 4494  C   GLY A 586     3567   3375   3415   1119    291   -167       C  
ATOM   4495  O   GLY A 586      29.064   9.635  39.243  1.00 18.07           O  
ANISOU 4495  O   GLY A 586     2356   2220   2290   1215    298   -137       O  
ATOM   4496  N   ARG A 587      27.156  10.644  39.878  1.00 16.31           N  
ANISOU 4496  N   ARG A 587     2210   1956   2031   1018    235   -141       N  
ATOM   4497  CA  ARG A 587      27.480  10.486  41.307  1.00 16.32           C  
ANISOU 4497  CA  ARG A 587     2195   1934   2072   1014    179    -74       C  
ATOM   4498  C   ARG A 587      26.385   9.776  42.085  1.00 20.95           C  
ANISOU 4498  C   ARG A 587     2892   2403   2665    969    143    -83       C  
ATOM   4499  O   ARG A 587      26.627   8.719  42.650  1.00 27.61           O  
ANISOU 4499  O   ARG A 587     3779   3170   3541   1032    129    -64       O  
ATOM   4500  CB  ARG A 587      27.784  11.841  41.937  1.00 19.09           C  
ANISOU 4500  CB  ARG A 587     2454   2379   2420    937    146    -17       C  
ATOM   4501  CG  ARG A 587      29.068  12.471  41.391  1.00 27.79           C  
ANISOU 4501  CG  ARG A 587     3431   3596   3532    982    178     11       C  
ATOM   4502  CD  ARG A 587      29.186  13.925  41.816  1.00 40.59           C  
ANISOU 4502  CD  ARG A 587     4973   5298   5151    885    149     52       C  
ATOM   4503  NE  ARG A 587      29.512  14.085  43.236  1.00 51.05           N  
ANISOU 4503  NE  ARG A 587     6268   6628   6500    858     79    105       N  
ATOM   4504  CZ  ARG A 587      30.715  13.873  43.761  1.00 59.04           C  
ANISOU 4504  CZ  ARG A 587     7195   7690   7546    921     55    153       C  
ATOM   4505  NH1 ARG A 587      31.720  13.481  42.985  1.00 60.76           N  
ANISOU 4505  NH1 ARG A 587     7344   7956   7786   1017    104    156       N  
ATOM   4506  NH2 ARG A 587      30.912  14.049  45.064  1.00 57.24           N  
ANISOU 4506  NH2 ARG A 587     6950   7472   7328    890    -17    197       N  
ATOM   4507  N   THR A 588      25.185  10.340  42.107  1.00 15.15           N  
ANISOU 4507  N   THR A 588     2200   1654   1904    863    129   -106       N  
ATOM   4508  CA  THR A 588      24.056   9.665  42.733  1.00 21.00           C  
ANISOU 4508  CA  THR A 588     3040   2287   2652    813    105   -118       C  
ATOM   4509  C   THR A 588      23.178   8.944  41.701  1.00 20.41           C  
ANISOU 4509  C   THR A 588     3049   2137   2568    810    135   -202       C  
ATOM   4510  O   THR A 588      22.644   7.872  41.977  1.00 22.19           O  
ANISOU 4510  O   THR A 588     3361   2251   2819    814    129   -220       O  
ATOM   4511  CB  THR A 588      23.185  10.655  43.549  1.00 20.38           C  
ANISOU 4511  CB  THR A 588     2956   2233   2554    696     70    -92       C  
ATOM   4512  OG1 THR A 588      23.942  11.167  44.652  1.00 13.97           O  
ANISOU 4512  OG1 THR A 588     2084   1475   1749    696     33    -22       O  
ATOM   4513  CG2 THR A 588      21.949   9.966  44.099  1.00 16.44           C  
ANISOU 4513  CG2 THR A 588     2553   1631   2062    639     56   -105       C  
ATOM   4514  N   VAL A 589      23.017   9.538  40.522  1.00 14.94           N  
ANISOU 4514  N   VAL A 589     2333   1506   1837    798    164   -253       N  
ATOM   4515  CA  VAL A 589      22.251   8.912  39.448  1.00 20.41           C  
ANISOU 4515  CA  VAL A 589     3099   2145   2510    798    186   -341       C  
ATOM   4516  C   VAL A 589      23.070   8.737  38.163  1.00 23.18           C  
ANISOU 4516  C   VAL A 589     3429   2547   2833    890    237   -388       C  
ATOM   4517  O   VAL A 589      24.086   9.406  37.967  1.00 21.22           O  
ANISOU 4517  O   VAL A 589     3092   2397   2575    932    260   -349       O  
ATOM   4518  CB  VAL A 589      20.987   9.720  39.121  1.00 19.13           C  
ANISOU 4518  CB  VAL A 589     2948   2008   2313    690    170   -369       C  
ATOM   4519  CG1 VAL A 589      20.214  10.011  40.409  1.00 13.74           C  
ANISOU 4519  CG1 VAL A 589     2275   1291   1654    602    130   -321       C  
ATOM   4520  CG2 VAL A 589      21.341  11.023  38.396  1.00 13.96           C  
ANISOU 4520  CG2 VAL A 589     2212   1477   1614    679    188   -356       C  
ATOM   4521  N   ASP A 590      22.636   7.825  37.292  1.00 16.64           N  
ANISOU 4521  N   ASP A 590     2679   1651   1991    919    256   -475       N  
ATOM   4522  CA  ASP A 590      23.308   7.656  36.005  1.00 24.74           C  
ANISOU 4522  CA  ASP A 590     3695   2730   2975   1006    309   -532       C  
ATOM   4523  C   ASP A 590      22.762   8.670  34.982  1.00 23.60           C  
ANISOU 4523  C   ASP A 590     3528   2684   2756    949    319   -561       C  
ATOM   4524  O   ASP A 590      21.976   9.562  35.335  1.00 16.00           O  
ANISOU 4524  O   ASP A 590     2545   1749   1784    850    284   -529       O  
ATOM   4525  CB  ASP A 590      23.182   6.209  35.486  1.00 18.55           C  
ANISOU 4525  CB  ASP A 590     2980   1851   2218   1026    316   -600       C  
ATOM   4526  CG  ASP A 590      21.745   5.768  35.255  1.00 23.48           C  
ANISOU 4526  CG  ASP A 590     3683   2398   2839    927    282   -664       C  
ATOM   4527  OD1 ASP A 590      20.872   6.616  34.991  1.00 22.96           O  
ANISOU 4527  OD1 ASP A 590     3614   2381   2729    850    262   -676       O  
ATOM   4528  OD2 ASP A 590      21.487   4.545  35.319  1.00 25.95           O  
ANISOU 4528  OD2 ASP A 590     4057   2603   3200    925    274   -702       O  
ATOM   4529  N   SER A 591      23.180   8.529  33.723  1.00 22.52           N  
ANISOU 4529  N   SER A 591     3379   2605   2571    990    361   -606       N  
ATOM   4530  CA  SER A 591      22.796   9.468  32.661  1.00 20.60           C  
ANISOU 4530  CA  SER A 591     3115   2463   2248    952    375   -624       C  
ATOM   4531  C   SER A 591      21.348   9.277  32.220  1.00 21.99           C  
ANISOU 4531  C   SER A 591     3362   2596   2398    863    332   -688       C  
ATOM   4532  O   SER A 591      20.811  10.078  31.464  1.00 17.66           O  
ANISOU 4532  O   SER A 591     2802   2123   1785    821    328   -697       O  
ATOM   4533  CB  SER A 591      23.733   9.330  31.452  1.00 26.48           C  
ANISOU 4533  CB  SER A 591     3826   3288   2948   1019    435   -644       C  
ATOM   4534  OG  SER A 591      25.066   9.691  31.801  1.00 33.09           O  
ANISOU 4534  OG  SER A 591     4575   4188   3810   1091    476   -575       O  
ATOM   4535  N   ASN A 592      20.722   8.211  32.695  1.00 22.16           N  
ANISOU 4535  N   ASN A 592     3449   2498   2472    833    299   -728       N  
ATOM   4536  CA  ASN A 592      19.295   8.022  32.495  1.00 17.31           C  
ANISOU 4536  CA  ASN A 592     2887   1839   1852    736    253   -780       C  
ATOM   4537  C   ASN A 592      18.511   8.520  33.705  1.00 18.59           C  
ANISOU 4537  C   ASN A 592     3051   1959   2052    665    210   -733       C  
ATOM   4538  O   ASN A 592      17.297   8.300  33.806  1.00 20.01           O  
ANISOU 4538  O   ASN A 592     3265   2091   2247    579    170   -765       O  
ATOM   4539  CB  ASN A 592      18.995   6.546  32.223  1.00 18.40           C  
ANISOU 4539  CB  ASN A 592     3089   1871   2029    733    247   -853       C  
ATOM   4540  CG  ASN A 592      19.615   6.059  30.929  1.00 27.86           C  
ANISOU 4540  CG  ASN A 592     4295   3110   3181    794    289   -914       C  
ATOM   4541  OD1 ASN A 592      19.763   6.825  29.974  1.00 25.36           O  
ANISOU 4541  OD1 ASN A 592     3947   2902   2785    804    309   -919       O  
ATOM   4542  ND2 ASN A 592      20.018   4.793  30.903  1.00 23.61           N  
ANISOU 4542  ND2 ASN A 592     3797   2483   2691    840    306   -958       N  
ATOM   4543  N   LEU A 593      19.233   9.185  34.608  1.00 17.69           N  
ANISOU 4543  N   LEU A 593     2893   1872   1958    698    220   -656       N  
ATOM   4544  CA  LEU A 593      18.691   9.779  35.838  1.00 18.50           C  
ANISOU 4544  CA  LEU A 593     2967   1960   2104    614    183   -585       C  
ATOM   4545  C   LEU A 593      18.261   8.741  36.876  1.00 18.44           C  
ANISOU 4545  C   LEU A 593     3020   1825   2163    590    160   -583       C  
ATOM   4546  O   LEU A 593      17.661   9.100  37.877  1.00 14.24           O  
ANISOU 4546  O   LEU A 593     2477   1275   1660    518    132   -535       O  
ATOM   4547  CB  LEU A 593      17.502  10.703  35.533  1.00 17.40           C  
ANISOU 4547  CB  LEU A 593     2813   1868   1932    521    154   -593       C  
ATOM   4548  CG  LEU A 593      17.739  11.904  34.621  1.00 20.16           C  
ANISOU 4548  CG  LEU A 593     3102   2340   2217    527    170   -576       C  
ATOM   4549  CD1 LEU A 593      16.429  12.628  34.374  1.00 13.22           C  
ANISOU 4549  CD1 LEU A 593     2221   1488   1316    442    133   -587       C  
ATOM   4550  CD2 LEU A 593      18.754  12.842  35.236  1.00 13.26           C  
ANISOU 4550  CD2 LEU A 593     2147   1529   1362    544    189   -485       C  
ATOM   4551  N   LYS A 594      18.567   7.468  36.640  1.00 15.87           N  
ANISOU 4551  N   LYS A 594     2761   1409   1861    653    174   -634       N  
ATOM   4552  CA  LYS A 594      18.233   6.412  37.590  1.00 16.25           C  
ANISOU 4552  CA  LYS A 594     2864   1332   1979    628    156   -618       C  
ATOM   4553  C   LYS A 594      19.189   6.415  38.789  1.00 26.57           C  
ANISOU 4553  C   LYS A 594     4146   2626   3324    683    159   -526       C  
ATOM   4554  O   LYS A 594      20.417   6.432  38.626  1.00 20.83           O  
ANISOU 4554  O   LYS A 594     3377   1944   2593    779    185   -503       O  
ATOM   4555  CB  LYS A 594      18.246   5.038  36.906  1.00 21.48           C  
ANISOU 4555  CB  LYS A 594     3570   1921   2672    649    167   -684       C  
ATOM   4556  CG  LYS A 594      17.682   3.910  37.776  1.00 28.17           C  
ANISOU 4556  CG  LYS A 594     4477   2633   3596    606    148   -671       C  
ATOM   4557  CD  LYS A 594      17.617   2.571  37.037  1.00 36.72           C  
ANISOU 4557  CD  LYS A 594     5603   3635   4714    621    158   -747       C  
ATOM   4558  CE  LYS A 594      19.001   1.931  36.854  1.00 45.92           C  
ANISOU 4558  CE  LYS A 594     6767   4784   5896    746    193   -741       C  
ATOM   4559  NZ  LYS A 594      19.705   1.573  38.139  1.00 43.13           N  
ANISOU 4559  NZ  LYS A 594     6420   4370   5597    799    191   -648       N  
ATOM   4560  N   VAL A 595      18.623   6.393  39.992  1.00 22.49           N  
ANISOU 4560  N   VAL A 595     3642   2062   2842    615    131   -468       N  
ATOM   4561  CA  VAL A 595      19.432   6.297  41.198  1.00 19.22           C  
ANISOU 4561  CA  VAL A 595     3205   1638   2458    655    124   -376       C  
ATOM   4562  C   VAL A 595      20.252   4.998  41.189  1.00 16.99           C  
ANISOU 4562  C   VAL A 595     2975   1261   2219    762    140   -381       C  
ATOM   4563  O   VAL A 595      19.703   3.887  41.116  1.00 21.61           O  
ANISOU 4563  O   VAL A 595     3638   1729   2843    747    140   -418       O  
ATOM   4564  CB  VAL A 595      18.560   6.369  42.469  1.00 24.50           C  
ANISOU 4564  CB  VAL A 595     3895   2265   3147    562     96   -319       C  
ATOM   4565  CG1 VAL A 595      19.420   6.231  43.702  1.00 15.55           C  
ANISOU 4565  CG1 VAL A 595     2747   1130   2033    608     82   -224       C  
ATOM   4566  CG2 VAL A 595      17.793   7.681  42.517  1.00 14.28           C  
ANISOU 4566  CG2 VAL A 595     2547   1064   1816    469     83   -315       C  
ATOM   4567  N   ILE A 596      21.573   5.145  41.229  1.00 17.27           N  
ANISOU 4567  N   ILE A 596     2951   1357   2255    861    153   -341       N  
ATOM   4568  CA  ILE A 596      22.472   3.995  41.244  1.00 18.47           C  
ANISOU 4568  CA  ILE A 596     3135   1432   2452    978    170   -337       C  
ATOM   4569  C   ILE A 596      22.199   3.085  42.454  1.00 21.22           C  
ANISOU 4569  C   ILE A 596     3544   1663   2853    961    143   -273       C  
ATOM   4570  O   ILE A 596      22.072   3.555  43.588  1.00 22.60           O  
ANISOU 4570  O   ILE A 596     3705   1858   3023    920    113   -193       O  
ATOM   4571  CB  ILE A 596      23.958   4.451  41.243  1.00 20.91           C  
ANISOU 4571  CB  ILE A 596     3346   1845   2756   1084    184   -289       C  
ATOM   4572  CG1 ILE A 596      24.227   5.355  40.032  1.00 22.59           C  
ANISOU 4572  CG1 ILE A 596     3490   2180   2913   1088    219   -340       C  
ATOM   4573  CG2 ILE A 596      24.905   3.244  41.217  1.00 20.05           C  
ANISOU 4573  CG2 ILE A 596     3242   1678   2698   1187    199   -280       C  
ATOM   4574  CD1 ILE A 596      25.560   6.095  40.082  1.00 21.22           C  
ANISOU 4574  CD1 ILE A 596     3195   2134   2734   1154    232   -282       C  
ATOM   4575  N   GLY A 597      22.098   1.785  42.199  1.00 20.06           N  
ANISOU 4575  N   GLY A 597     3451   1415   2757    973    152   -305       N  
ATOM   4576  CA  GLY A 597      21.784   0.817  43.233  1.00 26.25           C  
ANISOU 4576  CA  GLY A 597     4297   2083   3596    952    132   -246       C  
ATOM   4577  C   GLY A 597      20.300   0.488  43.328  1.00 30.13           C  
ANISOU 4577  C   GLY A 597     4852   2494   4102    824    123   -277       C  
ATOM   4578  O   GLY A 597      19.915  -0.425  44.062  1.00 34.48           O  
ANISOU 4578  O   GLY A 597     5456   2940   4703    795    114   -235       O  
ATOM   4579  N   THR A 598      19.462   1.210  42.584  1.00 19.75           N  
ANISOU 4579  N   THR A 598     3525   1233   2747    746    126   -348       N  
ATOM   4580  CA  THR A 598      18.021   0.942  42.593  1.00 23.90           C  
ANISOU 4580  CA  THR A 598     4092   1701   3290    620    115   -382       C  
ATOM   4581  C   THR A 598      17.529   0.444  41.260  1.00 25.26           C  
ANISOU 4581  C   THR A 598     4272   1857   3469    594    124   -497       C  
ATOM   4582  O   THR A 598      18.132   0.736  40.230  1.00 23.70           O  
ANISOU 4582  O   THR A 598     4043   1729   3234    654    141   -554       O  
ATOM   4583  CB  THR A 598      17.194   2.186  42.938  1.00 20.53           C  
ANISOU 4583  CB  THR A 598     3639   1347   2813    529    101   -366       C  
ATOM   4584  OG1 THR A 598      17.205   3.090  41.819  1.00 19.68           O  
ANISOU 4584  OG1 THR A 598     3485   1343   2651    533    107   -437       O  
ATOM   4585  CG2 THR A 598      17.746   2.865  44.172  1.00 17.78           C  
ANISOU 4585  CG2 THR A 598     3279   1032   2444    559     91   -263       C  
ATOM   4586  N   GLN A 599      16.421  -0.299  41.284  1.00 24.26           N  
ANISOU 4586  N   GLN A 599     4185   1646   3388    503    113   -528       N  
ATOM   4587  CA  GLN A 599      15.826  -0.804  40.057  1.00 23.56           C  
ANISOU 4587  CA  GLN A 599     4104   1539   3309    468    113   -641       C  
ATOM   4588  C   GLN A 599      15.057   0.281  39.348  1.00 21.57           C  
ANISOU 4588  C   GLN A 599     3808   1396   2992    399    100   -692       C  
ATOM   4589  O   GLN A 599      15.004   0.317  38.123  1.00 22.31           O  
ANISOU 4589  O   GLN A 599     3889   1535   3053    408    104   -781       O  
ATOM   4590  CB  GLN A 599      14.871  -1.969  40.329  1.00 25.13           C  
ANISOU 4590  CB  GLN A 599     4350   1609   3587    390    101   -658       C  
ATOM   4591  CG  GLN A 599      15.526  -3.270  40.754  1.00 33.54           C  
ANISOU 4591  CG  GLN A 599     5468   2548   4729    455    113   -628       C  
ATOM   4592  CD  GLN A 599      14.515  -4.396  40.873  1.00 45.35           C  
ANISOU 4592  CD  GLN A 599     7007   3915   6307    371    101   -655       C  
ATOM   4593  OE1 GLN A 599      13.477  -4.383  40.207  1.00 49.64           O  
ANISOU 4593  OE1 GLN A 599     7540   4467   6854    283     84   -735       O  
ATOM   4594  NE2 GLN A 599      14.802  -5.365  41.734  1.00 47.46           N  
ANISOU 4594  NE2 GLN A 599     7321   4065   6646    396    105   -585       N  
ATOM   4595  N   ASN A 600      14.459   1.175  40.120  1.00 19.37           N  
ANISOU 4595  N   ASN A 600     3505   1161   2693    333     85   -634       N  
ATOM   4596  CA  ASN A 600      13.363   1.935  39.569  1.00 18.73           C  
ANISOU 4596  CA  ASN A 600     3388   1153   2578    243     66   -683       C  
ATOM   4597  C   ASN A 600      13.088   3.236  40.259  1.00 17.44           C  
ANISOU 4597  C   ASN A 600     3186   1069   2372    205     59   -621       C  
ATOM   4598  O   ASN A 600      11.939   3.661  40.305  1.00 17.06           O  
ANISOU 4598  O   ASN A 600     3112   1046   2323    111     41   -633       O  
ATOM   4599  CB  ASN A 600      12.090   1.081  39.598  1.00 24.64           C  
ANISOU 4599  CB  ASN A 600     4155   1819   3387    143     46   -719       C  
ATOM   4600  CG  ASN A 600      11.615   0.798  41.018  1.00 24.78           C  
ANISOU 4600  CG  ASN A 600     4193   1766   3456     86     47   -628       C  
ATOM   4601  OD1 ASN A 600      12.409   0.815  41.962  1.00 21.36           O  
ANISOU 4601  OD1 ASN A 600     3781   1311   3023    139     63   -544       O  
ATOM   4602  ND2 ASN A 600      10.320   0.543  41.174  1.00 23.93           N  
ANISOU 4602  ND2 ASN A 600     4076   1629   3387    -21     30   -643       N  
ATOM   4603  N   VAL A 601      14.132   3.874  40.786  1.00 16.87           N  
ANISOU 4603  N   VAL A 601     3104   1036   2269    279     72   -559       N  
ATOM   4604  CA  VAL A 601      14.000   5.216  41.326  1.00 15.70           C  
ANISOU 4604  CA  VAL A 601     2918    969   2077    251     67   -512       C  
ATOM   4605  C   VAL A 601      14.825   6.161  40.473  1.00 19.85           C  
ANISOU 4605  C   VAL A 601     3399   1602   2541    322     75   -535       C  
ATOM   4606  O   VAL A 601      15.940   5.832  40.074  1.00 15.66           O  
ANISOU 4606  O   VAL A 601     2872   1074   2005    421     94   -542       O  
ATOM   4607  CB  VAL A 601      14.479   5.316  42.797  1.00 15.46           C  
ANISOU 4607  CB  VAL A 601     2896    917   2061    266     71   -409       C  
ATOM   4608  CG1 VAL A 601      14.212   6.700  43.334  1.00 14.37           C  
ANISOU 4608  CG1 VAL A 601     2679    894   1884    215     62   -362       C  
ATOM   4609  CG2 VAL A 601      13.787   4.273  43.664  1.00 16.14           C  
ANISOU 4609  CG2 VAL A 601     3042    886   2205    208     72   -375       C  
ATOM   4610  N   ARG A 602      14.273   7.332  40.187  1.00 18.44           N  
ANISOU 4610  N   ARG A 602     3159   1525   2323    268     64   -538       N  
ATOM   4611  CA  ARG A 602      15.006   8.348  39.450  1.00 19.67           C  
ANISOU 4611  CA  ARG A 602     3251   1799   2425    319     73   -538       C  
ATOM   4612  C   ARG A 602      14.991   9.658  40.222  1.00 21.07           C  
ANISOU 4612  C   ARG A 602     3355   2062   2590    281     66   -465       C  
ATOM   4613  O   ARG A 602      14.100   9.894  41.045  1.00 18.28           O  
ANISOU 4613  O   ARG A 602     2999   1691   2254    204     52   -438       O  
ATOM   4614  CB  ARG A 602      14.408   8.566  38.050  1.00 14.07           C  
ANISOU 4614  CB  ARG A 602     2543   1133   1669    303     66   -622       C  
ATOM   4615  CG  ARG A 602      14.323   7.314  37.195  1.00 15.27           C  
ANISOU 4615  CG  ARG A 602     2747   1222   1834    323     70   -700       C  
ATOM   4616  CD  ARG A 602      14.048   7.653  35.739  1.00 16.83           C  
ANISOU 4616  CD  ARG A 602     2922   1502   1970    322     66   -768       C  
ATOM   4617  NE  ARG A 602      13.488   6.508  35.026  1.00 27.86           N  
ANISOU 4617  NE  ARG A 602     4354   2844   3389    294     57   -846       N  
ATOM   4618  CZ  ARG A 602      13.948   6.029  33.871  1.00 25.87           C  
ANISOU 4618  CZ  ARG A 602     4115   2613   3101    344     75   -909       C  
ATOM   4619  NH1 ARG A 602      14.999   6.580  33.273  1.00 17.21           N  
ANISOU 4619  NH1 ARG A 602     2996   1597   1945    427    107   -897       N  
ATOM   4620  NH2 ARG A 602      13.355   4.982  33.321  1.00 23.77           N  
ANISOU 4620  NH2 ARG A 602     3885   2287   2859    308     65   -985       N  
ATOM   4621  N   VAL A 603      15.994  10.491  39.957  1.00 13.85           N  
ANISOU 4621  N   VAL A 603     2381   1235   1645    334     79   -434       N  
ATOM   4622  CA  VAL A 603      15.991  11.873  40.391  1.00 14.76           C  
ANISOU 4622  CA  VAL A 603     2427   1436   1745    297     71   -382       C  
ATOM   4623  C   VAL A 603      15.957  12.767  39.150  1.00 14.29           C  
ANISOU 4623  C   VAL A 603     2327   1463   1638    303     79   -410       C  
ATOM   4624  O   VAL A 603      16.780  12.614  38.267  1.00 12.89           O  
ANISOU 4624  O   VAL A 603     2144   1319   1435    370    102   -429       O  
ATOM   4625  CB  VAL A 603      17.227  12.209  41.242  1.00 15.93           C  
ANISOU 4625  CB  VAL A 603     2532   1617   1904    342     75   -312       C  
ATOM   4626  CG1 VAL A 603      17.244  13.686  41.542  1.00 10.94           C  
ANISOU 4626  CG1 VAL A 603     1832   1069   1257    300     67   -272       C  
ATOM   4627  CG2 VAL A 603      17.239  11.395  42.538  1.00 14.74           C  
ANISOU 4627  CG2 VAL A 603     2423   1391   1789    337     62   -272       C  
ATOM   4628  N   ALA A 604      15.013  13.700  39.083  1.00 13.32           N  
ANISOU 4628  N   ALA A 604     2178   1380   1504    237     63   -408       N  
ATOM   4629  CA  ALA A 604      14.821  14.472  37.859  1.00 21.34           C  
ANISOU 4629  CA  ALA A 604     3167   2470   2473    241     65   -431       C  
ATOM   4630  C   ALA A 604      14.732  15.977  38.090  1.00 17.81           C  
ANISOU 4630  C   ALA A 604     2655   2090   2020    208     61   -378       C  
ATOM   4631  O   ALA A 604      14.183  16.691  37.262  1.00 10.22           O  
ANISOU 4631  O   ALA A 604     1677   1179   1029    193     54   -388       O  
ATOM   4632  CB  ALA A 604      13.560  13.986  37.124  1.00 19.60           C  
ANISOU 4632  CB  ALA A 604     2985   2225   2237    201     42   -501       C  
ATOM   4633  N   ASP A 605      15.273  16.455  39.204  1.00 13.59           N  
ANISOU 4633  N   ASP A 605     2092   1556   1517    199     62   -323       N  
ATOM   4634  CA  ASP A 605      15.243  17.885  39.518  1.00 15.06           C  
ANISOU 4634  CA  ASP A 605     2224   1793   1707    166     58   -278       C  
ATOM   4635  C   ASP A 605      16.655  18.446  39.426  1.00 14.68           C  
ANISOU 4635  C   ASP A 605     2126   1794   1656    208     77   -233       C  
ATOM   4636  O   ASP A 605      17.570  17.736  38.991  1.00 12.04           O  
ANISOU 4636  O   ASP A 605     1796   1467   1312    268     97   -239       O  
ATOM   4637  CB  ASP A 605      14.643  18.138  40.915  1.00 14.32           C  
ANISOU 4637  CB  ASP A 605     2131   1663   1646    110     41   -258       C  
ATOM   4638  CG  ASP A 605      15.462  17.514  42.047  1.00 18.46           C  
ANISOU 4638  CG  ASP A 605     2668   2155   2190    129     39   -230       C  
ATOM   4639  OD1 ASP A 605      16.617  17.072  41.829  1.00 18.10           O  
ANISOU 4639  OD1 ASP A 605     2615   2121   2143    187     50   -217       O  
ATOM   4640  OD2 ASP A 605      14.951  17.480  43.190  1.00 15.74           O  
ANISOU 4640  OD2 ASP A 605     2339   1780   1860     88     29   -218       O  
ATOM   4641  N   LEU A 606      16.854  19.680  39.899  1.00 16.92           N  
ANISOU 4641  N   LEU A 606     2363   2110   1956    176     72   -190       N  
ATOM   4642  CA  LEU A 606      18.173  20.320  39.814  1.00 13.06           C  
ANISOU 4642  CA  LEU A 606     1818   1672   1474    201     88   -144       C  
ATOM   4643  C   LEU A 606      19.247  19.583  40.600  1.00 12.80           C  
ANISOU 4643  C   LEU A 606     1775   1628   1461    237     86   -128       C  
ATOM   4644  O   LEU A 606      20.437  19.803  40.372  1.00 11.16           O  
ANISOU 4644  O   LEU A 606     1515   1466   1258    272    102    -97       O  
ATOM   4645  CB  LEU A 606      18.114  21.779  40.286  1.00 10.63           C  
ANISOU 4645  CB  LEU A 606     1468   1383   1189    149     78   -108       C  
ATOM   4646  CG  LEU A 606      19.273  22.671  39.809  1.00  9.69           C  
ANISOU 4646  CG  LEU A 606     1285   1320   1078    159     99    -60       C  
ATOM   4647  CD1 LEU A 606      19.352  22.754  38.246  1.00 10.42           C  
ANISOU 4647  CD1 LEU A 606     1371   1459   1129    195    134    -56       C  
ATOM   4648  CD2 LEU A 606      19.155  24.069  40.418  1.00  8.93           C  
ANISOU 4648  CD2 LEU A 606     1157   1221   1016    100     83    -31       C  
ATOM   4649  N   SER A 607      18.858  18.700  41.517  1.00  9.54           N  
ANISOU 4649  N   SER A 607     1408   1158   1060    232     66   -142       N  
ATOM   4650  CA  SER A 607      19.892  17.988  42.272  1.00  9.93           C  
ANISOU 4650  CA  SER A 607     1449   1198   1126    275     58   -118       C  
ATOM   4651  C   SER A 607      20.619  17.008  41.343  1.00 16.30           C  
ANISOU 4651  C   SER A 607     2261   2007   1924    356     87   -135       C  
ATOM   4652  O   SER A 607      21.723  16.556  41.657  1.00 19.27           O  
ANISOU 4652  O   SER A 607     2610   2396   2317    411     89   -109       O  
ATOM   4653  CB  SER A 607      19.316  17.267  43.505  1.00 11.39           C  
ANISOU 4653  CB  SER A 607     1687   1319   1321    252     32   -117       C  
ATOM   4654  OG  SER A 607      18.595  16.103  43.133  1.00 17.31           O  
ANISOU 4654  OG  SER A 607     2503   2006   2068    266     42   -156       O  
ATOM   4655  N   ALA A 608      20.013  16.695  40.197  1.00 12.87           N  
ANISOU 4655  N   ALA A 608     1862   1567   1463    368    109   -181       N  
ATOM   4656  CA  ALA A 608      20.643  15.795  39.221  1.00 17.87           C  
ANISOU 4656  CA  ALA A 608     2508   2203   2078    448    142   -211       C  
ATOM   4657  C   ALA A 608      21.652  16.518  38.330  1.00 13.97           C  
ANISOU 4657  C   ALA A 608     1944   1798   1565    485    179   -186       C  
ATOM   4658  O   ALA A 608      22.452  15.880  37.639  1.00 16.46           O  
ANISOU 4658  O   ALA A 608     2252   2134   1867    562    215   -201       O  
ATOM   4659  CB  ALA A 608      19.579  15.114  38.351  1.00 11.51           C  
ANISOU 4659  CB  ALA A 608     1775   1356   1244    442    145   -281       C  
ATOM   4660  N   ALA A 609      21.601  17.843  38.329  1.00 12.20           N  
ANISOU 4660  N   ALA A 609     1669   1625   1340    431    175   -148       N  
ATOM   4661  CA  ALA A 609      22.447  18.626  37.425  1.00 17.17           C  
ANISOU 4661  CA  ALA A 609     2233   2338   1952    452    215   -115       C  
ATOM   4662  C   ALA A 609      23.937  18.298  37.612  1.00 12.26           C  
ANISOU 4662  C   ALA A 609     1547   1756   1356    515    238    -83       C  
ATOM   4663  O   ALA A 609      24.423  18.232  38.739  1.00 17.26           O  
ANISOU 4663  O   ALA A 609     2153   2374   2032    508    207    -55       O  
ATOM   4664  CB  ALA A 609      22.180  20.140  37.615  1.00 11.05           C  
ANISOU 4664  CB  ALA A 609     1416   1592   1189    377    202    -70       C  
ATOM   4665  N   ALA A 610      24.665  18.099  36.510  1.00 12.88           N  
ANISOU 4665  N   ALA A 610     1598   1891   1405    580    293    -86       N  
ATOM   4666  CA  ALA A 610      26.065  17.700  36.624  1.00 17.88           C  
ANISOU 4666  CA  ALA A 610     2162   2566   2066    650    321    -59       C  
ATOM   4667  C   ALA A 610      26.942  18.885  37.010  1.00 17.21           C  
ANISOU 4667  C   ALA A 610     1972   2548   2020    607    320     13       C  
ATOM   4668  O   ALA A 610      28.008  18.716  37.598  1.00 20.65           O  
ANISOU 4668  O   ALA A 610     2336   3011   2498    638    315     46       O  
ATOM   4669  CB  ALA A 610      26.561  17.075  35.315  1.00 20.32           C  
ANISOU 4669  CB  ALA A 610     2474   2919   2328    739    389    -91       C  
ATOM   4670  N   PHE A 611      26.492  20.083  36.658  1.00 15.44           N  
ANISOU 4670  N   PHE A 611     1735   2349   1784    534    323     39       N  
