CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  6pdb  ***

elNémo ID: 211018163851110526

Job options:

ID        	=	 211018163851110526
JOBID     	=	 6pdb
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 6pdb

HEADER    IMMUNE SYSTEM                           03-DEC-18   6N9O              
TITLE     CRYSTAL STRUCTURE OF HUMAN GSDMD                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GASDERMIN-D;                                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: GASDERMIN DOMAIN-CONTAINING PROTEIN 1;                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSDMD, DFNA5L, GSDMDC1, FKSG10;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PYROPTOSIS, GASDERMIN D, INFLAMMASOME, AUTOINHIBITION, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LIU,C.WANG,J.YANG,T.S.XIAO                                          
REVDAT   3   11-DEC-19 6N9O    1       REMARK                                   
REVDAT   2   31-JUL-19 6N9O    1       JRNL                                     
REVDAT   1   05-JUN-19 6N9O    0                                                
JRNL        AUTH   Z.LIU,C.WANG,J.YANG,B.ZHOU,R.YANG,R.RAMACHANDRAN,D.W.ABBOTT, 
JRNL        AUTH 2 T.S.XIAO                                                     
JRNL        TITL   CRYSTAL STRUCTURES OF THE FULL-LENGTH MURINE AND HUMAN       
JRNL        TITL 2 GASDERMIN D REVEAL MECHANISMS OF AUTOINHIBITION, LIPID       
JRNL        TITL 3 BINDING, AND OLIGOMERIZATION.                                
JRNL        REF    IMMUNITY                      V.  51    43 2019              
JRNL        REFN                   ISSN 1074-7613                               
JRNL        PMID   31097341                                                     
JRNL        DOI    10.1016/J.IMMUNI.2019.04.017                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.15.2_3472: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 23223                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.280                           
REMARK   3   R VALUE            (WORKING SET) : 0.276                           
REMARK   3   FREE R VALUE                     : 0.345                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1115                            
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 49.4876 -  6.9945    0.98     2809   131  0.1991 0.2543        
REMARK   3     2  6.9945 -  5.5541    0.99     2827   103  0.3277 0.4416        
REMARK   3     3  5.5541 -  4.8527    1.00     2741   159  0.2899 0.4041        
REMARK   3     4  4.8527 -  4.4093    1.00     2783   139  0.2994 0.3607        
REMARK   3     5  4.4093 -  4.0935    0.99     2753   157  0.3118 0.3609        
REMARK   3     6  4.0935 -  3.8522    0.99     2699   149  0.3869 0.4820        
REMARK   3     7  3.8522 -  3.6594    0.99     2704   134  0.3921 0.4870        
REMARK   3     8  3.6594 -  3.5001    0.99     2792   143  0.4021 0.4266        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.750            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 45.030           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 153.7                          
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      :  0.004          11809                                  
REMARK   3   ANGLE     :  0.891          16050                                  
REMARK   3   CHIRALITY :  0.047           1878                                  
REMARK   3   PLANARITY :  0.005           2072                                  
REMARK   3   DIHEDRAL  : 17.963           7167                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 286 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6291 -38.0854 -24.7020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8720 T22:   0.7273                                     
REMARK   3      T33:   0.9886 T12:  -0.0578                                     
REMARK   3      T13:   0.0931 T23:  -0.1314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8905 L22:  -2.5297                                     
REMARK   3      L33:  -0.6219 L12:   0.8138                                     
REMARK   3      L13:   3.9341 L23:  -1.4762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2788 S12:   0.6078 S13:   0.6447                       
REMARK   3      S21:   0.6404 S22:   0.2406 S23:   0.0690                       
REMARK   3      S31:   0.1736 S32:   0.2678 S33:  -0.0408                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 287 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5494 -21.2268 -39.8321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1835 T22:   1.5445                                     
REMARK   3      T33:   1.1225 T12:  -0.1767                                     
REMARK   3      T13:   0.0386 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8256 L22:   1.5251                                     
REMARK   3      L33:   3.3183 L12:  -2.5890                                     
REMARK   3      L13:   1.1159 L23:   0.7716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:   1.3097 S13:   0.4849                       
REMARK   3      S21:  -0.4647 S22:   0.1106 S23:  -0.1989                       
REMARK   3      S31:  -0.3729 S32:  -0.0731 S33:  -0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 381 THROUGH 480 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3545 -10.2887 -23.6102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1038 T22:   1.1427                                     
REMARK   3      T33:   1.2085 T12:  -0.2230                                     
REMARK   3      T13:   0.1219 T23:  -0.0574                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3663 L22:   1.6464                                     
REMARK   3      L33:  -0.0284 L12:   3.2727                                     
REMARK   3      L13:   0.2054 L23:   1.7256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5623 S12:  -0.2374 S13:   0.2815                       
REMARK   3      S21:  -0.4355 S22:  -0.6749 S23:   0.3018                       
REMARK   3      S31:   0.4843 S32:   0.5987 S33:  -0.0148                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 146 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3366 -36.4000  77.8056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9060 T22:   1.1930                                     
REMARK   3      T33:   1.0325 T12:   0.4876                                     
REMARK   3      T13:   0.1068 T23:   0.0961                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4839 L22:   1.5281                                     
REMARK   3      L33:  -0.2698 L12:   1.6491                                     
REMARK   3      L13:   3.8962 L23:  -0.6113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5439 S12:  -1.0815 S13:   0.6088                       
REMARK   3      S21:  -0.4691 S22:  -0.2995 S23:  -0.3776                       
REMARK   3      S31:   0.4336 S32:   1.3359 S33:   0.1149                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 147 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1670 -27.7576  83.6270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2483 T22:   1.5046                                     
REMARK   3      T33:   1.0209 T12:   0.4016                                     
REMARK   3      T13:  -0.1689 T23:   0.1833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7964 L22:  -0.6564                                     
REMARK   3      L33:   0.3968 L12:  -2.4332                                     
REMARK   3      L13:   0.5171 L23:  -3.8090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6217 S12:  -0.4637 S13:  -0.3015                       
REMARK   3      S21:  -0.3924 S22:   0.5666 S23:  -0.4655                       
REMARK   3      S31:  -0.7810 S32:   0.7768 S33:   0.0735                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 480 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6378 -13.6815  87.6712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5093 T22:   1.9663                                     
REMARK   3      T33:   1.2236 T12:  -0.0451                                     
REMARK   3      T13:  -0.0069 T23:   0.2551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5434 L22:   2.3826                                     
REMARK   3      L33:   0.0381 L12:   2.2131                                     
REMARK   3      L13:  -1.0115 L23:  -2.6057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3113 S12:  -0.0485 S13:   0.0704                       
REMARK   3      S21:  -0.5775 S22:   0.6039 S23:   0.1115                       
REMARK   3      S31:   0.5473 S32:   0.5616 S33:   0.0120                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 36 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9265 -26.4212  51.7958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9734 T22:   1.5479                                     
REMARK   3      T33:   1.2447 T12:   0.1267                                     
REMARK   3      T13:   0.2054 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0484 L22:   0.4324                                     
REMARK   3      L33:   0.9945 L12:  -0.2060                                     
REMARK   3      L13:  -0.3431 L23:  -0.9784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.8193 S12:  -0.2549 S13:  -0.2573                       
REMARK   3      S21:  -0.8392 S22:  -0.4947 S23:   0.6253                       
REMARK   3      S31:   1.0777 S32:   0.2966 S33:   0.1891                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 37 THROUGH 88 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7647  -9.9192  49.3883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2843 T22:   1.9222                                     
REMARK   3      T33:   1.2028 T12:  -0.3787                                     
REMARK   3      T13:  -0.0209 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2432 L22:   0.7237                                     
REMARK   3      L33:  -0.1569 L12:   2.2703                                     
REMARK   3      L13:   0.9648 L23:   2.5927                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.4011 S12:   0.8110 S13:   0.7752                       
REMARK   3      S21:  -0.6325 S22:   1.2842 S23:   0.3019                       
REMARK   3      S31:  -0.6246 S32:   1.1359 S33:   0.0056                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 89 THROUGH 146 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7654  -7.6639  56.7743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1020 T22:   2.2381                                     
REMARK   3      T33:   1.6349 T12:  -0.4482                                     
REMARK   3      T13:  -0.7955 T23:  -0.2409                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -1.2876 L22:   0.5486                                     
REMARK   3      L33:  -1.0654 L12:  -0.8464                                     
REMARK   3      L13:   0.7393 L23:  -0.3243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3541 S12:  -0.8406 S13:  -0.2596                       
REMARK   3      S21:   2.1977 S22:  -1.9567 S23:   1.1715                       
REMARK   3      S31:  -0.6058 S32:   3.6164 S33:  -0.0577                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 147 THROUGH 223 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0674 -15.7549  49.4887              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3424 T22:   1.9522                                     
REMARK   3      T33:   1.4297 T12:   0.0751                                     
REMARK   3      T13:  -0.1548 T23:   0.5006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.3508 L22:   0.2399                                     
REMARK   3      L33:   0.5611 L12:  -1.3981                                     
REMARK   3      L13:  -0.3647 L23:  -0.4724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3074 S12:  -0.0097 S13:  -0.2611                       
REMARK   3      S21:   0.2877 S22:  -0.0882 S23:   0.1854                       
REMARK   3      S31:  -0.7743 S32:   2.1394 S33:  -0.0336                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 224 THROUGH 286 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1551  -5.0866  55.1734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2183 T22:   0.5815                                     
REMARK   3      T33:   1.4272 T12:  -0.5361                                     
REMARK   3      T13:   0.0193 T23:  -0.1020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2612 L22:   0.6879                                     
REMARK   3      L33:   1.1507 L12:  -1.2282                                     
REMARK   3      L13:   0.0483 L23:  -0.0382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.9389 S12:  -3.7957 S13:   1.4687                       
REMARK   3      S21:  -0.4378 S22:   0.1337 S23:   0.1675                       
REMARK   3      S31:   0.9187 S32:  -0.3494 S33:  -0.2766                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 287 THROUGH 321 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2209 -23.7132  36.7303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4041 T22:   1.2186                                     
REMARK   3      T33:   1.1974 T12:  -0.1576                                     
REMARK   3      T13:  -0.0324 T23:   0.2242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8068 L22:  -0.2940                                     
REMARK   3      L33:   1.2231 L12:  -0.6193                                     
REMARK   3      L13:   0.6020 L23:  -0.1142                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2353 S12:   0.0053 S13:  -0.4441                       
REMARK   3      S21:  -0.7164 S22:   0.3332 S23:   0.5275                       
REMARK   3      S31:  -0.0194 S32:  -0.5236 S33:   0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 364 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3281 -13.9496  28.1607              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2139 T22:   1.5840                                     
REMARK   3      T33:   1.0091 T12:   0.1982                                     
REMARK   3      T13:  -0.0899 T23:   0.1743                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4818 L22:   0.8641                                     
REMARK   3      L33:   0.9563 L12:   0.5454                                     
REMARK   3      L13:  -0.4345 L23:  -0.5891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0199 S12:  -1.8631 S13:  -1.1902                       
REMARK   3      S21:  -1.2698 S22:   0.7190 S23:   0.6906                       
REMARK   3      S31:   0.1132 S32:  -0.5521 S33:   0.0003                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 365 THROUGH 395 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7621 -25.7711  37.1406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4379 T22:   0.8017                                     
REMARK   3      T33:   1.0534 T12:  -0.5356                                     
REMARK   3      T13:   0.6392 T23:   0.5415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2634 L22:   2.8411                                     
REMARK   3      L33:   8.3652 L12:   1.4028                                     
REMARK   3      L13:  -1.1802 L23:   3.1306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9400 S12:   0.6113 S13:  -1.0113                       
REMARK   3      S21:   3.6980 S22:   2.2619 S23:   0.4732                       
REMARK   3      S31:   3.0619 S32:   2.6413 S33:   0.6198                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 396 THROUGH 424 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2062 -34.7878  53.6233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4497 T22:   0.0093                                     
REMARK   3      T33:   1.7535 T12:   0.2042                                     
REMARK   3      T13:  -0.3077 T23:   0.5880                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0168 L22:   1.2748                                     
REMARK   3      L33:   0.8350 L12:   0.4864                                     
REMARK   3      L13:  -1.2398 L23:  -0.3461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0831 S12:  -3.1865 S13:  -2.0697                       
REMARK   3      S21:   1.1742 S22:   1.9459 S23:   1.6657                       
REMARK   3      S31:  -0.1259 S32:  -0.0918 S33:   0.0020                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 425 THROUGH 481 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3297 -36.7008  48.2384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1293 T22:   1.0844                                     
REMARK   3      T33:   1.2385 T12:   0.0983                                     
REMARK   3      T13:  -0.0380 T23:   0.2176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4122 L22:   1.7019                                     
REMARK   3      L33:   0.7274 L12:   2.1710                                     
REMARK   3      L13:   1.1484 L23:   0.2222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0521 S12:  -0.6232 S13:  -0.5766                       
REMARK   3      S21:  -2.5598 S22:  -0.1969 S23:   0.7045                       
REMARK   3      S31:  -0.1421 S32:  -0.8904 S33:   0.0002                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 286 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4316 -19.8173   3.7296              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9288 T22:   0.4503                                     
REMARK   3      T33:   0.9198 T12:   0.1605                                     
REMARK   3      T13:  -0.0479 T23:  -0.0837                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1610 L22:   2.0496                                     
REMARK   3      L33:   1.8475 L12:   1.7347                                     
REMARK   3      L13:  -0.6936 L23:   2.1582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4018 S12:  -0.2281 S13:   0.0513                       
REMARK   3      S21:  -0.4110 S22:   0.1593 S23:   0.0454                       
REMARK   3      S31:  -0.4410 S32:   0.0736 S33:  -0.0043                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 287 THROUGH 480 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6740 -36.2420  15.1885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7553 T22:   0.9772                                     
REMARK   3      T33:   1.0606 T12:   0.0942                                     
REMARK   3      T13:   0.0056 T23:  -0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.3641 L22:  -0.8797                                     
REMARK   3      L33:   2.9967 L12:  -1.1085                                     
REMARK   3      L13:  -0.9994 L23:   0.9709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1119 S12:  -0.4567 S13:  -0.1689                       
REMARK   3      S21:   0.2195 S22:  -0.6269 S23:  -0.0269                       
REMARK   3      S31:   0.4944 S32:   0.1233 S33:  -0.0037                       
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 6N9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000238380.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-18                          
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) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23251                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (1.14_3260: ???)                               
REMARK 200 STARTING MODEL: 5B5R, 6AO3, 6AO4                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BIS-TRIS PH 5.5, 200   
REMARK 280  MM NACL, AND 10 MM DTT, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.77500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     ASP A    73                                                      
REMARK 465     VAL A    74                                                      
REMARK 465     GLN A    75                                                      
REMARK 465     ARG A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     PHE A    80                                                      
REMARK 465     HIS A    81                                                      
REMARK 465     PHE A    82                                                      
REMARK 465     LEU A    96                                                      
REMARK 465     ALA A    97                                                      
REMARK 465     ALA A    98                                                      
REMARK 465     PRO A    99                                                      
REMARK 465     GLY A   100                                                      
REMARK 465     GLN A   101                                                      
REMARK 465     ALA A   102                                                      
REMARK 465     LYS A   103                                                      
REMARK 465     ILE A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     ALA A   108                                                      
REMARK 465     ALA A   109                                                      
REMARK 465     VAL A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     SER A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     THR A   116                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     GLU A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     GLY A   182                                                      
REMARK 465     ARG A   183                                                      
REMARK 465     PHE A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     LEU A   186                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     GLY A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     THR A   190                                                      
REMARK 465     CYS A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     GLN A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     GLU A   195                                                      
REMARK 465     GLY A   196                                                      
REMARK 465     GLN A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     HIS A   199                                                      
REMARK 465     LEU A   200                                                      
REMARK 465     SER A   201                                                      
REMARK 465     GLN A   202                                                      
REMARK 465     LYS A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     PRO A   242                                                      
REMARK 465     PRO A   243                                                      
REMARK 465     ALA A   244                                                      
REMARK 465     THR A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     HIS A   247                                                      
REMARK 465     LYS A   248                                                      
REMARK 465     ARG A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     THR A   251                                                      
REMARK 465     SER A   252                                                      
REMARK 465     GLU A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     TRP A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     LEU A   259                                                      
REMARK 465     PRO A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     LEU A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     MET A   265                                                      
REMARK 465     MET A   266                                                      
REMARK 465     ARG A   267                                                      
REMARK 465     CYS A   268                                                      
REMARK 465     LEU A   269                                                      
REMARK 465     HIS A   270                                                      
REMARK 465     ASN A   271                                                      
REMARK 465     PHE A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     THR A   274                                                      
REMARK 465     ASP A   275                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     VAL A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     ALA A   279                                                      
REMARK 465     GLU A   280                                                      
REMARK 465     LEU A   281                                                      
REMARK 465     ALA A   282                                                      
REMARK 465     PHE A   283                                                      
REMARK 465     GLN A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     PRO A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ALA B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     PRO B    72                                                      
REMARK 465     ASP B    73                                                      
REMARK 465     VAL B    74                                                      
REMARK 465     GLN B    75                                                      
REMARK 465     ARG B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     PHE B    80                                                      
REMARK 465     HIS B    81                                                      
REMARK 465     PHE B    82                                                      
REMARK 465     VAL B    94                                                      
REMARK 465     GLU B    95                                                      
REMARK 465     LEU B    96                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     ALA B    98                                                      
REMARK 465     PRO B    99                                                      
REMARK 465     GLY B   100                                                      
REMARK 465     GLN B   101                                                      
REMARK 465     ALA B   102                                                      
REMARK 465     LYS B   103                                                      
REMARK 465     ILE B   104                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     GLY B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     ALA B   108                                                      
REMARK 465     ALA B   109                                                      
REMARK 465     VAL B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     SER B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     SER B   115                                                      
REMARK 465     THR B   116                                                      
REMARK 465     THR B   173                                                      
REMARK 465     ARG B   174                                                      
REMARK 465     THR B   175                                                      
REMARK 465     HIS B   176                                                      
REMARK 465     LYS B   177                                                      
REMARK 465     ARG B   178                                                      
REMARK 465     GLU B   179                                                      
REMARK 465     GLY B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     GLY B   182                                                      
REMARK 465     ARG B   183                                                      
REMARK 465     PHE B   184                                                      
REMARK 465     SER B   185                                                      
REMARK 465     LEU B   186                                                      
REMARK 465     PRO B   187                                                      
REMARK 465     GLY B   188                                                      
REMARK 465     ALA B   189                                                      
REMARK 465     THR B   190                                                      
REMARK 465     CYS B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     GLN B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     GLU B   195                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     GLN B   197                                                      
REMARK 465     GLY B   198                                                      
REMARK 465     HIS B   199                                                      
REMARK 465     LEU B   200                                                      
REMARK 465     SER B   201                                                      
REMARK 465     GLN B   202                                                      
REMARK 465     LYS B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     PRO B   242                                                      
REMARK 465     PRO B   243                                                      
REMARK 465     ALA B   244                                                      
REMARK 465     THR B   245                                                      
REMARK 465     GLY B   246                                                      
REMARK 465     HIS B   247                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     ARG B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     THR B   251                                                      
REMARK 465     SER B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     GLY B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     TRP B   256                                                      
REMARK 465     PRO B   257                                                      
REMARK 465     GLN B   258                                                      
REMARK 465     LEU B   259                                                      
REMARK 465     PRO B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     LEU B   263                                                      
REMARK 465     SER B   264                                                      
REMARK 465     MET B   265                                                      
REMARK 465     MET B   266                                                      
REMARK 465     ARG B   267                                                      
REMARK 465     CYS B   268                                                      
REMARK 465     LEU B   269                                                      
REMARK 465     HIS B   270                                                      
REMARK 465     ASN B   271                                                      
REMARK 465     PHE B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     THR B   274                                                      