ATOM   4671  CA  PHE A 611      27.284  21.294  36.861  1.00 16.73           C  
ANISOU 4671  CA  PHE A 611     1802   2568   1986    483    328    105       C  
ATOM   4672  C   PHE A 611      26.331  22.469  36.718  1.00 15.01           C  
ANISOU 4672  C   PHE A 611     1611   2332   1760    397    313    119       C  
ATOM   4673  O   PHE A 611      25.459  22.433  35.863  1.00 17.06           O  
ANISOU 4673  O   PHE A 611     1932   2583   1967    403    330     94       O  
ATOM   4674  CB  PHE A 611      28.428  21.379  35.843  1.00 14.35           C  
ANISOU 4674  CB  PHE A 611     1421   2357   1673    535    402    139       C  
ATOM   4675  CG  PHE A 611      29.464  22.430  36.173  1.00 14.73           C  
ANISOU 4675  CG  PHE A 611     1354   2464   1780    485    407    210       C  
ATOM   4676  CD1 PHE A 611      29.288  23.752  35.777  1.00 15.55           C  
ANISOU 4676  CD1 PHE A 611     1433   2586   1888    407    421    256       C  
ATOM   4677  CD2 PHE A 611      30.610  22.096  36.879  1.00 20.81           C  
ANISOU 4677  CD2 PHE A 611     2038   3266   2603    514    393    231       C  
ATOM   4678  CE1 PHE A 611      30.241  24.721  36.074  1.00 17.25           C  
ANISOU 4678  CE1 PHE A 611     1543   2845   2166    350    425    319       C  
ATOM   4679  CE2 PHE A 611      31.566  23.059  37.178  1.00 26.61           C  
ANISOU 4679  CE2 PHE A 611     2659   4056   3396    459    392    292       C  
ATOM   4680  CZ  PHE A 611      31.385  24.371  36.768  1.00 15.68           C  
ANISOU 4680  CZ  PHE A 611     1254   2684   2021    373    409    334       C  
ATOM   4681  N   PRO A 612      26.451  23.487  37.587  1.00 16.07           N  
ANISOU 4681  N   PRO A 612     1705   2455   1946    321    275    154       N  
ATOM   4682  CA  PRO A 612      25.473  24.584  37.532  1.00 13.75           C  
ANISOU 4682  CA  PRO A 612     1445   2129   1652    247    259    162       C  
ATOM   4683  C   PRO A 612      25.487  25.280  36.168  1.00 16.72           C  
ANISOU 4683  C   PRO A 612     1806   2552   1994    248    315    201       C  
ATOM   4684  O   PRO A 612      26.565  25.527  35.630  1.00 16.36           O  
ANISOU 4684  O   PRO A 612     1687   2573   1958    263    363    247       O  
ATOM   4685  CB  PRO A 612      25.932  25.532  38.646  1.00 11.91           C  
ANISOU 4685  CB  PRO A 612     1158   1883   1485    174    217    192       C  
ATOM   4686  CG  PRO A 612      26.728  24.689  39.559  1.00 16.67           C  
ANISOU 4686  CG  PRO A 612     1729   2496   2110    208    188    181       C  
ATOM   4687  CD  PRO A 612      27.416  23.666  38.686  1.00 18.21           C  
ANISOU 4687  CD  PRO A 612     1903   2739   2276    300    240    180       C  
ATOM   4688  N   PRO A 613      24.304  25.582  35.618  1.00 11.97           N  
ANISOU 4688  N   PRO A 613     1270   1924   1353    233    311    186       N  
ATOM   4689  CA  PRO A 613      24.168  26.312  34.359  1.00 13.80           C  
ANISOU 4689  CA  PRO A 613     1499   2199   1545    232    356    230       C  
ATOM   4690  C   PRO A 613      24.754  27.717  34.486  1.00 15.20           C  
ANISOU 4690  C   PRO A 613     1611   2384   1780    165    368    306       C  
ATOM   4691  O   PRO A 613      24.922  28.213  35.612  1.00 13.55           O  
ANISOU 4691  O   PRO A 613     1377   2132   1640    109    326    307       O  
ATOM   4692  CB  PRO A 613      22.655  26.365  34.150  1.00 12.40           C  
ANISOU 4692  CB  PRO A 613     1403   1977   1331    220    322    194       C  
ATOM   4693  CG  PRO A 613      22.118  26.335  35.541  1.00 12.42           C  
ANISOU 4693  CG  PRO A 613     1425   1906   1387    178    263    159       C  
ATOM   4694  CD  PRO A 613      22.998  25.370  36.265  1.00 11.20           C  
ANISOU 4694  CD  PRO A 613     1246   1755   1253    209    258    136       C  
ATOM   4695  N   GLY A 614      25.066  28.337  33.354  1.00 13.30           N  
ANISOU 4695  N   GLY A 614     1346   2197   1510    168    423    367       N  
ATOM   4696  CA  GLY A 614      25.637  29.670  33.347  1.00 19.19           C  
ANISOU 4696  CA  GLY A 614     2033   2944   2315    101    442    447       C  
ATOM   4697  C   GLY A 614      24.570  30.741  33.430  1.00 13.38           C  
ANISOU 4697  C   GLY A 614     1345   2141   1598     48    410    466       C  
ATOM   4698  O   GLY A 614      24.305  31.448  32.448  1.00 19.99           O  
ANISOU 4698  O   GLY A 614     2194   2995   2405     45    443    526       O  
ATOM   4699  N   GLY A 615      23.960  30.860  34.602  1.00 12.67           N  
ANISOU 4699  N   GLY A 615     1283   1976   1557     12    347    418       N  
ATOM   4700  CA  GLY A 615      22.831  31.752  34.808  1.00 12.30           C  
ANISOU 4700  CA  GLY A 615     1285   1858   1531    -26    313    420       C  
ATOM   4701  C   GLY A 615      21.798  31.121  35.731  1.00 19.20           C  
ANISOU 4701  C   GLY A 615     2216   2679   2400    -18    256    337       C  
ATOM   4702  O   GLY A 615      22.024  30.040  36.280  1.00 12.99           O  
ANISOU 4702  O   GLY A 615     1431   1904   1600      9    241    285       O  
ATOM   4703  N   ASN A 616      20.651  31.776  35.896  1.00 17.11           N  
ANISOU 4703  N   ASN A 616     1995   2357   2149    -39    228    329       N  
ATOM   4704  CA  ASN A 616      19.621  31.273  36.806  1.00 16.80           C  
ANISOU 4704  CA  ASN A 616     2003   2271   2110    -37    181    255       C  
ATOM   4705  C   ASN A 616      19.137  29.859  36.447  1.00 11.57           C  
ANISOU 4705  C   ASN A 616     1377   1641   1379     18    178    202       C  
ATOM   4706  O   ASN A 616      19.152  29.461  35.278  1.00 14.70           O  
ANISOU 4706  O   ASN A 616     1782   2089   1714     61    206    217       O  
ATOM   4707  CB  ASN A 616      18.445  32.240  36.837  1.00 19.21           C  
ANISOU 4707  CB  ASN A 616     2341   2520   2439    -57    162    261       C  
ATOM   4708  CG  ASN A 616      18.878  33.670  37.028  1.00 18.52           C  
ANISOU 4708  CG  ASN A 616     2227   2387   2423   -109    169    315       C  
ATOM   4709  OD1 ASN A 616      19.504  34.244  36.154  1.00 20.78           O  
ANISOU 4709  OD1 ASN A 616     2487   2698   2711   -113    204    386       O  
ATOM   4710  ND2 ASN A 616      18.554  34.251  38.177  1.00 23.67           N  
ANISOU 4710  ND2 ASN A 616     2890   2970   3133   -150    138    279       N  
ATOM   4711  N   THR A 617      18.681  29.122  37.454  1.00  9.60           N  
ANISOU 4711  N   THR A 617     1154   1358   1136     15    145    140       N  
ATOM   4712  CA  THR A 617      18.621  27.669  37.370  1.00 17.30           C  
ANISOU 4712  CA  THR A 617     2155   2352   2065     59    144     92       C  
ATOM   4713  C   THR A 617      17.247  27.045  37.067  1.00  9.19           C  
ANISOU 4713  C   THR A 617     1181   1309   1000     75    124     43       C  
ATOM   4714  O   THR A 617      17.166  25.844  36.815  1.00  9.91           O  
ANISOU 4714  O   THR A 617     1301   1411   1054    110    125      2       O  
ATOM   4715  CB  THR A 617      19.126  27.031  38.692  1.00 14.07           C  
ANISOU 4715  CB  THR A 617     1741   1919   1686     48    121     62       C  
ATOM   4716  OG1 THR A 617      18.547  27.723  39.809  1.00 13.41           O  
ANISOU 4716  OG1 THR A 617     1667   1784   1643     -2     90     48       O  
ATOM   4717  CG2 THR A 617      20.660  27.116  38.801  1.00 12.90           C  
ANISOU 4717  CG2 THR A 617     1531   1809   1561     53    139     99       C  
ATOM   4718  N   TRP A 618      16.191  27.847  37.088  1.00  9.01           N  
ANISOU 4718  N   TRP A 618     1172   1260    993     51    106     47       N  
ATOM   4719  CA  TRP A 618      14.831  27.357  36.816  1.00  8.84           C  
ANISOU 4719  CA  TRP A 618     1187   1230    943     60     83      4       C  
ATOM   4720  C   TRP A 618      14.764  26.564  35.510  1.00 11.14           C  
ANISOU 4720  C   TRP A 618     1497   1572   1163    104     92    -10       C  
ATOM   4721  O   TRP A 618      14.237  25.440  35.485  1.00 16.67           O  
ANISOU 4721  O   TRP A 618     2229   2266   1838    116     77    -68       O  
ATOM   4722  CB  TRP A 618      13.859  28.555  36.788  1.00  8.82           C  
ANISOU 4722  CB  TRP A 618     1179   1204    968     40     68     27       C  
ATOM   4723  CG  TRP A 618      12.444  28.344  36.270  1.00 12.57           C  
ANISOU 4723  CG  TRP A 618     1672   1686   1417     51     42     -1       C  
ATOM   4724  CD1 TRP A 618      11.819  27.167  36.006  1.00  8.83           C  
ANISOU 4724  CD1 TRP A 618     1222   1226    906     62     25    -56       C  
ATOM   4725  CD2 TRP A 618      11.495  29.376  35.961  1.00 11.12           C  
ANISOU 4725  CD2 TRP A 618     1479   1495   1252     51     26     26       C  
ATOM   4726  NE1 TRP A 618      10.538  27.396  35.555  1.00 13.52           N  
ANISOU 4726  NE1 TRP A 618     1815   1830   1491     64     -4    -66       N  
ATOM   4727  CE2 TRP A 618      10.316  28.746  35.521  1.00 13.44           C  
ANISOU 4727  CE2 TRP A 618     1784   1809   1515     63     -3    -14       C  
ATOM   4728  CE3 TRP A 618      11.534  30.778  36.015  1.00 11.81           C  
ANISOU 4728  CE3 TRP A 618     1550   1555   1384     43     33     81       C  
ATOM   4729  CZ2 TRP A 618       9.186  29.463  35.133  1.00 17.00           C  
ANISOU 4729  CZ2 TRP A 618     2221   2265   1974     73    -28      2       C  
ATOM   4730  CZ3 TRP A 618      10.411  31.490  35.632  1.00 11.50           C  
ANISOU 4730  CZ3 TRP A 618     1505   1510   1356     58     12     99       C  
ATOM   4731  CH2 TRP A 618       9.254  30.834  35.195  1.00 16.89           C  
ANISOU 4731  CH2 TRP A 618     2191   2224   2003     76    -19     61       C  
ATOM   4732  N   ALA A 619      15.290  27.151  34.436  1.00  9.70           N  
ANISOU 4732  N   ALA A 619     1298   1439    947    126    118     42       N  
ATOM   4733  CA  ALA A 619      15.218  26.549  33.108  1.00 10.20           C  
ANISOU 4733  CA  ALA A 619     1385   1563    929    171    129     30       C  
ATOM   4734  C   ALA A 619      15.839  25.170  33.107  1.00 10.31           C  
ANISOU 4734  C   ALA A 619     1417   1585    915    203    144    -24       C  
ATOM   4735  O   ALA A 619      15.231  24.206  32.648  1.00 10.47           O  
ANISOU 4735  O   ALA A 619     1477   1610    891    223    126    -85       O  
ATOM   4736  CB  ALA A 619      15.909  27.445  32.070  1.00 10.80           C  
ANISOU 4736  CB  ALA A 619     1437   1695    971    189    167    108       C  
ATOM   4737  N   THR A 620      17.056  25.083  33.630  1.00 10.32           N  
ANISOU 4737  N   THR A 620     1388   1585    948    208    173     -3       N  
ATOM   4738  CA  THR A 620      17.753  23.809  33.732  1.00 11.65           C  
ANISOU 4738  CA  THR A 620     1569   1754   1103    248    189    -47       C  
ATOM   4739  C   THR A 620      16.980  22.795  34.589  1.00 12.42           C  
ANISOU 4739  C   THR A 620     1710   1787   1224    234    151   -114       C  
ATOM   4740  O   THR A 620      16.970  21.607  34.290  1.00 11.53           O  
ANISOU 4740  O   THR A 620     1635   1665   1082    269    154   -168       O  
ATOM   4741  CB  THR A 620      19.160  23.998  34.330  1.00 11.60           C  
ANISOU 4741  CB  THR A 620     1508   1757   1141    252    218     -6       C  
ATOM   4742  OG1 THR A 620      19.924  24.870  33.485  1.00 11.12           O  
ANISOU 4742  OG1 THR A 620     1403   1759   1062    260    261     60       O  
ATOM   4743  CG2 THR A 620      19.863  22.687  34.443  1.00 11.75           C  
ANISOU 4743  CG2 THR A 620     1538   1775   1150    304    233    -47       C  
ATOM   4744  N   ALA A 621      16.365  23.254  35.673  1.00 14.49           N  
ANISOU 4744  N   ALA A 621     1967   2000   1538    184    121   -109       N  
ATOM   4745  CA  ALA A 621      15.591  22.338  36.514  1.00 19.55           C  
ANISOU 4745  CA  ALA A 621     2647   2582   2200    164     92   -162       C  
ATOM   4746  C   ALA A 621      14.427  21.751  35.727  1.00 16.58           C  
ANISOU 4746  C   ALA A 621     2310   2204   1784    165     72   -215       C  
ATOM   4747  O   ALA A 621      14.188  20.543  35.762  1.00 12.25           O  
ANISOU 4747  O   ALA A 621     1803   1624   1228    175     64   -269       O  
ATOM   4748  CB  ALA A 621      15.076  23.044  37.794  1.00 14.14           C  
ANISOU 4748  CB  ALA A 621     1948   1855   1568    110     70   -147       C  
ATOM   4749  N   SER A 622      13.683  22.604  35.032  1.00 19.22           N  
ANISOU 4749  N   SER A 622     2633   2572   2097    153     59   -199       N  
ATOM   4750  CA  SER A 622      12.581  22.103  34.211  1.00 16.21           C  
ANISOU 4750  CA  SER A 622     2282   2204   1675    153     30   -249       C  
ATOM   4751  C   SER A 622      13.090  21.256  33.045  1.00 17.32           C  
ANISOU 4751  C   SER A 622     2454   2383   1745    203     46   -286       C  
ATOM   4752  O   SER A 622      12.441  20.284  32.641  1.00 13.65           O  
ANISOU 4752  O   SER A 622     2029   1905   1253    203     22   -354       O  
ATOM   4753  CB  SER A 622      11.734  23.252  33.690  1.00 13.04           C  
ANISOU 4753  CB  SER A 622     1856   1837   1263    140      9   -215       C  
ATOM   4754  OG  SER A 622      10.904  23.755  34.715  1.00 14.18           O  
ANISOU 4754  OG  SER A 622     1981   1938   1469     96    -10   -209       O  
ATOM   4755  N   MET A 623      14.257  21.612  32.516  1.00 10.72           N  
ANISOU 4755  N   MET A 623     1600   1594    880    244     88   -244       N  
ATOM   4756  CA  MET A 623      14.808  20.872  31.388  1.00 11.46           C  
ANISOU 4756  CA  MET A 623     1721   1733    899    301    113   -279       C  
ATOM   4757  C   MET A 623      15.061  19.418  31.766  1.00 14.22           C  
ANISOU 4757  C   MET A 623     2112   2026   1263    321    116   -349       C  
ATOM   4758  O   MET A 623      14.802  18.515  30.979  1.00 14.48           O  
ANISOU 4758  O   MET A 623     2194   2064   1245    347    110   -419       O  
ATOM   4759  CB  MET A 623      16.102  21.524  30.890  1.00 13.10           C  
ANISOU 4759  CB  MET A 623     1892   2004   1084    340    169   -213       C  
ATOM   4760  CG  MET A 623      16.740  20.789  29.715  1.00 17.75           C  
ANISOU 4760  CG  MET A 623     2507   2649   1588    406    208   -249       C  
ATOM   4761  SD  MET A 623      17.869  19.471  30.218  1.00 14.59           S  
ANISOU 4761  SD  MET A 623     2117   2209   1218    459    245   -295       S  
ATOM   4762  CE  MET A 623      19.248  20.394  30.904  1.00 12.66           C  
ANISOU 4762  CE  MET A 623     1787   1989   1035    458    289   -196       C  
ATOM   4763  N   ILE A 624      15.603  19.202  32.963  1.00 13.96           N  
ANISOU 4763  N   ILE A 624     2065   1940   1300    311    124   -330       N  
ATOM   4764  CA  ILE A 624      15.886  17.857  33.443  1.00 11.42           C  
ANISOU 4764  CA  ILE A 624     1783   1554   1002    334    127   -382       C  
ATOM   4765  C   ILE A 624      14.571  17.077  33.591  1.00 14.39           C  
ANISOU 4765  C   ILE A 624     2210   1869   1388    291     83   -449       C  
ATOM   4766  O   ILE A 624      14.468  15.939  33.131  1.00 14.79           O  
ANISOU 4766  O   ILE A 624     2314   1887   1420    315     81   -519       O  
ATOM   4767  CB  ILE A 624      16.665  17.890  34.777  1.00 19.17           C  
ANISOU 4767  CB  ILE A 624     2735   2497   2052    330    135   -336       C  
ATOM   4768  CG1 ILE A 624      18.066  18.486  34.563  1.00 11.20           C  
ANISOU 4768  CG1 ILE A 624     1668   1549   1038    373    178   -278       C  
ATOM   4769  CG2 ILE A 624      16.823  16.501  35.343  1.00 11.28           C  
ANISOU 4769  CG2 ILE A 624     1783   1421   1082    353    132   -379       C  
ATOM   4770  CD1 ILE A 624      18.771  18.864  35.856  1.00 13.55           C  
ANISOU 4770  CD1 ILE A 624     1921   1828   1399    355    173   -224       C  
ATOM   4771  N   GLY A 625      13.556  17.704  34.178  1.00 10.90           N  
ANISOU 4771  N   GLY A 625     1750   1413    979    227     50   -431       N  
ATOM   4772  CA  GLY A 625      12.237  17.092  34.245  1.00 11.01           C  
ANISOU 4772  CA  GLY A 625     1795   1383   1004    179     10   -488       C  
ATOM   4773  C   GLY A 625      11.726  16.750  32.843  1.00 15.21           C  
ANISOU 4773  C   GLY A 625     2356   1957   1467    194    -10   -550       C  
ATOM   4774  O   GLY A 625      11.173  15.674  32.637  1.00 18.62           O  
ANISOU 4774  O   GLY A 625     2834   2342   1898    179    -32   -624       O  
ATOM   4775  N   ALA A 626      11.923  17.656  31.884  1.00 11.85           N  
ANISOU 4775  N   ALA A 626     1906   1618    980    222     -4   -520       N  
ATOM   4776  CA  ALA A 626      11.483  17.439  30.503  1.00 12.62           C  
ANISOU 4776  CA  ALA A 626     2031   1772    992    241    -26   -573       C  
ATOM   4777  C   ALA A 626      12.119  16.185  29.912  1.00 15.55           C  
ANISOU 4777  C   ALA A 626     2462   2124   1323    291     -4   -649       C  
ATOM   4778  O   ALA A 626      11.443  15.343  29.330  1.00 17.53           O  
ANISOU 4778  O   ALA A 626     2760   2359   1544    279    -39   -735       O  
ATOM   4779  CB  ALA A 626      11.802  18.664  29.638  1.00 12.72           C  
ANISOU 4779  CB  ALA A 626     2008   1882    941    272    -11   -507       C  
ATOM   4780  N   ARG A 627      13.429  16.065  30.067  1.00 13.41           N  
ANISOU 4780  N   ARG A 627     2186   1853   1056    347     52   -620       N  
ATOM   4781  CA  ARG A 627      14.132  14.906  29.548  1.00 20.85           C  
ANISOU 4781  CA  ARG A 627     3181   2774   1966    408     81   -689       C  
ATOM   4782  C   ARG A 627      13.661  13.618  30.219  1.00 18.58           C  
ANISOU 4782  C   ARG A 627     2944   2371   1745    377     57   -755       C  
ATOM   4783  O   ARG A 627      13.570  12.577  29.567  1.00 18.87           O  
ANISOU 4783  O   ARG A 627     3019   2376   1774    379     56   -819       O  
ATOM   4784  CB  ARG A 627      15.650  15.089  29.707  1.00 16.66           C  
ANISOU 4784  CB  ARG A 627     2619   2270   1443    476    148   -634       C  
ATOM   4785  CG  ARG A 627      16.222  16.123  28.731  1.00 19.02           C  
ANISOU 4785  CG  ARG A 627     2877   2684   1664    511    185   -579       C  
ATOM   4786  CD  ARG A 627      17.682  15.835  28.422  1.00 16.48           C  
ANISOU 4786  CD  ARG A 627     2540   2397   1323    594    257   -567       C  
ATOM   4787  NE  ARG A 627      17.854  14.772  27.435  1.00 19.59           N  
ANISOU 4787  NE  ARG A 627     2983   2788   1672    633    272   -644       N  
ATOM   4788  CZ  ARG A 627      19.036  14.243  27.119  1.00 23.43           C  
ANISOU 4788  CZ  ARG A 627     3458   3288   2156    701    331   -647       C  
ATOM   4789  NH1 ARG A 627      20.127  14.682  27.731  1.00 20.81           N  
ANISOU 4789  NH1 ARG A 627     3068   2981   1859    743    379   -580       N  
ATOM   4790  NH2 ARG A 627      19.135  13.280  26.196  1.00 22.92           N  
ANISOU 4790  NH2 ARG A 627     3437   3214   2057    728    343   -718       N  
ATOM   4791  N   ALA A 628      13.370  13.695  31.517  1.00 20.80           N  
ANISOU 4791  N   ALA A 628     3207   2586   2109    330     43   -715       N  
ATOM   4792  CA  ALA A 628      12.887  12.544  32.270  1.00 20.48           C  
ANISOU 4792  CA  ALA A 628     3215   2432   2134    295     23   -762       C  
ATOM   4793  C   ALA A 628      11.589  11.977  31.671  1.00 14.39           C  
ANISOU 4793  C   ALA A 628     2464   1644   1361    226    -22   -829       C  
ATOM   4794  O   ALA A 628      11.399  10.751  31.630  1.00 15.46           O  
ANISOU 4794  O   ALA A 628     2638   1703   1533    207    -23   -882       O  
ATOM   4795  CB  ALA A 628      12.674  12.926  33.739  1.00 12.97           C  
ANISOU 4795  CB  ALA A 628     2227   1437   1262    244     18   -689       C  
ATOM   4796  N   VAL A 629      10.705  12.864  31.214  1.00 14.85           N  
ANISOU 4796  N   VAL A 629     2490   1772   1380    189    -60   -825       N  
ATOM   4797  CA  VAL A 629       9.499  12.440  30.500  1.00 20.32           C  
ANISOU 4797  CA  VAL A 629     3191   2470   2060    126   -106   -884       C  
ATOM   4798  C   VAL A 629       9.862  11.447  29.395  1.00 25.23           C  
ANISOU 4798  C   VAL A 629     3860   3089   2638    154    -91   -950       C  
ATOM   4799  O   VAL A 629       9.349  10.323  29.339  1.00 16.69           O  
ANISOU 4799  O   VAL A 629     2814   1936   1593    110   -104  -1012       O  
ATOM   4800  CB  VAL A 629       8.758  13.633  29.866  1.00 18.35           C  
ANISOU 4800  CB  VAL A 629     2898   2322   1751    113   -147   -863       C  
ATOM   4801  CG1 VAL A 629       7.563  13.149  29.051  1.00 15.50           C  
ANISOU 4801  CG1 VAL A 629     2546   1974   1370     54   -201   -923       C  
ATOM   4802  CG2 VAL A 629       8.338  14.649  30.944  1.00 13.64           C  
ANISOU 4802  CG2 VAL A 629     2249   1728   1206     83   -158   -798       C  
ATOM   4803  N   ASP A 630      10.798  11.847  28.548  1.00 16.21           N  
ANISOU 4803  N   ASP A 630     2717   2020   1421    228    -58   -937       N  
ATOM   4804  CA  ASP A 630      11.135  11.038  27.388  1.00 22.43           C  
ANISOU 4804  CA  ASP A 630     3548   2820   2154    258    -42  -1002       C  
ATOM   4805  C   ASP A 630      11.979   9.828  27.777  1.00 20.74           C  
ANISOU 4805  C   ASP A 630     3372   2513   1995    294      2  -1035       C  
ATOM   4806  O   ASP A 630      11.890   8.784  27.140  1.00 18.93           O  
ANISOU 4806  O   ASP A 630     3189   2245   1758    290      4  -1111       O  
ATOM   4807  CB  ASP A 630      11.853  11.891  26.343  1.00 23.49           C  
ANISOU 4807  CB  ASP A 630     3666   3072   2189    324    -15   -969       C  
ATOM   4808  CG  ASP A 630      10.908  12.834  25.620  1.00 24.95           C  
ANISOU 4808  CG  ASP A 630     3827   3347   2305    292    -66   -953       C  
ATOM   4809  OD1 ASP A 630       9.673  12.695  25.784  1.00 24.34           O  
ANISOU 4809  OD1 ASP A 630     3747   3245   2255    220   -126   -981       O  
ATOM   4810  OD2 ASP A 630      11.404  13.714  24.885  1.00 21.73           O  
ANISOU 4810  OD2 ASP A 630     3400   3037   1820    340    -45   -906       O  
ATOM   4811  N   LEU A 631      12.775   9.956  28.835  1.00 18.57           N  
ANISOU 4811  N   LEU A 631     3080   2200   1777    331     34   -979       N  
ATOM   4812  CA  LEU A 631      13.563   8.819  29.309  1.00 18.51           C  
ANISOU 4812  CA  LEU A 631     3105   2098   1828    372     69  -1000       C  
ATOM   4813  C   LEU A 631      12.642   7.727  29.867  1.00 22.31           C  
ANISOU 4813  C   LEU A 631     3623   2466   2390    299     39  -1048       C  
ATOM   4814  O   LEU A 631      12.781   6.557  29.537  1.00 24.86           O  
ANISOU 4814  O   LEU A 631     3990   2721   2734    310     51  -1112       O  
ATOM   4815  CB  LEU A 631      14.577   9.265  30.373  1.00 17.35           C  
ANISOU 4815  CB  LEU A 631     2930   1941   1722    427    101   -921       C  
ATOM   4816  CG  LEU A 631      15.836  10.009  29.892  1.00 16.73           C  
ANISOU 4816  CG  LEU A 631     2814   1957   1585    514    151   -876       C  
ATOM   4817  CD1 LEU A 631      16.577  10.607  31.070  1.00 18.26           C  
ANISOU 4817  CD1 LEU A 631     2971   2146   1821    546    170   -795       C  
ATOM   4818  CD2 LEU A 631      16.744   9.059  29.140  1.00 21.96           C  
ANISOU 4818  CD2 LEU A 631     3503   2610   2233    586    196   -923       C  
ATOM   4819  N   ILE A 632      11.670   8.123  30.680  1.00 20.59           N  
ANISOU 4819  N   ILE A 632     3382   2228   2214    223      1  -1018       N  
ATOM   4820  CA  ILE A 632      10.744   7.167  31.270  1.00 18.95           C  
ANISOU 4820  CA  ILE A 632     3196   1919   2086    146    -23  -1053       C  
ATOM   4821  C   ILE A 632       9.860   6.487  30.212  1.00 19.91           C  
ANISOU 4821  C   ILE A 632     3344   2039   2180     91    -49  -1144       C  
ATOM   4822  O   ILE A 632       9.684   5.261  30.238  1.00 25.21           O  
ANISOU 4822  O   ILE A 632     4055   2617   2905     68    -44  -1202       O  
ATOM   4823  CB  ILE A 632       9.860   7.861  32.333  1.00 18.94           C  
ANISOU 4823  CB  ILE A 632     3154   1913   2129     76    -53   -998       C  
ATOM   4824  CG1 ILE A 632      10.694   8.212  33.564  1.00 15.80           C  
ANISOU 4824  CG1 ILE A 632     2750   1485   1770    118    -27   -916       C  
ATOM   4825  CG2 ILE A 632       8.694   6.965  32.751  1.00 25.39           C  
ANISOU 4825  CG2 ILE A 632     3978   2648   3022    -16    -79  -1037       C  
ATOM   4826  CD1 ILE A 632      10.006   9.206  34.490  1.00 17.97           C  
ANISOU 4826  CD1 ILE A 632     2984   1782   2064     63    -48   -856       C  
ATOM   4827  N   LEU A 633       9.324   7.262  29.273  1.00 19.98           N  
ANISOU 4827  N   LEU A 633     3338   2148   2107     72    -79  -1156       N  
ATOM   4828  CA  LEU A 633       8.438   6.707  28.239  1.00 19.89           C  
ANISOU 4828  CA  LEU A 633     3357   2145   2055     17   -113  -1237       C  
ATOM   4829  C   LEU A 633       9.183   5.958  27.129  1.00 26.58           C  
ANISOU 4829  C   LEU A 633     4258   2995   2847     75    -84  -1308       C  
ATOM   4830  O   LEU A 633       8.576   5.183  26.398  1.00 28.58           O  
ANISOU 4830  O   LEU A 633     4554   3224   3081     30   -107  -1389       O  
ATOM   4831  CB  LEU A 633       7.577   7.813  27.629  1.00 19.60           C  
ANISOU 4831  CB  LEU A 633     3284   2216   1946    -17   -167  -1217       C  
ATOM   4832  CG  LEU A 633       6.670   8.468  28.682  1.00 29.38           C  
ANISOU 4832  CG  LEU A 633     4472   3447   3244    -82   -199  -1159       C  
ATOM   4833  CD1 LEU A 633       5.763   9.521  28.080  1.00 18.49           C  
ANISOU 4833  CD1 LEU A 633     3050   2170   1805   -107   -259  -1140       C  
ATOM   4834  CD2 LEU A 633       5.861   7.408  29.421  1.00 28.23           C  
ANISOU 4834  CD2 LEU A 633     4345   3192   3189   -169   -207  -1191       C  
ATOM   4835  N   GLY A 634      10.490   6.187  27.009  1.00 20.90           N  
ANISOU 4835  N   GLY A 634     3536   2304   2100    173    -34  -1278       N  
ATOM   4836  CA  GLY A 634      11.316   5.414  26.094  1.00 22.09           C  
ANISOU 4836  CA  GLY A 634     3734   2449   2209    238      5  -1343       C  
ATOM   4837  C   GLY A 634      11.325   5.911  24.654  1.00 24.67           C  
ANISOU 4837  C   GLY A 634     4071   2892   2412    262     -2  -1373       C  
ATOM   4838  O   GLY A 634      11.706   5.179  23.745  1.00 31.31           O  
ANISOU 4838  O   GLY A 634     4960   3729   3208    295     21  -1446       O  
ATOM   4839  N   PHE A 635      10.918   7.157  24.447  1.00 25.18           N  
ANISOU 4839  N   PHE A 635     4091   3058   2419    248    -33  -1314       N  
ATOM   4840  CA  PHE A 635      10.878   7.762  23.112  1.00 25.85           C  
ANISOU 4840  CA  PHE A 635     4180   3262   2382    272    -45  -1325       C  
ATOM   4841  C   PHE A 635      10.837   9.279  23.303  1.00 25.70           C  
ANISOU 4841  C   PHE A 635     4096   3339   2331    284    -58  -1225       C  
ATOM   4842  O   PHE A 635      10.344   9.742  24.329  1.00 27.37           O  
ANISOU 4842  O   PHE A 635     4269   3522   2610    243    -82  -1175       O  
ATOM   4843  CB  PHE A 635       9.665   7.254  22.319  1.00 23.71           C  
ANISOU 4843  CB  PHE A 635     3946   2991   2070    196   -108  -1406       C  
ATOM   4844  CG  PHE A 635       9.737   7.530  20.838  1.00 31.07           C  
ANISOU 4844  CG  PHE A 635     4903   4030   2872    228   -117  -1438       C  
ATOM   4845  CD1 PHE A 635      10.493   6.712  19.996  1.00 35.83           C  
ANISOU 4845  CD1 PHE A 635     5563   4627   3424    279    -70  -1511       C  
ATOM   4846  CD2 PHE A 635       9.048   8.605  20.282  1.00 29.08           C  
ANISOU 4846  CD2 PHE A 635     4618   3887   2546    210   -170  -1394       C  
ATOM   4847  CE1 PHE A 635      10.563   6.963  18.614  1.00 33.96           C  