REMARK 465     ASP B   275                                                      
REMARK 465     GLY B   276                                                      
REMARK 465     VAL B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     ALA B   279                                                      
REMARK 465     GLU B   280                                                      
REMARK 465     LEU B   281                                                      
REMARK 465     ALA B   282                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     PRO B   483                                                      
REMARK 465     HIS B   484                                                      
REMARK 465     SER C     0                                                      
REMARK 465     ASP C    68                                                      
REMARK 465     ALA C    69                                                      
REMARK 465     ALA C    70                                                      
REMARK 465     GLU C    71                                                      
REMARK 465     PRO C    72                                                      
REMARK 465     ASP C    73                                                      
REMARK 465     VAL C    74                                                      
REMARK 465     GLN C    75                                                      
REMARK 465     ARG C    76                                                      
REMARK 465     GLY C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     SER C    79                                                      
REMARK 465     PHE C    80                                                      
REMARK 465     HIS C    81                                                      
REMARK 465     PHE C    82                                                      
REMARK 465     TYR C    83                                                      
REMARK 465     GLN C   101                                                      
REMARK 465     ALA C   102                                                      
REMARK 465     LYS C   103                                                      
REMARK 465     ILE C   104                                                      
REMARK 465     ALA C   105                                                      
REMARK 465     GLY C   106                                                      
REMARK 465     GLY C   107                                                      
REMARK 465     ALA C   108                                                      
REMARK 465     ALA C   109                                                      
REMARK 465     VAL C   110                                                      
REMARK 465     SER C   111                                                      
REMARK 465     ASP C   112                                                      
REMARK 465     SER C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     SER C   115                                                      
REMARK 465     THR C   116                                                      
REMARK 465     THR C   173                                                      
REMARK 465     ARG C   174                                                      
REMARK 465     THR C   175                                                      
REMARK 465     HIS C   176                                                      
REMARK 465     LYS C   177                                                      
REMARK 465     ARG C   178                                                      
REMARK 465     GLU C   179                                                      
REMARK 465     GLY C   180                                                      
REMARK 465     SER C   181                                                      
REMARK 465     GLY C   182                                                      
REMARK 465     ARG C   183                                                      
REMARK 465     PHE C   184                                                      
REMARK 465     SER C   185                                                      
REMARK 465     LEU C   186                                                      
REMARK 465     PRO C   187                                                      
REMARK 465     GLY C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     THR C   190                                                      
REMARK 465     CYS C   191                                                      
REMARK 465     LEU C   192                                                      
REMARK 465     GLN C   193                                                      
REMARK 465     GLY C   194                                                      
REMARK 465     GLU C   195                                                      
REMARK 465     GLY C   196                                                      
REMARK 465     GLN C   197                                                      
REMARK 465     GLY C   198                                                      
REMARK 465     HIS C   199                                                      
REMARK 465     LEU C   200                                                      
REMARK 465     SER C   201                                                      
REMARK 465     GLN C   202                                                      
REMARK 465     LYS C   203                                                      
REMARK 465     PRO C   242                                                      
REMARK 465     PRO C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     THR C   245                                                      
REMARK 465     GLY C   246                                                      
REMARK 465     HIS C   247                                                      
REMARK 465     LYS C   248                                                      
REMARK 465     ARG C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     THR C   251                                                      
REMARK 465     SER C   252                                                      
REMARK 465     GLU C   253                                                      
REMARK 465     GLY C   254                                                      
REMARK 465     ALA C   255                                                      
REMARK 465     TRP C   256                                                      
REMARK 465     PRO C   257                                                      
REMARK 465     GLN C   258                                                      
REMARK 465     LEU C   259                                                      
REMARK 465     PRO C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     GLY C   262                                                      
REMARK 465     LEU C   263                                                      
REMARK 465     SER C   264                                                      
REMARK 465     MET C   265                                                      
REMARK 465     MET C   266                                                      
REMARK 465     ARG C   267                                                      
REMARK 465     CYS C   268                                                      
REMARK 465     LEU C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     ASN C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     LEU C   273                                                      
REMARK 465     THR C   274                                                      
REMARK 465     ASP C   275                                                      
REMARK 465     GLY C   276                                                      
REMARK 465     VAL C   277                                                      
REMARK 465     PRO C   278                                                      
REMARK 465     ALA C   279                                                      
REMARK 465     GLN C   481                                                      
REMARK 465     GLU C   482                                                      
REMARK 465     PRO C   483                                                      
REMARK 465     HIS C   484                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D    70                                                      
REMARK 465     GLU D    71                                                      
REMARK 465     PRO D    72                                                      
REMARK 465     ASP D    73                                                      
REMARK 465     VAL D    74                                                      
REMARK 465     GLN D    75                                                      
REMARK 465     ARG D    76                                                      
REMARK 465     GLY D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     SER D    79                                                      
REMARK 465     PHE D    80                                                      
REMARK 465     HIS D    81                                                      
REMARK 465     PHE D    82                                                      
REMARK 465     LEU D    96                                                      
REMARK 465     ALA D    97                                                      
REMARK 465     ALA D    98                                                      
REMARK 465     PRO D    99                                                      
REMARK 465     GLY D   100                                                      
REMARK 465     GLN D   101                                                      
REMARK 465     ALA D   102                                                      
REMARK 465     LYS D   103                                                      
REMARK 465     ILE D   104                                                      
REMARK 465     ALA D   105                                                      
REMARK 465     GLY D   106                                                      
REMARK 465     GLY D   107                                                      
REMARK 465     ALA D   108                                                      
REMARK 465     ALA D   109                                                      
REMARK 465     VAL D   110                                                      
REMARK 465     SER D   111                                                      
REMARK 465     ASP D   112                                                      
REMARK 465     SER D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     SER D   115                                                      
REMARK 465     ARG D   174                                                      
REMARK 465     THR D   175                                                      
REMARK 465     HIS D   176                                                      
REMARK 465     LYS D   177                                                      
REMARK 465     ARG D   178                                                      
REMARK 465     GLU D   179                                                      
REMARK 465     GLY D   180                                                      
REMARK 465     SER D   181                                                      
REMARK 465     GLY D   182                                                      
REMARK 465     ARG D   183                                                      
REMARK 465     PHE D   184                                                      
REMARK 465     SER D   185                                                      
REMARK 465     LEU D   186                                                      
REMARK 465     PRO D   187                                                      
REMARK 465     GLY D   188                                                      
REMARK 465     ALA D   189                                                      
REMARK 465     THR D   190                                                      
REMARK 465     CYS D   191                                                      
REMARK 465     LEU D   192                                                      
REMARK 465     GLN D   193                                                      
REMARK 465     GLY D   194                                                      
REMARK 465     GLU D   195                                                      
REMARK 465     GLY D   196                                                      
REMARK 465     GLN D   197                                                      
REMARK 465     GLY D   198                                                      
REMARK 465     HIS D   199                                                      
REMARK 465     LEU D   200                                                      
REMARK 465     SER D   201                                                      
REMARK 465     GLN D   202                                                      
REMARK 465     LYS D   203                                                      
REMARK 465     LYS D   204                                                      
REMARK 465     PRO D   243                                                      
REMARK 465     ALA D   244                                                      
REMARK 465     THR D   245                                                      
REMARK 465     GLY D   246                                                      
REMARK 465     HIS D   247                                                      
REMARK 465     LYS D   248                                                      
REMARK 465     ARG D   249                                                      
REMARK 465     SER D   250                                                      
REMARK 465     THR D   251                                                      
REMARK 465     SER D   252                                                      
REMARK 465     GLU D   253                                                      
REMARK 465     GLY D   254                                                      
REMARK 465     ALA D   255                                                      
REMARK 465     TRP D   256                                                      
REMARK 465     PRO D   257                                                      
REMARK 465     GLN D   258                                                      
REMARK 465     LEU D   259                                                      
REMARK 465     PRO D   260                                                      
REMARK 465     SER D   261                                                      
REMARK 465     GLY D   262                                                      
REMARK 465     LEU D   263                                                      
REMARK 465     SER D   264                                                      
REMARK 465     MET D   265                                                      
REMARK 465     MET D   266                                                      
REMARK 465     ARG D   267                                                      
REMARK 465     CYS D   268                                                      
REMARK 465     LEU D   269                                                      
REMARK 465     HIS D   270                                                      
REMARK 465     ASN D   271                                                      
REMARK 465     PHE D   272                                                      
REMARK 465     LEU D   273                                                      
REMARK 465     THR D   274                                                      
REMARK 465     ASP D   275                                                      
REMARK 465     GLY D   276                                                      
REMARK 465     VAL D   277                                                      
REMARK 465     PRO D   278                                                      
REMARK 465     ALA D   279                                                      
REMARK 465     GLU D   280                                                      
REMARK 465     GLN D   481                                                      
REMARK 465     GLU D   482                                                      
REMARK 465     PRO D   483                                                      
REMARK 465     HIS D   484                                                      
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    SER A  46     -160.59    -77.92                                   
REMARK 500    SER A  47      157.39    -46.02                                   
REMARK 500    ASP A  68       62.39   -103.43                                   
REMARK 500    ASP A  87     -173.24    -67.46                                   
REMARK 500    GLN A 167       41.17   -102.27                                   
REMARK 500    ASP A 224      -38.80   -132.97                                   
REMARK 500    SER A 225      -33.61   -130.80                                   
REMARK 500    GLU A 285     -163.44   -103.35                                   
REMARK 500    ASP A 286     -164.99   -112.92                                   
REMARK 500    GLU A 302       47.73    -81.95                                   
REMARK 500    GLU A 334      -71.51   -118.02                                   
REMARK 500    GLN A 337       48.85     35.33                                   
REMARK 500    THR B  26      -61.16    -93.57                                   
REMARK 500    SER B  31       47.60     34.97                                   
REMARK 500    TYR B  37       49.15    -97.29                                   
REMARK 500    ASP B  87       65.59     60.52                                   
REMARK 500    GLN B 167       42.83   -103.12                                   
REMARK 500    ASP B 224     -152.18   -140.66                                   
REMARK 500    SER B 225      -33.56    -38.22                                   
REMARK 500    LEU B 303       48.52    -97.23                                   
REMARK 500    GLU B 334      -70.19    -72.14                                   
REMARK 500    GLN B 335       29.21   -140.91                                   
REMARK 500    GLN B 337     -157.85   -139.46                                   
REMARK 500    SER B 338       76.62     65.80                                   
REMARK 500    PRO B 454        0.12    -67.13                                   
REMARK 500    CYS B 457     -168.69   -115.64                                   
REMARK 500    PHE C  22       62.04     34.88                                   
REMARK 500    PHE C  34       70.76    -68.36                                   
REMARK 500    ASP C  87       64.59     39.29                                   
REMARK 500    GLN C 167       68.04   -103.09                                   
REMARK 500    PHE C 216     -179.20   -170.14                                   
REMARK 500    PHE C 283      109.09    -59.25                                   
REMARK 500    GLU C 334     -163.81    -79.22                                   
REMARK 500    GLN C 335       46.14    -78.20                                   
REMARK 500    SER C 338       99.35    -67.65                                   
REMARK 500    GLN C 416       11.32   -150.87                                   
REMARK 500    SER D  46      -72.43    -63.33                                   
REMARK 500    ASP D  68       58.02   -103.24                                   
REMARK 500    GLN D  89       64.25     66.40                                   
REMARK 500    SER D  93       61.66     37.58                                   
REMARK 500    GLN D 167       40.53   -104.56                                   
REMARK 500    ASP D 224      -69.98   -125.54                                   
REMARK 500    GLU D 285      -61.36   -105.10                                   
REMARK 500    ASP D 286     -162.03   -165.89                                   
REMARK 500    SER D 338      116.72    -39.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6N9O A    1   484  UNP    P57764   GSDMD_HUMAN      1    484             
DBREF  6N9O B    1   484  UNP    P57764   GSDMD_HUMAN      1    484             
DBREF  6N9O C    1   484  UNP    P57764   GSDMD_HUMAN      1    484             
DBREF  6N9O D    1   484  UNP    P57764   GSDMD_HUMAN      1    484             
SEQADV 6N9O SER A    0  UNP  P57764              EXPRESSION TAG                 
SEQADV 6N9O LEU A  281  UNP  P57764    GLY   281 CONFLICT                       
SEQADV 6N9O SER B    0  UNP  P57764              EXPRESSION TAG                 
SEQADV 6N9O LEU B  281  UNP  P57764    GLY   281 CONFLICT                       
SEQADV 6N9O SER C    0  UNP  P57764              EXPRESSION TAG                 
SEQADV 6N9O LEU C  281  UNP  P57764    GLY   281 CONFLICT                       
SEQADV 6N9O SER D    0  UNP  P57764              EXPRESSION TAG                 
SEQADV 6N9O LEU D  281  UNP  P57764    GLY   281 CONFLICT                       
SEQRES   1 A  485  SER MET GLY SER ALA PHE GLU ARG VAL VAL ARG ARG VAL          
SEQRES   2 A  485  VAL GLN GLU LEU ASP HIS GLY GLY GLU PHE ILE PRO VAL          
SEQRES   3 A  485  THR SER LEU GLN SER SER THR GLY PHE GLN PRO TYR CYS          
SEQRES   4 A  485  LEU VAL VAL ARG LYS PRO SER SER SER TRP PHE TRP LYS          
SEQRES   5 A  485  PRO ARG TYR LYS CYS VAL ASN LEU SER ILE LYS ASP ILE          
SEQRES   6 A  485  LEU GLU PRO ASP ALA ALA GLU PRO ASP VAL GLN ARG GLY          
SEQRES   7 A  485  ARG SER PHE HIS PHE TYR ASP ALA MET ASP GLY GLN ILE          
SEQRES   8 A  485  GLN GLY SER VAL GLU LEU ALA ALA PRO GLY GLN ALA LYS          
SEQRES   9 A  485  ILE ALA GLY GLY ALA ALA VAL SER ASP SER SER SER THR          
SEQRES  10 A  485  SER MET ASN VAL TYR SER LEU SER VAL ASP PRO ASN THR          
SEQRES  11 A  485  TRP GLN THR LEU LEU HIS GLU ARG HIS LEU ARG GLN PRO          
SEQRES  12 A  485  GLU HIS LYS VAL LEU GLN GLN LEU ARG SER ARG GLY ASP          
SEQRES  13 A  485  ASN VAL TYR VAL VAL THR GLU VAL LEU GLN THR GLN LYS          
SEQRES  14 A  485  GLU VAL GLU VAL THR ARG THR HIS LYS ARG GLU GLY SER          
SEQRES  15 A  485  GLY ARG PHE SER LEU PRO GLY ALA THR CYS LEU GLN GLY          
SEQRES  16 A  485  GLU GLY GLN GLY HIS LEU SER GLN LYS LYS THR VAL THR          
SEQRES  17 A  485  ILE PRO SER GLY SER THR LEU ALA PHE ARG VAL ALA GLN          
SEQRES  18 A  485  LEU VAL ILE ASP SER ASP LEU ASP VAL LEU LEU PHE PRO          
SEQRES  19 A  485  ASP LYS LYS GLN ARG THR PHE GLN PRO PRO ALA THR GLY          
SEQRES  20 A  485  HIS LYS ARG SER THR SER GLU GLY ALA TRP PRO GLN LEU          
SEQRES  21 A  485  PRO SER GLY LEU SER MET MET ARG CYS LEU HIS ASN PHE          
SEQRES  22 A  485  LEU THR ASP GLY VAL PRO ALA GLU LEU ALA PHE THR GLU          
SEQRES  23 A  485  ASP PHE GLN GLY LEU ARG ALA GLU VAL GLU THR ILE SER          
SEQRES  24 A  485  LYS GLU LEU GLU LEU LEU ASP ARG GLU LEU CYS GLN LEU          
SEQRES  25 A  485  LEU LEU GLU GLY LEU GLU GLY VAL LEU ARG ASP GLN LEU          