ANISOU 4847  CE1 PHE A 635     5352   4493   3057    309    -75  -1541       C  
ATOM   4848  CE2 PHE A 635       9.109   8.860  18.907  1.00 31.46           C  
ANISOU 4848  CE2 PHE A 635     4943   4290   2719    241   -179  -1418       C  
ATOM   4849  CZ  PHE A 635       9.869   8.036  18.072  1.00 33.71           C  
ANISOU 4849  CZ  PHE A 635     5289   4572   2949    288   -130  -1492       C  
ATOM   4850  N   PRO A 636      11.390  10.055  22.343  1.00 23.10           N  
ANISOU 4850  N   PRO A 636     3755   3122   1901    341    -35  -1193       N  
ATOM   4851  CA  PRO A 636      11.458  11.516  22.503  1.00 22.92           C  
ANISOU 4851  CA  PRO A 636     3672   3186   1850    358    -38  -1093       C  
ATOM   4852  C   PRO A 636      10.152  12.235  22.241  1.00 21.58           C  
ANISOU 4852  C   PRO A 636     3480   3070   1650    299   -116  -1078       C  
ATOM   4853  O   PRO A 636      10.132  13.147  21.411  1.00 20.81           O  
ANISOU 4853  O   PRO A 636     3365   3076   1465    325   -124  -1034       O  
ATOM   4854  CB  PRO A 636      12.491  11.943  21.450  1.00 24.31           C  
ANISOU 4854  CB  PRO A 636     3850   3459   1927    436     18  -1067       C  
ATOM   4855  CG  PRO A 636      13.225  10.705  21.093  1.00 30.47           C  
ANISOU 4855  CG  PRO A 636     4680   4188   2709    474     65  -1146       C  
ATOM   4856  CD  PRO A 636      12.229   9.600  21.222  1.00 25.07           C  
ANISOU 4856  CD  PRO A 636     4043   3412   2069    405     13  -1239       C  
ATOM   4857  N   TYR A 637       9.092  11.851  22.940  1.00 22.39           N  
ANISOU 4857  N   TYR A 637     3579   3103   1826    223   -170  -1106       N  
ATOM   4858  CA  TYR A 637       7.778  12.461  22.738  1.00 26.07           C  
ANISOU 4858  CA  TYR A 637     4014   3617   2276    167   -249  -1096       C  
ATOM   4859  C   TYR A 637       7.814  13.968  22.979  1.00 23.74           C  
ANISOU 4859  C   TYR A 637     3658   3401   1963    194   -252   -996       C  
ATOM   4860  O   TYR A 637       7.404  14.746  22.122  1.00 19.72           O  
ANISOU 4860  O   TYR A 637     3130   2986   1374    205   -287   -967       O  
ATOM   4861  CB  TYR A 637       6.727  11.807  23.644  1.00 24.68           C  
ANISOU 4861  CB  TYR A 637     3833   3347   2199     80   -294  -1132       C  
ATOM   4862  CG  TYR A 637       6.461  10.358  23.298  1.00 29.13           C  
ANISOU 4862  CG  TYR A 637     4459   3834   2775     39   -302  -1232       C  
ATOM   4863  CD1 TYR A 637       5.930  10.013  22.063  1.00 32.83           C  
ANISOU 4863  CD1 TYR A 637     4961   4350   3161     21   -346  -1296       C  
ATOM   4864  CD2 TYR A 637       6.727   9.337  24.205  1.00 26.54           C  
ANISOU 4864  CD2 TYR A 637     4159   3384   2541     16   -267  -1261       C  
ATOM   4865  CE1 TYR A 637       5.677   8.695  21.730  1.00 35.07           C  
ANISOU 4865  CE1 TYR A 637     5308   4561   3455    -21   -355  -1392       C  
ATOM   4866  CE2 TYR A 637       6.471   8.005  23.877  1.00 26.97           C  
ANISOU 4866  CE2 TYR A 637     4275   3363   2611    -24   -271  -1352       C  
ATOM   4867  CZ  TYR A 637       5.947   7.698  22.640  1.00 31.50           C  
ANISOU 4867  CZ  TYR A 637     4884   3984   3101    -44   -315  -1420       C  
ATOM   4868  OH  TYR A 637       5.696   6.391  22.297  1.00 39.87           O  
ANISOU 4868  OH  TYR A 637     6009   4965   4174    -86   -320  -1517       O  
ATOM   4869  N   LEU A 638       8.319  14.390  24.131  1.00 18.15           N  
ANISOU 4869  N   LEU A 638     2918   2652   1326    206   -216   -941       N  
ATOM   4870  CA  LEU A 638       8.315  15.816  24.440  1.00 19.84           C  
ANISOU 4870  CA  LEU A 638     3077   2932   1530    226   -218   -850       C  
ATOM   4871  C   LEU A 638       9.286  16.596  23.544  1.00 21.41           C  
ANISOU 4871  C   LEU A 638     3274   3226   1635    299   -171   -790       C  
ATOM   4872  O   LEU A 638       9.006  17.729  23.137  1.00 19.78           O  
ANISOU 4872  O   LEU A 638     3035   3102   1379    313   -190   -723       O  
ATOM   4873  CB  LEU A 638       8.660  16.041  25.905  1.00 16.10           C  
ANISOU 4873  CB  LEU A 638     2577   2390   1151    219   -190   -812       C  
ATOM   4874  CG  LEU A 638       8.586  17.468  26.441  1.00 15.21           C  
ANISOU 4874  CG  LEU A 638     2410   2327   1044    231   -194   -727       C  
ATOM   4875  CD1 LEU A 638       7.247  18.123  26.136  1.00 15.37           C  
ANISOU 4875  CD1 LEU A 638     2391   2399   1049    193   -268   -719       C  
ATOM   4876  CD2 LEU A 638       8.832  17.451  27.942  1.00 14.22           C  
ANISOU 4876  CD2 LEU A 638     2260   2109   1033    202   -165   -693       C  
ATOM   4877  N   ARG A 639      10.433  16.000  23.244  1.00 17.98           N  
ANISOU 4877  N   ARG A 639     2871   2780   1181    346   -105   -807       N  
ATOM   4878  CA  ARG A 639      11.374  16.639  22.336  1.00 24.98           C  
ANISOU 4878  CA  ARG A 639     3754   3757   1981    410    -52   -752       C  
ATOM   4879  C   ARG A 639      10.720  16.829  20.963  1.00 29.71           C  
ANISOU 4879  C   ARG A 639     4372   4441   2475    408    -94   -766       C  
ATOM   4880  O   ARG A 639      10.968  17.815  20.279  1.00 35.35           O  
ANISOU 4880  O   ARG A 639     5067   5245   3117    440    -79   -690       O  
ATOM   4881  CB  ARG A 639      12.645  15.815  22.200  1.00 26.05           C  
ANISOU 4881  CB  ARG A 639     3915   3866   2116    461     23   -782       C  
ATOM   4882  CG  ARG A 639      13.822  16.602  21.645  1.00 29.87           C  
ANISOU 4882  CG  ARG A 639     4373   4434   2541    524     96   -703       C  
ATOM   4883  CD  ARG A 639      14.985  15.687  21.264  1.00 31.75           C  
ANISOU 4883  CD  ARG A 639     4635   4659   2767    579    166   -746       C  
ATOM   4884  NE  ARG A 639      14.676  14.864  20.097  1.00 39.43           N  
ANISOU 4884  NE  ARG A 639     5665   5650   3665    582    150   -831       N  
ATOM   4885  CZ  ARG A 639      15.349  13.769  19.753  1.00 49.65           C  
ANISOU 4885  CZ  ARG A 639     6997   6912   4955    618    193   -904       C  
ATOM   4886  NH1 ARG A 639      15.008  13.086  18.662  1.00 46.80           N  
ANISOU 4886  NH1 ARG A 639     6692   6571   4518    617    177   -985       N  
ATOM   4887  NH2 ARG A 639      16.359  13.352  20.509  1.00 50.17           N  
ANISOU 4887  NH2 ARG A 639     7045   6924   5092    658    249   -896       N  
ATOM   4888  N   ASP A 640       9.854  15.896  20.578  1.00 27.81           N  
ANISOU 4888  N   ASP A 640     4168   4170   2228    365   -150   -858       N  
ATOM   4889  CA  ASP A 640       9.240  15.946  19.253  1.00 37.12           C  
ANISOU 4889  CA  ASP A 640     5372   5429   3303    362   -196   -882       C  
ATOM   4890  C   ASP A 640       7.972  16.795  19.184  1.00 36.25           C  
ANISOU 4890  C   ASP A 640     5223   5367   3183    325   -280   -843       C  
ATOM   4891  O   ASP A 640       7.406  16.973  18.103  1.00 31.85           O  
ANISOU 4891  O   ASP A 640     4679   4886   2538    324   -327   -850       O  
ATOM   4892  CB  ASP A 640       8.903  14.536  18.760  1.00 34.91           C  
ANISOU 4892  CB  ASP A 640     5153   5099   3011    332   -219  -1004       C  
ATOM   4893  CG  ASP A 640      10.134  13.743  18.359  1.00 36.56           C  
ANISOU 4893  CG  ASP A 640     5407   5290   3192    385   -139  -1047       C  
ATOM   4894  OD1 ASP A 640      11.237  14.343  18.273  1.00 29.01           O  
ANISOU 4894  OD1 ASP A 640     4431   4380   2211    447    -67   -978       O  
ATOM   4895  OD2 ASP A 640       9.980  12.528  18.092  1.00 37.70           O  
ANISOU 4895  OD2 ASP A 640     5606   5378   3341    364   -147  -1149       O  
ATOM   4896  N   LEU A 641       7.512  17.301  20.323  1.00 24.53           N  
ANISOU 4896  N   LEU A 641     3689   3842   1788    296   -301   -804       N  
ATOM   4897  CA  LEU A 641       6.272  18.073  20.333  1.00 22.21           C  
ANISOU 4897  CA  LEU A 641     3349   3591   1499    264   -381   -771       C  
ATOM   4898  C   LEU A 641       6.502  19.429  19.672  1.00 23.15           C  
ANISOU 4898  C   LEU A 641     3443   3812   1540    316   -372   -662       C  
ATOM   4899  O   LEU A 641       7.462  20.112  20.000  1.00 23.28           O  
ANISOU 4899  O   LEU A 641     3447   3836   1561    356   -305   -586       O  
ATOM   4900  CB  LEU A 641       5.752  18.243  21.750  1.00 18.95           C  
ANISOU 4900  CB  LEU A 641     2890   3108   1204    222   -399   -761       C  
ATOM   4901  CG  LEU A 641       4.366  18.863  21.933  1.00 22.07           C  
ANISOU 4901  CG  LEU A 641     3225   3533   1626    183   -484   -742       C  
ATOM   4902  CD1 LEU A 641       3.290  17.933  21.386  1.00 19.96           C  
ANISOU 4902  CD1 LEU A 641     2970   3259   1354    125   -556   -830       C  
ATOM   4903  CD2 LEU A 641       4.110  19.190  23.416  1.00 17.67           C  
ANISOU 4903  CD2 LEU A 641     2619   2912   1182    154   -479   -721       C  
ATOM   4904  N   PRO A 642       5.639  19.802  18.709  1.00 24.76           N  
ANISOU 4904  N   PRO A 642     3642   4094   1673    313   -440   -651       N  
ATOM   4905  CA  PRO A 642       5.793  21.083  17.998  1.00 30.05           C  
ANISOU 4905  CA  PRO A 642     4294   4856   2268    362   -434   -538       C  
ATOM   4906  C   PRO A 642       5.694  22.282  18.949  1.00 32.49           C  
ANISOU 4906  C   PRO A 642     4543   5156   2646    371   -428   -437       C  
ATOM   4907  O   PRO A 642       4.889  22.252  19.888  1.00 19.75           O  
ANISOU 4907  O   PRO A 642     2890   3496   1120    332   -474   -460       O  
ATOM   4908  CB  PRO A 642       4.631  21.083  16.988  1.00 30.37           C  
ANISOU 4908  CB  PRO A 642     4335   4964   2240    346   -528   -560       C  
ATOM   4909  CG  PRO A 642       4.183  19.670  16.890  1.00 35.80           C  
ANISOU 4909  CG  PRO A 642     5059   5604   2940    294   -564   -693       C  
ATOM   4910  CD  PRO A 642       4.519  18.999  18.189  1.00 22.23           C  
ANISOU 4910  CD  PRO A 642     3335   3775   1336    263   -524   -740       C  
ATOM   4911  N   VAL A 643       6.507  23.311  18.703  1.00 20.37           N  
ANISOU 4911  N   VAL A 643     3003   3662   1076    418   -369   -325       N  
ATOM   4912  CA  VAL A 643       6.642  24.436  19.628  1.00 25.00           C  
ANISOU 4912  CA  VAL A 643     3543   4229   1729    429   -347   -225       C  
ATOM   4913  C   VAL A 643       5.412  25.314  19.714  1.00 22.29           C  
ANISOU 4913  C   VAL A 643     3151   3911   1409    424   -428   -170       C  
ATOM   4914  O   VAL A 643       5.312  26.150  20.606  1.00 22.99           O  
ANISOU 4914  O   VAL A 643     3198   3971   1566    427   -423   -103       O  
ATOM   4915  CB  VAL A 643       7.823  25.352  19.256  1.00 21.52           C  
ANISOU 4915  CB  VAL A 643     3106   3820   1249    473   -262   -108       C  
ATOM   4916  CG1 VAL A 643       9.128  24.581  19.310  1.00 26.18           C  
ANISOU 4916  CG1 VAL A 643     3728   4386   1834    483   -175   -151       C  
ATOM   4917  CG2 VAL A 643       7.589  25.977  17.886  1.00 23.92           C  
ANISOU 4917  CG2 VAL A 643     3425   4209   1455    502   -281    -40       C  
ATOM   4918  N   ASN A 644       4.505  25.180  18.762  1.00 20.51           N  
ANISOU 4918  N   ASN A 644     2928   3741   1125    421   -501   -194       N  
ATOM   4919  CA  ASN A 644       3.288  25.986  18.808  1.00 32.09           C  
ANISOU 4919  CA  ASN A 644     4339   5234   2620    422   -581   -142       C  
ATOM   4920  C   ASN A 644       2.217  25.307  19.662  1.00 27.62           C  
ANISOU 4920  C   ASN A 644     3730   4624   2141    368   -648   -237       C  
ATOM   4921  O   ASN A 644       1.159  25.883  19.923  1.00 25.07           O  
ANISOU 4921  O   ASN A 644     3345   4315   1866    365   -713   -206       O  
ATOM   4922  CB  ASN A 644       2.769  26.286  17.397  1.00 29.12           C  
ANISOU 4922  CB  ASN A 644     3978   4944   2143    447   -634   -108       C  
ATOM   4923  CG  ASN A 644       2.173  25.075  16.712  1.00 38.38           C  
ANISOU 4923  CG  ASN A 644     5177   6140   3264    410   -694   -231       C  
ATOM   4924  OD1 ASN A 644       2.436  23.932  17.086  1.00 39.16           O  
ANISOU 4924  OD1 ASN A 644     5303   6188   3388    372   -675   -339       O  
ATOM   4925  ND2 ASN A 644       1.359  25.324  15.690  1.00 42.14           N  
ANISOU 4925  ND2 ASN A 644     5650   6690   3671    421   -768   -213       N  
ATOM   4926  N   ASP A 645       2.502  24.075  20.079  1.00 24.94           N  
ANISOU 4926  N   ASP A 645     3421   4228   1829    325   -627   -349       N  
ATOM   4927  CA  ASP A 645       1.618  23.359  20.991  1.00 27.04           C  
ANISOU 4927  CA  ASP A 645     3649   4436   2190    262   -673   -436       C  
ATOM   4928  C   ASP A 645       2.132  23.570  22.403  1.00 18.11           C  
ANISOU 4928  C   ASP A 645     2497   3228   1154    254   -617   -421       C  
ATOM   4929  O   ASP A 645       3.079  22.919  22.823  1.00 20.69           O  
ANISOU 4929  O   ASP A 645     2868   3496   1499    246   -550   -458       O  
ATOM   4930  CB  ASP A 645       1.560  21.860  20.667  1.00 24.33           C  
ANISOU 4930  CB  ASP A 645     3354   4056   1835    213   -683   -560       C  
ATOM   4931  CG  ASP A 645       0.611  21.081  21.591  1.00 25.59           C  
ANISOU 4931  CG  ASP A 645     3474   4146   2102    137   -725   -642       C  
ATOM   4932  OD1 ASP A 645       0.467  21.416  22.799  1.00 24.70           O  
ANISOU 4932  OD1 ASP A 645     3314   3986   2084    121   -710   -624       O  
ATOM   4933  OD2 ASP A 645       0.005  20.107  21.104  1.00 24.85           O  
ANISOU 4933  OD2 ASP A 645     3399   4045   1999     90   -770   -724       O  
ATOM   4934  N   VAL A 646       1.471  24.453  23.137  1.00 17.62           N  
ANISOU 4934  N   VAL A 646     2368   3135   1192    244   -627   -354       N  
ATOM   4935  CA  VAL A 646       1.887  24.798  24.499  1.00 16.41           C  
ANISOU 4935  CA  VAL A 646     2193   2876   1167    222   -556   -317       C  
ATOM   4936  C   VAL A 646       0.710  24.660  25.463  1.00 16.12           C  
ANISOU 4936  C   VAL A 646     2089   2792   1243    169   -592   -352       C  
ATOM   4937  O   VAL A 646      -0.432  24.764  25.040  1.00 16.84           O  
ANISOU 4937  O   VAL A 646     2132   2940   1325    164   -670   -365       O  
ATOM   4938  CB  VAL A 646       2.438  26.244  24.553  1.00 18.68           C  
ANISOU 4938  CB  VAL A 646     2467   3160   1471    269   -509   -185       C  
ATOM   4939  CG1 VAL A 646       3.713  26.362  23.731  1.00 16.88           C  
ANISOU 4939  CG1 VAL A 646     2298   2974   1144    313   -456   -143       C  
ATOM   4940  CG2 VAL A 646       1.389  27.224  24.069  1.00 16.80           C  
ANISOU 4940  CG2 VAL A 646     2177   2979   1226    300   -575   -120       C  
ATOM   4941  N   PRO A 647       0.984  24.435  26.768  1.00 17.65           N  
ANISOU 4941  N   PRO A 647     2277   2888   1541    130   -536   -364       N  
ATOM   4942  CA  PRO A 647      -0.112  24.319  27.737  1.00 19.13           C  
ANISOU 4942  CA  PRO A 647     2400   3034   1833     80   -557   -393       C  
ATOM   4943  C   PRO A 647      -0.990  25.567  27.735  1.00 18.75           C  
ANISOU 4943  C   PRO A 647     2281   3020   1823    112   -588   -318       C  
ATOM   4944  O   PRO A 647      -0.470  26.674  27.656  1.00 22.74           O  
ANISOU 4944  O   PRO A 647     2792   3523   2327    162   -556   -229       O  
ATOM   4945  CB  PRO A 647       0.616  24.160  29.087  1.00 19.16           C  
ANISOU 4945  CB  PRO A 647     2422   2937   1921     52   -476   -389       C  
ATOM   4946  CG  PRO A 647       1.962  23.569  28.716  1.00 17.71           C  
ANISOU 4946  CG  PRO A 647     2316   2742   1673     70   -433   -405       C  
ATOM   4947  CD  PRO A 647       2.304  24.234  27.398  1.00 14.33           C  
ANISOU 4947  CD  PRO A 647     1905   2400   1141    131   -452   -354       C  
ATOM   4948  N   ILE A 648      -2.302  25.382  27.810  1.00 15.71           N  
ANISOU 4948  N   ILE A 648     1827   2664   1478     83   -648   -354       N  
ATOM   4949  CA  ILE A 648      -3.236  26.495  27.813  1.00 16.09           C  
ANISOU 4949  CA  ILE A 648     1797   2746   1570    120   -682   -290       C  
ATOM   4950  C   ILE A 648      -3.451  26.956  29.244  1.00 21.68           C  
ANISOU 4950  C   ILE A 648     2464   3372   2401    103   -621   -271       C  
ATOM   4951  O   ILE A 648      -3.823  26.159  30.114  1.00 17.01           O  
ANISOU 4951  O   ILE A 648     1854   2739   1871     40   -603   -334       O  
ATOM   4952  CB  ILE A 648      -4.598  26.108  27.184  1.00 17.20           C  
ANISOU 4952  CB  ILE A 648     1867   2970   1697    102   -781   -336       C  
ATOM   4953  CG1 ILE A 648      -4.388  25.496  25.790  1.00 28.99           C  
ANISOU 4953  CG1 ILE A 648     3411   4547   3056    111   -846   -376       C  
ATOM   4954  CG2 ILE A 648      -5.546  27.303  27.165  1.00 17.70           C  
ANISOU 4954  CG2 ILE A 648     1844   3072   1809    155   -816   -262       C  
ATOM   4955  CD1 ILE A 648      -3.542  26.354  24.865  1.00 26.35           C  
ANISOU 4955  CD1 ILE A 648     3132   4258   2624    190   -835   -289       C  
ATOM   4956  N   LEU A 649      -3.219  28.242  29.483  1.00 18.67           N  
ANISOU 4956  N   LEU A 649     2074   2967   2053    158   -588   -185       N  
ATOM   4957  CA  LEU A 649      -3.307  28.781  30.828  1.00 23.95           C  
ANISOU 4957  CA  LEU A 649     2716   3557   2827    149   -526   -170       C  
ATOM   4958  C   LEU A 649      -4.743  29.048  31.237  1.00 30.09           C  
ANISOU 4958  C   LEU A 649     3395   4356   3681    149   -556   -181       C  
ATOM   4959  O   LEU A 649      -5.500  29.709  30.524  1.00 33.15           O  
ANISOU 4959  O   LEU A 649     3730   4805   4062    200   -613   -139       O  
ATOM   4960  CB  LEU A 649      -2.491  30.068  30.956  1.00 24.56           C  
ANISOU 4960  CB  LEU A 649     2825   3589   2919    204   -478    -82       C  
ATOM   4961  CG  LEU A 649      -2.499  30.735  32.332  1.00 30.00           C  
ANISOU 4961  CG  LEU A 649     3496   4192   3709    200   -414    -73       C  
ATOM   4962  CD1 LEU A 649      -1.770  29.882  33.360  1.00 22.78           C  
ANISOU 4962  CD1 LEU A 649     2624   3219   2810    138   -357   -128       C  
ATOM   4963  CD2 LEU A 649      -1.872  32.121  32.237  1.00 33.51           C  
ANISOU 4963  CD2 LEU A 649     3966   4596   4171    256   -385     15       C  
ATOM   4964  N   ASN A 650      -5.086  28.539  32.416  1.00 30.73           N  
ANISOU 4964  N   ASN A 650     3450   4390   3834     95   -514   -231       N  
ATOM   4965  CA  ASN A 650      -6.361  28.783  33.064  1.00 30.67           C  
ANISOU 4965  CA  ASN A 650     3346   4395   3913     91   -517   -243       C  
ATOM   4966  C   ASN A 650      -6.014  29.443  34.389  1.00 33.01           C  
ANISOU 4966  C   ASN A 650     3655   4608   4279     99   -430   -224       C  
ATOM   4967  O   ASN A 650      -5.232  28.887  35.164  1.00 30.42           O  
ANISOU 4967  O   ASN A 650     3386   4223   3951     54   -375   -252       O  
ATOM   4968  CB  ASN A 650      -7.126  27.467  33.274  1.00 32.93           C  
ANISOU 4968  CB  ASN A 650     3590   4706   4215      8   -541   -323       C  
ATOM   4969  CG  ASN A 650      -8.557  27.675  33.749  1.00 40.50           C  
ANISOU 4969  CG  ASN A 650     4429   5701   5259      2   -553   -333       C  
ATOM   4970  OD1 ASN A 650      -8.824  28.512  34.609  1.00 39.28           O  
ANISOU 4970  OD1 ASN A 650     4239   5514   5171     37   -499   -304       O  
ATOM   4971  ND2 ASN A 650      -9.487  26.897  33.192  1.00 37.85           N  
ANISOU 4971  ND2 ASN A 650     4028   5434   4920    -43   -623   -380       N  
ATOM   4972  N   VAL A 651      -6.566  30.628  34.648  1.00 36.21           N  
ANISOU 4972  N   VAL A 651     4009   5006   4743    161   -419   -180       N  
ATOM   4973  CA  VAL A 651      -6.241  31.355  35.872  1.00 35.28           C  
ANISOU 4973  CA  VAL A 651     3910   4809   4687    174   -339   -170       C  
ATOM   4974  C   VAL A 651      -7.168  30.927  37.009  1.00 49.00           C  
ANISOU 4974  C   VAL A 651     5582   6545   6492    134   -299   -222       C  
ATOM   4975  O   VAL A 651      -6.922  31.272  38.176  1.00 42.35           O  
ANISOU 4975  O   VAL A 651     4760   5642   5690    130   -227   -232       O  
ATOM   4976  CB  VAL A 651      -6.327  32.881  35.671  1.00 35.16           C  
ANISOU 4976  CB  VAL A 651     3881   4769   4708    264   -338   -100       C  
ATOM   4977  CG1 VAL A 651      -5.330  33.348  34.597  1.00 36.40           C  
ANISOU 4977  CG1 VAL A 651     4108   4924   4799    298   -365    -36       C  
ATOM   4978  CG2 VAL A 651      -7.760  33.298  35.330  1.00 32.39           C  
ANISOU 4978  CG2 VAL A 651     3422   4479   4405    314   -384    -88       C  
ATOM   4979  N   ASN A 652      -8.240  30.226  36.605  1.00 49.15           N  
ATOM   4980  CA  ASN A 652      -9.257  29.517  37.417  1.00 57.35           C  
ATOM   4981  C   ASN A 652     -10.652  29.622  36.800  1.00 52.83           C  
ATOM   4982  O   ASN A 652     -11.390  30.573  37.069  1.00 47.59           O  
ATOM   4983  CB  ASN A 652      -9.308  29.984  38.861  1.00 67.87           C  
ATOM   4984  CG  ASN A 652      -8.728  28.960  39.796  1.00 77.35           C  
ATOM   4985  OD1 ASN A 652      -7.533  28.674  39.747  1.00 74.74           O  
ATOM   4986  ND2 ASN A 652      -9.574  28.371  40.631  1.00 85.56           N  
TER    4987      ASN A 652                                                      
HETATM 9989  PA  FAD A 901      11.919  23.140  43.469  1.00 10.41           P  
HETATM 9990  O1A FAD A 901      11.473  24.144  42.484  1.00 17.06           O  
HETATM 9991  O2A FAD A 901      12.392  24.002  44.580  1.00 18.35           O  
HETATM 9992  O5B FAD A 901      10.691  22.204  43.867  1.00 13.69           O  
HETATM 9993  C5B FAD A 901      10.795  21.359  45.021  1.00  7.95           C  
HETATM 9994  C4B FAD A 901       9.425  20.862  45.358  1.00  9.90           C  
HETATM 9995  O4B FAD A 901       9.551  19.675  46.154  1.00  9.00           O  
HETATM 9996  C3B FAD A 901       8.742  21.873  46.219  1.00 13.01           C  
HETATM 9997  O3B FAD A 901       7.463  22.139  45.687  1.00 13.96           O  
HETATM 9998  C2B FAD A 901       8.692  21.227  47.539  1.00  9.26           C  
HETATM 9999  O2B FAD A 901       7.574  21.644  48.343  1.00  5.15           O  
HETATM10000  C1B FAD A 901       8.616  19.795  47.206  1.00  8.05           C  
HETATM10001  N9A FAD A 901       9.053  19.035  48.289  1.00  8.08           N  
HETATM10002  C8A FAD A 901      10.211  19.137  48.976  1.00  8.97           C  
HETATM10003  N7A FAD A 901      10.235  18.221  49.952  1.00  7.81           N  
HETATM10004  C5A FAD A 901       9.014  17.492  49.901  1.00  6.36           C  
HETATM10005  C6A FAD A 901       8.394  16.380  50.657  1.00 11.00           C  
HETATM10006  N6A FAD A 901       9.045  15.757  51.764  1.00 12.11           N  
HETATM10007  N1A FAD A 901       7.167  15.949  50.297  1.00  9.33           N  
HETATM10008  C2A FAD A 901       6.494  16.489  49.261  1.00 12.82           C  
HETATM10009  N3A FAD A 901       6.996  17.509  48.522  1.00  5.85           N  
HETATM10010  C4A FAD A 901       8.267  18.006  48.836  1.00  9.38           C  
HETATM10011  N1  FAD A 901      15.755  30.649  39.268  1.00 11.96           N  
HETATM10012  C2  FAD A 901      15.664  31.307  38.116  1.00 14.17           C  
HETATM10013  O2  FAD A 901      15.916  30.583  36.909  1.00 18.19           O  
HETATM10014  N3  FAD A 901      15.377  32.601  38.050  1.00 16.23           N  
HETATM10015  C4  FAD A 901      15.165  33.300  39.188  1.00 11.52           C  
HETATM10016  O4  FAD A 901      14.859  34.641  39.136  1.00 11.03           O  
HETATM10017  C4X FAD A 901      15.246  32.626  40.475  1.00  8.98           C  
HETATM10018  N5  FAD A 901      15.048  33.310  41.661  1.00 10.58           N  
HETATM10019  C5X FAD A 901      14.885  32.565  42.822  1.00 11.83           C  
HETATM10020  C6  FAD A 901      14.472  33.239  44.018  1.00  6.85           C  
HETATM10021  C7  FAD A 901      14.124  32.480  45.158  1.00 14.13           C  
HETATM10022  C7M FAD A 901      13.689  33.183  46.441  1.00 15.29           C  
HETATM10023  C8  FAD A 901      14.189  31.090  45.117  1.00 10.96           C  
HETATM10024  C8M FAD A 901      13.817  30.223  46.378  1.00 16.75           C  
HETATM10025  C9  FAD A 901      14.598  30.419  43.932  1.00 13.87           C  
HETATM10026  C9A FAD A 901      14.941  31.189  42.782  1.00 14.31           C  
HETATM10027  N10 FAD A 901      15.360  30.513  41.627  1.00 17.92           N  
HETATM10028  C10 FAD A 901      15.543  31.267  40.480  1.00 14.00           C  
HETATM10029  C1' FAD A 901      15.753  29.124  41.672  1.00 10.38           C  
HETATM10030  C2' FAD A 901      14.720  28.226  40.938  1.00 15.41           C  
HETATM10031  O2' FAD A 901      13.427  28.671  41.236  1.00 17.95           O  
HETATM10032  C3' FAD A 901      14.977  26.800  41.361  1.00 17.53           C  
HETATM10033  O3' FAD A 901      16.312  26.500  41.117  1.00 19.05           O  
HETATM10034  C4' FAD A 901      14.125  25.760  40.615  1.00 15.36           C  
HETATM10035  O4' FAD A 901      12.789  25.873  40.951  1.00 11.26           O  
HETATM10036  C5' FAD A 901      14.586  24.372  41.071  1.00 12.57           C  
HETATM10037  O5' FAD A 901      13.534  23.484  40.690  1.00 13.88           O  
HETATM10038  P   FAD A 901      13.412  22.056  41.386  1.00 10.99           P  
HETATM10039  O1P FAD A 901      12.442  21.191  40.662  1.00 11.26           O  
HETATM10040  O2P FAD A 901      14.739  21.344  41.318  1.00  5.45           O  
HETATM10041  O3P FAD A 901      13.065  22.222  42.936  1.00 15.12           O  
HETATM10095  O   HOH A1001      17.768  51.510  20.398  1.00 40.01           O  
HETATM10096  O   HOH A1002      24.486  62.632  42.950  1.00 32.21           O  
HETATM10097  O   HOH A1003      33.288  12.383  43.905  1.00 47.09           O  
HETATM10098  O   HOH A1004      46.810  52.243  37.971  1.00 49.19           O  
HETATM10099  O   HOH A1005     -10.304  27.988  42.622  1.00 28.55           O  
HETATM10100  O   HOH A1006      19.869  25.921  14.501  1.00 34.70           O  
HETATM10101  O   HOH A1007      21.475  63.128  27.046  1.00 41.55           O  
HETATM10102  O   HOH A1008       3.427  46.124  29.736  1.00 31.43           O  
HETATM10103  O   HOH A1009      32.509  12.309  41.210  1.00 44.72           O  
HETATM10104  O   HOH A1010      -5.485  30.595  28.409  1.00 44.00           O  
HETATM10105  O   HOH A1011      30.928  61.613  33.389  1.00 39.29           O  
HETATM10106  O   HOH A1012      50.425  28.677  58.965  1.00 37.58           O  
HETATM10107  O   HOH A1013      26.292  58.591  51.447  1.00 51.42           O  
HETATM10108  O   HOH A1014      37.562  37.160  13.859  1.00 38.20           O  
HETATM10109  O   HOH A1015      -4.249  13.274  63.275  1.00 36.07           O  
HETATM10110  O   HOH A1016      61.553  39.221  50.247  1.00 33.24           O  
HETATM10111  O   HOH A1017      36.867  44.759  17.118  1.00 33.91           O  
HETATM10112  O   HOH A1018      37.784  39.306  57.566  1.00 21.13           O  
HETATM10113  O   HOH A1019      25.701  12.715  44.405  1.00 18.58           O  
HETATM10114  O   HOH A1020      20.270  23.103  14.633  1.00 38.05           O  
HETATM10115  O   HOH A1021      -0.536  31.104  40.952  1.00 10.47           O  
HETATM10116  O   HOH A1022      16.420  30.120  34.604  1.00  8.23           O  
HETATM10117  O   HOH A1023      19.028  27.067  33.900  1.00  9.02           O  
HETATM10118  O   HOH A1024      -2.296   4.161  53.262  1.00 27.51           O  
HETATM10119  O   HOH A1025      33.902  57.967  47.853  1.00 32.34           O  
HETATM10120  O   HOH A1026       3.652  35.762  58.277  1.00 15.00           O  
HETATM10121  O   HOH A1027       9.627   2.783  33.260  1.00 37.26           O  
HETATM10122  O   HOH A1028      45.335  58.006  39.707  1.00 41.41           O  