SEQRES  26 A  485  ALA LEU ARG ALA LEU GLU GLU ALA LEU GLU GLN GLY GLN          
SEQRES  27 A  485  SER LEU GLY PRO VAL GLU PRO LEU ASP GLY PRO ALA GLY          
SEQRES  28 A  485  ALA VAL LEU GLU CYS LEU VAL LEU SER SER GLY MET LEU          
SEQRES  29 A  485  VAL PRO GLU LEU ALA ILE PRO VAL VAL TYR LEU LEU GLY          
SEQRES  30 A  485  ALA LEU THR MET LEU SER GLU THR GLN HIS LYS LEU LEU          
SEQRES  31 A  485  ALA GLU ALA LEU GLU SER GLN THR LEU LEU GLY PRO LEU          
SEQRES  32 A  485  GLU LEU VAL GLY SER LEU LEU GLU GLN SER ALA PRO TRP          
SEQRES  33 A  485  GLN GLU ARG SER THR MET SER LEU PRO PRO GLY LEU LEU          
SEQRES  34 A  485  GLY ASN SER TRP GLY GLU GLY ALA PRO ALA TRP VAL LEU          
SEQRES  35 A  485  LEU ASP GLU CYS GLY LEU GLU LEU GLY GLU ASP THR PRO          
SEQRES  36 A  485  HIS VAL CYS TRP GLU PRO GLN ALA GLN GLY ARG MET CYS          
SEQRES  37 A  485  ALA LEU TYR ALA SER LEU ALA LEU LEU SER GLY LEU SER          
SEQRES  38 A  485  GLN GLU PRO HIS                                              
SEQRES   1 B  485  SER MET GLY SER ALA PHE GLU ARG VAL VAL ARG ARG VAL          
SEQRES   2 B  485  VAL GLN GLU LEU ASP HIS GLY GLY GLU PHE ILE PRO VAL          
SEQRES   3 B  485  THR SER LEU GLN SER SER THR GLY PHE GLN PRO TYR CYS          
SEQRES   4 B  485  LEU VAL VAL ARG LYS PRO SER SER SER TRP PHE TRP LYS          
SEQRES   5 B  485  PRO ARG TYR LYS CYS VAL ASN LEU SER ILE LYS ASP ILE          
SEQRES   6 B  485  LEU GLU PRO ASP ALA ALA GLU PRO ASP VAL GLN ARG GLY          
SEQRES   7 B  485  ARG SER PHE HIS PHE TYR ASP ALA MET ASP GLY GLN ILE          
SEQRES   8 B  485  GLN GLY SER VAL GLU LEU ALA ALA PRO GLY GLN ALA LYS          
SEQRES   9 B  485  ILE ALA GLY GLY ALA ALA VAL SER ASP SER SER SER THR          
SEQRES  10 B  485  SER MET ASN VAL TYR SER LEU SER VAL ASP PRO ASN THR          
SEQRES  11 B  485  TRP GLN THR LEU LEU HIS GLU ARG HIS LEU ARG GLN PRO          
SEQRES  12 B  485  GLU HIS LYS VAL LEU GLN GLN LEU ARG SER ARG GLY ASP          
SEQRES  13 B  485  ASN VAL TYR VAL VAL THR GLU VAL LEU GLN THR GLN LYS          
SEQRES  14 B  485  GLU VAL GLU VAL THR ARG THR HIS LYS ARG GLU GLY SER          
SEQRES  15 B  485  GLY ARG PHE SER LEU PRO GLY ALA THR CYS LEU GLN GLY          
SEQRES  16 B  485  GLU GLY GLN GLY HIS LEU SER GLN LYS LYS THR VAL THR          
SEQRES  17 B  485  ILE PRO SER GLY SER THR LEU ALA PHE ARG VAL ALA GLN          
SEQRES  18 B  485  LEU VAL ILE ASP SER ASP LEU ASP VAL LEU LEU PHE PRO          
SEQRES  19 B  485  ASP LYS LYS GLN ARG THR PHE GLN PRO PRO ALA THR GLY          
SEQRES  20 B  485  HIS LYS ARG SER THR SER GLU GLY ALA TRP PRO GLN LEU          
SEQRES  21 B  485  PRO SER GLY LEU SER MET MET ARG CYS LEU HIS ASN PHE          
SEQRES  22 B  485  LEU THR ASP GLY VAL PRO ALA GLU LEU ALA PHE THR GLU          
SEQRES  23 B  485  ASP PHE GLN GLY LEU ARG ALA GLU VAL GLU THR ILE SER          
SEQRES  24 B  485  LYS GLU LEU GLU LEU LEU ASP ARG GLU LEU CYS GLN LEU          
SEQRES  25 B  485  LEU LEU GLU GLY LEU GLU GLY VAL LEU ARG ASP GLN LEU          
SEQRES  26 B  485  ALA LEU ARG ALA LEU GLU GLU ALA LEU GLU GLN GLY GLN          
SEQRES  27 B  485  SER LEU GLY PRO VAL GLU PRO LEU ASP GLY PRO ALA GLY          
SEQRES  28 B  485  ALA VAL LEU GLU CYS LEU VAL LEU SER SER GLY MET LEU          
SEQRES  29 B  485  VAL PRO GLU LEU ALA ILE PRO VAL VAL TYR LEU LEU GLY          
SEQRES  30 B  485  ALA LEU THR MET LEU SER GLU THR GLN HIS LYS LEU LEU          
SEQRES  31 B  485  ALA GLU ALA LEU GLU SER GLN THR LEU LEU GLY PRO LEU          
SEQRES  32 B  485  GLU LEU VAL GLY SER LEU LEU GLU GLN SER ALA PRO TRP          
SEQRES  33 B  485  GLN GLU ARG SER THR MET SER LEU PRO PRO GLY LEU LEU          
SEQRES  34 B  485  GLY ASN SER TRP GLY GLU GLY ALA PRO ALA TRP VAL LEU          
SEQRES  35 B  485  LEU ASP GLU CYS GLY LEU GLU LEU GLY GLU ASP THR PRO          
SEQRES  36 B  485  HIS VAL CYS TRP GLU PRO GLN ALA GLN GLY ARG MET CYS          
SEQRES  37 B  485  ALA LEU TYR ALA SER LEU ALA LEU LEU SER GLY LEU SER          
SEQRES  38 B  485  GLN GLU PRO HIS                                              
SEQRES   1 C  485  SER MET GLY SER ALA PHE GLU ARG VAL VAL ARG ARG VAL          
SEQRES   2 C  485  VAL GLN GLU LEU ASP HIS GLY GLY GLU PHE ILE PRO VAL          
SEQRES   3 C  485  THR SER LEU GLN SER SER THR GLY PHE GLN PRO TYR CYS          
SEQRES   4 C  485  LEU VAL VAL ARG LYS PRO SER SER SER TRP PHE TRP LYS          
SEQRES   5 C  485  PRO ARG TYR LYS CYS VAL ASN LEU SER ILE LYS ASP ILE          
SEQRES   6 C  485  LEU GLU PRO ASP ALA ALA GLU PRO ASP VAL GLN ARG GLY          
SEQRES   7 C  485  ARG SER PHE HIS PHE TYR ASP ALA MET ASP GLY GLN ILE          
SEQRES   8 C  485  GLN GLY SER VAL GLU LEU ALA ALA PRO GLY GLN ALA LYS          
SEQRES   9 C  485  ILE ALA GLY GLY ALA ALA VAL SER ASP SER SER SER THR          
SEQRES  10 C  485  SER MET ASN VAL TYR SER LEU SER VAL ASP PRO ASN THR          
SEQRES  11 C  485  TRP GLN THR LEU LEU HIS GLU ARG HIS LEU ARG GLN PRO          
SEQRES  12 C  485  GLU HIS LYS VAL LEU GLN GLN LEU ARG SER ARG GLY ASP          
SEQRES  13 C  485  ASN VAL TYR VAL VAL THR GLU VAL LEU GLN THR GLN LYS          
SEQRES  14 C  485  GLU VAL GLU VAL THR ARG THR HIS LYS ARG GLU GLY SER          
SEQRES  15 C  485  GLY ARG PHE SER LEU PRO GLY ALA THR CYS LEU GLN GLY          
SEQRES  16 C  485  GLU GLY GLN GLY HIS LEU SER GLN LYS LYS THR VAL THR          
SEQRES  17 C  485  ILE PRO SER GLY SER THR LEU ALA PHE ARG VAL ALA GLN          
SEQRES  18 C  485  LEU VAL ILE ASP SER ASP LEU ASP VAL LEU LEU PHE PRO          
SEQRES  19 C  485  ASP LYS LYS GLN ARG THR PHE GLN PRO PRO ALA THR GLY          
SEQRES  20 C  485  HIS LYS ARG SER THR SER GLU GLY ALA TRP PRO GLN LEU          
SEQRES  21 C  485  PRO SER GLY LEU SER MET MET ARG CYS LEU HIS ASN PHE          
SEQRES  22 C  485  LEU THR ASP GLY VAL PRO ALA GLU LEU ALA PHE THR GLU          
SEQRES  23 C  485  ASP PHE GLN GLY LEU ARG ALA GLU VAL GLU THR ILE SER          
SEQRES  24 C  485  LYS GLU LEU GLU LEU LEU ASP ARG GLU LEU CYS GLN LEU          
SEQRES  25 C  485  LEU LEU GLU GLY LEU GLU GLY VAL LEU ARG ASP GLN LEU          
SEQRES  26 C  485  ALA LEU ARG ALA LEU GLU GLU ALA LEU GLU GLN GLY GLN          
SEQRES  27 C  485  SER LEU GLY PRO VAL GLU PRO LEU ASP GLY PRO ALA GLY          
SEQRES  28 C  485  ALA VAL LEU GLU CYS LEU VAL LEU SER SER GLY MET LEU          
SEQRES  29 C  485  VAL PRO GLU LEU ALA ILE PRO VAL VAL TYR LEU LEU GLY          
SEQRES  30 C  485  ALA LEU THR MET LEU SER GLU THR GLN HIS LYS LEU LEU          
SEQRES  31 C  485  ALA GLU ALA LEU GLU SER GLN THR LEU LEU GLY PRO LEU          
SEQRES  32 C  485  GLU LEU VAL GLY SER LEU LEU GLU GLN SER ALA PRO TRP          
SEQRES  33 C  485  GLN GLU ARG SER THR MET SER LEU PRO PRO GLY LEU LEU          
SEQRES  34 C  485  GLY ASN SER TRP GLY GLU GLY ALA PRO ALA TRP VAL LEU          
SEQRES  35 C  485  LEU ASP GLU CYS GLY LEU GLU LEU GLY GLU ASP THR PRO          
SEQRES  36 C  485  HIS VAL CYS TRP GLU PRO GLN ALA GLN GLY ARG MET CYS          
SEQRES  37 C  485  ALA LEU TYR ALA SER LEU ALA LEU LEU SER GLY LEU SER          
SEQRES  38 C  485  GLN GLU PRO HIS                                              
SEQRES   1 D  485  SER MET GLY SER ALA PHE GLU ARG VAL VAL ARG ARG VAL          
SEQRES   2 D  485  VAL GLN GLU LEU ASP HIS GLY GLY GLU PHE ILE PRO VAL          
SEQRES   3 D  485  THR SER LEU GLN SER SER THR GLY PHE GLN PRO TYR CYS          
SEQRES   4 D  485  LEU VAL VAL ARG LYS PRO SER SER SER TRP PHE TRP LYS          
SEQRES   5 D  485  PRO ARG TYR LYS CYS VAL ASN LEU SER ILE LYS ASP ILE          
SEQRES   6 D  485  LEU GLU PRO ASP ALA ALA GLU PRO ASP VAL GLN ARG GLY          
SEQRES   7 D  485  ARG SER PHE HIS PHE TYR ASP ALA MET ASP GLY GLN ILE          
SEQRES   8 D  485  GLN GLY SER VAL GLU LEU ALA ALA PRO GLY GLN ALA LYS          
SEQRES   9 D  485  ILE ALA GLY GLY ALA ALA VAL SER ASP SER SER SER THR          
SEQRES  10 D  485  SER MET ASN VAL TYR SER LEU SER VAL ASP PRO ASN THR          
SEQRES  11 D  485  TRP GLN THR LEU LEU HIS GLU ARG HIS LEU ARG GLN PRO          
SEQRES  12 D  485  GLU HIS LYS VAL LEU GLN GLN LEU ARG SER ARG GLY ASP          
SEQRES  13 D  485  ASN VAL TYR VAL VAL THR GLU VAL LEU GLN THR GLN LYS          
SEQRES  14 D  485  GLU VAL GLU VAL THR ARG THR HIS LYS ARG GLU GLY SER          
SEQRES  15 D  485  GLY ARG PHE SER LEU PRO GLY ALA THR CYS LEU GLN GLY          
SEQRES  16 D  485  GLU GLY GLN GLY HIS LEU SER GLN LYS LYS THR VAL THR          
SEQRES  17 D  485  ILE PRO SER GLY SER THR LEU ALA PHE ARG VAL ALA GLN          
SEQRES  18 D  485  LEU VAL ILE ASP SER ASP LEU ASP VAL LEU LEU PHE PRO          
SEQRES  19 D  485  ASP LYS LYS GLN ARG THR PHE GLN PRO PRO ALA THR GLY          
SEQRES  20 D  485  HIS LYS ARG SER THR SER GLU GLY ALA TRP PRO GLN LEU          
SEQRES  21 D  485  PRO SER GLY LEU SER MET MET ARG CYS LEU HIS ASN PHE          
SEQRES  22 D  485  LEU THR ASP GLY VAL PRO ALA GLU LEU ALA PHE THR GLU          
SEQRES  23 D  485  ASP PHE GLN GLY LEU ARG ALA GLU VAL GLU THR ILE SER          
SEQRES  24 D  485  LYS GLU LEU GLU LEU LEU ASP ARG GLU LEU CYS GLN LEU          
SEQRES  25 D  485  LEU LEU GLU GLY LEU GLU GLY VAL LEU ARG ASP GLN LEU          
SEQRES  26 D  485  ALA LEU ARG ALA LEU GLU GLU ALA LEU GLU GLN GLY GLN          
SEQRES  27 D  485  SER LEU GLY PRO VAL GLU PRO LEU ASP GLY PRO ALA GLY          
SEQRES  28 D  485  ALA VAL LEU GLU CYS LEU VAL LEU SER SER GLY MET LEU          
SEQRES  29 D  485  VAL PRO GLU LEU ALA ILE PRO VAL VAL TYR LEU LEU GLY          
SEQRES  30 D  485  ALA LEU THR MET LEU SER GLU THR GLN HIS LYS LEU LEU          
SEQRES  31 D  485  ALA GLU ALA LEU GLU SER GLN THR LEU LEU GLY PRO LEU          
SEQRES  32 D  485  GLU LEU VAL GLY SER LEU LEU GLU GLN SER ALA PRO TRP          
SEQRES  33 D  485  GLN GLU ARG SER THR MET SER LEU PRO PRO GLY LEU LEU          
SEQRES  34 D  485  GLY ASN SER TRP GLY GLU GLY ALA PRO ALA TRP VAL LEU          
SEQRES  35 D  485  LEU ASP GLU CYS GLY LEU GLU LEU GLY GLU ASP THR PRO          
SEQRES  36 D  485  HIS VAL CYS TRP GLU PRO GLN ALA GLN GLY ARG MET CYS          
SEQRES  37 D  485  ALA LEU TYR ALA SER LEU ALA LEU LEU SER GLY LEU SER          
SEQRES  38 D  485  GLN GLU PRO HIS                                              
HELIX    1 AA1 SER A    3  ASP A   17  1                                  15    
HELIX    2 AA2 ASP A  126  ARG A  137  1                                  12    
HELIX    3 AA3 VAL A  146  GLY A  154  1                                   9    
HELIX    4 AA4 ASP A  286  GLU A  300  1                                  15    
HELIX    5 AA5 ASP A  305  ARG A  321  1                                  17    
HELIX    6 AA6 ASP A  322  LEU A  333  1                                  12    
HELIX    7 AA7 ASP A  346  VAL A  357  1                                  12    
HELIX    8 AA8 VAL A  364  LEU A  381  1                                  18    
HELIX    9 AA9 SER A  382  SER A  395  1                                  14    
HELIX   10 AB1 LEU A  399  SER A  412  1                                  14    
HELIX   11 AB2 PRO A  424  GLY A  429  1                                   6    
HELIX   12 AB3 ALA A  436  GLY A  446  1                                  11    
HELIX   13 AB4 GLU A  459  GLN A  461  5                                   3    
HELIX   14 AB5 ALA A  462  SER A  480  1                                  19    
HELIX   15 AB6 ALA B    4  ASP B   17  1                                  14    
HELIX   16 AB7 ILE B   61  LEU B   65  5                                   5    
HELIX   17 AB8 ASP B  126  ARG B  137  1                                  12    
HELIX   18 AB9 VAL B  146  GLY B  154  1                                   9    
HELIX   19 AC1 ASP B  286  GLU B  300  1                                  15    
HELIX   20 AC2 ASP B  305  ASP B  322  1                                  18    
HELIX   21 AC3 ASP B  322  LEU B  333  1                                  12    
HELIX   22 AC4 ASP B  346  GLU B  354  1                                   9    
HELIX   23 AC5 VAL B  364  LEU B  381  1                                  18    
HELIX   24 AC6 SER B  382  GLN B  396  1                                  15    
HELIX   25 AC7 LEU B  399  SER B  412  1                                  14    
HELIX   26 AC8 PRO B  424  GLY B  429  1                                   6    
HELIX   27 AC9 ALA B  436  GLY B  446  1                                  11    
HELIX   28 AD1 ALA B  462  GLN B  481  1                                  20    
HELIX   29 AD2 SER C    3  LEU C   16  1                                  14    
HELIX   30 AD3 SER C   27  THR C   32  1                                   6    
HELIX   31 AD4 LYS C   62  LEU C   65  5                                   4    
HELIX   32 AD5 PRO C  127  ARG C  137  1                                  11    
HELIX   33 AD6 VAL C  146  GLY C  154  1                                   9    
HELIX   34 AD7 ASP C  286  GLU C  300  1                                  15    
HELIX   35 AD8 ASP C  305  ARG C  321  1                                  17    
HELIX   36 AD9 ASP C  322  LEU C  333  1                                  12    
HELIX   37 AE1 ASP C  346  VAL C  357  1                                  12    
HELIX   38 AE2 VAL C  364  LEU C  381  1                                  18    
HELIX   39 AE3 SER C  382  GLN C  396  1                                  15    
HELIX   40 AE4 LEU C  399  SER C  412  1                                  14    
HELIX   41 AE5 ALA C  436  CYS C  445  1                                  10    
HELIX   42 AE6 GLU C  459  GLN C  461  5                                   3    
HELIX   43 AE7 ALA C  462  SER C  480  1                                  19    
HELIX   44 AE8 SER D    3  GLU D   15  1                                  13    
HELIX   45 AE9 SER D   27  THR D   32  1                                   6    
HELIX   46 AF1 LYS D   62  LEU D   65  5                                   4    
HELIX   47 AF2 PRO D  127  ARG D  137  1                                  11    
HELIX   48 AF3 VAL D  146  GLY D  154  1                                   9    
HELIX   49 AF4 ASP D  286  GLU D  300  1                                  15    
HELIX   50 AF5 ASP D  305  ARG D  321  1                                  17    
HELIX   51 AF6 ASP D  322  LEU D  333  1                                  12    
HELIX   52 AF7 ASP D  346  GLU D  354  1                                   9    
HELIX   53 AF8 VAL D  364  LEU D  381  1                                  18    
HELIX   54 AF9 SER D  382  GLN D  396  1                                  15    
HELIX   55 AG1 LEU D  399  SER D  412  1                                  14    
HELIX   56 AG2 ALA D  436  GLY D  446  1                                  11    
HELIX   57 AG3 ALA D  462  SER D  480  1                                  19    
SHEET    1 AA1 4 ILE A  23  PRO A  24  0                                        
SHEET    2 AA1 4 ALA A 215  LEU A 221 -1  O  PHE A 216   N  ILE A  23           
SHEET    3 AA1 4 ASN A 156  GLN A 165 -1  N  THR A 161   O  ARG A 217           
SHEET    4 AA1 4 TYR A 121  LEU A 123 -1  N  TYR A 121   O  GLN A 165           
SHEET    1 AA2 5 LYS A  55  CYS A  56  0                                        
SHEET    2 AA2 5 LEU A  39  ARG A  42 -1  N  VAL A  41   O  LYS A  55           
SHEET    3 AA2 5 ASN A 156  GLN A 165 -1  O  TYR A 158   N  VAL A  40           
SHEET    4 AA2 5 ALA A 215  LEU A 221 -1  O  ARG A 217   N  THR A 161           
SHEET    5 AA2 5 VAL A 229  LEU A 230 -1  O  LEU A 230   N  GLN A 220           
SHEET    1 AA3 2 GLU A 448  LEU A 449  0                                        
SHEET    2 AA3 2 VAL A 456  CYS A 457 -1  O  CYS A 457   N  GLU A 448           
SHEET    1 AA4 4 LYS B  55  CYS B  56  0                                        
SHEET    2 AA4 4 VAL B  40  ARG B  42 -1  N  VAL B  41   O  LYS B  55           
SHEET    3 AA4 4 ASN B 156  GLN B 165 -1  O  TYR B 158   N  VAL B  40           
SHEET    4 AA4 4 TYR B 121  SER B 124 -1  N  LEU B 123   O  VAL B 163           
SHEET    1 AA5 5 LYS B  55  CYS B  56  0                                        
SHEET    2 AA5 5 VAL B  40  ARG B  42 -1  N  VAL B  41   O  LYS B  55           
SHEET    3 AA5 5 ASN B 156  GLN B 165 -1  O  TYR B 158   N  VAL B  40           
SHEET    4 AA5 5 ALA B 215  ILE B 223 -1  O  ALA B 219   N  VAL B 159           
SHEET    5 AA5 5 LEU B 227  LEU B 230 -1  O  LEU B 230   N  GLN B 220           
SHEET    1 AA6 4 ILE C  23  PRO C  24  0                                        
SHEET    2 AA6 4 SER C 212  ILE C 223 -1  O  PHE C 216   N  ILE C  23           
SHEET    3 AA6 4 ASN C 156  THR C 166 -1  N  LEU C 164   O  ALA C 215           
SHEET    4 AA6 4 TYR C 121  LEU C 123 -1  N  TYR C 121   O  GLN C 165           
SHEET    1 AA7 5 LYS C  55  SER C  60  0                                        
SHEET    2 AA7 5 CYS C  38  ARG C  42 -1  N  VAL C  41   O  LYS C  55           
SHEET    3 AA7 5 ASN C 156  THR C 166 -1  O  TYR C 158   N  VAL C  40           
SHEET    4 AA7 5 SER C 212  ILE C 223 -1  O  ALA C 215   N  LEU C 164           
SHEET    5 AA7 5 LEU C 227  LEU C 230 -1  O  LEU C 230   N  GLN C 220           
SHEET    1 AA8 4 LYS D  55  SER D  60  0                                        
SHEET    2 AA8 4 CYS D  38  ARG D  42 -1  N  VAL D  41   O  LYS D  55           
SHEET    3 AA8 4 ASN D 156  THR D 166 -1  O  TYR D 158   N  VAL D  40           
SHEET    4 AA8 4 VAL D 120  LEU D 123 -1  N  TYR D 121   O  GLN D 165           
SHEET    1 AA9 5 LYS D  55  SER D  60  0                                        
SHEET    2 AA9 5 CYS D  38  ARG D  42 -1  N  VAL D  41   O  LYS D  55           
SHEET    3 AA9 5 ASN D 156  THR D 166 -1  O  TYR D 158   N  VAL D  40           
SHEET    4 AA9 5 ALA D 215  ILE D 223 -1  O  ALA D 215   N  LEU D 164           
SHEET    5 AA9 5 LEU D 227  LEU D 230 -1  O  LEU D 230   N  GLN D 220           
SHEET    1 AB1 2 THR D 420  MET D 421  0                                        
SHEET    2 AB1 2 VAL D 456  CYS D 457 -1  O  VAL D 456   N  MET D 421           
CISPEP   1 ALA A  413    PRO A  414          0        -2.24                     
CISPEP   2 THR A  453    PRO A  454          0        -8.85                     
CISPEP   3 ALA B  413    PRO B  414          0        -1.00                     
CISPEP   4 ALA C  413    PRO C  414          0        -2.91                     
CISPEP   5 THR C  453    PRO C  454          0         5.84                     
CISPEP   6 ALA D  413    PRO D  414          0        -1.55                     
CISPEP   7 THR D  453    PRO D  454          0        -3.07                     
CRYST1   58.640  105.550  151.790  90.00  94.47  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017053  0.000000  0.001332        0.00000                         
SCALE2      0.000000  0.009474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006608        0.00000                         
ATOM      1  N   SER A   3      18.864 -20.230  88.885  1.00190.86           N  
ANISOU    1  N   SER A   3    16696  29208  26613   1431    361  -2866       N  
ATOM      2  CA  SER A   3      19.804 -19.117  88.802  1.00197.51           C  
ANISOU    2  CA  SER A   3    17231  30046  27767   1394    120  -2788       C  
ATOM      3  C   SER A   3      20.207 -18.867  87.354  1.00201.51           C  
ANISOU    3  C   SER A   3    17821  30244  28500   1481     82  -2424       C  
ATOM      4  O   SER A   3      19.355 -18.791  86.470  1.00201.76           O  
ANISOU    4  O   SER A   3    18018  29937  28705   1448     68  -2506       O  
ATOM      5  CB  SER A   3      21.047 -19.394  89.653  1.00197.75           C  
ANISOU    5  CB  SER A   3    17135  30438  27564   1442    164  -2531       C  
ATOM      6  OG  SER A   3      20.696 -19.916  90.923  1.00198.49           O  
ANISOU    6  OG  SER A   3    17222  30845  27350   1346    251  -2784       O  
ATOM      7  N   ALA A   4      21.517 -18.731  87.129  1.00202.06           N  
ANISOU    7  N   ALA A   4    17771  30438  28565   1571     59  -2011       N  
ATOM      8  CA  ALA A   4      22.040 -18.514  85.783  1.00205.93           C  
ANISOU    8  CA  ALA A   4    18304  30727  29214   1638     34  -1625       C  
ATOM      9  C   ALA A   4      21.617 -19.633  84.843  1.00204.10           C  
ANISOU    9  C   ALA A   4    18474  30334  28742   1791    334  -1420       C  
ATOM     10  O   ALA A   4      21.403 -19.401  83.647  1.00207.85           O  
ANISOU   10  O   ALA A   4    19055  30530  29387   1774    300  -1284       O  
ATOM     11  CB  ALA A   4      23.562 -18.388  85.823  1.00213.34           C  
ANISOU   11  CB  ALA A   4    19053  31900  30105   1736     17  -1189       C  
ATOM     12  N   PHE A   5      21.516 -20.850  85.378  1.00198.64           N  
ANISOU   12  N   PHE A   5    18002  29813  27657   1928    593  -1381       N  
ATOM     13  CA  PHE A   5      21.111 -22.034  84.627  1.00197.15           C  
ANISOU   13  CA  PHE A   5    18206  29490  27213   2108    843  -1192       C  
ATOM     14  C   PHE A   5      19.855 -21.819  83.785  1.00206.34           C  
ANISOU   14  C   PHE A   5    19581  30241  28576   2027    797  -1382       C  
ATOM     15  O   PHE A   5      19.681 -22.484  82.758  1.00203.90           O  
ANISOU   15  O   PHE A   5    19579  29727  28165   2170    946  -1147       O  
ATOM     16  CB  PHE A   5      20.922 -23.177  85.630  1.00188.75           C  
ANISOU   16  CB  PHE A   5    17278  28671  25767   2180    995  -1245       C  
ATOM     17  CG  PHE A   5      20.404 -24.452  85.041  1.00178.87           C  
ANISOU   17  CG  PHE A   5    16423  27289  24251   2370   1185  -1081       C  
ATOM     18  CD1 PHE A   5      21.177 -25.206  84.173  1.00170.60           C  
ANISOU   18  CD1 PHE A   5    15540  26229  23053   2617   1337   -680       C  
ATOM     19  CD2 PHE A   5      19.155 -24.925  85.407  1.00175.35           C  
ANISOU   19  CD2 PHE A   5    16172  26756  23697   2311   1193  -1332       C  
ATOM     20  CE1 PHE A   5      20.693 -26.388  83.653  1.00167.19           C  
ANISOU   20  CE1 PHE A   5    15472  25666  22388   2814   1466   -544       C  
ATOM     21  CE2 PHE A   5      18.668 -26.104  84.894  1.00170.15           C  
ANISOU   21  CE2 PHE A   5    15882  25963  22804   2495   1314  -1153       C  
ATOM     22  CZ  PHE A   5      19.440 -26.838  84.018  1.00167.03           C  
ANISOU   22  CZ  PHE A   5    15659  25528  22275   2755   1438   -763       C  
ATOM     23  N   GLU A   6      18.956 -20.930  84.206  1.00199.60           N  
ANISOU   23  N   GLU A   6    18577  29246  28016   1803    586  -1815       N  
ATOM     24  CA  GLU A   6      17.792 -20.616  83.381  1.00199.27           C  
ANISOU   24  CA  GLU A   6    18713  28756  28245   1691    503  -1994       C  
ATOM     25  C   GLU A   6      18.181 -19.871  82.104  1.00197.63           C  
ANISOU   25  C   GLU A   6    18464  28278  28348   1615    355  -1761       C  
ATOM     26  O   GLU A   6      17.874 -20.323  80.995  1.00200.86           O  
ANISOU   26  O   GLU A   6    19184  28403  28730   1675    465  -1545       O  
ATOM     27  CB  GLU A   6      16.777 -19.812  84.195  1.00207.93           C  
ANISOU   27  CB  GLU A   6    19609  29779  29617   1465    291  -2555       C  
ATOM     28  CG  GLU A   6      15.824 -20.660  85.040  1.00212.84           C  
ANISOU   28  CG  GLU A   6    20399  30517  29952   1492    455  -2806       C  