HETATM10123  O   HOH A1029      27.624   3.275  43.832  1.00 31.34           O  
HETATM10124  O   HOH A1030      49.969  45.614  34.041  1.00 48.08           O  
HETATM10125  O   HOH A1031      32.327  15.381  46.579  1.00 52.32           O  
HETATM10126  O   HOH A1032      55.590  45.420  46.008  1.00 26.67           O  
HETATM10127  O   HOH A1033      36.243  25.755  56.494  1.00 23.39           O  
HETATM10128  O   HOH A1034      30.190  43.373  48.038  1.00  8.33           O  
HETATM10129  O   HOH A1035      55.495  40.540  44.683  1.00 35.99           O  
HETATM10130  O   HOH A1036      12.403   2.788  23.691  1.00 44.57           O  
HETATM10131  O   HOH A1037      41.472  43.467  56.588  1.00 41.68           O  
HETATM10132  O   HOH A1038      35.242  26.132  20.699  1.00 36.88           O  
HETATM10133  O   HOH A1039      17.305  48.725  50.953  1.00 42.12           O  
HETATM10134  O   HOH A1040      27.893   3.974  62.141  1.00 33.36           O  
HETATM10135  O   HOH A1041      15.092  13.725  58.570  1.00 12.81           O  
HETATM10136  O   HOH A1042      19.158  34.043  47.633  1.00 27.55           O  
HETATM10137  O   HOH A1043      16.088  36.565  54.967  1.00 33.05           O  
HETATM10138  O   HOH A1044      60.552  42.297  51.280  1.00 55.30           O  
HETATM10139  O   HOH A1045      -4.874  19.689  51.178  1.00 18.46           O  
HETATM10140  O   HOH A1046      15.265   3.434  55.687  1.00 18.29           O  
HETATM10141  O   HOH A1047      -4.624  36.103  42.451  1.00 23.27           O  
HETATM10142  O   HOH A1048      50.751  52.964  52.233  1.00 47.61           O  
HETATM10143  O   HOH A1049      41.717  39.488  18.801  1.00 33.98           O  
HETATM10144  O   HOH A1050      31.141  52.070  59.066  1.00 48.65           O  
HETATM10145  O   HOH A1051       1.615  27.992  28.278  1.00 20.51           O  
HETATM10146  O   HOH A1052      -7.487  13.382  56.437  1.00 35.88           O  
HETATM10147  O   HOH A1053      -8.297  26.229  41.162  1.00 22.30           O  
HETATM10148  O   HOH A1054      21.628  45.055  18.448  1.00 20.28           O  
HETATM10149  O   HOH A1055      15.144  32.628  53.720  1.00 28.15           O  
HETATM10150  O   HOH A1056      24.676  40.941  61.811  1.00 14.41           O  
HETATM10151  O   HOH A1057      59.108  45.966  58.164  1.00 50.59           O  
HETATM10152  O   HOH A1058       0.775  28.612  51.946  1.00 12.70           O  
HETATM10153  O   HOH A1059      17.803  61.069  41.043  1.00 37.12           O  
HETATM10154  O   HOH A1060      13.209  16.174  18.444  1.00 41.45           O  
HETATM10155  O   HOH A1061      51.594  53.964  49.834  1.00 53.82           O  
HETATM10156  O   HOH A1062      32.812  38.634  18.957  1.00 26.31           O  
HETATM10157  O   HOH A1063      14.574   5.201  28.275  1.00 33.82           O  
HETATM10158  O   HOH A1064       5.317  28.725  20.760  1.00 28.31           O  
HETATM10159  O   HOH A1065     -15.749  21.201  44.193  1.00 38.03           O  
HETATM10160  O   HOH A1066      51.358  22.154  52.196  1.00 30.81           O  
HETATM10161  O   HOH A1067      29.499  33.856  51.932  1.00 11.41           O  
HETATM10162  O   HOH A1068      16.173  47.134  30.334  1.00 23.76           O  
HETATM10163  O   HOH A1069      13.143  -7.115  42.686  1.00 52.09           O  
HETATM10164  O   HOH A1070       4.617   4.612  20.743  1.00 25.76           O  
HETATM10165  O   HOH A1071      54.537  35.673  45.602  1.00 32.22           O  
HETATM10166  O   HOH A1072      27.914  52.696  64.821  1.00 28.69           O  
HETATM10167  O   HOH A1073     -11.014  29.857  42.211  1.00 57.51           O  
HETATM10168  O   HOH A1074      56.818  35.924  46.712  1.00 41.08           O  
HETATM10169  O   HOH A1075      45.823  35.238  37.547  1.00 18.37           O  
HETATM10170  O   HOH A1076      19.762  48.329  23.205  1.00 18.54           O  
HETATM10171  O   HOH A1077       9.323  -4.096  51.795  1.00 48.57           O  
HETATM10172  O   HOH A1078      43.738  33.444  53.016  1.00 34.11           O  
HETATM10173  O   HOH A1079       8.183  49.388  41.240  1.00 28.50           O  
HETATM10174  O   HOH A1080      19.121  38.875  26.134  1.00 19.32           O  
HETATM10175  O   HOH A1081      27.985  42.168  62.360  1.00 16.54           O  
HETATM10176  O   HOH A1082      32.931  21.803  42.541  1.00 27.64           O  
HETATM10177  O   HOH A1083      10.177  19.594  40.979  1.00  8.88           O  
HETATM10178  O   HOH A1084      32.502  14.630  27.693  1.00 31.79           O  
HETATM10179  O   HOH A1085      28.441  27.736  35.269  1.00 15.25           O  
HETATM10180  O   HOH A1086      49.542  35.059  55.299  1.00 20.42           O  
HETATM10181  O   HOH A1087      23.092  31.617  24.463  1.00 11.96           O  
HETATM10182  O   HOH A1088      20.681  33.066  60.100  1.00 28.78           O  
HETATM10183  O   HOH A1089      43.118  47.138  22.845  1.00 28.89           O  
HETATM10184  O   HOH A1090      35.540  36.378  18.598  1.00 20.16           O  
HETATM10185  O   HOH A1091      29.031  10.755  52.676  1.00 42.36           O  
HETATM10186  O   HOH A1092     -10.866  22.087  36.472  1.00 19.59           O  
HETATM10187  O   HOH A1093      -8.592  32.832  40.030  1.00 34.59           O  
HETATM10188  O   HOH A1094       1.670  25.931  49.676  1.00 10.09           O  
HETATM10189  O   HOH A1095      27.066  56.777  24.648  1.00 34.44           O  
HETATM10190  O   HOH A1096      15.273  59.193  38.321  1.00 34.58           O  
HETATM10191  O   HOH A1097      -4.939  19.729  60.575  1.00 21.72           O  
HETATM10192  O   HOH A1098       5.098  -4.932  48.068  1.00 48.34           O  
HETATM10193  O   HOH A1099      36.340  33.858  24.374  1.00 18.39           O  
HETATM10194  O   HOH A1100      -4.510  32.621  38.827  1.00 16.61           O  
HETATM10195  O   HOH A1101      38.621  48.916  30.818  1.00 19.03           O  
HETATM10196  O   HOH A1102      10.174  18.401  60.514  1.00 21.95           O  
HETATM10197  O   HOH A1103      21.651  -2.294  44.736  1.00 36.40           O  
HETATM10198  O   HOH A1104      28.995  26.402  44.096  1.00 11.92           O  
HETATM10199  O   HOH A1105      35.389  27.501  49.609  1.00 15.25           O  
HETATM10200  O   HOH A1106      24.001  59.210  48.069  1.00 30.38           O  
HETATM10201  O   HOH A1107      18.880   6.337  27.530  1.00 48.79           O  
HETATM10202  O   HOH A1108      56.391  33.137  47.703  1.00 19.60           O  
HETATM10203  O   HOH A1109      -8.345  31.340  32.824  1.00 39.86           O  
HETATM10204  O   HOH A1110      15.558  48.383  39.106  1.00 16.91           O  
HETATM10205  O   HOH A1111      16.893  59.624  30.181  1.00 43.10           O  
HETATM10206  O   HOH A1112      30.986  60.272  47.127  1.00 35.80           O  
HETATM10207  O   HOH A1113       9.206  20.179  22.148  1.00 18.95           O  
HETATM10208  O   HOH A1114      41.609  39.277  22.156  1.00 22.72           O  
HETATM10209  O   HOH A1115      21.285   0.640  60.294  1.00 33.98           O  
HETATM10210  O   HOH A1116      -2.243  20.883  26.398  1.00 23.82           O  
HETATM10211  O   HOH A1117      25.951  14.120  52.105  1.00 11.87           O  
HETATM10212  O   HOH A1118       4.852  42.348  28.017  1.00 24.95           O  
HETATM10213  O   HOH A1119      14.058  55.394  37.915  1.00 20.12           O  
HETATM10214  O   HOH A1120      43.790  26.738  32.951  1.00 43.07           O  
HETATM10215  O   HOH A1121      -2.238   8.950  31.336  1.00 26.97           O  
HETATM10216  O   HOH A1122      15.898  31.619  49.607  1.00  8.73           O  
HETATM10217  O   HOH A1123      56.026  19.134  51.404  1.00 27.93           O  
HETATM10218  O   HOH A1124      27.817  30.836  63.808  1.00 21.73           O  
HETATM10219  O   HOH A1125      33.103  34.306  43.699  1.00 14.34           O  
HETATM10220  O   HOH A1126      13.046   2.788  53.024  1.00 26.29           O  
HETATM10221  O   HOH A1127      27.419  49.853  41.600  1.00 23.97           O  
HETATM10222  O   HOH A1128      34.453  31.204  42.573  1.00 13.44           O  
HETATM10223  O   HOH A1129       5.495  30.347  23.507  1.00 31.11           O  
HETATM10224  O   HOH A1130      43.824  35.957  28.595  1.00 22.53           O  
HETATM10225  O   HOH A1131      39.206  44.768  30.142  1.00 18.25           O  
HETATM10226  O   HOH A1132      -0.297  36.641  27.291  1.00 36.05           O  
HETATM10227  O   HOH A1133      21.385   3.651  38.250  1.00 40.05           O  
HETATM10228  O   HOH A1134      59.208  27.679  47.365  1.00 15.67           O  
HETATM10229  O   HOH A1135       3.603  40.533  48.692  1.00 18.94           O  
HETATM10230  O   HOH A1136      59.909  43.437  47.884  1.00 41.84           O  
HETATM10231  O   HOH A1137      25.630  30.184  24.720  1.00 14.74           O  
HETATM10232  O   HOH A1138      27.037   9.750  29.988  1.00 27.21           O  
HETATM10233  O   HOH A1139      11.691  50.281  34.543  1.00 15.47           O  
HETATM10234  O   HOH A1140      -3.836  11.153  31.535  1.00 20.81           O  
HETATM10235  O   HOH A1141      31.379  37.760  41.854  1.00 13.30           O  
HETATM10236  O   HOH A1142      -4.313  15.897  50.462  1.00 33.52           O  
HETATM10237  O   HOH A1143      18.295  14.711  23.216  1.00 25.92           O  
HETATM10238  O   HOH A1144      21.009  30.731  17.797  1.00 32.31           O  
HETATM10239  O   HOH A1145      52.226  33.157  37.233  1.00 35.01           O  
HETATM10240  O   HOH A1146      16.244  44.783  43.101  1.00 27.30           O  
HETATM10241  O   HOH A1147      13.102  15.578  53.711  1.00 24.76           O  
HETATM10242  O   HOH A1148      48.130  53.450  46.656  1.00 40.75           O  
HETATM10243  O   HOH A1149      -5.636  22.886  39.279  1.00 16.52           O  
HETATM10244  O   HOH A1150      27.262  45.041  13.867  1.00 42.66           O  
HETATM10245  O   HOH A1151      45.973  40.122  52.289  1.00 14.31           O  
HETATM10246  O   HOH A1152      -1.619  22.462  24.138  1.00 22.66           O  
HETATM10247  O   HOH A1153      -8.684  11.854  36.916  1.00 24.98           O  
HETATM10248  O   HOH A1154     -13.533  20.854  46.352  1.00 35.44           O  
HETATM10249  O   HOH A1155      15.646  -3.534  50.857  1.00 30.15           O  
HETATM10250  O   HOH A1156      26.362  19.954  21.741  1.00 16.48           O  
HETATM10251  O   HOH A1157      37.204  50.861  31.641  1.00 30.52           O  
HETATM10252  O   HOH A1158      -2.997   5.831  49.976  1.00 26.72           O  
HETATM10253  O   HOH A1159      34.290  56.155  38.106  1.00 33.21           O  
HETATM10254  O   HOH A1160      28.057  38.029  61.249  1.00 11.40           O  
HETATM10255  O   HOH A1161     -12.208  28.653  41.144  1.00 35.52           O  
HETATM10256  O   HOH A1162      -1.735  12.662  23.998  1.00 38.38           O  
HETATM10257  O   HOH A1163      26.956  29.799  52.317  1.00 13.42           O  
HETATM10258  O   HOH A1164       3.519  37.642  56.229  1.00 22.90           O  
HETATM10259  O   HOH A1165      32.130  50.061  53.322  1.00 22.46           O  
HETATM10260  O   HOH A1166      48.045  23.688  52.127  1.00 48.26           O  
HETATM10261  O   HOH A1167      31.566  18.577  35.500  1.00 28.04           O  
HETATM10262  O   HOH A1168      41.705  43.898  28.729  1.00 47.23           O  
HETATM10263  O   HOH A1169       7.343  -1.182  42.148  1.00 29.50           O  
HETATM10264  O   HOH A1170      35.119  35.558  27.519  1.00 15.45           O  
HETATM10265  O   HOH A1171      47.405  49.136  47.587  1.00 32.33           O  
HETATM10266  O   HOH A1172      30.379  27.756  23.099  1.00 24.99           O  
HETATM10267  O   HOH A1173      18.444  68.484  33.579  1.00 43.93           O  
HETATM10268  O   HOH A1174      18.230  53.961  41.776  1.00 26.93           O  
HETATM10269  O   HOH A1175      22.057  22.955  58.437  1.00  7.46           O  
HETATM10270  O   HOH A1176      37.781  27.313  48.700  1.00 16.95           O  
HETATM10271  O   HOH A1177      27.193  36.135  54.826  1.00 20.22           O  
HETATM10272  O   HOH A1178      30.024  28.221  33.231  1.00 18.47           O  
HETATM10273  O   HOH A1179       7.773  52.891  30.565  1.00 62.93           O  
HETATM10274  O   HOH A1180      -4.233  13.061  51.120  1.00 20.45           O  
HETATM10275  O   HOH A1181      47.359  49.425  44.826  1.00 21.61           O  
HETATM10276  O   HOH A1182      22.392   8.123  67.230  1.00 36.59           O  
HETATM10277  O   HOH A1183      24.823  37.818  18.628  1.00 29.88           O  
HETATM10278  O   HOH A1184      51.822  48.140  44.978  1.00 37.76           O  
HETATM10279  O   HOH A1185      41.409  54.514  38.433  1.00 43.24           O  
HETATM10280  O   HOH A1186      22.987  38.332  52.691  1.00 38.25           O  
HETATM10281  O   HOH A1187      28.739  18.781  42.097  1.00 27.91           O  
HETATM10282  O   HOH A1188      19.019  33.953  55.694  1.00 23.65           O  
HETATM10283  O   HOH A1189      25.234  68.271  36.068  1.00 49.64           O  
HETATM10284  O   HOH A1190       0.481  22.040  16.959  1.00 37.03           O  
HETATM10285  O   HOH A1191      51.365  31.017  41.586  1.00 24.15           O  
HETATM10286  O   HOH A1192       0.368  20.236  27.188  1.00 17.46           O  
HETATM10287  O   HOH A1193      18.108  55.948  32.660  1.00 24.17           O  
HETATM10288  O   HOH A1194      17.201  25.065  43.396  1.00  7.62           O  
HETATM10289  O   HOH A1195      25.897  49.930  13.543  1.00 34.87           O  
HETATM10290  O   HOH A1196      28.752  25.573  56.078  1.00 13.02           O  
HETATM10291  O   HOH A1197      -6.997  18.313  30.343  1.00 26.49           O  
HETATM10292  O   HOH A1198      21.726  37.502  41.781  1.00 36.47           O  
HETATM10293  O   HOH A1199     -11.634  31.158  39.734  1.00 45.48           O  
HETATM10294  O   HOH A1200      29.113  46.553  18.914  1.00 27.73           O  
HETATM10295  O   HOH A1201       4.899  37.116  43.014  1.00 11.79           O  
HETATM10296  O   HOH A1202      30.865  24.532  23.093  1.00 19.58           O  
HETATM10297  O   HOH A1203       8.847  54.677  33.544  1.00 44.11           O  
HETATM10298  O   HOH A1204      39.272  31.867  40.841  1.00 15.33           O  
HETATM10299  O   HOH A1205       0.890  27.623  43.204  1.00 10.43           O  
HETATM10300  O   HOH A1206      18.949  61.289  47.289  1.00 40.94           O  
HETATM10301  O   HOH A1207      32.631  40.735  22.322  1.00 15.72           O  
HETATM10302  O   HOH A1208      35.281  22.652  31.738  1.00 22.40           O  
HETATM10303  O   HOH A1209      18.480  63.717  41.581  1.00 35.14           O  
HETATM10304  O   HOH A1210      23.461  34.069  60.183  1.00 20.93           O  
HETATM10305  O   HOH A1211      12.366  11.348  17.395  1.00 38.80           O  
HETATM10306  O   HOH A1212      43.413  25.113  24.984  1.00 41.14           O  
HETATM10307  O   HOH A1213      47.312  52.393  44.204  1.00 46.12           O  
HETATM10308  O   HOH A1214      13.099  41.535  31.465  1.00 14.98           O  
HETATM10309  O   HOH A1215      -1.228  14.906  22.892  1.00 22.65           O  
HETATM10310  O   HOH A1216      31.158  51.847  51.346  1.00 17.44           O  
HETATM10311  O   HOH A1217       6.594  49.073  26.090  1.00 41.33           O  
HETATM10312  O   HOH A1218      31.677  23.514  51.994  1.00 13.96           O  
HETATM10313  O   HOH A1219      23.567  24.964  41.399  1.00 24.79           O  
HETATM10314  O   HOH A1220      16.521  40.480  25.335  1.00 16.83           O  
HETATM10315  O   HOH A1221      -5.022  16.612  47.398  1.00 17.89           O  
HETATM10316  O   HOH A1222      36.676  53.630  28.183  1.00 39.79           O  
HETATM10317  O   HOH A1223      11.457  21.751  21.449  1.00 28.75           O  
HETATM10318  O   HOH A1224      44.557  56.630  48.442  1.00 54.49           O  
HETATM10319  O   HOH A1225      27.628  29.388  26.837  1.00 12.79           O  
HETATM10320  O   HOH A1226      15.042  16.885  55.756  1.00  7.17           O  
HETATM10321  O   HOH A1227      13.383  13.824  61.630  1.00 30.81           O  
HETATM10322  O   HOH A1228      19.423  45.095  43.812  1.00 14.31           O  
HETATM10323  O   HOH A1229      17.578  18.778  22.182  1.00 29.50           O  
HETATM10324  O   HOH A1230       1.173   4.137  28.424  1.00 14.28           O  
HETATM10325  O   HOH A1231      -2.315   1.892  35.425  1.00 46.84           O  
HETATM10326  O   HOH A1232      -1.677  40.830  38.627  1.00 36.46           O  
HETATM10327  O   HOH A1233      37.538  23.909  22.625  1.00 30.21           O  
HETATM10328  O   HOH A1234      25.888  44.008  18.194  1.00 22.92           O  
HETATM10329  O   HOH A1235      18.540  42.494  43.855  1.00 31.98           O  
HETATM10330  O   HOH A1236      16.404  -0.540  35.889  1.00 36.81           O  
HETATM10331  O   HOH A1237      43.210  25.458  52.145  1.00 22.00           O  
HETATM10332  O   HOH A1238      49.710  28.628  41.799  1.00 18.41           O  
HETATM10333  O   HOH A1239      42.024  41.109  27.019  1.00 27.86           O  
HETATM10334  O   HOH A1240       8.801  25.460  34.112  1.00  8.91           O  
HETATM10335  O   HOH A1241      16.574  49.608  29.793  1.00 21.39           O  
HETATM10336  O   HOH A1242       2.739   9.535  23.502  1.00 28.94           O  
HETATM10337  O   HOH A1243      30.256  24.685  59.774  1.00 15.06           O  
HETATM10338  O   HOH A1244      52.016  50.232  53.865  1.00 38.21           O  
HETATM10339  O   HOH A1245       7.506  42.764  59.781  1.00 24.83           O  
HETATM10340  O   HOH A1246       3.438  -2.270  47.545  1.00 32.40           O  
HETATM10341  O   HOH A1247      19.780  28.636  24.757  1.00 12.65           O  
HETATM10342  O   HOH A1248      27.022  15.299  43.464  1.00 25.59           O  
HETATM10343  O   HOH A1249      12.974  36.262  48.040  1.00  9.56           O  
HETATM10344  O   HOH A1250      -0.946  25.472  22.200  1.00 25.15           O  
HETATM10345  O   HOH A1251      13.946  37.866  51.244  1.00 26.24           O  
HETATM10346  O   HOH A1252      32.472  25.244  40.293  1.00 21.84           O  
HETATM10347  O   HOH A1253      19.784  -1.927  60.592  1.00 52.31           O  
HETATM10348  O   HOH A1254      19.020  10.079  65.757  1.00 22.97           O  
HETATM10349  O   HOH A1255      28.988  29.811  21.600  1.00 25.33           O  
HETATM10350  O   HOH A1256      46.641  26.930  37.360  1.00 33.01           O  
HETATM10351  O   HOH A1257      40.855  33.127  22.370  1.00 36.66           O  
HETATM10352  O   HOH A1258      15.506  42.792  32.057  1.00 11.63           O  
HETATM10353  O   HOH A1259      24.172  55.548  25.343  1.00 36.07           O  
HETATM10354  O   HOH A1260      36.344  30.916  28.232  1.00 17.99           O  
HETATM10355  O   HOH A1261      23.245  26.982  51.617  1.00  8.72           O  
HETATM10356  O   HOH A1262      23.185  57.448  50.779  1.00 30.27           O  
HETATM10357  O   HOH A1263      18.462  37.117  38.062  1.00 17.09           O  
HETATM10358  O   HOH A1264      -4.186  42.415  43.285  1.00 39.72           O  
HETATM10359  O   HOH A1265      35.129  23.716  42.500  1.00 39.68           O  
HETATM10360  O   HOH A1266      23.483  27.204  40.463  1.00 24.09           O  
HETATM10361  O   HOH A1267      -5.959  23.014  44.157  1.00 29.78           O  
HETATM10362  O   HOH A1268      42.637  43.563  33.317  1.00 31.49           O  
HETATM10363  O   HOH A1269      17.166  50.029  47.818  1.00 24.88           O  
HETATM10364  O   HOH A1270      11.505  17.786  52.414  1.00 10.28           O  
HETATM10365  O   HOH A1271      17.787  17.205  60.249  1.00  9.04           O  
HETATM10366  O   HOH A1272      50.488  49.250  47.107  1.00 24.13           O  
HETATM10367  O   HOH A1273      -6.100  27.152  37.314  1.00 15.61           O  
HETATM10368  O   HOH A1274       1.678  34.021  55.249  1.00 14.08           O  
HETATM10369  O   HOH A1275      -7.793  28.473  29.473  1.00 33.56           O  
HETATM10370  O   HOH A1276      -4.671  18.711  44.572  1.00  7.46           O  
HETATM10371  O   HOH A1277      22.948   6.159  44.293  1.00 15.56           O  
HETATM10372  O   HOH A1278      17.743  42.660  25.053  1.00 11.20           O  
HETATM10373  O   HOH A1279      21.246  31.489  28.584  1.00 10.29           O  
HETATM10374  O   HOH A1280      29.798  21.753  20.331  1.00 36.67           O  
HETATM10375  O   HOH A1281      38.555  56.424  41.965  1.00 40.13           O  
HETATM10376  O   HOH A1282      20.127  50.015  58.204  1.00 26.12           O  
HETATM10377  O   HOH A1283       1.575  43.974  38.799  1.00 25.45           O  
HETATM10378  O   HOH A1284     -15.845  18.532  43.353  1.00 50.18           O  
HETATM10379  O   HOH A1285       8.076  50.547  35.538  1.00 27.02           O  
HETATM10380  O   HOH A1286      16.938  31.698  19.315  1.00 27.73           O  
HETATM10381  O   HOH A1287      24.686  55.324  58.287  1.00 28.86           O  
HETATM10382  O   HOH A1288      16.720  22.202  43.255  1.00  4.37           O  
HETATM10383  O   HOH A1289      29.219  31.414  15.054  1.00 47.68           O  
HETATM10384  O   HOH A1290      -3.413   8.612  38.856  1.00 34.83           O  
HETATM10385  O   HOH A1291      15.952  26.992  44.733  1.00 12.70           O  
HETATM10386  O   HOH A1292      58.342  20.023  48.773  1.00 30.82           O  
HETATM10387  O   HOH A1293      17.109  64.535  43.311  1.00 51.61           O  
HETATM10388  O   HOH A1294      13.909  38.396  21.846  1.00 22.63           O  
HETATM10389  O   HOH A1295     -12.828  15.703  41.644  1.00 29.18           O  
HETATM10390  O   HOH A1296      29.523  42.209  42.090  1.00 14.42           O  
HETATM10391  O   HOH A1297      -9.798  21.424  30.008  1.00 36.69           O  
HETATM10392  O   HOH A1298      48.826  30.167  38.356  1.00 29.43           O  
HETATM10393  O   HOH A1299      31.705  19.807  50.259  1.00 32.15           O  
HETATM10394  O   HOH A1300      25.490   6.928  33.363  1.00 39.77           O  
HETATM10395  O   HOH A1301      40.624  46.322  27.772  1.00 34.23           O  
HETATM10396  O   HOH A1302      20.644  18.299  18.258  1.00 47.97           O  
HETATM10397  O   HOH A1303       0.947  22.988  53.523  1.00 16.38           O  
HETATM10398  O   HOH A1304      35.365  33.376  29.314  1.00 10.14           O  
HETATM10399  O   HOH A1305      -3.544   8.485  50.014  1.00 30.07           O  
HETATM10400  O   HOH A1306      10.811  45.388  47.969  1.00 36.11           O  
HETATM10401  O   HOH A1307      41.858  24.060  24.134  1.00 38.38           O  
HETATM10402  O   HOH A1308      27.389  66.148  27.959  1.00 49.86           O  
HETATM10403  O   HOH A1309      44.236  46.871  36.230  1.00 25.87           O  
HETATM10404  O   HOH A1310      43.230  43.618  57.746  1.00 54.92           O  
HETATM10405  O   HOH A1311      24.890  51.245  18.846  1.00 26.84           O  
HETATM10406  O   HOH A1312      37.018  35.730  36.430  1.00 15.33           O  
HETATM10407  O   HOH A1313      16.626  -6.776  45.005  1.00 33.19           O  
HETATM10408  O   HOH A1314      36.523  48.418  54.520  1.00 24.36           O  
HETATM10409  O   HOH A1315      34.479  26.991  39.809  1.00 22.32           O  
HETATM10410  O   HOH A1316      42.808  25.698  41.036  1.00 38.70           O  
HETATM10411  O   HOH A1317      28.544  13.397  35.140  1.00 36.63           O  
HETATM10412  O   HOH A1318      18.725  43.490  55.070  1.00 19.14           O  
HETATM10413  O   HOH A1319      -4.094  22.943  46.195  1.00 21.06           O  
HETATM10414  O   HOH A1320      46.638  30.211  35.773  1.00 35.23           O  
HETATM10415  O   HOH A1321      -8.032  16.446  27.076  1.00 35.08           O  
HETATM10416  O   HOH A1322      -1.038  29.329  26.779  1.00 39.64           O  
HETATM10417  O   HOH A1323      46.541  24.489  54.809  1.00 31.83           O  
HETATM10418  O   HOH A1324      39.994  40.017  56.059  1.00 23.54           O  
HETATM10419  O   HOH A1325       2.595   3.237  55.437  1.00 32.94           O  
HETATM10420  O   HOH A1326      36.789  55.354  49.503  1.00 25.56           O  
HETATM10421  O   HOH A1327       8.450  25.677  31.490  1.00  9.73           O  
HETATM10422  O   HOH A1328      21.196   2.080  63.411  1.00 44.00           O  
HETATM10423  O   HOH A1329      59.518  25.299  53.663  1.00 19.60           O  
HETATM10424  O   HOH A1330      -3.637  28.753  37.533  1.00 20.02           O  
HETATM10425  O   HOH A1331      28.265  40.253  17.750  1.00 34.90           O  
HETATM10426  O   HOH A1332       2.945  21.144  54.345  1.00 13.64           O  
HETATM10427  O   HOH A1333      25.780   0.281  58.492  1.00 30.28           O  
HETATM10428  O   HOH A1334      31.253  18.709  23.618  1.00 39.57           O  
HETATM10429  O   HOH A1335       7.137  43.507  27.265  1.00 23.30           O  
HETATM10430  O   HOH A1336      26.828  13.292  23.628  1.00 34.46           O  
HETATM10431  O   HOH A1337      45.766  24.823  41.426  1.00 24.82           O  
HETATM10432  O   HOH A1338      11.741  -6.512  44.532  1.00 38.69           O  
HETATM10433  O   HOH A1339      38.350  31.739  49.292  1.00 22.56           O  
HETATM10434  O   HOH A1340       0.302  45.170  25.339  1.00 44.28           O  
HETATM10435  O   HOH A1341       0.046  43.309  59.736  1.00 41.64           O  
HETATM10436  O   HOH A1342      -4.762  30.600  46.165  1.00 13.55           O  
HETATM10437  O   HOH A1343      29.844   6.040  45.510  1.00 47.32           O  
HETATM10438  O   HOH A1344       3.031  29.673  26.146  1.00 24.30           O  
HETATM10439  O   HOH A1345      20.467  61.372  49.836  1.00 51.01           O  
HETATM10440  O   HOH A1346      -8.252   7.698  33.325  1.00 32.65           O  
HETATM10441  O   HOH A1347      18.337  54.149  45.927  1.00 35.67           O  
HETATM10442  O   HOH A1348      26.859  15.000  64.736  1.00 20.71           O  
HETATM10443  O   HOH A1349      55.094  45.798  37.436  1.00 47.44           O  
HETATM10444  O   HOH A1350      29.943  28.434  30.460  1.00  7.49           O  
HETATM10445  O   HOH A1351      -4.327   5.708  52.872  1.00 48.02           O  
HETATM10446  O   HOH A1352      25.530  13.751  64.375  1.00 38.78           O  
HETATM10447  O   HOH A1353       6.749  38.961  49.535  1.00 25.13           O  
HETATM10448  O   HOH A1354      30.742   9.780  36.899  1.00 51.48           O  
HETATM10449  O   HOH A1355      23.183  65.417  42.960  1.00 50.89           O  
HETATM10450  O   HOH A1356      15.469  56.910  30.803  1.00 20.33           O  
HETATM10451  O   HOH A1357      -3.350  16.710  53.206  1.00 22.13           O  
HETATM10452  O   HOH A1358      30.921  54.188  52.530  1.00 18.65           O  
HETATM10453  O   HOH A1359      -6.189  11.112  21.991  1.00 43.76           O  
HETATM10454  O   HOH A1360      -5.852  14.698  45.148  1.00 27.51           O  
HETATM10455  O   HOH A1361      40.191  37.569  55.331  1.00 21.21           O  
HETATM10456  O   HOH A1362      35.676  19.644  27.986  1.00 39.82           O  
HETATM10457  O   HOH A1363      39.808  22.254  32.713  1.00 29.28           O  
HETATM10458  O   HOH A1364      -0.066  20.102  18.212  1.00 35.77           O  
HETATM10459  O   HOH A1365      20.716  12.135  24.060  1.00 48.50           O  
HETATM10460  O   HOH A1366      34.514  38.980  21.277  1.00 21.56           O  
HETATM10461  O   HOH A1367      -4.098  47.553  34.318  1.00 45.13           O  
HETATM10462  O   HOH A1368      15.859   5.097  30.940  1.00 35.11           O  
HETATM10463  O   HOH A1369      13.730   3.312  30.985  1.00 35.02           O  
HETATM10464  O   HOH A1370      29.956  36.812  63.005  1.00 14.01           O  
HETATM10465  O   HOH A1371      17.617  26.089  23.680  1.00 18.62           O  
HETATM10466  O   HOH A1372       2.607  38.251  27.556  1.00 14.12           O  
HETATM10467  O   HOH A1373      44.664  49.706  52.097  1.00 35.54           O  
HETATM10468  O   HOH A1374      42.221  44.974  35.384  1.00 28.29           O  
HETATM10469  O   HOH A1375      23.633  55.294  20.608  1.00 39.06           O  
HETATM10470  O   HOH A1376      45.633  32.400  32.968  1.00 49.09           O  
HETATM10471  O   HOH A1377      13.554   8.334  24.742  1.00 41.38           O  
HETATM10472  O   HOH A1378      10.249  46.574  25.017  1.00 44.35           O  
HETATM10473  O   HOH A1379      10.294  35.114  47.618  1.00 10.81           O  
HETATM10474  O   HOH A1380      42.490  51.723  33.679  1.00 36.98           O  
HETATM10475  O   HOH A1381      30.788  31.835  21.615  1.00 19.70           O  