ATOM     29  CD  GLU A   6      14.808 -21.466  84.232  1.00217.78           C  
ANISOU   29  CD  GLU A   6    21455  30780  30511   1568    594  -2714       C  
ATOM     30  OE1 GLU A   6      15.078 -21.825  83.066  1.00219.85           O  
ANISOU   30  OE1 GLU A   6    21973  30796  30765   1688    674  -2342       O  
ATOM     31  OE2 GLU A   6      13.719 -21.743  84.781  1.00219.45           O  
ANISOU   31  OE2 GLU A   6    21747  30963  30670   1504    620  -3014       O  
ATOM     32  N   ARG A   7      18.840 -18.714  82.245  1.00203.06           N  
ANISOU   32  N   ARG A   7    18767  29052  29334   1465     75  -1792       N  
ATOM     33  CA  ARG A   7      19.201 -17.879  81.094  1.00206.59           C  
ANISOU   33  CA  ARG A   7    19112  29279  30102   1324   -145  -1569       C  
ATOM     34  C   ARG A   7      19.860 -18.665  79.966  1.00221.27           C  
ANISOU   34  C   ARG A   7    21228  31157  31688   1503    118  -1063       C  
ATOM     35  O   ARG A   7      19.525 -18.479  78.790  1.00220.31           O  
ANISOU   35  O   ARG A   7    21262  30720  31727   1394     62   -930       O  
ATOM     36  CB  ARG A   7      20.112 -16.729  81.537  1.00196.97           C  
ANISOU   36  CB  ARG A   7    17430  28270  29141   1202   -478  -1556       C  
ATOM     37  CG  ARG A   7      21.026 -16.170  80.421  1.00192.69           C  
ANISOU   37  CG  ARG A   7    16756  27714  28746   1128   -634  -1111       C  
ATOM     38  CD  ARG A   7      20.343 -15.470  79.238  1.00194.18           C  
ANISOU   38  CD  ARG A   7    16988  27464  29327    853   -905  -1126       C  
ATOM     39  NE  ARG A   7      19.833 -14.134  79.522  1.00196.44           N  
ANISOU   39  NE  ARG A   7    16943  27530  30167    552  -1430  -1491       N  
ATOM     40  CZ  ARG A   7      19.412 -13.299  78.577  1.00196.22           C  
ANISOU   40  CZ  ARG A   7    16890  27129  30536    243  -1788  -1473       C  
ATOM     41  NH1 ARG A   7      19.458 -13.670  77.304  1.00196.44           N  
ANISOU   41  NH1 ARG A   7    17129  27001  30507    193  -1662  -1124       N  
ATOM     42  NH2 ARG A   7      18.960 -12.096  78.899  1.00196.24           N  
ANISOU   42  NH2 ARG A   7    17019  26871  30671    -31  -2179  -1686       N  
ATOM     43  N   VAL A   8      20.824 -19.524  80.296  1.00198.34           N  
ANISOU   43  N   VAL A   8    18355  28620  28387   1763    387   -785       N  
ATOM     44  CA  VAL A   8      21.561 -20.241  79.257  1.00206.46           C  
ANISOU   44  CA  VAL A   8    19569  29718  29159   1958    630   -337       C  
ATOM     45  C   VAL A   8      20.603 -21.080  78.422  1.00199.47           C  
ANISOU   45  C   VAL A   8    19141  28500  28149   2044    815   -332       C  
ATOM     46  O   VAL A   8      20.660 -21.076  77.186  1.00209.04           O  
ANISOU   46  O   VAL A   8    20504  29535  29385   2024    851    -97       O  
ATOM     47  CB  VAL A   8      22.675 -21.102  79.877  1.00210.63           C  
ANISOU   47  CB  VAL A   8    20048  30667  29316   2232    871   -103       C  
ATOM     48  CG1 VAL A   8      23.992 -20.334  79.862  1.00211.56           C  
ANISOU   48  CG1 VAL A   8    19785  31055  29542   2190    740    168       C  
ATOM     49  CG2 VAL A   8      22.296 -21.568  81.266  1.00215.84           C  
ANISOU   49  CG2 VAL A   8    20711  31468  29828   2269    908   -388       C  
ATOM     50  N   VAL A   9      19.723 -21.832  79.088  1.00219.03           N  
ANISOU   50  N   VAL A   9    21847  30902  30473   2134    924   -569       N  
ATOM     51  CA  VAL A   9      18.751 -22.650  78.371  1.00187.43           C  
ANISOU   51  CA  VAL A   9    18297  26553  26364   2229   1062   -550       C  
ATOM     52  C   VAL A   9      17.912 -21.784  77.437  1.00180.51           C  
ANISOU   52  C   VAL A   9    17496  25198  25891   1951    856   -649       C  
ATOM     53  O   VAL A   9      17.542 -22.215  76.338  1.00174.60           O  
ANISOU   53  O   VAL A   9    17089  24148  25102   1996    948   -465       O  
ATOM     54  CB  VAL A   9      17.880 -23.437  79.368  1.00174.08           C  
ANISOU   54  CB  VAL A   9    16775  24877  24488   2314   1136   -798       C  
ATOM     55  CG1 VAL A   9      16.910 -24.325  78.628  1.00168.28           C  
ANISOU   55  CG1 VAL A   9    16521  23775  23643   2439   1249   -724       C  
ATOM     56  CG2 VAL A   9      18.755 -24.272  80.287  1.00174.08           C  
ANISOU   56  CG2 VAL A   9    16684  25342  24118   2530   1285   -677       C  
ATOM     57  N   ARG A  10      17.589 -20.559  77.860  1.00172.58           N  
ANISOU   57  N   ARG A  10    16176  24096  25301   1650    544   -951       N  
ATOM     58  CA  ARG A  10      16.931 -19.610  76.965  1.00178.21           C  
ANISOU   58  CA  ARG A  10    16890  24350  26470   1333    268  -1032       C  
ATOM     59  C   ARG A  10      17.743 -19.388  75.695  1.00183.18           C  
ANISOU   59  C   ARG A  10    17524  24979  27099   1278    258   -613       C  
ATOM     60  O   ARG A  10      17.244 -19.596  74.584  1.00190.89           O  
ANISOU   60  O   ARG A  10    18815  25593  28120   1207    291   -468       O  
ATOM     61  CB  ARG A  10      16.687 -18.278  77.677  1.00182.29           C  
ANISOU   61  CB  ARG A  10    16981  24830  27452   1037   -127  -1419       C  
ATOM     62  CG  ARG A  10      15.419 -18.189  78.503  1.00190.16           C  
ANISOU   62  CG  ARG A  10    18006  25615  28631    951   -206  -1922       C  
ATOM     63  CD  ARG A  10      14.224 -18.143  77.555  1.00201.29           C  
ANISOU   63  CD  ARG A  10    19735  26413  30334    774   -289  -1992       C  
ATOM     64  NE  ARG A  10      12.930 -18.127  78.229  1.00213.73           N  
ANISOU   64  NE  ARG A  10    21367  27749  32093    698   -342  -2455       N  
ATOM     65  CZ  ARG A  10      11.779 -17.879  77.609  1.00223.13           C  
ANISOU   65  CZ  ARG A  10    22761  28362  33656    493   -487  -2613       C  
ATOM     66  NH1 ARG A  10      11.770 -17.614  76.310  1.00226.33           N  
ANISOU   66  NH1 ARG A  10    23343  28364  34288    319   -608  -2340       N  
ATOM     67  NH2 ARG A  10      10.642 -17.867  78.288  1.00225.59           N  
ANISOU   67  NH2 ARG A  10    23087  28500  34127    437   -522  -3044       N  
ATOM     68  N   ARG A  11      19.006 -18.970  75.838  1.00207.63           N  
ANISOU   68  N   ARG A  11    20271  28488  30133   1300    209   -400       N  
ATOM     69  CA  ARG A  11      19.822 -18.718  74.653  1.00190.04           C  
ANISOU   69  CA  ARG A  11    17994  26333  27879   1226    194      9       C  
ATOM     70  C   ARG A  11      20.004 -19.988  73.830  1.00186.94           C  
ANISOU   70  C   ARG A  11    18010  25974  27045   1522    599    303       C  
ATOM     71  O   ARG A  11      20.235 -19.912  72.618  1.00195.81           O  
ANISOU   71  O   ARG A  11    19235  27018  28147   1427    618    579       O  
ATOM     72  CB  ARG A  11      21.172 -18.093  75.036  1.00183.91           C  
ANISOU   72  CB  ARG A  11    16758  26023  27098   1223     74    210       C  
ATOM     73  CG  ARG A  11      22.325 -19.063  75.250  1.00182.82           C  
ANISOU   73  CG  ARG A  11    16628  26353  26481   1597    446    504       C  
ATOM     74  CD  ARG A  11      23.695 -18.385  75.056  1.00180.90           C  
ANISOU   74  CD  ARG A  11    15979  26493  26263   1541    322    849       C  
ATOM     75  NE  ARG A  11      24.035 -17.397  76.081  1.00177.10           N  
ANISOU   75  NE  ARG A  11    15082  26144  26062   1401    -16    710       N  
ATOM     76  CZ  ARG A  11      25.185 -16.725  76.121  1.00173.16           C  
ANISOU   76  CZ  ARG A  11    14203  25959  25631   1350   -193   1000       C  
ATOM     77  NH1 ARG A  11      26.116 -16.926  75.196  1.00164.11           N  
ANISOU   77  NH1 ARG A  11    13013  25062  24280   1413    -40   1437       N  
ATOM     78  NH2 ARG A  11      25.407 -15.845  77.088  1.00179.12           N  
ANISOU   78  NH2 ARG A  11    14614  26788  26656   1239   -531    854       N  
ATOM     79  N   VAL A  12      19.917 -21.159  74.466  1.00187.97           N  
ANISOU   79  N   VAL A  12    18365  26236  26821   1870    896    248       N  
ATOM     80  CA  VAL A  12      19.941 -22.416  73.721  1.00184.47           C  
ANISOU   80  CA  VAL A  12    18331  25765  25994   2176   1223    475       C  
ATOM     81  C   VAL A  12      18.735 -22.506  72.791  1.00179.10           C  
ANISOU   81  C   VAL A  12    18062  24524  25465   2039   1177    430       C  
ATOM     82  O   VAL A  12      18.873 -22.735  71.585  1.00183.46           O  
ANISOU   82  O   VAL A  12    18830  24962  25915   2047   1273    684       O  
ATOM     83  CB  VAL A  12      20.000 -23.616  74.686  1.00188.70           C  
ANISOU   83  CB  VAL A  12    18999  26520  26179   2538   1449    407       C  
ATOM     84  CG1 VAL A  12      19.738 -24.915  73.933  1.00187.97           C  
ANISOU   84  CG1 VAL A  12    19371  26288  25760   2849   1696    579       C  
ATOM     85  CG2 VAL A  12      21.346 -23.664  75.393  1.00194.85           C  
ANISOU   85  CG2 VAL A  12    19421  27828  26786   2685   1525    536       C  
ATOM     86  N   VAL A  13      17.531 -22.337  73.342  1.00184.70           N  
ANISOU   86  N   VAL A  13    18887  24875  26415   1906   1032    106       N  
ATOM     87  CA  VAL A  13      16.323 -22.449  72.528  1.00174.22           C  
ANISOU   87  CA  VAL A  13    17971  22957  25267   1773    976     68       C  
ATOM     88  C   VAL A  13      16.042 -21.167  71.753  1.00182.06           C  
ANISOU   88  C   VAL A  13    18821  23611  26743   1306    649     45       C  
ATOM     89  O   VAL A  13      15.335 -21.201  70.740  1.00182.35           O  
ANISOU   89  O   VAL A  13    19195  23171  26918   1151    603    135       O  
ATOM     90  CB  VAL A  13      15.111 -22.832  73.392  1.00157.74           C  
ANISOU   90  CB  VAL A  13    16070  20615  23250   1818    954   -252       C  
ATOM     91  CG1 VAL A  13      15.192 -24.293  73.798  1.00145.67           C  
ANISOU   91  CG1 VAL A  13    14818  19296  21235   2253   1238   -136       C  
ATOM     92  CG2 VAL A  13      14.999 -21.914  74.589  1.00164.18           C  
ANISOU   92  CG2 VAL A  13    16450  21587  24342   1616    735   -626       C  
ATOM     93  N   GLN A  14      16.539 -20.023  72.231  1.00162.68           N  
ANISOU   93  N   GLN A  14    15875  21359  24577   1057    372    -75       N  
ATOM     94  CA  GLN A  14      16.384 -18.768  71.500  1.00194.78           C  
ANISOU   94  CA  GLN A  14    19746  25137  29124    587    -21    -68       C  
ATOM     95  C   GLN A  14      16.836 -18.908  70.053  1.00224.97           C  
ANISOU   95  C   GLN A  14    23756  28919  32805    498     58    349       C  
ATOM     96  O   GLN A  14      16.065 -18.664  69.118  1.00225.36           O  
ANISOU   96  O   GLN A  14    24058  28459  33108    209    -93    386       O  
ATOM     97  CB  GLN A  14      17.178 -17.657  72.191  1.00205.02           C  
ANISOU   97  CB  GLN A  14    20460  26784  30653    417   -327   -153       C  
ATOM     98  CG  GLN A  14      16.809 -16.251  71.754  1.00212.05           C  
ANISOU   98  CG  GLN A  14    21082  27332  32154    -99   -867   -263       C  
ATOM     99  CD  GLN A  14      17.861 -15.223  72.138  1.00216.69           C  
ANISOU   99  CD  GLN A  14    21108  28319  32905   -240  -1190   -185       C  
ATOM    100  OE1 GLN A  14      19.045 -15.541  72.259  1.00217.70           O  
ANISOU  100  OE1 GLN A  14    21089  28967  32661     -6   -979    111       O  
ATOM    101  NE2 GLN A  14      17.428 -13.986  72.346  1.00218.33           N  