HETATM10476  O   HOH A1382       9.389  34.285  24.856  1.00 24.87           O  
HETATM10477  O   HOH A1383       5.331  36.172  52.642  1.00 15.85           O  
HETATM10478  O   HOH A1384       5.220  -3.771  40.398  1.00 39.73           O  
HETATM10479  O   HOH A1385      27.499  28.020  29.150  1.00 11.08           O  
HETATM10480  O   HOH A1386      42.774  24.003  47.789  1.00 27.71           O  
HETATM10481  O   HOH A1387      25.879  -0.498  41.754  1.00 40.39           O  
HETATM10482  O   HOH A1388      32.317  29.597  22.544  1.00 13.81           O  
HETATM10483  O   HOH A1389      -1.594   7.649  60.608  1.00 37.19           O  
HETATM10484  O   HOH A1390      10.169  20.326  18.940  1.00 34.99           O  
HETATM10485  O   HOH A1391       2.292  21.688  25.381  1.00 13.06           O  
HETATM10486  O   HOH A1392      28.644   6.782  41.820  1.00 39.63           O  
HETATM10487  O   HOH A1393      16.227  38.999  19.356  1.00 42.95           O  
HETATM10488  O   HOH A1394      33.466  16.976  26.293  1.00 45.52           O  
HETATM10489  O   HOH A1395      32.024  23.295  57.983  1.00 14.58           O  
HETATM10490  O   HOH A1396      10.242  41.729  58.871  1.00 17.76           O  
HETATM10491  O   HOH A1397      29.117  20.234  39.837  1.00 21.45           O  
HETATM10492  O   HOH A1398      11.541  57.098  36.378  1.00 31.51           O  
HETATM10493  O   HOH A1399      14.084  26.933  17.494  1.00 30.43           O  
HETATM10494  O   HOH A1400      32.458  60.914  40.262  1.00 35.36           O  
HETATM10495  O   HOH A1401      -9.469  35.525  42.409  1.00 25.74           O  
HETATM10496  O   HOH A1402      52.657  37.815  38.088  1.00 14.79           O  
HETATM10497  O   HOH A1403      -6.979  11.691  39.491  1.00 30.33           O  
HETATM10498  O   HOH A1404      26.268  17.429  17.783  1.00 45.65           O  
HETATM10499  O   HOH A1405      19.637  39.262  17.629  1.00 32.32           O  
HETATM10500  O   HOH A1406      35.605  30.996  60.272  1.00 30.28           O  
HETATM10501  O   HOH A1407      19.644  49.861  25.413  1.00 26.11           O  
HETATM10502  O   HOH A1408      47.981  43.137  34.585  1.00 23.21           O  
HETATM10503  O   HOH A1409      -2.472  30.497  27.758  1.00 43.05           O  
HETATM10504  O   HOH A1410      15.397   6.719  58.405  1.00 34.37           O  
HETATM10505  O   HOH A1411      28.100  28.005  40.146  1.00 14.64           O  
HETATM10506  O   HOH A1412      48.775  32.931  38.660  1.00 21.84           O  
HETATM10507  O   HOH A1413      16.620  28.446  23.496  1.00 28.52           O  
HETATM10508  O   HOH A1414      21.942  22.972  61.133  1.00 32.76           O  
HETATM10509  O   HOH A1415       7.858  31.738  23.141  1.00 38.83           O  
HETATM10510  O   HOH A1416      30.808  17.674  48.344  1.00 27.11           O  
HETATM10511  O   HOH A1417      31.600  55.101  50.336  1.00 25.35           O  
HETATM10512  O   HOH A1418      29.055   3.343  54.723  1.00 37.23           O  
HETATM10513  O   HOH A1419      36.742  33.889  17.334  1.00 27.31           O  
HETATM10514  O   HOH A1420      48.100  43.786  22.740  1.00 46.94           O  
HETATM10515  O   HOH A1421       8.363  41.054  25.185  1.00 23.62           O  
HETATM10516  O   HOH A1422       7.757   4.439  23.666  1.00 31.40           O  
HETATM10517  O   HOH A1423      23.905  26.800  48.984  1.00 11.46           O  
HETATM10518  O   HOH A1424      23.121  29.522  65.220  1.00 20.96           O  
HETATM10519  O   HOH A1425       7.997  22.728  16.225  1.00 34.78           O  
HETATM10520  O   HOH A1426      27.517  -0.010  47.386  1.00 35.45           O  
HETATM10521  O   HOH A1427      57.013  50.634  48.657  1.00 26.77           O  
HETATM10522  O   HOH A1428      -0.280  31.766  28.385  1.00 49.15           O  
HETATM10523  O   HOH A1429      33.847  24.985  49.823  1.00 19.97           O  
HETATM10524  O   HOH A1430      16.747  36.747  40.010  1.00 35.31           O  
HETATM10525  O   HOH A1431      39.134  22.199  29.769  1.00 29.64           O  
HETATM10526  O   HOH A1432      28.628   3.205  45.969  1.00 33.86           O  
HETATM10527  O   HOH A1433     -12.038  26.408  34.620  1.00 49.14           O  
HETATM10528  O   HOH A1434      51.304  38.927  34.571  1.00 38.76           O  
HETATM10529  O   HOH A1435      33.790  20.278  34.860  1.00 30.57           O  
HETATM10530  O   HOH A1436      23.764  11.762  22.573  1.00 37.47           O  
HETATM10531  O   HOH A1437      41.575  37.323  52.832  1.00 29.92           O  
HETATM10532  O   HOH A1438      -2.961  36.210  50.359  1.00 23.45           O  
HETATM10533  O   HOH A1439       8.581  36.937  48.044  1.00  8.51           O  
HETATM10534  O   HOH A1440      -6.162  12.854  53.185  1.00 32.77           O  
HETATM10535  O   HOH A1441      30.579  48.566  55.113  1.00 22.10           O  
HETATM10536  O   HOH A1442      35.467  29.406  37.761  1.00 19.41           O  
HETATM10537  O   HOH A1443      18.111  21.927  15.342  1.00 37.86           O  
HETATM10538  O   HOH A1444      59.302  49.338  55.090  1.00 47.52           O  
HETATM10539  O   HOH A1445       1.725  22.883  14.031  1.00 48.68           O  
HETATM10540  O   HOH A1446      19.632   3.212  33.414  1.00 26.25           O  
HETATM10541  O   HOH A1447       5.165  43.668  64.047  1.00 41.75           O  
HETATM10542  O   HOH A1448      34.607  19.739  24.999  1.00 32.49           O  
HETATM10543  O   HOH A1449      21.293  36.849  45.163  1.00 36.96           O  
HETATM10544  O   HOH A1450      22.569  -3.163  50.682  1.00 52.67           O  
HETATM10545  O   HOH A1451      18.903  -2.636  57.010  1.00 32.00           O  
HETATM10546  O   HOH A1452      31.494   3.262  51.994  1.00 43.99           O  
HETATM10547  O   HOH A1453      30.572   8.153  57.290  1.00 36.63           O  
HETATM10548  O   HOH A1454      35.290  33.911  57.908  1.00 18.97           O  
HETATM10549  O   HOH A1455      19.106  51.211  56.266  1.00 30.52           O  
HETATM10550  O   HOH A1456     -15.269  20.296  39.526  1.00 52.20           O  
HETATM10551  O   HOH A1457       6.910  36.132  22.726  1.00 47.38           O  
HETATM10552  O   HOH A1458      33.184  23.168  23.598  1.00 23.55           O  
HETATM10553  O   HOH A1459      10.188  43.286  23.291  1.00 34.81           O  
HETATM10554  O   HOH A1460      -5.009   5.521  42.836  1.00 36.94           O  
HETATM10555  O   HOH A1461      14.459  32.636  23.457  1.00 23.85           O  
HETATM10556  O   HOH A1462       8.024  45.956  52.125  1.00 39.89           O  
HETATM10557  O   HOH A1463      14.789  65.343  35.387  1.00 41.36           O  
HETATM10558  O   HOH A1464      -9.182  13.736  45.457  1.00 53.02           O  
HETATM10559  O   HOH A1465      -0.697  26.928  30.846  1.00 32.73           O  
HETATM10560  O   HOH A1466      31.027  11.782  29.619  1.00 26.26           O  
HETATM10561  O   HOH A1467     -12.371  14.663  32.920  1.00 35.84           O  
HETATM10562  O   HOH A1468      40.093  42.779  32.383  1.00 22.61           O  
HETATM10563  O   HOH A1469      46.437  55.919  50.530  1.00 43.20           O  
HETATM10564  O   HOH A1470      43.631  26.595  35.744  1.00 54.51           O  
HETATM10565  O   HOH A1471      38.138  30.499  56.800  1.00 24.53           O  
HETATM10566  O   HOH A1472      16.447  64.379  46.565  1.00 48.35           O  
HETATM10567  O   HOH A1473      12.336   0.193  52.737  1.00 16.22           O  
HETATM10568  O   HOH A1474      38.754  57.516  46.682  1.00 40.40           O  
HETATM10569  O   HOH A1475      -1.242   1.750  26.592  1.00 42.23           O  
HETATM10570  O   HOH A1476      20.832  11.960  65.620  1.00 30.67           O  
HETATM10571  O   HOH A1477      57.382  27.758  54.091  1.00 41.75           O  
HETATM10572  O   HOH A1478      55.210  29.195  55.621  1.00 36.25           O  
HETATM10573  O   HOH A1479      11.028  40.715  48.960  1.00 37.76           O  
HETATM10574  O   HOH A1480      33.997  55.379  48.965  1.00 26.75           O  
HETATM10575  O   HOH A1481       3.676  46.108  54.311  1.00 37.08           O  
HETATM10576  O   HOH A1482      12.223  49.390  41.922  1.00 24.55           O  
HETATM10577  O   HOH A1483       3.765   6.400  24.910  1.00 48.84           O  
HETATM10578  O   HOH A1484     -13.499  15.498  45.968  1.00 58.03           O  
HETATM10579  O   HOH A1485       4.154  -2.239  44.759  1.00 30.94           O  
HETATM10580  O   HOH A1486      14.421  33.831  25.980  1.00 21.05           O  
HETATM10581  O   HOH A1487      44.364  43.560  27.165  1.00 48.00           O  
HETATM10582  O   HOH A1488       4.341  48.557  33.382  1.00 26.79           O  
HETATM10583  O   HOH A1489     -14.142  21.774  38.162  1.00 33.35           O  
HETATM10584  O   HOH A1490      38.007  32.994  24.931  1.00 33.99           O  
HETATM10585  O   HOH A1491      53.793  50.699  55.533  1.00 41.31           O  
HETATM10586  O   HOH A1492      -3.222  23.363  53.689  1.00 30.26           O  
HETATM10587  O   HOH A1493       6.722  46.765  57.413  1.00 52.41           O  
HETATM10588  O   HOH A1494      20.471  37.081  19.592  1.00 14.32           O  
HETATM10589  O   HOH A1495      13.508  -5.395  51.561  1.00 45.89           O  
HETATM10590  O   HOH A1496      15.672  19.573  15.992  1.00 41.25           O  
HETATM10591  O   HOH A1497      17.719  34.800  41.597  1.00 35.75           O  
HETATM10592  O   HOH A1498      37.768  28.641  18.684  1.00 45.60           O  
HETATM10593  O   HOH A1499      -3.696  17.003  23.112  1.00 44.93           O  
HETATM10594  O   HOH A1500      18.461  33.907  43.832  1.00 16.98           O  
HETATM10595  O   HOH A1501       5.164  24.202  15.713  1.00 31.51           O  
HETATM10596  O   HOH A1502       1.666  25.454  52.373  1.00 14.90           O  
HETATM10597  O   HOH A1503      -2.886  29.519  50.075  1.00 18.68           O  
HETATM10598  O   HOH A1504      34.517  23.403  53.430  1.00 40.10           O  
HETATM10599  O   HOH A1505      49.834  44.268  55.523  1.00 36.50           O  
HETATM10600  O   HOH A1506      37.921  21.429  23.767  1.00 32.22           O  
HETATM10601  O   HOH A1507      16.189  12.395  26.412  1.00 29.95           O  
HETATM10602  O   HOH A1508       2.100  32.873  26.585  1.00 34.91           O  
HETATM10603  O   HOH A1509      19.998  67.910  29.008  1.00 50.75           O  
HETATM10604  O   HOH A1510      17.732  46.812  44.767  1.00 39.24           O  
HETATM10605  O   HOH A1511      24.953  -1.403  48.949  1.00 28.59           O  
HETATM10606  O   HOH A1512      29.551  -0.238  49.215  1.00 44.47           O  
HETATM10607  O   HOH A1513      11.741  40.985  53.952  1.00 37.25           O  
HETATM10608  O   HOH A1514      -5.920   3.087  26.218  1.00 38.54           O  
HETATM10609  O   HOH A1515      -5.370  20.582  42.523  1.00 18.97           O  
HETATM10610  O   HOH A1516      25.494  41.972  56.179  1.00 34.02           O  
HETATM10611  O   HOH A1517      15.941  39.759  56.296  1.00 33.94           O  
HETATM10612  O   HOH A1518      28.677  57.550  52.902  1.00 32.02           O  
HETATM10613  O   HOH A1519      16.305  38.784  44.831  1.00 23.25           O  
HETATM10614  O   HOH A1520      36.581  56.655  41.006  1.00 45.65           O  
HETATM10615  O   HOH A1521      37.044  30.918  37.991  1.00 41.58           O  
HETATM10616  O   HOH A1522      41.986  40.467  58.370  1.00 39.96           O  
HETATM10617  O   HOH A1523      33.754  33.302  14.890  1.00 37.06           O  
HETATM10618  O   HOH A1524     -13.735  18.039  37.648  1.00 34.88           O  
HETATM10619  O   HOH A1525       4.054  36.614  26.758  1.00 19.70           O  
HETATM10620  O   HOH A1526      47.599  25.948  39.498  1.00 36.08           O  
HETATM10621  O   HOH A1527      54.253  40.241  51.704  1.00 26.00           O  
HETATM10622  O   HOH A1528      -5.614  17.573  52.222  1.00 41.35           O  
HETATM10623  O   HOH A1529      13.827  14.381  64.831  1.00 44.18           O  
HETATM10624  O   HOH A1530      -1.318  -0.573  48.816  1.00 34.91           O  
HETATM10625  O   HOH A1531      21.304   3.977  28.187  1.00 46.57           O  
HETATM10626  O   HOH A1532      30.639  17.059  37.770  1.00 50.05           O  
HETATM10627  O   HOH A1533      22.605   0.822  39.278  1.00 30.54           O  
HETATM10628  O   HOH A1534      24.904  53.554  18.946  1.00 55.08           O  
HETATM10629  O   HOH A1535      26.570  53.981  20.219  1.00 44.38           O  
HETATM10630  O   HOH A1536      13.807  20.882  15.716  1.00 38.21           O  
HETATM10631  O   HOH A1537      29.570  14.512  37.986  1.00 54.74           O  
HETATM10632  O   HOH A1538      35.825  23.812  46.043  1.00 47.36           O  
HETATM10633  O   HOH A1539      -6.119  36.841  29.213  1.00 45.94           O  
HETATM10634  O   HOH A1540      31.653  40.569  42.146  1.00 13.15           O  
HETATM10635  O   HOH A1541       1.822  47.932  48.782  1.00 45.81           O  
HETATM10636  O   HOH A1542      37.523  53.761  30.212  1.00 49.13           O  
HETATM10637  O   HOH A1543      -5.804   8.652  37.808  1.00 31.85           O  
HETATM10638  O   HOH A1544      29.934  57.040  50.233  1.00 31.40           O  
HETATM10639  O   HOH A1545      22.881  35.336  52.091  1.00 29.28           O  
HETATM10640  O   HOH A1546      26.938  27.637  18.128  1.00 33.36           O  
HETATM10641  O   HOH A1547      33.650  16.926  55.918  1.00 32.14           O  
HETATM10642  O   HOH A1548      -7.016   5.141  49.311  1.00 61.48           O  
HETATM10643  O   HOH A1549      26.134  10.931  64.010  1.00 38.79           O  
HETATM10644  O   HOH A1550      26.739   9.015  34.377  1.00 39.52           O  
HETATM10645  O   HOH A1551     -11.513  23.984  30.210  1.00 50.13           O  
HETATM10646  O   HOH A1552       0.158  36.170  52.641  1.00 34.31           O  
HETATM10647  O   HOH A1553      21.740  29.897  26.261  1.00 15.82           O  
HETATM10648  O   HOH A1554       1.810  34.797  26.872  1.00 54.72           O  
HETATM10649  O   HOH A1555      -7.459  11.154  55.831  1.00 59.59           O  
HETATM10650  O   HOH A1556      17.920  -4.015  51.655  1.00 45.12           O  
HETATM10651  O   HOH A1557      43.931  38.451  52.828  1.00 28.22           O  
HETATM10652  O   HOH A1558      36.571  30.209  40.583  1.00 11.76           O  
HETATM10653  O   HOH A1559      52.652  39.241  43.014  1.00 43.73           O  
HETATM10654  O   HOH A1560      34.687  23.092  48.386  1.00 36.51           O  
HETATM10655  O   HOH A1561      43.503  49.959  59.066  1.00 45.90           O  
HETATM10656  O   HOH A1562      16.394  -2.553  54.599  1.00 41.79           O  
HETATM10657  O   HOH A1563      18.935  15.196  20.194  1.00 42.30           O  
HETATM10658  O   HOH A1564      11.164  54.453  36.672  1.00 32.10           O  
HETATM10659  O   HOH A1565      42.117  45.173  26.566  1.00 30.24           O  
HETATM10660  O   HOH A1566       4.380   3.696  57.458  1.00 41.59           O  
HETATM10661  O   HOH A1567      27.025  32.607  52.322  1.00 29.41           O  
HETATM10662  O   HOH A1568      45.787  44.985  34.821  1.00 28.01           O  
HETATM10663  O   HOH A1569      37.236  26.481  45.947  1.00 36.86           O  
HETATM10664  O   HOH A1570      32.668   5.137  56.724  1.00 47.67           O  
HETATM10665  O   HOH A1571      43.921  26.215  54.074  1.00 25.08           O  
HETATM10666  O   HOH A1572       8.776  40.750  50.243  1.00 19.47           O  
HETATM10667  O   HOH A1573     -10.227  11.944  27.722  1.00 44.01           O  
HETATM10668  O   HOH A1574      32.061   1.571  51.331  1.00 45.23           O  
HETATM10669  O   HOH A1575      41.617  56.879  46.058  1.00 45.78           O  
HETATM10670  O   HOH A1576      24.266   9.995  53.954  1.00 20.23           O  
HETATM10671  O   HOH A1577      -0.379  38.454  59.428  1.00 43.79           O  
HETATM10672  O   HOH A1578      20.096  21.085  15.099  1.00 46.92           O  
HETATM10673  O   HOH A1579      29.424  53.272  60.392  1.00 43.09           O  
HETATM10674  O   HOH A1580      -1.323  33.976  29.142  1.00 40.87           O  
HETATM10675  O   HOH A1581      46.915  36.213  32.609  1.00 45.06           O  
HETATM10676  O   HOH A1582      57.729  47.142  46.098  1.00 44.74           O  
HETATM10677  O   HOH A1583      36.818  21.098  29.036  1.00 43.26           O  
HETATM10678  O   HOH A1584      -1.466  28.016  53.505  1.00 16.09           O  
HETATM10679  O   HOH A1585     -14.799  27.169  39.323  1.00 39.42           O  
HETATM10680  O   HOH A1586      30.946   4.936  54.198  1.00 33.55           O  
HETATM10681  O   HOH A1587      53.323  42.020  53.053  1.00 36.36           O  
HETATM10682  O   HOH A1588      48.688  50.714  38.181  1.00 40.55           O  
HETATM10683  O   HOH A1589      30.624  56.185  22.956  1.00 37.45           O  
HETATM10684  O   HOH A1590      15.069  30.853  22.254  1.00 48.75           O  
HETATM10685  O   HOH A1591      11.999  28.910  23.105  1.00 42.36           O  
HETATM10686  O   HOH A1592     -14.276  29.055  37.559  1.00 42.40           O  
HETATM10687  O   HOH A1593      -1.594   1.274  33.391  1.00 42.02           O  
HETATM10688  O   HOH A1594       5.164  -2.700  51.516  1.00 46.94           O  
HETATM10689  O   HOH A1595      -5.632  32.455  48.126  1.00 14.55           O  
HETATM10690  O   HOH A1596      18.196  70.682  39.342  1.00 41.50           O  
HETATM10691  O   HOH A1597      10.343  -0.399  59.778  1.00 41.38           O  
HETATM10692  O   HOH A1598      -9.398  29.511  31.083  1.00 43.67           O  
HETATM10693  O   HOH A1599      -1.491  -2.973  41.778  1.00 41.37           O  
HETATM10694  O   HOH A1600      46.037  22.127  44.039  1.00 45.18           O  
HETATM10695  O   HOH A1601      22.395  19.600  15.922  1.00 34.35           O  
HETATM10696  O   HOH A1602      -2.316  31.234  38.679  1.00 15.13           O  
HETATM10697  O   HOH A1603      40.506  49.981  32.965  1.00 38.32           O  
HETATM10698  O   HOH A1604      31.005  35.869  43.984  1.00 10.81           O  
HETATM10699  O   HOH A1605      60.112  28.851  50.058  1.00 17.49           O  
HETATM10700  O   HOH A1606      18.062  17.421  19.275  1.00 47.70           O  
HETATM10701  O   HOH A1607      15.653  60.292  40.744  1.00 39.38           O  
HETATM10702  O   HOH A1608      32.666  32.220  63.593  1.00 38.71           O  
HETATM10703  O   HOH A1609       9.458   2.967  22.373  1.00 45.03           O  
HETATM10704  O   HOH A1610      29.307   8.689  61.725  1.00 51.68           O  
HETATM10705  O   HOH A1611      10.110  30.934  24.030  1.00 38.72           O  
HETATM10706  O   HOH A1612      26.012   3.079  64.202  1.00 36.75           O  
HETATM10707  O   HOH A1613      27.286  58.373  22.417  1.00 54.62           O  
HETATM10708  O   HOH A1614      14.597  57.669  27.899  1.00 43.81           O  
HETATM10709  O   HOH A1615      -3.275   0.790  38.750  1.00 45.79           O  
HETATM10710  O   HOH A1616      17.446  46.450  12.502  1.00 36.67           O  
HETATM10711  O   HOH A1617      -6.137   9.079  29.926  1.00 47.09           O  
HETATM10712  O   HOH A1618      12.026   2.522  55.439  1.00 51.86           O  
HETATM10713  O   HOH A1619      36.991  34.797  21.975  1.00 27.05           O  
HETATM10714  O   HOH A1620      26.373  41.592  17.688  1.00 48.52           O  
HETATM10715  O   HOH A1621      15.401  56.673  46.352  1.00 66.28           O  
HETATM10716  O   HOH A1622      -4.037  -1.591  43.067  1.00 46.03           O  
HETATM10717  O   HOH A1623      61.248  48.299  53.022  1.00 44.23           O  
HETATM10718  O   HOH A1624      56.009  31.247  55.714  1.00 52.37           O  
HETATM10719  O   HOH A1625      28.281  54.791  61.417  1.00 36.38           O  
HETATM10720  O   HOH A1626      11.919  43.231  48.393  1.00 34.58           O  
HETATM10721  O   HOH A1627      -4.560   7.221  41.474  1.00 45.63           O  
HETATM10722  O   HOH A1628      12.667  16.346  64.308  1.00 30.72           O  
HETATM10723  O   HOH A1629      26.292  56.464  20.994  1.00 38.26           O  
HETATM10724  O   HOH A1630      12.307  39.334  48.017  1.00 38.14           O  
HETATM10725  O   HOH A1631      29.973  26.203  39.226  1.00 18.90           O  
HETATM10726  O   HOH A1632      23.920   5.512  31.961  1.00 40.64           O  
HETATM10727  O   HOH A1633      42.488  49.063  32.454  1.00 46.59           O  
HETATM10728  O   HOH A1634       0.366   3.606  55.728  1.00 38.99           O  
HETATM10729  O   HOH A1635      47.293  42.570  55.579  1.00 33.96           O  
HETATM10730  O   HOH A1636      -7.652  12.623  63.652  1.00 44.15           O  
HETATM10731  O   HOH A1637       0.947  36.768  56.738  1.00 33.47           O  
HETATM10732  O   HOH A1638      50.537  51.844  40.381  1.00 56.10           O  
HETATM10733  O   HOH A1639      11.369  26.410  16.122  1.00 39.99           O  
HETATM10734  O   HOH A1640      32.908  16.151  31.977  1.00 52.59           O  
HETATM10735  O   HOH A1641      -4.576   7.630  31.645  1.00 32.37           O  
HETATM10736  O   HOH A1642      58.000  18.603  46.737  1.00 33.93           O  
HETATM10737  O   HOH A1643      24.769  62.194  48.756  1.00 43.71           O  
HETATM10738  O   HOH A1644      17.949  19.098  16.963  1.00 48.86           O  
HETATM10739  O   HOH A1645      37.301  33.805  57.524  1.00 30.93           O  
HETATM10740  O   HOH A1646      42.034  26.294  56.329  1.00 39.25           O  
HETATM10741  O   HOH A1647      31.793  58.946  49.722  1.00 41.03           O  
HETATM10742  O   HOH A1648      -0.908   0.353  54.609  1.00 46.35           O  
HETATM10743  O   HOH A1649      14.241  53.776  40.096  1.00 34.77           O  
HETATM10744  O   HOH A1650       6.287  52.125  29.164  1.00 47.01           O  
HETATM10745  O   HOH A1651      -7.555  36.790  31.138  1.00 41.51           O  
HETATM10746  O   HOH A1652      54.465  37.590  44.212  1.00 32.06           O  
HETATM10747  O   HOH A1653      49.166  49.251  54.691  1.00 50.01           O  
HETATM10748  O   HOH A1654      55.317  37.539  39.350  1.00 48.67           O  
HETATM10749  O   HOH A1655      -2.181  43.325  39.035  1.00 39.60           O  
HETATM10750  O   HOH A1656       6.707   3.233  29.442  1.00 48.21           O  
HETATM10751  O   HOH A1657      40.137  30.242  19.179  1.00 42.12           O  
HETATM10752  O   HOH A1658       6.471  50.886  37.714  1.00 32.60           O  
HETATM10753  O   HOH A1659      24.494  -2.004  60.247  1.00 45.47           O  
HETATM10754  O   HOH A1660      15.473  10.824  25.355  1.00 38.69           O  
HETATM10755  O   HOH A1661      -7.212  16.657  55.024  1.00 42.59           O  
HETATM10756  O   HOH A1662      -6.592  33.218  31.070  1.00 45.45           O  
HETATM10757  O   HOH A1663      54.617  35.725  36.920  1.00 44.04           O  
HETATM10758  O   HOH A1664      46.353  51.232  36.257  1.00 49.35           O  
HETATM10759  O   HOH A1665      14.165  -2.050  52.745  1.00 29.58           O  
HETATM10760  O   HOH A1666      16.745  15.870  58.040  1.00 14.20           O  
HETATM10761  O   HOH A1667       9.932  52.331  34.874  1.00 33.55           O  
HETATM10762  O   HOH A1668       3.966   5.468  26.802  1.00 30.02           O  
HETATM10763  O   HOH A1669      10.666  -0.768  54.766  1.00 29.36           O  
HETATM10764  O   HOH A1670      14.585  45.856  13.310  1.00 51.99           O  
HETATM10765  O   HOH A1671      57.636  29.440  52.797  1.00 30.06           O  
HETATM10766  O   HOH A1672      46.201  34.287  34.990  1.00 31.12           O  
HETATM10767  O   HOH A1673      17.315  49.525  26.664  1.00 31.71           O  
HETATM10768  O   HOH A1674      10.005  44.368  51.794  1.00 43.85           O  
HETATM10769  O   HOH A1675      55.947  43.275  40.567  1.00 42.72           O  
HETATM10770  O   HOH A1676      25.693  10.888  22.794  1.00 35.32           O  
HETATM10771  O   HOH A1677      14.767  44.244  44.910  1.00 40.85           O  
HETATM10772  O   HOH A1678      37.309  28.403  39.786  1.00 36.27           O  
HETATM10773  O   HOH A1679      14.571  47.655  41.802  1.00 26.28           O  
HETATM10774  O   HOH A1680      34.352  32.463  61.986  1.00 32.12           O  
HETATM10775  O   HOH A1681      42.268  24.963  36.912  1.00 50.21           O  
HETATM10776  O   HOH A1682       5.098  37.424  24.506  1.00 33.81           O  
HETATM10777  O   HOH A1683      14.349  41.483  56.101  1.00 28.92           O  
HETATM10778  O   HOH A1684       3.449  40.828  26.477  1.00 25.36           O  
HETATM10779  O   HOH A1685      -9.565   1.758  49.598  1.00 49.85           O  
HETATM10780  O   HOH A1686      -5.890  11.794  48.917  1.00 37.73           O  
HETATM10781  O   HOH A1687      34.558  54.259  39.158  1.00 31.61           O  
HETATM10782  O   HOH A1688      57.737  39.277  46.101  1.00 38.38           O  
HETATM10783  O   HOH A1689      20.895  39.832  53.719  1.00 38.61           O  
HETATM10784  O   HOH A1690      42.691  50.628  26.217  1.00 43.71           O  
HETATM10785  O   HOH A1691      32.392  50.718  58.940  1.00 37.43           O  
HETATM10786  O   HOH A1692       3.131  37.292  53.179  1.00 22.98           O  
HETATM10787  O   HOH A1693      29.821   9.108  59.479  1.00 50.21           O  
HETATM10788  O   HOH A1694      16.359  54.535  44.310  1.00 33.82           O  
HETATM10789  O   HOH A1695      44.385  46.907  25.289  1.00 43.85           O  
HETATM10790  O   HOH A1696      24.169  36.536  61.948  1.00 34.74           O  
HETATM10791  O   HOH A1697      14.527  52.308  44.264  1.00 31.30           O  
HETATM10792  O   HOH A1698      16.145  70.234  39.891  1.00 48.04           O  
HETATM10793  O   HOH A1699      23.431  35.712  57.070  1.00 31.86           O  
HETATM10794  O   HOH A1700      41.879  53.454  27.041  1.00 47.55           O  
HETATM10795  O   HOH A1701      32.259  11.609  50.305  1.00 53.86           O  
HETATM10796  O   HOH A1702      20.809  63.788  43.252  1.00 41.50           O  
HETATM10797  O   HOH A1703     -13.966  19.728  48.781  1.00 34.44           O  
HETATM10798  O   HOH A1704      16.501  35.793  44.355  1.00 39.30           O  
HETATM10799  O   HOH A1705      32.461  29.269  17.781  1.00 28.09           O  
HETATM10800  O   HOH A1706      38.284  28.096  56.886  1.00 30.43           O  
HETATM10801  O   HOH A1707      20.321  63.354  46.239  1.00 51.33           O  
HETATM10802  O   HOH A1708      36.973  22.840  33.858  1.00 34.67           O  
HETATM10803  O   HOH A1709      -1.477  27.563  22.379  1.00 37.23           O  
HETATM10804  O   HOH A1710      10.311  24.378  15.492  1.00 37.77           O  
HETATM10805  O   HOH A1711       4.503  48.036  38.760  1.00 41.85           O  
HETATM10806  O   HOH A1712      57.784  31.456  53.603  1.00 39.10           O  
HETATM10807  O   HOH A1713      31.729  14.499  32.646  1.00 48.59           O  
HETATM10808  O   HOH A1714      17.668  67.731  28.352  1.00 43.76           O  
HETATM10809  O   HOH A1715      14.611  40.895  46.691  1.00 47.72           O  
HETATM10810  O   HOH A1716      36.977  58.326  48.102  1.00 47.62           O  
HETATM10811  O   HOH A1717      -6.967  23.972  41.564  1.00 13.68           O  
HETATM10812  O   HOH A1718      -6.220  35.976  40.224  1.00 45.12           O  
HETATM10813  O   HOH A1719      27.645  69.052  36.994  1.00 57.51           O  
HETATM10814  O   HOH A1720       6.736  -4.553  50.689  1.00 44.42           O  
HETATM10815  O   HOH A1721      -3.880  18.695  25.745  1.00 32.42           O  
HETATM10816  O   HOH A1722       7.402  45.501  25.860  1.00 34.59           O  
HETATM10817  O   HOH A1723      36.996  37.565  20.657  1.00 18.46           O  
HETATM10818  O   HOH A1724      49.769  38.908  29.818  1.00 50.96           O  
HETATM10819  O   HOH A1725      18.120  31.241  16.758  1.00 34.16           O  
HETATM10820  O   HOH A1726      33.225  20.637  23.097  1.00 41.98           O  
HETATM10821  O   HOH A1727      16.505  -3.287  36.954  1.00 41.33           O  
HETATM10822  O   HOH A1728      41.199  21.903  23.987  1.00 37.38           O  
HETATM10823  O   HOH A1729      -8.413  11.276  23.228  1.00 51.04           O  
HETATM10824  O   HOH A1730     -16.300  16.267  41.720  1.00 47.54           O  
HETATM10825  O   HOH A1731      -4.309  33.193  50.260  1.00 30.96           O  
HETATM10826  O   HOH A1732      32.143  28.710  61.568  1.00 25.15           O  
HETATM10827  O   HOH A1733      59.129  42.060  45.571  1.00 35.21           O  
HETATM10828  O   HOH A1734      -8.790  45.844  35.309  1.00 49.16           O  
HETATM10829  O   HOH A1735      57.798  44.159  44.228  1.00 47.21           O  
HETATM10830  O   HOH A1736      31.522   1.040  48.135  1.00 63.37           O  
HETATM10831  O   HOH A1737      47.340  46.030  32.986  1.00 44.69           O  
HETATM10832  O   HOH A1738      33.543  51.581  55.464  1.00 34.97           O  
HETATM10833  O   HOH A1739      15.450   6.929  26.039  1.00 45.15           O  
HETATM10834  O   HOH A1740      35.759  34.589  60.971  1.00 45.87           O  
HETATM10835  O   HOH A1741      -2.063   2.321  55.605  1.00 43.79           O  
HETATM10836  O   HOH A1742      -2.505  31.909  52.217  1.00 21.08           O  
HETATM10837  O   HOH A1743      25.034  26.704  14.484  1.00 42.92           O  
HETATM10838  O   HOH A1744      42.995  36.744  18.508  1.00 43.94           O  
HETATM10839  O   HOH A1745      -7.238  10.078  43.924  1.00 36.01           O  
HETATM10840  O   HOH A1746      42.563  46.765  31.029  1.00 41.69           O  
HETATM10841  O   HOH A1747      -3.321  -1.604  40.862  1.00 43.39           O  
HETATM10842  O   HOH A1748      39.016  25.504  18.327  1.00 59.18           O  
HETATM10843  O   HOH A1749      10.890  -6.468  52.523  1.00 59.31           O  
HETATM10844  O   HOH A1750      11.342  -0.072  61.588  1.00 49.65           O  
HETATM10845  O   HOH A1751      39.658  37.873  20.367  1.00 30.69           O  
HETATM10846  O   HOH A1752      12.889  52.008  41.743  1.00 33.60           O  
HETATM10847  O   HOH A1753      49.937  52.138  42.541  1.00 50.26           O  
HETATM10848  O   HOH A1754      29.071  10.887  34.203  1.00 28.16           O  
HETATM10849  O   HOH A1755      56.010  52.947  48.175  1.00 51.14           O  
HETATM10850  O   HOH A1756      21.473  38.959  45.564  1.00 41.24           O  
HETATM10851  O   HOH A1757      35.066  23.871  21.876  1.00 22.09           O  
HETATM10852  O   HOH A1758      -6.662  13.859  47.366  1.00 53.20           O  
HETATM10853  O   HOH A1759      18.332  27.705  14.280  1.00 47.06           O  
HETATM10854  O   HOH A1760      48.711  37.462  32.353  1.00 61.75           O  
HETATM10855  O   HOH A1761      31.931   7.417  47.869  1.00 45.10           O  
HETATM10856  O   HOH A1762      31.603  20.852  39.985  1.00 29.30           O  
HETATM10857  O   HOH A1763      28.697  28.572  18.863  1.00 28.17           O  
HETATM10858  O   HOH A1764      33.025  27.956  20.264  1.00 23.60           O  
HETATM10859  O   HOH A1765      35.390  18.809  33.637  1.00 41.44           O  
HETATM10860  O   HOH A1766      18.822  38.741  46.161  1.00 38.92           O  
HETATM10861  O   HOH A1767      25.017  11.235  66.814  1.00 42.47           O  
HETATM10862  O   HOH A1768       3.210   4.229  28.454  1.00 37.72           O  
HETATM10863  O   HOH A1769      -7.774  11.251  52.924  1.00 38.18           O  
HETATM10864  O   HOH A1770      14.335  28.060  21.982  1.00 32.28           O  
HETATM10865  O   HOH A1771      11.267  41.725  20.694  1.00 45.91           O  
HETATM10866  O   HOH A1772      30.799   3.322  46.757  1.00 47.46           O  
HETATM10867  O   HOH A1773       5.816  27.052  15.032  1.00 45.26           O  
HETATM10868  O   HOH A1774      -4.550  40.247  41.888  1.00 29.85           O  
HETATM10869  O   HOH A1775      39.924  23.409  48.086  1.00 38.05           O  
HETATM10870  O   HOH A1776      31.948  13.226  38.612  1.00 47.78           O  
HETATM10871  O   HOH A1777      20.629  39.538  43.596  1.00 38.53           O  
HETATM10872  O   HOH A1778      34.103  29.734  61.483  1.00 35.53           O  
HETATM10873  O   HOH A1779      18.497   8.213  25.995  1.00 48.07           O  
HETATM10874  O   HOH A1780      38.184  54.804  52.354  1.00 38.93           O  
HETATM10875  O   HOH A1781      20.007  35.189  18.049  1.00 40.51           O  
HETATM10876  O   HOH A1782      11.708  28.020  17.878  1.00 46.40           O  
HETATM10877  O   HOH A1783     -13.177  13.607  37.225  1.00 48.34           O  
HETATM10878  O   HOH A1784      30.760  26.113  20.668  1.00 38.92           O  
HETATM10879  O   HOH A1785      30.233  29.287  16.384  1.00 42.68           O  
HETATM10880  O   HOH A1786       1.971  -3.285  51.720  1.00 41.73           O  
HETATM10881  O   HOH A1787      31.769  15.628  49.808  1.00 43.65           O  
HETATM10882  O   HOH A1788      26.522  11.520  54.245  1.00 32.28           O  
HETATM10883  O   HOH A1789      24.426  40.055  57.030  1.00 42.83           O  
HETATM10884  O   HOH A1790      27.121   6.683  36.081  1.00 35.62           O  
HETATM10885  O   HOH A1791      38.719  26.120  40.977  1.00 31.14           O  
HETATM10886  O   HOH A1792      28.377  13.653  53.487  1.00 42.81           O  
HETATM10887  O   HOH A1793       0.541  -2.715  49.011  1.00 41.26           O  
HETATM10888  O   HOH A1794      46.946  22.312  52.653  1.00 45.23           O  
HETATM10889  O   HOH A1795      43.218  48.762  25.689  1.00 42.96           O  
HETATM10890  O   HOH A1796      -6.652  11.721  44.926  1.00 43.43           O  
HETATM10891  O   HOH A1797      39.091  55.482  31.720  1.00 44.52           O  
HETATM10892  O   HOH A1798       2.352  45.929  38.409  1.00 42.71           O  
HETATM10893  O   HOH A1799      38.583  24.971  50.264  1.00 27.70           O  
HETATM10894  O   HOH A1800      30.281   6.244  63.375  1.00 47.69           O  
HETATM10895  O   HOH A1801     -14.610  32.929  34.885  1.00 35.06           O  
HETATM10896  O   HOH A1802      32.923  48.431  57.099  1.00 30.13           O  
HETATM10897  O   HOH A1803      56.004  41.003  42.228  1.00 43.69           O  
HETATM10898  O   HOH A1804      52.386  37.188  33.644  1.00 43.77           O  
HETATM10899  O   HOH A1805     -13.077  20.626  36.334  1.00 24.76           O  
HETATM10900  O   HOH A1806      22.063  10.089  24.070  1.00 52.32           O  
HETATM10901  O   HOH A1807      47.713  32.323  35.863  1.00 38.14           O  
HETATM10902  O   HOH A1808       8.007  34.841  20.405  1.00 57.03           O  
HETATM10903  O   HOH A1809     -11.385  11.150  37.529  1.00 36.80           O  
HETATM10904  O   HOH A1810      12.784  55.307  40.463  1.00 49.87           O  
HETATM10905  O   HOH A1811       4.563  49.353  41.083  1.00 50.97           O  
HETATM10906  O   HOH A1812      -7.392  15.663  53.378  1.00 36.25           O  
HETATM10907  O   HOH A1813      -4.725  35.953  38.015  1.00 45.84           O  
HETATM10908  O   HOH A1814      50.998  42.175  55.383  1.00 43.51           O  
HETATM10909  O   HOH A1815      15.521  36.181  46.803  1.00 26.38           O  
HETATM10910  O   HOH A1816      11.605  32.861  25.035  1.00 31.48           O  
HETATM10911  O   HOH A1817      23.719  43.778  16.851  1.00 27.44           O  
HETATM10912  O   HOH A1818      -4.131  22.214  23.064  1.00 45.67           O  
HETATM10913  O   HOH A1819       4.167  21.641  13.394  1.00 48.24           O  
HETATM10914  O   HOH A1820      -6.526  18.476  27.634  1.00 37.20           O  
HETATM10915  O   HOH A1821      29.744   9.340  31.034  1.00 47.30           O  
HETATM10916  O   HOH A1822       9.809  40.149  22.809  1.00 41.61           O  
HETATM10917  O   HOH A1823     -13.214  15.834  35.007  1.00 48.72           O  
HETATM10918  O   HOH A1824      16.483  -5.591  36.796  1.00 50.84           O  
HETATM10919  O   HOH A1825      31.168  14.893  52.971  1.00 39.87           O  
HETATM10920  O   HOH A1826      29.833  17.085  22.270  1.00 46.72           O  
HETATM10921  O   HOH A1827       5.871  39.474  24.801  1.00 41.91           O  
HETATM10922  O   HOH A1828      -1.111  40.842  60.293  1.00 45.84           O  
HETATM10923  O   HOH A1829      35.562  26.758  17.062  1.00 47.38           O  
HETATM10924  O   HOH A1830      -6.273   8.919  48.609  1.00 55.10           O  
HETATM10925  O   HOH A1831      38.972  38.009  59.942  1.00 29.41           O  
HETATM10926  O   HOH A1832      36.703  24.571  17.775  1.00 41.02           O  
HETATM10927  O   HOH A1833      22.415  30.599  15.226  1.00 28.85           O  
HETATM10928  O   HOH A1834       6.949  52.585  39.532  1.00 43.59           O  
HETATM10929  O   HOH A1835     -12.801  13.539  27.923  1.00 48.99           O  
HETATM10930  O   HOH A1836      40.488  51.494  54.326  1.00 44.80           O  
HETATM10931  O   HOH A1837      42.519  42.820  60.353  1.00 44.70           O  
HETATM10932  O   HOH A1838      -2.128  47.292  46.676  1.00 42.28           O  
HETATM10933  O   HOH A1839      33.056   9.084  49.068  1.00 43.92           O  
HETATM10934  O   HOH A1840      32.057  20.853  19.656  1.00 54.03           O  
HETATM10935  O   HOH A1841      48.106  26.470  61.517  1.00 38.09           O  
HETATM10936  O   HOH A1842      38.200  50.135  55.269  1.00 42.75           O  
HETATM10937  O   HOH A1843      14.033  28.731  19.157  1.00 51.43           O  
HETATM10938  O   HOH A1844      36.261  24.196  51.806  1.00 42.28           O  
HETATM10939  O   HOH A1845      18.313  38.003  15.724  1.00 39.41           O  
HETATM10940  O   HOH A1846      -0.155  21.643  12.681  1.00 55.44           O  
HETATM10941  O   HOH A1847      61.423  49.456  50.640  1.00 37.06           O  
HETATM10942  O   HOH A1848      37.300  23.887  47.528  1.00 49.75           O  
HETATM10943  O   HOH A1849      10.344  28.485  19.534  1.00 34.53           O  
HETATM10944  O   HOH A1850      25.720  36.780  15.754  1.00 43.98           O  
HETATM10945  O   HOH A1851       2.656  47.098  35.135  1.00 43.44           O  
HETATM10946  O   HOH A1852      39.296  33.474  60.643  1.00 48.29           O  
HETATM10947  O   HOH A1853     -18.188  17.339  42.590  1.00 55.19           O  
HETATM10948  O   HOH A1854      -8.727   9.201  61.704  1.00 41.71           O  
HETATM10949  O   HOH A1855      39.165  33.716  18.127  1.00 41.12           O  
HETATM10950  O   HOH A1856      33.260   5.037  52.088  1.00 43.09           O  
HETATM10951  O   HOH A1857      -7.166   6.813  57.703  1.00 45.76           O  
HETATM10952  O   HOH A1858      -9.545   5.483  51.226  1.00 44.35           O  
HETATM10953  O   HOH A1859     -17.084  23.255  35.770  1.00 43.43           O  
HETATM10954  O   HOH A1860      -6.532  36.345  36.293  1.00 47.54           O  
HETATM10955  O   HOH A1861      15.418  28.737  15.550  1.00 47.44           O  
HETATM10956  O   HOH A1862      33.106   6.509  60.958  1.00 45.15           O  
HETATM10957  O   HOH A1863       5.928  -1.480  54.515  1.00 42.25           O  
HETATM10958  O   HOH A1864      50.635  35.047  32.755  1.00 47.12           O  
HETATM10959  O   HOH A1865      24.550  29.571  14.805  1.00 30.80           O  
HETATM10960  O   HOH A1866      60.936  49.834  47.479  1.00 53.40           O  
HETATM10961  O   HOH A1867      32.180   5.258  62.622  1.00 49.95           O  
HETATM10962  O   HOH A1868      23.354  32.902  14.517  1.00 45.68           O  
HETATM10963  O   HOH A1869     -13.927  18.844  30.862  1.00 38.89           O  
HETATM10964  O   HOH A1870      27.148   4.405  34.618  1.00 53.65           O  
HETATM10965  O   HOH A1871      -7.869  36.533  34.112  1.00 39.43           O  
HETATM10966  O   HOH A1872      33.820   4.948  50.243  1.00 44.25           O  
HETATM10967  O   HOH A1873      17.598  43.788  11.707  1.00 40.38           O  
HETATM10968  O   HOH A1874     -10.771  -0.860  49.569  1.00 53.79           O  
HETATM10969  O   HOH A1875      -8.618  25.960  24.625  1.00 48.09           O  
HETATM10970  O   HOH A1876      54.061  35.648  33.824  1.00 40.20           O  
HETATM10971  O   HOH A1877      40.770  34.475  61.942  1.00 50.37           O  
HETATM10972  O   HOH A1878      40.605  56.310  29.816  1.00 46.57           O  
HETATM10973  O   HOH A1879       1.422  22.354  10.045  1.00 45.49           O  
HETATM10974  O   HOH A1880      39.690  54.483  56.279  1.00 58.41           O  
HETATM10975  O   HOH A1881      -7.827   7.789  59.507  1.00 56.69           O  
HETATM10976  O   HOH A1882      37.221  54.644  54.839  1.00 38.08           O  
HETATM10977  O   HOH A1883      31.241  10.197  22.808  1.00 48.15           O  
HETATM10978  O   HOH A1884      -6.967  27.475  23.587  1.00 48.00           O  
HETATM10979  O   HOH A1885      32.868   9.648  24.266  1.00 47.49           O  
HETATM10980  O   HOH A1886     -15.696  22.681  33.058  1.00 39.01           O  
HETATM10981  O   HOH A1887     -14.463  21.387  30.328  1.00 50.02           O  
HETATM10982  O   HOH A1888      33.023   9.101  62.470  1.00 48.85           O  
HETATM10983  O   HOH A1889       4.650  -2.388  56.289  1.00 47.28           O  
HETATM10984  O   HOH A1890      33.683  21.206  17.553  1.00 51.63           O  
ATOM   4988  N   ASN B   4       1.025  -0.140  70.636  1.00 49.28           N  
ATOM   4989  CA  ASN B   4      -0.262  -0.036  71.321  1.00 47.29           C  
ATOM   4990  C   ASN B   4      -0.114   0.466  72.759  1.00 40.59           C  
ATOM   4991  O   ASN B   4      -0.804   0.002  73.672  1.00 41.81           O  
ATOM   4992  CB  ASN B   4      -0.972  -1.390  71.301  1.00 47.77           C  
ATOM   4993  CG  ASN B   4      -2.099  -1.440  70.293  1.00 54.50           C  
ATOM   4994  OD1 ASN B   4      -3.254  -1.166  70.627  1.00 57.39           O  
ATOM   4995  ND2 ASN B   4      -1.773  -1.781  69.048  1.00 60.16           N  
ATOM   4996  N   LEU B   5       0.768   1.444  72.935  1.00 40.00           N  
ANISOU 4996  N   LEU B   5     5932   4645   4622   -728   -178    456       N  
ATOM   4997  CA  LEU B   5       0.998   2.064  74.231  1.00 36.02           C  
ANISOU 4997  CA  LEU B   5     5351   4214   4120   -689   -145    457       C  
ATOM   4998  C   LEU B   5      -0.242   2.726  74.833  1.00 31.57           C  
ANISOU 4998  C   LEU B   5     4684   3742   3571   -743   -130    474       C  
ATOM   4999  O   LEU B   5      -1.008   3.403  74.145  1.00 26.79           O  
ANISOU 4999  O   LEU B   5     4017   3167   2994   -769   -138    467       O  
ATOM   5000  CB  LEU B   5       2.108   3.110  74.115  1.00 35.45           C  
ANISOU 5000  CB  LEU B   5     5237   4162   4069   -592   -124    411       C  
ATOM   5001  CG  LEU B   5       3.542   2.699  74.438  1.00 44.19           C  
ANISOU 5001  CG  LEU B   5     6400   5227   5162   -514   -116    404       C  
ATOM   5002  CD1 LEU B   5       3.640   2.250  75.897  1.00 46.06           C  
ANISOU 5002  CD1 LEU B   5     6640   5490   5372   -518   -106    437       C  
ATOM   5003  CD2 LEU B   5       4.017   1.604  73.499  1.00 50.02           C  
ANISOU 5003  CD2 LEU B   5     7253   5864   5888   -507   -134    407       C  
ATOM   5004  N   THR B   6      -0.413   2.524  76.136  1.00 23.55           N  
ANISOU 5004  N   THR B   6     3648   2767   2532   -755   -108    500       N  
ATOM   5005  CA  THR B   6      -1.498   3.129  76.878  1.00 22.61           C  
ANISOU 5005  CA  THR B   6     3432   2738   2422   -795    -80    516       C  
ATOM   5006  C   THR B   6      -0.947   3.684  78.184  1.00 23.59           C  
ANISOU 5006  C   THR B   6     3522   2914   2527   -743    -39    504       C  
ATOM   5007  O   THR B   6      -0.301   2.967  78.941  1.00 22.92           O  
ANISOU 5007  O   THR B   6     3499   2803   2406   -733    -41    521       O  
ATOM   5008  CB  THR B   6      -2.618   2.108  77.179  1.00 24.87           C  
ANISOU 5008  CB  THR B   6     3737   3027   2686   -900    -93    574       C  
ATOM   5009  OG1 THR B   6      -3.204   1.656  75.948  1.00 30.32           O  
ANISOU 5009  OG1 THR B   6     4458   3672   3391   -960   -137    587       O  
ATOM   5010  CG2 THR B   6      -3.700   2.723  78.083  1.00 20.93           C  
ANISOU 5010  CG2 THR B   6     3129   2629   2194   -934    -52    594       C  
ATOM   5011  N   GLY B   7      -1.196   4.958  78.453  1.00 22.90           N  
ANISOU 5011  N   GLY B   7     3342   2896   2462   -710     -6    475       N  
ATOM   5012  CA  GLY B   7      -0.745   5.540  79.704  1.00 15.14           C  
ANISOU 5012  CA  GLY B   7     2335   1963   1456   -668     32    461       C  
ATOM   5013  C   GLY B   7      -1.803   6.391  80.384  1.00 19.38           C  
ANISOU 5013  C   GLY B   7     2778   2585   1999   -685     81    461       C  
ATOM   5014  O   GLY B   7      -2.733   6.880  79.736  1.00 19.90           O  
ANISOU 5014  O   GLY B   7     2777   2678   2105   -705     85    461       O  
ATOM   5015  N   ASP B   8      -1.651   6.584  81.692  1.00 18.45           N  
ANISOU 5015  N   ASP B   8     2657   2511   1843   -676    119    461       N  
ATOM   5016  CA  ASP B   8      -2.511   7.503  82.425  1.00 15.92           C  
ANISOU 5016  CA  ASP B   8     2255   2271   1524   -676    178    452       C  
ATOM   5017  C   ASP B   8      -2.074   8.934  82.157  1.00 15.38           C  
ANISOU 5017  C   ASP B   8     2144   2217   1484   -601    194    395       C  
ATOM   5018  O   ASP B   8      -2.878   9.773  81.736  1.00 22.17           O  
ANISOU 5018  O   ASP B   8     2927   3111   2384   -591    216    382       O  
ATOM   5019  CB  ASP B   8      -2.465   7.203  83.918  1.00 16.41           C  
ANISOU 5019  CB  ASP B   8     2343   2369   1524   -695    214    470       C  
ATOM   5020  CG  ASP B   8      -2.997   5.822  84.244  1.00 23.68           C  
ANISOU 5020  CG  ASP B   8     3305   3278   2414   -776    201    530       C  
ATOM   5021  OD1 ASP B   8      -4.080   5.477  83.738  1.00 22.44           O  
ANISOU 5021  OD1 ASP B   8     3108   3136   2284   -833    200    562       O  
ATOM   5022  OD2 ASP B   8      -2.324   5.082  84.990  1.00 26.01           O  
ANISOU 5022  OD2 ASP B   8     3674   3548   2660   -785    187    550       O  
ATOM   5023  N   ILE B   9      -0.791   9.194  82.399  1.00 14.95           N  
ANISOU 5023  N   ILE B   9     2137   2136   1408   -551    179    365       N  
ATOM   5024  CA  ILE B   9      -0.181  10.488  82.114  1.00 18.16           C  
ANISOU 5024  CA  ILE B   9     2519   2546   1836   -485    184    313       C  
ATOM   5025  C   ILE B   9       0.813  10.324  80.976  1.00 20.13           C  
ANISOU 5025  C   ILE B   9     2804   2734   2111   -455    131    300       C  
ATOM   5026  O   ILE B   9       1.758   9.549  81.086  1.00 18.02           O  
ANISOU 5026  O   ILE B   9     2599   2428   1820   -449    102    313       O  
ATOM   5027  CB  ILE B   9       0.570  11.070  83.328  1.00 24.00           C  
ANISOU 5027  CB  ILE B   9     3281   3311   2526   -455    208    288       C  
ATOM   5028  CG1 ILE B   9      -0.262  10.952  84.604  1.00 23.97           C  
ANISOU 5028  CG1 ILE B   9     3266   3362   2478   -491    263    307       C  
ATOM   5029  CG2 ILE B   9       1.016  12.513  83.050  1.00 19.94           C  
ANISOU 5029  CG2 ILE B   9     2738   2803   2034   -397    217    234       C  
ATOM   5030  CD1 ILE B   9      -1.479  11.836  84.624  1.00 22.69           C  
ANISOU 5030  CD1 ILE B   9     3027   3252   2344   -486    320    292       C  
ATOM   5031  N   VAL B  10       0.592  11.059  79.892  1.00 19.31           N  
ANISOU 5031  N   VAL B  10     2661   2621   2056   -435    122    276       N  
ATOM   5032  CA  VAL B  10       1.487  11.036  78.742  1.00 12.98           C  
ANISOU 5032  CA  VAL B  10     1889   1765   1277   -406     79    260       C  
ATOM   5033  C   VAL B  10       2.173  12.384  78.658  1.00 12.55           C  
ANISOU 5033  C   VAL B  10     1810   1723   1236   -349     87    213       C  
ATOM   5034  O   VAL B  10       1.514  13.422  78.601  1.00 12.56           O  
ANISOU 5034  O   VAL B  10     1757   1755   1261   -337    111    191       O  
ATOM   5035  CB  VAL B  10       0.726  10.727  77.431  1.00 12.97           C  
ANISOU 5035  CB  VAL B  10     1875   1737   1316   -438     54    273       C  
ATOM   5036  CG1 VAL B  10       1.641  10.894  76.221  1.00 12.46           C  
ANISOU 5036  CG1 VAL B  10     1841   1620   1272   -404     19    250       C  
ATOM   5037  CG2 VAL B  10       0.158   9.310  77.489  1.00 15.72           C  
ANISOU 5037  CG2 VAL B  10     2263   2063   1645   -502     38    321       C  
ATOM   5038  N   ILE B  11       3.501  12.363  78.688  1.00 12.25           N  
ANISOU 5038  N   ILE B  11     1812   1661   1182   -315     66    201       N  
ATOM   5039  CA  ILE B  11       4.297  13.584  78.747  1.00 11.92           C  
ANISOU 5039  CA  ILE B  11     1754   1631   1144   -271     68    161       C  
ATOM   5040  C   ILE B  11       5.077  13.771  77.440  1.00 16.29           C  
ANISOU 5040  C   ILE B  11     2317   2144   1729   -244     36    147       C  
ATOM   5041  O   ILE B  11       5.799  12.866  77.009  1.00 16.46           O  
ANISOU 5041  O   ILE B  11     2380   2128   1747   -238     12    164       O  
ATOM   5042  CB  ILE B  11       5.280  13.546  79.921  1.00 12.04           C  
ANISOU 5042  CB  ILE B  11     1801   1662   1112   -258     68    163       C  
ATOM   5043  CG1 ILE B  11       4.529  13.277  81.241  1.00 13.61           C  
ANISOU 5043  CG1 ILE B  11     2002   1900   1270   -290    102    179       C  
ATOM   5044  CG2 ILE B  11       6.119  14.830  79.984  1.00 11.77           C  
ANISOU 5044  CG2 ILE B  11     1754   1640   1078   -222     64    124       C  
ATOM   5045  CD1 ILE B  11       5.447  12.954  82.377  1.00 12.79           C  
ANISOU 5045  CD1 ILE B  11     1940   1807   1114   -289     92    193       C  
ATOM   5046  N   ILE B  12       4.966  14.943  76.824  1.00 13.60           N  
ANISOU 5046  N   ILE B  12     1941   1808   1417   -224     38    115       N  
ATOM   5047  CA  ILE B  12       5.629  15.148  75.539  1.00 10.80           C  
ANISOU 5047  CA  ILE B  12     1595   1419   1090   -205     11    102       C  
ATOM   5048  C   ILE B  12       6.873  16.022  75.696  1.00 10.55           C  
ANISOU 5048  C   ILE B  12     1564   1394   1050   -169      4     77       C  
ATOM   5049  O   ILE B  12       6.769  17.245  75.844  1.00 10.47           O  
ANISOU 5049  O   ILE B  12     1528   1404   1047   -158     13     48       O  
ATOM   5050  CB  ILE B  12       4.663  15.769  74.511  1.00 15.03           C  
ANISOU 5050  CB  ILE B  12     2096   1948   1666   -215      7     92       C  
ATOM   5051  CG1 ILE B  12       3.389  14.934  74.403  1.00 11.06           C  
ANISOU 5051  CG1 ILE B  12     1583   1447   1171   -259     10    123       C  
ATOM   5052  CG2 ILE B  12       5.330  15.869  73.145  1.00 13.82           C  
ANISOU 5052  CG2 ILE B  12     1963   1757   1533   -203    -21     82       C  
ATOM   5053  CD1 ILE B  12       2.242  15.679  73.792  1.00 11.15           C  
ANISOU 5053  CD1 ILE B  12     1541   1472   1222   -270     11    121       C  
ATOM   5054  N   GLY B  13       8.046  15.388  75.668  1.00 14.51           N  
ANISOU 5054  N   GLY B  13     2096   1879   1537   -153    -13     91       N  
ATOM   5055  CA  GLY B  13       9.319  16.099  75.798  1.00 10.35           C  
ANISOU 5055  CA  GLY B  13     1564   1364   1003   -125    -26     77       C  
ATOM   5056  C   GLY B  13      10.107  15.834  77.083  1.00 10.61           C  
ANISOU 5056  C   GLY B  13     1610   1423    998   -121    -31     94       C  
ATOM   5057  O   GLY B  13       9.693  16.252  78.164  1.00 12.78           O  
ANISOU 5057  O   GLY B  13     1882   1728   1245   -137    -17     86       O  
ATOM   5058  N   ALA B  14      11.250  15.155  76.965  1.00 11.06           N  
ANISOU 5058  N   ALA B  14     1681   1469   1052    -98    -50    118       N  
ATOM   5059  CA  ALA B  14      12.105  14.832  78.112  1.00 14.61           C  
ANISOU 5059  CA  ALA B  14     2140   1943   1468    -94    -65    144       C  
ATOM   5060  C   ALA B  14      13.132  15.930  78.375  1.00 17.88           C  
ANISOU 5060  C   ALA B  14     2530   2388   1874    -86    -83    131       C  
ATOM   5061  O   ALA B  14      14.348  15.683  78.345  1.00 11.07           O  
ANISOU 5061  O   ALA B  14     1658   1533   1014    -64   -106    156       O  
ATOM   5062  CB  ALA B  14      12.813  13.496  77.900  1.00 11.19           C  
ANISOU 5062  CB  ALA B  14     1731   1481   1039    -67    -77    185       C  
ATOM   5063  N   GLY B  15      12.642  17.148  78.595  1.00 10.84           N  
ANISOU 5063  N   GLY B  15     1628   1515    976   -105    -74     94       N  
ATOM   5064  CA  GLY B  15      13.536  18.272  78.820  1.00 10.85           C  
ANISOU 5064  CA  GLY B  15     1616   1541    967   -109    -95     79       C  
ATOM   5065  C   GLY B  15      13.769  18.523  80.292  1.00 14.70           C  
ANISOU 5065  C   GLY B  15     2123   2062   1402   -133   -105     84       C  
ATOM   5066  O   GLY B  15      13.577  17.622  81.113  1.00 18.44           O  
ANISOU 5066  O   GLY B  15     2616   2541   1848   -141   -103    111       O  
ATOM   5067  N   ALA B  16      14.143  19.755  80.627  1.00 13.53           N  
ANISOU 5067  N   ALA B  16     1976   1930   1234   -151   -117     58       N  
ATOM   5068  CA  ALA B  16      14.358  20.142  82.026  1.00 13.87           C  
ANISOU 5068  CA  ALA B  16     2051   2003   1218   -182   -129     57       C  
ATOM   5069  C   ALA B  16      13.136  19.826  82.885  1.00 14.61           C  
ANISOU 5069  C   ALA B  16     2174   2098   1281   -195    -89     46       C  
ATOM   5070  O   ALA B  16      13.251  19.357  84.022  1.00 12.46           O  
ANISOU 5070  O   ALA B  16     1930   1846    959   -216    -96     68       O  
ATOM   5071  CB  ALA B  16      14.689  21.620  82.117  1.00 15.67           C  
ANISOU 5071  CB  ALA B  16     2288   2235   1429   -203   -141     20       C  
ATOM   5072  N   ALA B  17      11.963  20.078  82.324  1.00 14.12           N  
ANISOU 5072  N   ALA B  17     2101   2015   1246   -183    -48     17       N  
ATOM   5073  CA  ALA B  17      10.715  19.874  83.043  1.00 17.18           C  
ANISOU 5073  CA  ALA B  17     2505   2410   1612   -193     -3      7       C  
ATOM   5074  C   ALA B  17      10.237  18.442  82.893  1.00 17.22           C  
ANISOU 5074  C   ALA B  17     2503   2409   1631   -192      5     46       C  
ATOM   5075  O   ALA B  17       9.881  17.794  83.870  1.00 12.41           O  
ANISOU 5075  O   ALA B  17     1918   1817    982   -212     19     66       O  
ATOM   5076  CB  ALA B  17       9.654  20.833  82.544  1.00 11.94           C  
ANISOU 5076  CB  ALA B  17     1826   1733    977   -179     37    -36       C  
ATOM   5077  N   GLY B  18      10.239  17.944  81.664  1.00 11.65           N  
ANISOU 5077  N   GLY B  18     1771   1676    977   -172     -5     58       N  
ATOM   5078  CA  GLY B  18       9.641  16.647  81.408  1.00 14.14           C  
ANISOU 5078  CA  GLY B  18     2089   1976   1307   -176      4     90       C  
ATOM   5079  C   GLY B  18      10.312  15.473  82.092  1.00 20.21           C  
ANISOU 5079  C   GLY B  18     2886   2747   2046   -182    -19    136       C  
ATOM   5080  O   GLY B  18       9.632  14.540  82.525  1.00 12.22           O  
ANISOU 5080  O   GLY B  18     1892   1732   1018   -201     -5    161       O  
ATOM   5081  N   SER B  19      11.640  15.507  82.162  1.00 11.97           N  
ANISOU 5081  N   SER B  19     1845   1708    997   -167    -57    152       N  
ATOM   5082  CA  SER B  19      12.416  14.425  82.767  1.00 12.31           C  
ANISOU 5082  CA  SER B  19     1909   1752   1017   -163    -85    201       C  
ATOM   5083  C   SER B  19      12.126  14.329  84.253  1.00 15.78           C  
ANISOU 5083  C   SER B  19     2381   2222   1395   -199    -81    214       C  
ATOM   5084  O   SER B  19      11.928  13.238  84.800  1.00 13.88           O  
ANISOU 5084  O   SER B  19     2168   1974   1133   -211    -84    252       O  
ATOM   5085  CB  SER B  19      13.917  14.641  82.571  1.00 18.28           C  
ANISOU 5085  CB  SER B  19     2646   2516   1783   -138   -127    219       C  
ATOM   5086  OG  SER B  19      14.237  14.775  81.204  1.00 18.20           O  
ANISOU 5086  OG  SER B  19     2608   2481   1824   -106   -125    207       O  
ATOM   5087  N   LEU B  20      12.144  15.488  84.896  1.00 18.62           N  
ANISOU 5087  N   LEU B  20     2743   2610   1720   -218    -75    181       N  
ATOM   5088  CA  LEU B  20      11.874  15.580  86.321  1.00 19.90           C  
ANISOU 5088  CA  LEU B  20     2944   2802   1814   -256    -66    184       C  
ATOM   5089  C   LEU B  20      10.442  15.118  86.587  1.00 17.10           C  
ANISOU 5089  C   LEU B  20     2601   2447   1451   -274    -14    179       C  
ATOM   5090  O   LEU B  20      10.191  14.334  87.517  1.00 15.99           O  
ANISOU 5090  O   LEU B  20     2492   2317   1265   -301     -9    211       O  
ATOM   5091  CB  LEU B  20      12.085  17.009  86.814  1.00 18.56           C  
ANISOU 5091  CB  LEU B  20     2787   2655   1611   -272    -64    140       C  
ATOM   5092  CG  LEU B  20      12.052  17.312  88.323  1.00 14.19           C  
ANISOU 5092  CG  LEU B  20     2286   2131    973   -314    -60    137       C  
ATOM   5093  CD1 LEU B  20      12.759  18.641  88.583  1.00 14.30           C  
ANISOU 5093  CD1 LEU B  20     2317   2156    960   -328    -83    103       C  
ATOM   5094  CD2 LEU B  20      10.628  17.334  88.870  1.00 14.44           C  
ANISOU 5094  CD2 LEU B  20     2338   2170    979   -329      8    113       C  
ATOM   5095  N   LEU B  21       9.508  15.630  85.791  1.00 14.94           N  
ANISOU 5095  N   LEU B  21     2297   2163   1218   -262     25    144       N  
ATOM   5096  CA  LEU B  21       8.084  15.338  85.998  1.00 17.03           C  
ANISOU 5096  CA  LEU B  21     2555   2434   1480   -280     78    141       C  
ATOM   5097  C   LEU B  21       7.810  13.845  85.904  1.00 13.59           C  
ANISOU 5097  C   LEU B  21     2131   1983   1051   -295     69    192       C  
ATOM   5098  O   LEU B  21       7.144  13.269  86.751  1.00 14.05           O  
ANISOU 5098  O   LEU B  21     2210   2058   1070   -328     93    213       O  
ATOM   5099  CB  LEU B  21       7.223  16.085  84.980  1.00 16.15           C  
ANISOU 5099  CB  LEU B  21     2399   2313   1424   -260    108    105       C  
ATOM   5100  CG  LEU B  21       5.712  15.795  84.988  1.00 13.96           C  
ANISOU 5100  CG  LEU B  21     2098   2048   1160   -276    160    108       C  
ATOM   5101  CD1 LEU B  21       5.032  16.186  86.317  1.00 13.98           C  
ANISOU 5101  CD1 LEU B  21     2118   2091   1105   -296    213     95       C  
ATOM   5102  CD2 LEU B  21       5.052  16.502  83.830  1.00 13.02           C  
ANISOU 5102  CD2 LEU B  21     1929   1916   1103   -252    173     81       C  
ATOM   5103  N   ALA B  22       8.350  13.228  84.862  1.00 19.54           N  
ANISOU 5103  N   ALA B  22     2876   2699   1849   -272     34    210       N  
ATOM   5104  CA  ALA B  22       8.139  11.810  84.600  1.00 18.25           C  
ANISOU 5104  CA  ALA B  22     2733   2505   1696   -282     23    255       C  
ATOM   5105  C   ALA B  22       8.661  10.969  85.751  1.00 16.83           C  
ANISOU 5105  C   ALA B  22     2600   2333   1463   -301      2    299       C  
ATOM   5106  O   ALA B  22       8.006  10.032  86.208  1.00 15.95           O  
ANISOU 5106  O   ALA B  22     2515   2216   1329   -334     12    332       O  
ATOM   5107  CB  ALA B  22       8.829  11.404  83.294  1.00 17.31           C  
ANISOU 5107  CB  ALA B  22     2608   2340   1628   -245     -8    261       C  
ATOM   5108  N   HIS B  23       9.864  11.311  86.191  1.00 14.96           N  
ANISOU 5108  N   HIS B  23     2370   2107   1205   -283    -34    304       N  
ATOM   5109  CA  HIS B  23      10.568  10.595  87.242  1.00 19.26           C  
ANISOU 5109  CA  HIS B  23     2955   2659   1702   -295    -67    352       C  
ATOM   5110  C   HIS B  23       9.780  10.546  88.560  1.00 14.97           C  
ANISOU 5110  C   HIS B  23     2446   2151   1092   -348    -38    358       C  
ATOM   5111  O   HIS B  23       9.522   9.476  89.091  1.00 15.39           O  
ANISOU 5111  O   HIS B  23     2536   2195   1118   -373    -43    402       O  
ATOM   5112  CB  HIS B  23      11.938  11.249  87.440  1.00 15.86           C  
ANISOU 5112  CB  HIS B  23     2514   2247   1265   -272   -111    352       C  
ATOM   5113  CG  HIS B  23      12.715  10.723  88.599  1.00 17.22           C  
ANISOU 5113  CG  HIS B  23     2722   2437   1385   -289   -153    402       C  
ATOM   5114  ND1 HIS B  23      13.763   9.835  88.448  1.00 15.21           N  
ANISOU 5114  ND1 HIS B  23     2469   2160   1150   -256   -202    455       N  
ATOM   5115  CD2 HIS B  23      12.654  11.012  89.924  1.00 15.52           C  
ANISOU 5115  CD2 HIS B  23     2542   2259   1097   -333   -156    407       C  
ATOM   5116  CE1 HIS B  23      14.284   9.573  89.634  1.00 21.91           C  
ANISOU 5116  CE1 HIS B  23     3349   3033   1943   -281   -238    496       C  
ATOM   5117  NE2 HIS B  23      13.637  10.281  90.543  1.00 16.00           N  
ANISOU 5117  NE2 HIS B  23     2624   2320   1134   -332   -213    467       N  
ATOM   5118  N   TYR B  24       9.371  11.701  89.064  1.00 15.02           N  
ANISOU 5118  N   TYR B  24     2445   2194   1068   -364     -4    313       N  
ATOM   5119  CA  TYR B  24       8.676  11.750  90.352  1.00 17.82           C  
ANISOU 5119  CA  TYR B  24     2836   2585   1351   -411     31    315       C  
ATOM   5120  C   TYR B  24       7.217  11.309  90.293  1.00 20.83           C  
ANISOU 5120  C   TYR B  24     3206   2971   1739   -436     90    316       C  
ATOM   5121  O   TYR B  24       6.693  10.812  91.300  1.00 16.74           O  
ANISOU 5121  O   TYR B  24     2722   2476   1164   -479    113    341       O  
ATOM   5122  CB  TYR B  24       8.765  13.156  90.927  1.00 15.72           C  
ANISOU 5122  CB  TYR B  24     2576   2351   1047   -415     53    263       C  
ATOM   5123  CG  TYR B  24      10.123  13.431  91.530  1.00 20.72           C  
ANISOU 5123  CG  TYR B  24     3238   2993   1640   -420     -9    278       C  
ATOM   5124  CD1 TYR B  24      10.581  12.714  92.648  1.00 18.15           C  
ANISOU 5124  CD1 TYR B  24     2965   2683   1250   -455    -42    327       C  
ATOM   5125  CD2 TYR B  24      10.953  14.392  90.982  1.00 15.56           C  
ANISOU 5125  CD2 TYR B  24     2562   2337   1014   -394    -38    249       C  
ATOM   5126  CE1 TYR B  24      11.827  12.974  93.209  1.00 16.80           C  
ANISOU 5126  CE1 TYR B  24     2815   2525   1043   -464   -106    347       C  
ATOM   5127  CE2 TYR B  24      12.199  14.648  91.522  1.00 15.82           C  
ANISOU 5127  CE2 TYR B  24     2614   2384   1012   -406    -99    268       C  
ATOM   5128  CZ  TYR B  24      12.637  13.947  92.628  1.00 16.44           C  
ANISOU 5128  CZ  TYR B  24     2739   2480   1028   -440   -134    318       C  
ATOM   5129  OH  TYR B  24      13.884  14.232  93.133  1.00 17.03           O  
ANISOU 5129  OH  TYR B  24     2826   2572   1071   -455   -202    343       O  
ATOM   5130  N   LEU B  25       6.566  11.477  89.132  1.00 18.78           N  
ANISOU 5130  N   LEU B  25     2896   2693   1545   -415    111    294       N  
ATOM   5131  CA  LEU B  25       5.194  10.982  88.965  1.00 18.81           C  
ANISOU 5131  CA  LEU B  25     2879   2703   1563   -444    157    305       C  
ATOM   5132  C   LEU B  25       5.177   9.461  89.094  1.00 24.93           C  
ANISOU 5132  C   LEU B  25     3693   3453   2327   -475    130    367       C  
ATOM   5133  O   LEU B  25       4.246   8.888  89.671  1.00 16.31           O  
ANISOU 5133  O   LEU B  25     2611   2381   1206   -523    163    393       O  
ATOM   5134  CB  LEU B  25       4.590  11.391  87.624  1.00 19.27           C  
ANISOU 5134  CB  LEU B  25     2880   2746   1697   -419    170    279       C  
ATOM   5135  CG  LEU B  25       3.977  12.782  87.425  1.00 24.49           C  
ANISOU 5135  CG  LEU B  25     3493   3433   2378   -396    217    224       C  
ATOM   5136  CD1 LEU B  25       3.523  12.960  85.976  1.00 16.15           C  
ANISOU 5136  CD1 LEU B  25     2385   2351   1399   -374    211    212       C  
ATOM   5137  CD2 LEU B  25       2.806  13.038  88.403  1.00 15.53           C  
ANISOU 5137  CD2 LEU B  25     2349   2348   1204   -425    288    219       C  
ATOM   5138  N   ALA B  26       6.208   8.816  88.546  1.00 16.92           N  
ANISOU 5138  N   ALA B  26     2699   2392   1336   -448     72    391       N  
ATOM   5139  CA  ALA B  26       6.357   7.376  88.644  1.00 15.88           C  
ANISOU 5139  CA  ALA B  26     2615   2223   1195   -468     40    449       C  
ATOM   5140  C   ALA B  26       6.676   6.977  90.079  1.00 23.40           C  
ANISOU 5140  C   ALA B  26     3620   3199   2072   -500     30    485       C  
ATOM   5141  O   ALA B  26       6.162   5.968  90.574  1.00 20.60           O  
ANISOU 5141  O   ALA B  26     3304   2835   1687   -545     33    530       O  
ATOM   5142  CB  ALA B  26       7.437   6.886  87.707  1.00 17.70           C  
ANISOU 5142  CB  ALA B  26     2856   2397   1471   -417    -11    462       C  
ATOM   5143  N   ARG B  27       7.542   7.755  90.735  1.00 17.83           N  
ANISOU 5143  N   ARG B  27     2920   2521   1334   -484     13    470       N  
ATOM   5144  CA  ARG B  27       7.956   7.438  92.096  1.00 18.51           C  
ANISOU 5144  CA  ARG B  27     3059   2629   1343   -517     -7    506       C  
ATOM   5145  C   ARG B  27       6.793   7.561  93.068  1.00 17.74           C  
ANISOU 5145  C   ARG B  27     2978   2577   1184   -577     55    500       C  
ATOM   5146  O   ARG B  27       6.614   6.714  93.931  1.00 19.49           O  
ANISOU 5146  O   ARG B  27     3250   2803   1353   -622     50    548       O  
ATOM   5147  CB  ARG B  27       9.110   8.349  92.566  1.00 17.17           C  
ANISOU 5147  CB  ARG B  27     2893   2484   1148   -496    -42    488       C  
ATOM   5148  CG  ARG B  27       9.505   8.122  94.048  1.00 17.93           C  
ANISOU 5148  CG  ARG B  27     3049   2609   1154   -540    -66    525       C  
ATOM   5149  CD  ARG B  27      10.801   8.808  94.473  1.00 18.01           C  
ANISOU 5149  CD  ARG B  27     3065   2637   1140   -527   -121    525       C  
ATOM   5150  NE  ARG B  27      11.127   8.468  95.862  1.00 24.50           N  
ANISOU 5150  NE  ARG B  27     3951   3484   1873   -576   -151    568       N  
ATOM   5151  CZ  ARG B  27      12.162   8.938  96.555  1.00 21.48           C  
ANISOU 5151  CZ  ARG B  27     3589   3125   1446   -587   -206    581       C  
ATOM   5152  NH1 ARG B  27      13.010   9.799  96.006  1.00 18.74           N  
ANISOU 5152  NH1 ARG B  27     3202   2783   1137   -553   -237    554       N  
ATOM   5153  NH2 ARG B  27      12.344   8.553  97.821  1.00 19.93           N  
ANISOU 5153  NH2 ARG B  27     3443   2944   1187   -627   -229    614       N  
ATOM   5154  N   PHE B  28       6.001   8.617  92.914  1.00 17.56           N  
ANISOU 5154  N   PHE B  28     2914   2588   1171   -574    115    445       N  
ATOM   5155  CA  PHE B  28       4.996   8.968  93.915  1.00 18.16           C  
ANISOU 5155  CA  PHE B  28     3000   2714   1185   -619    184    432       C  
ATOM   5156  C   PHE B  28       3.583   8.474  93.581  1.00 27.10           C  
ANISOU 5156  C   PHE B  28     4097   3857   2343   -649    240    444       C  
ATOM   5157  O   PHE B  28       2.648   8.793  94.304  1.00 26.76           O  
ANISOU 5157  O   PHE B  28     4048   3861   2258   -681    308    434       O  
ATOM   5158  CB  PHE B  28       4.946  10.489  94.112  1.00 18.06           C  
ANISOU 5158  CB  PHE B  28     2969   2734   1160   -596    226    364       C  
ATOM   5159  CG  PHE B  28       6.162  11.069  94.765  1.00 18.15           C  
ANISOU 5159  CG  PHE B  28     3026   2749   1122   -590    180    354       C  
ATOM   5160  CD1 PHE B  28       6.690  10.499  95.915  1.00 29.01           C  
ANISOU 5160  CD1 PHE B  28     4468   4135   2417   -632    147    396       C  
ATOM   5161  CD2 PHE B  28       6.769  12.207  94.240  1.00 17.68           C  
ANISOU 5161  CD2 PHE B  28     2942   2682   1092   -548    165    304       C  
ATOM   5162  CE1 PHE B  28       7.804  11.039  96.525  1.00 26.87           C  
ANISOU 5162  CE1 PHE B  28     4238   3873   2100   -634     97    392       C  
ATOM   5163  CE2 PHE B  28       7.896  12.756  94.844  1.00 17.83           C  
ANISOU 5163  CE2 PHE B  28     3003   2709   1064   -553    117    299       C  
ATOM   5164  CZ  PHE B  28       8.412  12.168  95.990  1.00 27.95           C  
ANISOU 5164  CZ  PHE B  28     4349   4005   2268   -597     81    343       C  
ATOM   5165  N   SER B  29       3.412   7.721  92.494  1.00 21.78           N  
ANISOU 5165  N   SER B  29     3400   3142   1736   -641    213    467       N  
ATOM   5166  CA  SER B  29       2.082   7.216  92.148  1.00 18.20           C  
ANISOU 5166  CA  SER B  29     2911   2699   1306   -681    255    486       C  
ATOM   5167  C   SER B  29       2.119   5.741  91.725  1.00 24.53           C  
ANISOU 5167  C   SER B  29     3749   3448   2123   -711    207    546       C  
ATOM   5168  O   SER B  29       3.194   5.149  91.589  1.00 22.60           O  
ANISOU 5168  O   SER B  29     3553   3155   1880   -688    144    568       O  
ATOM   5169  CB  SER B  29       1.458   8.062  91.030  1.00 17.69           C  
ANISOU 5169  CB  SER B  29     2767   2639   1315   -645    283    441       C  
ATOM   5170  OG  SER B  29       1.958   7.671  89.759  1.00 17.08           O  
ANISOU 5170  OG  SER B  29     2683   2503   1302   -616    228    445       O  
ATOM   5171  N   ASN B  30       0.943   5.146  91.541  1.00 20.70           N  
ANISOU 5171  N   ASN B  30     3244   2974   1649   -764    237    573       N  
ATOM   5172  CA  ASN B  30       0.843   3.798  90.977  1.00 18.78           C  
ANISOU 5172  CA  ASN B  30     3039   2673   1425   -798    192    625       C  
ATOM   5173  C   ASN B  30       0.355   3.853  89.536  1.00 21.72           C  
ANISOU 5173  C   ASN B  30     3361   3016   1874   -786    183    609       C  
ATOM   5174  O   ASN B  30      -0.129   2.857  88.999  1.00 26.74           O  
ANISOU 5174  O   ASN B  30     4018   3615   2527   -830    161    647       O  
ATOM   5175  CB  ASN B  30      -0.103   2.916  91.786  1.00 23.93           C  
ANISOU 5175  CB  ASN B  30     3715   3350   2026   -884    219    680       C  
ATOM   5176  CG  ASN B  30       0.479   2.502  93.126  1.00 28.04           C  
ANISOU 5176  CG  ASN B  30     4309   3879   2465   -907    208    712       C  
ATOM   5177  OD1 ASN B  30       1.701   2.385  93.286  1.00 19.99           O  
ANISOU 5177  OD1 ASN B  30     3339   2822   1434   -865    155    715       O  
ATOM   5178  ND2 ASN B  30      -0.401   2.237  94.087  1.00 20.98           N  
ANISOU 5178  ND2 ASN B  30     3411   3031   1529   -964    254    732       N  
ATOM   5179  N   MET B  31       0.454   5.028  88.927  1.00 17.73           N  
ANISOU 5179  N   MET B  31     2795   2529   1412   -731    200    554       N  
ATOM   5180  CA  MET B  31      -0.061   5.248  87.569  1.00 22.59           C  
ANISOU 5180  CA  MET B  31     3359   3125   2099   -720    193    536       C  
ATOM   5181  C   MET B  31       0.936   4.864  86.494  1.00 20.96           C  
ANISOU 5181  C   MET B  31     3191   2842   1930   -677    132    529       C  
ATOM   5182  O   MET B  31       2.148   4.811  86.742  1.00 21.41           O  
ANISOU 5182  O   MET B  31     3291   2872   1972   -633    101    525       O  
ATOM   5183  CB  MET B  31      -0.457   6.716  87.371  1.00 22.84           C  
ANISOU 5183  CB  MET B  31     3310   3208   2161   -680    239    481       C  
ATOM   5184  CG  MET B  31      -1.628   7.172  88.235  1.00 29.32           C  
ANISOU 5184  CG  MET B  31     4079   4104   2956   -713    313    484       C  
ATOM   5185  SD  MET B  31      -2.077   8.866  87.844  1.00 25.29           S  
ANISOU 5185  SD  MET B  31     3480   3638   2492   -653    364    421       S  
ATOM   5186  CE  MET B  31      -0.591   9.715  88.326  1.00 36.39           C  
ANISOU 5186  CE  MET B  31     4937   5025   3864   -590    345    371       C  
ATOM   5187  N   LYS B  32       0.413   4.616  85.296  1.00 21.27           N  
ANISOU 5187  N   LYS B  32     3212   2851   2020   -690    116    531       N  
ATOM   5188  CA  LYS B  32       1.238   4.409  84.116  1.00 21.66           C  
ANISOU 5188  CA  LYS B  32     3292   2831   2108   -646     70    516       C  
ATOM   5189  C   LYS B  32       1.639   5.768  83.566  1.00 24.81           C  
ANISOU 5189  C   LYS B  32     3632   3251   2544   -582     80    459       C  
ATOM   5190  O   LYS B  32       0.785   6.536  83.104  1.00 19.51           O  
ANISOU 5190  O   LYS B  32     2894   2614   1906   -589    105    437       O  
ATOM   5191  CB  LYS B  32       0.483   3.610  83.050  1.00 23.02           C  
ANISOU 5191  CB  LYS B  32     3479   2959   2310   -695     47    539       C  
ATOM   5192  CG  LYS B  32       0.017   2.242  83.503  1.00 35.48           C  
ANISOU 5192  CG  LYS B  32     5121   4508   3851   -767     32    597       C  
ATOM   5193  CD  LYS B  32       1.197   1.372  83.880  1.00 45.36           C  
ANISOU 5193  CD  LYS B  32     6466   5697   5073   -736     -2    618       C  
ATOM   5194  CE  LYS B  32       0.755   0.005  84.379  1.00 51.66           C  
ANISOU 5194  CE  LYS B  32     7337   6460   5831   -809    -19    678       C  
ATOM   5195  NZ  LYS B  32       0.304   0.061  85.804  1.00 55.93           N  
ANISOU 5195  NZ  LYS B  32     7862   7069   6322   -852     14    705       N  
ATOM   5196  N   ILE B  33       2.940   6.046  83.615  1.00 18.26           N  
ANISOU 5196  N   ILE B  33     2827   2400   1710   -522     59    439       N  
ATOM   5197  CA  ILE B  33       3.506   7.283  83.104  1.00 14.45           C  
ANISOU 5197  CA  ILE B  33     2300   1930   1258   -465     62    389       C  
ATOM   5198  C   ILE B  33       4.293   7.000  81.832  1.00 17.39           C  
ANISOU 5198  C   ILE B  33     2697   2240   1669   -426     25    380       C  
ATOM   5199  O   ILE B  33       5.201   6.162  81.828  1.00 18.79           O  
ANISOU 5199  O   ILE B  33     2931   2372   1836   -405     -4    403       O  
ATOM   5200  CB  ILE B  33       4.452   7.944  84.135  1.00 16.74           C  
ANISOU 5200  CB  ILE B  33     2596   2253   1513   -431     65    374       C  
ATOM   5201  CG1 ILE B  33       3.822   7.954  85.539  1.00 17.97           C  
ANISOU 5201  CG1 ILE B  33     2755   2462   1613   -474    101    389       C  
ATOM   5202  CG2 ILE B  33       4.891   9.330  83.660  1.00 15.50           C  
ANISOU 5202  CG2 ILE B  33     2392   2113   1384   -383     71    321       C  
ATOM   5203  CD1 ILE B  33       2.443   8.619  85.619  1.00 18.68           C  
ANISOU 5203  CD1 ILE B  33     2784   2601   1712   -502    156    372       C  
ATOM   5204  N   ILE B  34       3.951   7.707  80.757  1.00 23.62           N  
ANISOU 5204  N   ILE B  34     3445   3028   2503   -414     28    349       N  
ATOM   5205  CA  ILE B  34       4.651   7.556  79.483  1.00 21.86           C  
ANISOU 5205  CA  ILE B  34     3245   2749   2313   -379     -1    335       C  
ATOM   5206  C   ILE B  34       5.306   8.873  79.089  1.00 23.55           C  
ANISOU 5206  C   ILE B  34     3413   2984   2550   -328      3    290       C  
ATOM   5207  O   ILE B  34       4.630   9.909  78.996  1.00 20.19           O  
ANISOU 5207  O   ILE B  34     2933   2597   2142   -333     24    264       O  
ATOM   5208  CB  ILE B  34       3.703   7.096  78.364  1.00 20.09           C  
ANISOU 5208  CB  ILE B  34     3026   2492   2114   -421    -11    343       C  
ATOM   5209  CG1 ILE B  34       3.065   5.753  78.739  1.00 13.91           C  
ANISOU 5209  CG1 ILE B  34     2296   1683   1305   -481    -19    391       C  
ATOM   5210  CG2 ILE B  34       4.446   6.992  77.052  1.00 12.98           C  
ANISOU 5210  CG2 ILE B  34     2159   1534   1240   -384    -34    325       C  
ATOM   5211  CD1 ILE B  34       2.173   5.180  77.648  1.00 27.39           C  
ANISOU 5211  CD1 ILE B  34     4022   3353   3031   -534    -39    404       C  
ATOM   5212  N   LEU B  35       6.628   8.834  78.894  1.00 13.49           N  
ANISOU 5212  N   LEU B  35     2163   1687   1278   -278    -16    286       N  
ATOM   5213  CA  LEU B  35       7.372  10.001  78.435  1.00 12.08           C  
ANISOU 5213  CA  LEU B  35     1947   1524   1121   -235    -18    248       C  
ATOM   5214  C   LEU B  35       7.830   9.796  76.975  1.00 11.81           C  
ANISOU 5214  C   LEU B  35     1930   1439   1120   -209    -32    238       C  
ATOM   5215  O   LEU B  35       8.515   8.825  76.650  1.00 14.14           O  
ANISOU 5215  O   LEU B  35     2273   1688   1412   -188    -45    259       O  
ATOM   5216  CB  LEU B  35       8.553  10.261  79.354  1.00 12.99           C  
ANISOU 5216  CB  LEU B  35     2063   1662   1211   -203    -27    253       C  
ATOM   5217  CG  LEU B  35       9.612  11.313  79.041  1.00 11.80           C  
ANISOU 5217  CG  LEU B  35     1881   1528   1075   -162    -37    225       C  
ATOM   5218  CD1 LEU B  35       9.044  12.735  79.033  1.00 12.33           C  
ANISOU 5218  CD1 LEU B  35     1904   1631   1151   -171    -19    183       C  
ATOM   5219  CD2 LEU B  35      10.713  11.183  80.078  1.00 12.42           C  
ANISOU 5219  CD2 LEU B  35     1969   1628   1123   -144    -56    249       C  
ATOM   5220  N   LEU B  36       7.407  10.691  76.096  1.00 12.26           N  
ANISOU 5220  N   LEU B  36     1951   1501   1205   -211    -28    207       N  
ATOM   5221  CA  LEU B  36       7.781  10.628  74.676  1.00 12.58           C  
ANISOU 5221  CA  LEU B  36     2011   1498   1272   -193    -40    194       C  
ATOM   5222  C   LEU B  36       8.822  11.694  74.373  1.00 12.22           C  
ANISOU 5222  C   LEU B  36     1933   1470   1239   -149    -41    166       C  
ATOM   5223  O   LEU B  36       8.598  12.876  74.653  1.00 12.97           O  
ANISOU 5223  O   LEU B  36     1981   1605   1340   -151    -35    143       O  
ATOM   5224  CB  LEU B  36       6.554  10.820  73.794  1.00 11.20           C  
ANISOU 5224  CB  LEU B  36     1824   1314   1118   -234    -42    186       C  
ATOM   5225  CG  LEU B  36       5.372   9.926  74.199  1.00 14.96           C  
ANISOU 5225  CG  LEU B  36     2315   1787   1581   -291    -42    217       C  
ATOM   5226  CD1 LEU B  36       4.120  10.336  73.437  1.00 14.10           C  
ANISOU 5226  CD1 LEU B  36     2173   1687   1499   -333    -49    214       C  
ATOM   5227  CD2 LEU B  36       5.697   8.457  73.950  1.00 11.94           C  
ANISOU 5227  CD2 LEU B  36     2014   1343   1181   -299    -56    245       C  
ATOM   5228  N   GLU B  37       9.965  11.281  73.831  1.00 10.89           N  
ANISOU 5228  N   GLU B  37     1791   1273   1075   -109    -47    171       N  
ATOM   5229  CA  GLU B  37      11.045  12.214  73.537  1.00 10.64           C  
ANISOU 5229  CA  GLU B  37     1726   1262   1055    -72    -48    153       C  
ATOM   5230  C   GLU B  37      11.520  12.074  72.079  1.00 10.53           C  
ANISOU 5230  C   GLU B  37     1734   1208   1060    -50    -45    142       C  
ATOM   5231  O   GLU B  37      11.751  10.963  71.594  1.00 10.79           O  
ANISOU 5231  O   GLU B  37     1819   1192   1089    -35    -41    158       O  
ATOM   5232  CB  GLU B  37      12.212  12.002  74.509  1.00 10.86           C  
ANISOU 5232  CB  GLU B  37     1747   1313   1067    -39    -55    176       C  
ATOM   5233  CG  GLU B  37      13.525  12.704  74.120  1.00 10.75           C  
ANISOU 5233  CG  GLU B  37     1699   1318   1066      0    -60    169       C  
ATOM   5234  CD  GLU B  37      13.368  14.196  73.835  1.00 18.48           C  
ANISOU 5234  CD  GLU B  37     2637   2328   2056    -17    -62    133       C  
ATOM   5235  OE1 GLU B  37      12.625  14.862  74.589  1.00 12.26           O  
ANISOU 5235  OE1 GLU B  37     1835   1568   1257    -47    -62    118       O  
ATOM   5236  OE2 GLU B  37      13.986  14.709  72.852  1.00 14.82           O  
ANISOU 5236  OE2 GLU B  37     2160   1859   1610      0    -60    119       O  
ATOM   5237  N   ALA B  38      11.673  13.211  71.403  1.00 10.22           N  
ANISOU 5237  N   ALA B  38     1661   1184   1037    -48    -46    114       N  
ATOM   5238  CA  ALA B  38      12.049  13.227  69.982  1.00 10.94           C  
ANISOU 5238  CA  ALA B  38     1774   1241   1141    -35    -41    101       C  
ATOM   5239  C   ALA B  38      13.456  12.679  69.782  1.00 16.56           C  
ANISOU 5239  C   ALA B  38     2498   1942   1852     19    -28    116       C  
ATOM   5240  O   ALA B  38      13.746  12.052  68.767  1.00 11.72           O  
ANISOU 5240  O   ALA B  38     1929   1284   1239     37    -13    115       O  
ATOM   5241  CB  ALA B  38      11.948  14.642  69.416  1.00 10.04           C  
ANISOU 5241  CB  ALA B  38     1621   1151   1043    -47    -47     72       C  
ATOM   5242  N   GLY B  39      14.333  12.934  70.753  1.00 15.85           N  
ANISOU 5242  N   GLY B  39     2369   1894   1759     43    -33    131       N  
ATOM   5243  CA  GLY B  39      15.690  12.424  70.698  1.00 13.92           C  
ANISOU 5243  CA  GLY B  39     2120   1649   1519     98    -23    155       C  
ATOM   5244  C   GLY B  39      15.882  11.177  71.541  1.00 15.85           C  
ANISOU 5244  C   GLY B  39     2395   1876   1753    122    -24    192       C  
ATOM   5245  O   GLY B  39      14.925  10.459  71.823  1.00 14.21           O  
ANISOU 5245  O   GLY B  39     2230   1637   1531     94    -28    196       O  
ATOM   5246  N   HIS B  40      17.129  10.921  71.928  1.00 13.65           N  
ANISOU 5246  N   HIS B  40     2090   1617   1480    171    -24    222       N  
ATOM   5247  CA  HIS B  40      17.485   9.753  72.724  1.00 15.81           C  
ANISOU 5247  CA  HIS B  40     2388   1873   1746    203    -30    264       C  
ATOM   5248  C   HIS B  40      18.547  10.104  73.770  1.00 14.08           C  
ANISOU 5248  C   HIS B  40     2107   1714   1528    224    -54    298       C  
ATOM   5249  O   HIS B  40      18.971  11.256  73.877  1.00 14.31           O  
ANISOU 5249  O   HIS B  40     2080   1798   1562    208    -66    287       O  
ATOM   5250  CB  HIS B  40      17.964   8.616  71.815  1.00 12.44           C  
ANISOU 5250  CB  HIS B  40     2015   1382   1330    260      0    275       C  
ATOM   5251  CG  HIS B  40      18.954   9.045  70.781  1.00 14.81           C  
ANISOU 5251  CG  HIS B  40     2284   1692   1653    305     28    266       C  
ATOM   5252  ND1 HIS B  40      18.600   9.307  69.473  1.00 12.27           N  
ANISOU 5252  ND1 HIS B  40     1993   1338   1332    293     53    229       N  
ATOM   5253  CD2 HIS B  40      20.288   9.273  70.866  1.00 15.86           C  
ANISOU 5253  CD2 HIS B  40     2355   1866   1805    357     34    293       C  
ATOM   5254  CE1 HIS B  40      19.679   9.661  68.792  1.00 16.53           C  
ANISOU 5254  CE1 HIS B  40     2495   1898   1888    337     79    230       C  
ATOM   5255  NE2 HIS B  40      20.714   9.644  69.609  1.00 12.78           N  
ANISOU 5255  NE2 HIS B  40     1959   1469   1428    378     69    270       N  
ATOM   5256  N   SER B  41      18.985   9.118  74.539  1.00 15.72           N  
ANISOU 5256  N   SER B  41     2331   1911   1730    256    -65    343       N  
ATOM   5257  CA  SER B  41      19.973   9.389  75.572  1.00 16.94           C  
ANISOU 5257  CA  SER B  41     2429   2125   1884    270    -96    383       C  
ATOM   5258  C   SER B  41      21.372   9.472  74.982  1.00 19.16           C  
ANISOU 5258  C   SER B  41     2656   2427   2198    334    -85    407       C  
ATOM   5259  O   SER B  41      21.689   8.760  74.029  1.00 16.43           O  
ANISOU 5259  O   SER B  41     2334   2034   1873    389    -49    409       O  
ATOM   5260  CB  SER B  41      19.923   8.318  76.657  1.00 17.47           C  
ANISOU 5260  CB  SER B  41     2531   2174   1932    279   -118    429       C  
ATOM   5261  OG  SER B  41      20.206   7.031  76.132  1.00 17.33           O  
ANISOU 5261  OG  SER B  41     2562   2091   1931    341    -96    453       O  
ATOM   5262  N   HIS B  42      22.206  10.329  75.571  1.00 19.86           N  
ANISOU 5262  N   HIS B  42     2672   2587   2288    323   -116    427       N  
ATOM   5263  CA  HIS B  42      23.601  10.493  75.157  1.00 13.97           C  
ANISOU 5263  CA  HIS B  42     1856   1879   1575    376   -111    460       C  
ATOM   5264  C   HIS B  42      24.541  10.229  76.333  1.00 22.08           C  
ANISOU 5264  C   HIS B  42     2834   2954   2602    393   -157    527       C  
ATOM   5265  O   HIS B  42      25.529  10.959  76.543  1.00 17.24           O  
ANISOU 5265  O   HIS B  42     2142   2408   2000    389   -182    554       O  
ATOM   5266  CB  HIS B  42      23.828  11.904  74.607  1.00 13.58           C  
ANISOU 5266  CB  HIS B  42     1754   1875   1529    336   -111    428       C  
ATOM   5267  CG  HIS B  42      23.193  12.142  73.266  1.00 13.53           C  
ANISOU 5267  CG  HIS B  42     1784   1827   1531    332    -67    374       C  
ATOM   5268  ND1 HIS B  42      23.921  12.526  72.155  1.00 13.18           N  
ANISOU 5268  ND1 HIS B  42     1704   1793   1510    359    -35    368       N  
ATOM   5269  CD2 HIS B  42      21.909  12.033  72.854  1.00 12.62           C  
ANISOU 5269  CD2 HIS B  42     1736   1658   1400    300    -51    329       C  
ATOM   5270  CE1 HIS B  42      23.111  12.657  71.123  1.00 16.81           C  
ANISOU 5270  CE1 HIS B  42     2215   2208   1966    343     -4    320       C  
ATOM   5271  NE2 HIS B  42      21.880  12.363  71.519  1.00 12.40           N  
ANISOU 5271  NE2 HIS B  42     1717   1610   1385    307    -16    296       N  
ATOM   5272  N   PHE B  43      24.243   9.162  77.078  1.00 17.93           N  
ANISOU 5272  N   PHE B  43     2356   2392   2063    410   -170    557       N  
ATOM   5273  CA  PHE B  43      24.979   8.826  78.288  1.00 16.26           C  
ANISOU 5273  CA  PHE B  43     2113   2221   1845    420   -221    624       C  
ATOM   5274  C   PHE B  43      26.365   8.303  77.947  1.00 16.36           C  
ANISOU 5274  C   PHE B  43     2061   2251   1906    508   -214    684       C  
ATOM   5275  O   PHE B  43      27.231   8.255  78.810  1.00 17.04           O  
ANISOU 5275  O   PHE B  43     2092   2388   1996    518   -262    747       O  
ATOM   5276  CB  PHE B  43      24.229   7.759  79.111  1.00 20.58           C  
ANISOU 5276  CB  PHE B  43     2738   2719   2365    414   -234    642       C  
ATOM   5277  CG  PHE B  43      22.879   8.206  79.631  1.00 15.18           C  
ANISOU 5277  CG  PHE B  43     2108   2028   1632    328   -240    594       C  
ATOM   5278  CD1 PHE B  43      22.600   9.555  79.827  1.00 20.05           C  
ANISOU 5278  CD1 PHE B  43     2695   2695   2227    261   -253    554       C  
ATOM   5279  CD2 PHE B  43      21.895   7.265  79.931  1.00 15.19           C  
ANISOU 5279  CD2 PHE B  43     2190   1971   1611    315   -231    592       C  
ATOM   5280  CE1 PHE B  43      21.364   9.964  80.317  1.00 17.70           C  
ANISOU 5280  CE1 PHE B  43     2443   2392   1889    192   -251    511       C  
ATOM   5281  CE2 PHE B  43      20.656   7.661  80.420  1.00 18.80           C  
ANISOU 5281  CE2 PHE B  43     2687   2429   2028    239   -231    553       C  
ATOM   5282  CZ  PHE B  43      20.381   9.006  80.613  1.00 14.28           C  
ANISOU 5282  CZ  PHE B  43     2080   1908   1436    182   -238    512       C  
ATOM   5283  N   ASN B  44      26.573   7.907  76.691  1.00 16.41           N  
ANISOU 5283  N   ASN B  44     2075   2215   1946    573   -154    667       N  
ATOM   5284  CA  ASN B  44      27.881   7.390  76.264  1.00 17.24           C  
ANISOU 5284  CA  ASN B  44     2115   2334   2100    669   -133    722       C  
ATOM   5285  C   ASN B  44      28.528   8.331  75.253  1.00 23.45           C  
ANISOU 5285  C   ASN B  44     2830   3168   2912    673   -100    702       C  
ATOM   5286  O   ASN B  44      29.454   7.959  74.531  1.00 17.71           O  
ANISOU 5286  O   ASN B  44     2057   2445   2226    756    -58    730       O  
ATOM   5287  CB  ASN B  44      27.745   5.995  75.644  1.00 17.66           C  
ANISOU 5287  CB  ASN B  44     2244   2294   2171    756    -81    725       C  
ATOM   5288  CG  ASN B  44      27.249   4.950  76.640  1.00 48.51           C  
ANISOU 5288  CG  ASN B  44     6222   6152   6057    758   -114    757       C  
ATOM   5289  OD1 ASN B  44      26.217   4.315  76.421  1.00 53.78           O  
ANISOU 5289  OD1 ASN B  44     6992   6741   6702    742    -94    721       O  
ATOM   5290  ND2 ASN B  44      27.982   4.771  77.739  1.00 43.62           N  
ANISOU 5290  ND2 ASN B  44     5550   5580   5444    772   -170    829       N  
ATOM   5291  N   ASP B  45      28.033   9.562  75.232  1.00 19.02           N  
ANISOU 5291  N   ASP B  45     2260   2642   2324    585   -119    655       N  
ATOM   5292  CA  ASP B  45      28.471  10.571  74.276  1.00 20.62           C  
ANISOU 5292  CA  ASP B  45     2407   2884   2542    571    -93    629       C  
ATOM   5293  C   ASP B  45      29.295  11.641  74.982  1.00 19.84           C  
ANISOU 5293  C   ASP B  45     2214   2883   2442    518   -151    665       C  
ATOM   5294  O   ASP B  45      28.745  12.481  75.689  1.00 19.37           O  
ANISOU 5294  O   ASP B  45     2170   2844   2344    433   -197    641       O  
ATOM   5295  CB  ASP B  45      27.257  11.189  73.587  1.00 17.59           C  
ANISOU 5295  CB  ASP B  45     2093   2460   2131    510    -70    548       C  
ATOM   5296  CG  ASP B  45      27.632  12.216  72.521  1.00 21.21           C  
ANISOU 5296  CG  ASP B  45     2507   2950   2601    491    -42    520       C  
ATOM   5297  OD1 ASP B  45      28.832  12.414  72.231  1.00 17.59           O  
ANISOU 5297  OD1 ASP B  45     1965   2545   2173    527    -32    561       O  
ATOM   5298  OD2 ASP B  45      26.699  12.819  71.963  1.00 18.30           O  
ANISOU 5298  OD2 ASP B  45     2188   2552   2213    440    -30    459       O  
ATOM   5299  N   PRO B  46      30.622  11.611  74.799  1.00 17.14           N  
ANISOU 5299  N   PRO B  46     1775   2599   2140    569   -148    725       N  
ATOM   5300  CA  PRO B  46      31.514  12.553  75.487  1.00 17.50           C  
ANISOU 5300  CA  PRO B  46     1725   2740   2185    515   -211    772       C  
ATOM   5301  C   PRO B  46      31.223  14.015  75.138  1.00 23.21           C  
ANISOU 5301  C   PRO B  46     2443   3492   2883    422   -222    719       C  
ATOM   5302  O   PRO B  46      31.538  14.889  75.939  1.00 16.97           O  
ANISOU 5302  O   PRO B  46     1615   2761   2070    348   -287    738       O  
ATOM   5303  CB  PRO B  46      32.910  12.131  75.009  1.00 23.17           C  
ANISOU 5303  CB  PRO B  46     2338   3506   2960    601   -184    842       C  
ATOM   5304  CG  PRO B  46      32.677  11.424  73.718  1.00 24.33           C  
ANISOU 5304  CG  PRO B  46     2531   3584   3130    683    -90    805       C  
ATOM   5305  CD  PRO B  46      31.350  10.722  73.883  1.00 20.37           C  
ANISOU 5305  CD  PRO B  46     2158   2986   2596    678    -81    753       C  
ATOM   5306  N   VAL B  47      30.631  14.267  73.969  1.00 24.69           N  
ANISOU 5306  N   VAL B  47     2675   3635   3071    424   -163    656       N  
ATOM   5307  CA  VAL B  47      30.222  15.619  73.582  1.00 25.09           C  
ANISOU 5307  CA  VAL B  47     2736   3699   3098    340   -172    603       C  
ATOM   5308  C   VAL B  47      29.269  16.180  74.640  1.00 20.07           C  
ANISOU 5308  C   VAL B  47     2160   3052   2414    259   -227    570       C  
ATOM   5309  O   VAL B  47      29.321  17.354  75.004  1.00 17.93           O  
ANISOU 5309  O   VAL B  47     1875   2818   2118    181   -269    557       O  
ATOM   5310  CB  VAL B  47      29.524  15.633  72.195  1.00 15.10           C  
ANISOU 5310  CB  VAL B  47     1528   2372   1836    357   -103    540       C  
ATOM   5311  CG1 VAL B  47      29.033  17.034  71.845  1.00 18.45           C  
ANISOU 5311  CG1 VAL B  47     1968   2806   2236    271   -118    488       C  
ATOM   5312  CG2 VAL B  47      30.469  15.122  71.089  1.00 15.68           C  
ANISOU 5312  CG2 VAL B  47     1551   2456   1950    437    -38    567       C  
ATOM   5313  N   VAL B  48      28.428  15.299  75.159  1.00 17.13           N  
ANISOU 5313  N   VAL B  48     1856   2626   2026    279   -224    558       N  
ATOM   5314  CA  VAL B  48      27.443  15.648  76.181  1.00 17.15           C  
ANISOU 5314  CA  VAL B  48     1921   2614   1982    213   -263    527       C  
ATOM   5315  C   VAL B  48      27.952  15.458  77.609  1.00 19.70           C  
ANISOU 5315  C   VAL B  48     2221   2981   2283    192   -327    583       C  
ATOM   5316  O   VAL B  48      27.846  16.359  78.442  1.00 21.88           O  
ANISOU 5316  O   VAL B  48     2504   3290   2520    117   -376    574       O  
ATOM   5317  CB  VAL B  48      26.160  14.791  75.999  1.00 17.65           C  
ANISOU 5317  CB  VAL B  48     2074   2598   2036    236   -225    486       C  
ATOM   5318  CG1 VAL B  48      25.246  14.903  77.212  1.00 16.03           C  
ANISOU 5318  CG1 VAL B  48     1923   2385   1784    180   -260    470       C  
ATOM   5319  CG2 VAL B  48      25.457  15.165  74.694  1.00 13.47           C  
ANISOU 5319  CG2 VAL B  48     1578   2024   1515    233   -175    425       C  
ATOM   5320  N   THR B  49      28.535  14.297  77.874  1.00 17.85           N  
ANISOU 5320  N   THR B  49     1963   2746   2072    260   -328    643       N  
ATOM   5321  CA  THR B  49      28.828  13.895  79.240  1.00 23.24           C  
ANISOU 5321  CA  THR B  49     2642   3458   2732    245   -389    697       C  
ATOM   5322  C   THR B  49      30.003  14.657  79.795  1.00 26.31           C  
ANISOU 5322  C   THR B  49     2945   3933   3119    203   -453    752       C  
ATOM   5323  O   THR B  49      30.066  14.892  80.994  1.00 26.66           O  
ANISOU 5323  O   THR B  49     3001   4009   3121    146   -517    777       O  
ATOM   5324  CB  THR B  49      29.129  12.394  79.339  1.00 31.02           C  
ANISOU 5324  CB  THR B  49     3630   4411   3746    334   -375    751       C  
ATOM   5325  OG1 THR B  49      30.314  12.100  78.588  1.00 41.92           O  
ANISOU 5325  OG1 THR B  49     4924   5820   5183    409   -352    800       O  
ATOM   5326  CG2 THR B  49      27.966  11.585  78.794  1.00 21.63           C  
ANISOU 5326  CG2 THR B  49     2533   3132   2554    366   -318    700       C  
ATOM   5327  N   ASP B  50      30.951  15.014  78.930  1.00 17.16           N  
ANISOU 5327  N   ASP B  50     1704   2815   2003    229   -435    775       N  
ATOM   5328  CA  ASP B  50      32.054  15.866  79.351  1.00 18.83           C  
ANISOU 5328  CA  ASP B  50     1827   3113   2213    176   -497    826       C  
ATOM   5329  C   ASP B  50      31.599  17.307  79.178  1.00 17.18           C  
ANISOU 5329  C   ASP B  50     1650   2911   1967     81   -508    762       C  
ATOM   5330  O   ASP B  50      31.246  17.727  78.071  1.00 19.58           O  
ANISOU 5330  O   ASP B  50     1966   3186   2287     89   -453    710       O  
ATOM   5331  CB  ASP B  50      33.329  15.565  78.560  1.00 18.48           C  
ANISOU 5331  CB  ASP B  50     1671   3118   2233    246   -473    889       C  
ATOM   5332  CG  ASP B  50      34.525  16.391  79.024  1.00 30.01           C  
ANISOU 5332  CG  ASP B  50     3029   4678   3696    186   -544    955       C  
ATOM   5333  OD1 ASP B  50      34.333  17.402  79.721  1.00 28.72           O  
ANISOU 5333  OD1 ASP B  50     2894   4538   3481     81   -604    936       O  
ATOM   5334  OD2 ASP B  50      35.675  16.020  78.709  1.00 31.67           O  
ANISOU 5334  OD2 ASP B  50     3131   4944   3959    243   -539   1030       O  
ATOM   5335  N   PRO B  51      31.563  18.059  80.291  1.00 17.33           N  
ANISOU 5335  N   PRO B  51     1692   2960   1932     -9   -579    765       N  
ATOM   5336  CA  PRO B  51      31.104  19.451  80.258  1.00 18.73           C  
ANISOU 5336  CA  PRO B  51     1913   3134   2069   -100   -592    703       C  
ATOM   5337  C   PRO B  51      31.877  20.297  79.248  1.00 16.97           C  
ANISOU 5337  C   PRO B  51     1620   2950   1878   -117   -582    709       C  
ATOM   5338  O   PRO B  51      31.326  21.217  78.665  1.00 18.48           O  
ANISOU 5338  O   PRO B  51     1852   3113   2055   -157   -560    646       O  
ATOM   5339  CB  PRO B  51      31.368  19.939  81.688  1.00 17.40           C  
ANISOU 5339  CB  PRO B  51     1763   3007   1841   -185   -679    732       C  
ATOM   5340  CG  PRO B  51      31.318  18.701  82.516  1.00 19.78           C  
ANISOU 5340  CG  PRO B  51     2076   3302   2139   -139   -694    778       C  
ATOM   5341  CD  PRO B  51      31.939  17.638  81.657  1.00 18.01           C  
ANISOU 5341  CD  PRO B  51     1775   3079   1988    -32   -650    826       C  
ATOM   5342  N   MET B  52      33.152  19.985  79.057  1.00 19.28           N  
ANISOU 5342  N   MET B  52     1804   3309   2213    -87   -598    788       N  
ATOM   5343  CA  MET B  52      33.964  20.737  78.125  1.00 17.98           C  
ANISOU 5343  CA  MET B  52     1563   3190   2078   -105   -587    803       C  
ATOM   5344  C   MET B  52      33.569  20.429  76.680  1.00 25.63           C  
ANISOU 5344  C   MET B  52     2540   4111   3086    -33   -492    758       C  
ATOM   5345  O   MET B  52      33.953  21.154  75.768  1.00 23.21           O  
ANISOU 5345  O   MET B  52     2196   3826   2795    -55   -470    749       O  
ATOM   5346  CB  MET B  52      35.452  20.453  78.359  1.00 19.10           C  
ANISOU 5346  CB  MET B  52     1574   3425   2257    -91   -629    908       C  
ATOM   5347  CG  MET B  52      35.940  20.901  79.728  1.00 19.76           C  
ANISOU 5347  CG  MET B  52     1647   3564   2296   -181   -734    959       C  
ATOM   5348  SD  MET B  52      35.431  22.611  80.043  1.00 24.03           S  
ANISOU 5348  SD  MET B  52     2274   4093   2764   -325   -782    890       S  
ATOM   5349  CE  MET B  52      36.520  23.468  78.909  1.00 32.62           C  
ANISOU 5349  CE  MET B  52     3253   5246   3893   -356   -773    923       C  
ATOM   5350  N   GLY B  53      32.802  19.360  76.482  1.00 23.91           N  
ANISOU 5350  N   GLY B  53     2377   3827   2880     45   -440    731       N  
ATOM   5351  CA  GLY B  53      32.274  19.018  75.171  1.00 16.48           C  
ANISOU 5351  CA  GLY B  53     1467   2830   1966    106   -355    681       C  
ATOM   5352  C   GLY B  53      31.417  20.134  74.604  1.00 20.95           C  
ANISOU 5352  C   GLY B  53     2098   3359   2504     40   -342    603       C  
ATOM   5353  O   GLY B  53      31.315  20.312  73.385  1.00 15.42           O  
ANISOU 5353  O   GLY B  53     1400   2637   1823     61   -287    573       O  
ATOM   5354  N   PHE B  54      30.803  20.890  75.503  1.00 15.42           N  
ANISOU 5354  N   PHE B  54     1454   2649   1755    -37   -394    572       N  
ATOM   5355  CA  PHE B  54      30.041  22.078  75.140  1.00 14.81           C  
ANISOU 5355  CA  PHE B  54     1437   2539   1651   -103   -393    504       C  
ATOM   5356  C   PHE B  54      30.873  23.050  74.305  1.00 15.05           C  
ANISOU 5356  C   PHE B  54     1410   2612   1696   -142   -395    517       C  
ATOM   5357  O   PHE B  54      30.368  23.655  73.362  1.00 23.78           O  
ANISOU 5357  O   PHE B  54     2551   3682   2803   -155   -361    467       O  
ATOM   5358  CB  PHE B  54      29.542  22.783  76.404  1.00 14.76           C  
ANISOU 5358  CB  PHE B  54     1490   2530   1589   -179   -452    482       C  
ATOM   5359  CG  PHE B  54      28.887  24.099  76.140  1.00 20.39           C  
ANISOU 5359  CG  PHE B  54     2262   3211   2274   -245   -457    419       C  
ATOM   5360  CD1 PHE B  54      27.529  24.167  75.878  1.00 13.60           C  
ANISOU 5360  CD1 PHE B  54     1482   2280   1404   -232   -419    350       C  
ATOM   5361  CD2 PHE B  54      29.638  25.278  76.137  1.00 20.30           C  
ANISOU 5361  CD2 PHE B  54     2224   3240   2248   -322   -502    432       C  
ATOM   5362  CE1 PHE B  54      26.932  25.377  75.632  1.00 13.27           C  
ANISOU 5362  CE1 PHE B  54     1493   2207   1341   -284   -422    295       C  
ATOM   5363  CE2 PHE B  54      29.039  26.493  75.877  1.00 18.19           C  
ANISOU 5363  CE2 PHE B  54     2020   2936   1956   -379   -506    375       C  
ATOM   5364  CZ  PHE B  54      27.684  26.543  75.627  1.00 13.64           C  
ANISOU 5364  CZ  PHE B  54     1522   2287   1373   -355   -465    306       C  
ATOM   5365  N   PHE B  55      32.141  23.216  74.687  1.00 17.92           N  
ANISOU 5365  N   PHE B  55     1686   3055   2069   -167   -438    587       N  
ATOM   5366  CA  PHE B  55      33.049  24.144  74.011  1.00 23.04           C  
ANISOU 5366  CA  PHE B  55     2269   3756   2729   -216   -447    612       C  
ATOM   5367  C   PHE B  55      33.736  23.557  72.770  1.00 23.83           C  
ANISOU 5367  C   PHE B  55     2292   3879   2881   -142   -378    642       C  
ATOM   5368  O   PHE B  55      34.552  24.220  72.131  1.00 20.36           O  
ANISOU 5368  O   PHE B  55     1789   3491   2455   -176   -375    670       O  
ATOM   5369  CB  PHE B  55      34.102  24.641  75.008  1.00 24.80           C  
ANISOU 5369  CB  PHE B  55     2428   4060   2936   -288   -532    679       C  
ATOM   5370  CG  PHE B  55      33.515  25.404  76.162  1.00 23.86           C  
ANISOU 5370  CG  PHE B  55     2394   3918   2755   -375   -599    646       C  
ATOM   5371  CD1 PHE B  55      33.056  26.698  75.983  1.00 21.92           C  
ANISOU 5371  CD1 PHE B  55     2215   3641   2473   -455   -616    591       C  
ATOM   5372  CD2 PHE B  55      33.399  24.824  77.413  1.00 23.44           C  
ANISOU 5372  CD2 PHE B  55     2361   3870   2676   -373   -642    668       C  
ATOM   5373  CE1 PHE B  55      32.501  27.402  77.026  1.00 20.96           C  
ANISOU 5373  CE1 PHE B  55     2180   3491   2292   -527   -668    555       C  
ATOM   5374  CE2 PHE B  55      32.851  25.530  78.472  1.00 21.55           C  
ANISOU 5374  CE2 PHE B  55     2208   3607   2372   -452   -697    633       C  
ATOM   5375  CZ  PHE B  55      32.401  26.817  78.280  1.00 20.82           C  
ANISOU 5375  CZ  PHE B  55     2183   3482   2245   -527   -707    575       C  
ATOM   5376  N   GLY B  56      33.406  22.318  72.430  1.00 21.62           N  
ANISOU 5376  N   GLY B  56     2025   3561   2628    -42   -319    638       N  
ATOM   5377  CA  GLY B  56      33.852  21.745  71.175  1.00 21.82           C  
ANISOU 5377  CA  GLY B  56     2007   3589   2695     34   -240    649       C  
ATOM   5378  C   GLY B  56      34.989  20.762  71.288  1.00 23.36           C  
ANISOU 5378  C   GLY B  56     2100   3842   2935    113   -222    731       C  
ATOM   5379  O   GLY B  56      35.549  20.360  70.272  1.00 19.37           O  
ANISOU 5379  O   GLY B  56     1546   3350   2463    177   -153    748       O  
ATOM   5380  N   LYS B  57      35.284  20.343  72.522  1.00 22.59           N  
ANISOU 5380  N   LYS B  57     1974   3773   2835    114   -282    779       N  
ATOM   5381  CA  LYS B  57      36.400  19.450  72.837  1.00 26.13           C  
ANISOU 5381  CA  LYS B  57     2318   4282   3328    186   -283    869       C  
ATOM   5382  C   LYS B  57      36.408  18.176  71.997  1.00 29.01           C  
ANISOU 5382  C   LYS B  57     2685   4603   3733    316   -190    869       C  
ATOM   5383  O   LYS B  57      37.476  17.656  71.664  1.00 28.02           O  
ANISOU 5383  O   LYS B  57     2460   4532   3656    388   -156    935       O  
ATOM   5384  CB  LYS B  57      36.365  19.080  74.328  1.00 22.43           C  
ANISOU 5384  CB  LYS B  57     1857   3825   2840    168   -363    906       C  
ATOM   5385  CG  LYS B  57      37.521  18.206  74.797  1.00 22.98           C  
ANISOU 5385  CG  LYS B  57     1815   3960   2956    238   -380   1009       C  
ATOM   5386  CD  LYS B  57      37.517  18.111  76.309  1.00 20.57           C  
ANISOU 5386  CD  LYS B  57     1521   3675   2620    190   -476   1048       C  
ATOM   5387  CE  LYS B  57      38.416  17.015  76.814  1.00 21.61           C  
ANISOU 5387  CE  LYS B  57     1564   3849   2799    276   -492   1144       C  
ATOM   5388  NZ  LYS B  57      38.209  16.824  78.295  1.00 21.79           N  
ANISOU 5388  NZ  LYS B  57     1623   3874   2780    229   -585   1174       N  
ATOM   5389  N   TYR B  58      35.220  17.670  71.669  1.00 22.31           N  
ANISOU 5389  N   TYR B  58     1954   3658   2866    346   -148    796       N  
ATOM   5390  CA  TYR B  58      35.109  16.433  70.906  1.00 28.14           C  
ANISOU 5390  CA  TYR B  58     2720   4339   3632    462    -64    789       C  
ATOM   5391  C   TYR B  58      34.480  16.651  69.530  1.00 34.58           C  
ANISOU 5391  C   TYR B  58     3604   5097   4436    466     11    716       C  
ATOM   5392  O   TYR B  58      33.978  15.707  68.925  1.00 39.25           O  
ANISOU 5392  O   TYR B  58     4265   5616   5032    538     74    685       O  
ATOM   5393  CB  TYR B  58      34.301  15.392  71.677  1.00 24.78           C  
ANISOU 5393  CB  TYR B  58     2376   3843   3194    501    -78    776       C  
ATOM   5394  CG  TYR B  58      34.892  15.054  73.018  1.00 25.92           C  
ANISOU 5394  CG  TYR B  58     2464   4038   3347    503   -151    851       C  
ATOM   5395  CD1 TYR B  58      35.909  14.108  73.133  1.00 28.44           C  
ANISOU 5395  CD1 TYR B  58     2701   4389   3714    600   -135    930       C  
ATOM   5396  CD2 TYR B  58      34.442  15.679  74.171  1.00 26.38           C  
ANISOU 5396  CD2 TYR B  58     2551   4110   3362    409   -236    844       C  
ATOM   5397  CE1 TYR B  58      36.460  13.799  74.355  1.00 32.79           C  
ANISOU 5397  CE1 TYR B  58     3198   4987   4273    599   -209   1004       C  
ATOM   5398  CE2 TYR B  58      34.990  15.373  75.398  1.00 28.77           C  
ANISOU 5398  CE2 TYR B  58     2808   4459   3665    404   -307    913       C  
ATOM   5399  CZ  TYR B  58      35.992  14.433  75.486  1.00 32.31           C  
ANISOU 5399  CZ  TYR B  58     3173   4941   4164    496   -297    996       C  
ATOM   5400  OH  TYR B  58      36.527  14.131  76.715  1.00 39.13           O  
ANISOU 5400  OH  TYR B  58     3991   5850   5027    488   -375   1071       O  
ATOM   5401  N   ASN B  59      34.491  17.889  69.045  1.00 30.19           N  
ANISOU 5401  N   ASN B  59     3037   4571   3863    383      0    691       N  
ATOM   5402  CA  ASN B  59      34.005  18.165  67.693  1.00 31.37           C  
ANISOU 5402  CA  ASN B  59     3244   4674   4001    382     66    631       C  
ATOM   5403  C   ASN B  59      34.914  17.579  66.620  1.00 26.01           C  
ANISOU 5403  C   ASN B  59     2510   4016   3356    468    155    661       C  
ATOM   5404  O   ASN B  59      36.113  17.828  66.627  1.00 26.59           O  
ANISOU 5404  O   ASN B  59     2467   4177   3459    476    158    726       O  
ATOM   5405  CB  ASN B  59      33.882  19.672  67.457  1.00 27.49           C  
ANISOU 5405  CB  ASN B  59     2751   4211   3483    271     29    605       C  
ATOM   5406  CG  ASN B  59      32.754  20.298  68.231  1.00 27.28           C  
ANISOU 5406  CG  ASN B  59     2806   4142   3418    194    -37    555       C  
ATOM   5407  OD1 ASN B  59      32.094  19.645  69.051  1.00 25.71           O  
ANISOU 5407  OD1 ASN B  59     2656   3902   3209    214    -60    544       O  
ATOM   5408  ND2 ASN B  59      32.539  21.586  67.999  1.00 21.43           N  
ANISOU 5408  ND2 ASN B  59     2080   3409   2653    105    -67    526       N  
ATOM   5409  N   PRO B  60      34.350  16.825  65.671  1.00 30.31           N  
ANISOU 5409  N   PRO B  60     3139   4482   3894    530    231    615       N  
ATOM   5410  CA  PRO B  60      35.223  16.501  64.542  1.00 32.07           C  
ANISOU 5410  CA  PRO B  60     3316   4729   4140    599    323    635       C  
ATOM   5411  C   PRO B  60      35.628  17.790  63.842  1.00 31.22           C  
ANISOU 5411  C   PRO B  60     3161   4680   4021    519    324    632       C  
ATOM   5412  O   PRO B  60      34.771  18.630  63.604  1.00 37.51           O  
ANISOU 5412  O   PRO B  60     4029   5443   4781    434    293    577       O  
ATOM   5413  CB  PRO B  60      34.349  15.615  63.651  1.00 34.00           C  
ANISOU 5413  CB  PRO B  60     3688   4867   4364    655    392    573       C  
ATOM   5414  CG  PRO B  60      32.948  15.840  64.110  1.00 33.77           C  
ANISOU 5414  CG  PRO B  60     3762   4770   4298    586    332    514       C  
ATOM   5415  CD  PRO B  60      33.028  16.187  65.565  1.00 33.61           C  
ANISOU 5415  CD  PRO B  60     3690   4796   4286    542    241    550       C  
ATOM   5416  N   PRO B  61      36.924  17.951  63.543  1.00 30.73           N  
ANISOU 5416  N   PRO B  61     2978   4707   3990    544    359    696       N  
ATOM   5417  CA  PRO B  61      37.541  19.153  62.960  1.00 30.07           C  
ANISOU 5417  CA  PRO B  61     2829   4697   3901    466    359    712       C  
ATOM   5418  C   PRO B  61      36.943  19.589  61.623  1.00 34.42           C  
ANISOU 5418  C   PRO B  61     3469   5195   4414    435    415    645       C  
ATOM   5419  O   PRO B  61      37.031  20.769  61.270  1.00 29.36           O  
ANISOU 5419  O   PRO B  61     2813   4589   3753    341    390    640       O  
ATOM   5420  CB  PRO B  61      39.009  18.748  62.781  1.00 32.12           C  
ANISOU 5420  CB  PRO B  61     2946   5049   4209    540    414    795       C  
ATOM   5421  CG  PRO B  61      39.022  17.265  62.872  1.00 34.62           C  
ANISOU 5421  CG  PRO B  61     3285   5315   4553    674    471    804       C  
ATOM   5422  CD  PRO B  61      37.919  16.902  63.805  1.00 33.11           C  
ANISOU 5422  CD  PRO B  61     3193   5047   4342    657    401    765       C  
ATOM   5423  N   ASN B  62      36.379  18.646  60.875  1.00 35.61           N  
ANISOU 5423  N   ASN B  62     3714   5262   4552    510    489    599       N  
ATOM   5424  CA  ASN B  62      35.777  18.962  59.579  1.00 39.90           C  
ANISOU 5424  CA  ASN B  62     4354   5751   5056    481    540    538       C  
ATOM   5425  C   ASN B  62      34.302  19.336  59.733  1.00 31.39           C  
ANISOU 5425  C   ASN B  62     3398   4589   3939    411    478    468       C  
ATOM   5426  O   ASN B  62      33.701  19.900  58.829  1.00 23.53           O  
ANISOU 5426  O   ASN B  62     2476   3556   2909    358    489    421       O  
ATOM   5427  CB  ASN B  62      35.940  17.787  58.603  1.00 50.08           C  
ANISOU 5427  CB  ASN B  62     5693   6993   6345    592    654    523       C  
ATOM   5428  CG  ASN B  62      35.646  16.442  59.251  1.00 60.76           C  
ANISOU 5428  CG  ASN B  62     7086   8285   7716    687    661    524       C  
ATOM   5429  OD1 ASN B  62      35.969  16.215  60.423  1.00 62.56           O  
ANISOU 5429  OD1 ASN B  62     7244   8549   7977    705    606    570       O  
ATOM   5430  ND2 ASN B  62      35.026  15.542  58.492  1.00 62.57           N  
ANISOU 5430  ND2 ASN B  62     7434   8419   7919    742    724    474       N  
ATOM   5431  N   GLU B  63      33.721  19.014  60.884  1.00 27.02           N  
ANISOU 5431  N   GLU B  63     2864   4009   3394    411    412    465       N  
ATOM   5432  CA  GLU B  63      32.365  19.457  61.188  1.00 22.54           C  
ANISOU 5432  CA  GLU B  63     2393   3377   2796    342    349    408       C  
ATOM   5433  C   GLU B  63      32.339  20.068  62.575  1.00 22.20           C  
ANISOU 5433  C   GLU B  63     2302   3373   2760    286    256    431       C  
ATOM   5434  O   GLU B  63      31.712  19.539  63.506  1.00 23.22           O  
ANISOU 5434  O   GLU B  63     2466   3467   2890    300    217    422       O  
ATOM   5435  CB  GLU B  63      31.363  18.314  61.056  1.00 20.02           C  
ANISOU 5435  CB  GLU B  63     2182   2960   2464    397    374    365       C  
ATOM   5436  CG  GLU B  63      31.278  17.810  59.636  1.00 24.17           C  
ANISOU 5436  CG  GLU B  63     2778   3437   2969    437    460    334       C  
ATOM   5437  CD  GLU B  63      30.123  16.869  59.394  1.00 26.10           C  
ANISOU 5437  CD  GLU B  63     3148   3579   3191    462    473    285       C  
ATOM   5438  OE1 GLU B  63      29.358  16.580  60.348  1.00 25.19           O  
ANISOU 5438  OE1 GLU B  63     3061   3433   3079    451    416    277       O  
ATOM   5439  OE2 GLU B  63      29.980  16.427  58.229  1.00 22.27           O  
ANISOU 5439  OE2 GLU B  63     2736   3044   2681    488    539    256       O  
ATOM   5440  N   ASN B  64      33.030  21.197  62.691  1.00 17.56           N  
ANISOU 5440  N   ASN B  64     1640   2858   2174    217    220    460       N  
ATOM   5441  CA  ASN B  64      33.254  21.855  63.967  1.00 17.01           C  
ANISOU 5441  CA  ASN B  64     1518   2836   2107    157    133    490       C  
ATOM   5442  C   ASN B  64      32.114  22.795  64.305  1.00 18.31           C  
ANISOU 5442  C   ASN B  64     1765   2953   2239     72     71    435       C  
ATOM   5443  O   ASN B  64      32.202  24.017  64.127  1.00 17.93           O  
ANISOU 5443  O   ASN B  64     17