ANISOU  101  NE2 GLN A  14    20992  28268  33696   -617  -1732   -452       N  
ATOM    102  N   GLU A  15      18.097 -19.288  69.848  1.00205.71           N  
ANISOU  102  N   GLU A  15    21182  27015  29963    726    289    664       N  
ATOM    103  CA  GLU A  15      18.603 -19.449  68.491  1.00215.90           C  
ANISOU  103  CA  GLU A  15    22614  28361  31058    656    398   1047       C  
ATOM    104  C   GLU A  15      18.084 -20.711  67.809  1.00216.69           C  
ANISOU  104  C   GLU A  15    23292  28221  30818    943    747   1147       C  
ATOM    105  O   GLU A  15      18.197 -20.821  66.584  1.00224.49           O  
ANISOU  105  O   GLU A  15    24482  29119  31694    830    809   1409       O  
ATOM    106  CB  GLU A  15      20.131 -19.457  68.505  1.00222.92           C  
ANISOU  106  CB  GLU A  15    23146  29927  31629    824    543   1335       C  
ATOM    107  CG  GLU A  15      20.797 -18.890  67.255  1.00231.95           C  
ANISOU  107  CG  GLU A  15    24146  31226  32757    524    438   1699       C  
ATOM    108  CD  GLU A  15      20.386 -17.458  66.931  1.00236.98           C  
ANISOU  108  CD  GLU A  15    24524  31560  33958    -80   -119   1668       C  
ATOM    109  OE1 GLU A  15      19.224 -17.218  66.538  1.00236.65           O  
ANISOU  109  OE1 GLU A  15    24749  30916  34250   -366   -323   1506       O  
ATOM    110  OE2 GLU A  15      21.239 -16.560  67.082  1.00240.52           O  
ANISOU  110  OE2 GLU A  15    24486  32358  34541   -277   -391   1815       O  
ATOM    111  N   LEU A  16      17.530 -21.664  68.560  1.00229.63           N  
ANISOU  111  N   LEU A  16    25197  29768  32283   1301    950    960       N  
ATOM    112  CA  LEU A  16      16.976 -22.874  67.963  1.00184.14           C  
ANISOU  112  CA  LEU A  16    19993  23741  26229   1593   1213   1061       C  
ATOM    113  C   LEU A  16      15.529 -22.715  67.505  1.00175.59           C  
ANISOU  113  C   LEU A  16    19303  21919  25493   1335   1032    942       C  
ATOM    114  O   LEU A  16      15.018 -23.594  66.803  1.00175.99           O  
ANISOU  114  O   LEU A  16    19853  21663  25355   1516   1194   1078       O  
ATOM    115  CB  LEU A  16      17.085 -24.037  68.962  1.00160.68           C  
ANISOU  115  CB  LEU A  16    17120  21029  22902   2091   1464    968       C  
ATOM    116  CG  LEU A  16      16.797 -25.463  68.487  1.00150.77           C  
ANISOU  116  CG  LEU A  16    16378  19641  21266   2507   1723   1108       C  
ATOM    117  CD1 LEU A  16      17.488 -25.737  67.162  1.00149.73           C  
ANISOU  117  CD1 LEU A  16    16379  19631  20881   2578   1892   1413       C  
ATOM    118  CD2 LEU A  16      17.235 -26.466  69.537  1.00151.08           C  
ANISOU  118  CD2 LEU A  16    16361  20072  20971   2945   1895   1052       C  
ATOM    119  N   ASP A  17      14.881 -21.606  67.861  1.00184.73           N  
ANISOU  119  N   ASP A  17    20245  22769  27176    919    678    694       N  
ATOM    120  CA  ASP A  17      13.500 -21.300  67.472  1.00178.05           C  
ANISOU  120  CA  ASP A  17    19712  21181  26759    614    456    551       C  
ATOM    121  C   ASP A  17      12.538 -22.457  67.756  1.00192.96           C  
ANISOU  121  C   ASP A  17    22094  22753  28468    956    658    482       C  
ATOM    122  O   ASP A  17      11.714 -22.834  66.919  1.00201.02           O  
ANISOU  122  O   ASP A  17    23595  23221  29561    901    659    603       O  
ATOM    123  CB  ASP A  17      13.428 -20.875  66.007  1.00170.35           C  
ANISOU  123  CB  ASP A  17    18925  19858  25942    241    319    819       C  
ATOM    124  CG  ASP A  17      14.355 -19.717  65.695  1.00176.54           C  
ANISOU  124  CG  ASP A  17    19202  20969  26906   -139     60    931       C  
ATOM    125  OD1 ASP A  17      14.194 -18.645  66.315  1.00178.66           O  
ANISOU  125  OD1 ASP A  17    19069  21181  27632   -449   -308    683       O  
ATOM    126  OD2 ASP A  17      15.248 -19.882  64.837  1.00179.72           O  
ANISOU  126  OD2 ASP A  17    19593  21703  26989   -123    206   1267       O  
ATOM    127  N   HIS A  18      12.651 -23.016  68.963  1.00191.43           N  
ANISOU  127  N   HIS A  18    21777  22915  28043   1293    803    309       N  
ATOM    128  CA  HIS A  18      11.764 -24.078  69.448  1.00188.47           C  
ANISOU  128  CA  HIS A  18    21786  22329  27496   1603    939    238       C  
ATOM    129  C   HIS A  18      11.658 -25.228  68.442  1.00185.46           C  
ANISOU  129  C   HIS A  18    21960  21733  26774   1899   1145    575       C  
ATOM    130  O   HIS A  18      10.567 -25.651  68.056  1.00185.51           O  
ANISOU  130  O   HIS A  18    22423  21168  26893   1902   1102    611       O  
ATOM    131  CB  HIS A  18      10.388 -23.494  69.775  1.00192.85           C  
ANISOU  131  CB  HIS A  18    22409  22314  28552   1298    690    -69       C  
ATOM    132  CG  HIS A  18       9.573 -24.322  70.722  1.00197.11           C  
ANISOU  132  CG  HIS A  18    23129  22819  28945   1563    781   -229       C  
ATOM    133  ND1 HIS A  18      10.069 -24.792  71.919  1.00198.85           N  
ANISOU  133  ND1 HIS A  18    23095  23624  28833   1833    912   -345       N  
ATOM    134  CD2 HIS A  18       8.283 -24.732  70.664  1.00196.03           C  
ANISOU  134  CD2 HIS A  18    23386  22137  28960   1562    731   -276       C  
ATOM    135  CE1 HIS A  18       9.125 -25.467  72.551  1.00196.25           C  
ANISOU  135  CE1 HIS A  18    22983  23150  28432   1977    935   -453       C  
ATOM    136  NE2 HIS A  18       8.031 -25.446  71.810  1.00194.35           N  
ANISOU  136  NE2 HIS A  18    23134  22230  28480   1832    832   -410       N  
ATOM    137  N   GLY A  19      12.812 -25.737  68.014  1.00172.29           N  
ANISOU  137  N   GLY A  19    20245  20522  24696   2160   1358    820       N  
ATOM    138  CA  GLY A  19      12.835 -26.799  67.024  1.00172.38           C  
ANISOU  138  CA  GLY A  19    20740  20388  24370   2464   1543   1112       C  
ATOM    139  C   GLY A  19      12.321 -28.131  67.532  1.00180.23           C  
ANISOU  139  C   GLY A  19    22087  21317  25076   2921   1643   1134       C  
ATOM    140  O   GLY A  19      12.971 -28.786  68.351  1.00179.27           O  
ANISOU  140  O   GLY A  19    21778  21697  24640   3253   1760   1107       O  
ATOM    141  N   GLY A  20      11.158 -28.545  67.038  1.00187.82           N  
ANISOU  141  N   GLY A  20    23561  21643  26158   2924   1563   1208       N  
ATOM    142  CA  GLY A  20      10.516 -29.773  67.490  1.00187.60           C  
ANISOU  142  CA  GLY A  20    23891  21484  25903   3321   1581   1263       C  
ATOM    143  C   GLY A  20      10.064 -29.739  68.934  1.00182.62           C  
ANISOU  143  C   GLY A  20    23010  21030  25349   3311   1494   1003       C  
ATOM    144  O   GLY A  20      10.225 -30.732  69.650  1.00167.55           O  
ANISOU  144  O   GLY A  20    21121  19430  23108   3671   1541   1040       O  
ATOM    145  N   GLU A  21       9.482 -28.624  69.364  1.00183.59           N  
ANISOU  145  N   GLU A  21    22890  20960  25907   2890   1342    732       N  
ATOM    146  CA  GLU A  21       8.964 -28.406  70.719  1.00196.39           C  
ANISOU  146  CA  GLU A  21    24236  22741  27642   2809   1255    423       C  
ATOM    147  C   GLU A  21       9.912 -28.974  71.786  1.00203.01           C  
ANISOU  147  C   GLU A  21    24744  24316  28075   3093   1375    384       C  
ATOM    148  O   GLU A  21       9.555 -29.805  72.623  1.00212.51           O  
ANISOU  148  O   GLU A  21    26016  25675  29054   3309   1369    368       O  
ATOM    149  CB  GLU A  21       7.530 -28.931  70.869  1.00202.59           C  
ANISOU  149  CB  GLU A  21    25428  23001  28547   2844   1149    418       C  
ATOM    150  CG  GLU A  21       7.277 -30.439  70.779  1.00207.80           C  
ANISOU  150  CG  GLU A  21    26539  23613  28802   3302   1196    719       C  
ATOM    151  CD  GLU A  21       5.957 -30.834  71.440  1.00206.88           C  
ANISOU  151  CD  GLU A  21    26626  23197  28783   3304   1063    652       C  
ATOM    152  OE1 GLU A  21       5.180 -29.925  71.807  1.00204.73           O  
ANISOU  152  OE1 GLU A  21    26190  22679  28918   2948    962    362       O  
ATOM    153  OE2 GLU A  21       5.700 -32.047  71.603  1.00206.16           O  
ANISOU  153  OE2 GLU A  21    26835  23128  28370   3658   1034    885       O  
ATOM    154  N   PHE A  22      11.149 -28.473  71.740  1.00213.00           N  
ANISOU  154  N   PHE A  22    25632  26031  29268   3055   1458    389       N  
ATOM    155  CA  PHE A  22      12.195 -28.792  72.713  1.00192.10           C  
ANISOU  155  CA  PHE A  22    22612  24062  26313   3249   1556    349       C  
ATOM    156  C   PHE A  22      11.896 -28.073  74.025  1.00189.98           C  
ANISOU  156  C   PHE A  22    21947  24002  26235   3006   1445    -10       C  
ATOM    157  O   PHE A  22      12.398 -26.979  74.305  1.00206.26           O  
ANISOU  157  O   PHE A  22    23590  26257  28523   2748   1381   -189       O  
ATOM    158  CB  PHE A  22      13.580 -28.422  72.197  1.00172.15           C  
ANISOU  158  CB  PHE A  22    19813  21909  23688   3268   1671    487       C  
ATOM    159  CG  PHE A  22      14.287 -29.543  71.489  1.00152.07           C  
ANISOU  159  CG  PHE A  22    17513  19517  20750   3674   1844    788       C  
ATOM    160  CD1 PHE A  22      13.712 -30.805  71.405  1.00133.35           C  
ANISOU  160  CD1 PHE A  22    15572  16952  18144   4010   1848    920       C  
ATOM    161  CD2 PHE A  22      15.553 -29.356  70.964  1.00158.29           C  
ANISOU  161  CD2 PHE A  22    18070  20674  21400   3737   1981    932       C  
ATOM    162  CE1 PHE A  22      14.376 -31.844  70.772  1.00137.19           C  
ANISOU  162  CE1 PHE A  22    16259  17580  18288   4409   1968   1156       C  
ATOM    163  CE2 PHE A  22      16.223 -30.388  70.333  1.00160.48           C  
ANISOU  163  CE2 PHE A  22    18534  21119  21322   4128   2143   1157       C  
ATOM    164  CZ  PHE A  22      15.631 -31.635  70.238  1.00152.80           C  
ANISOU  164  CZ  PHE A  22    17993  19928  20138   4473   2129   1251       C  
ATOM    165  N   ILE A  23      11.024 -28.686  74.823  1.00170.43           N  
ANISOU  165  N   ILE A  23    19604  21482  23668   3084   1398   -114       N  
ATOM    166  CA  ILE A  23      10.624 -28.131  76.112  1.00153.72           C  
ANISOU  166  CA  ILE A  23    17138  19591  21678   2871   1308   -478       C  
ATOM    167  C   ILE A  23      11.879 -27.960  76.960  1.00159.35           C  
ANISOU  167  C   ILE A  23    17398  20952  22196   2906   1372   -536       C  
ATOM    168  O   ILE A  23      12.604 -28.936  77.206  1.00173.51           O  
ANISOU  168  O   ILE A  23    19226  23094  23607   3192   1470   -325       O  
ATOM    169  CB  ILE A  23       9.605 -29.040  76.815  1.00153.78           C  
ANISOU  169  CB  ILE A  23    17372  19550  21507   2986   1268   -505       C  
ATOM    170  CG1 ILE A  23       8.345 -29.218  75.961  1.00143.00           C  
ANISOU  170  CG1 ILE A  23    16481  17492  20360   2960   1192   -410       C  
ATOM    171  CG2 ILE A  23       9.257 -28.479  78.178  1.00171.84           C  
ANISOU  171  CG2 ILE A  23    19263  22159  23870   2758   1202   -903       C  
ATOM    172  CD1 ILE A  23       7.341 -30.202  76.546  1.00132.46           C  
ANISOU  172  CD1 ILE A  23    15404  16096  18831   3101   1128   -353       C  
ATOM    173  N   PRO A  24      12.176 -26.745  77.411  1.00141.90           N  
ANISOU  173  N   PRO A  24    14760  18893  20264   2624   1287   -810       N  
ATOM    174  CA  PRO A  24      13.386 -26.514  78.202  1.00133.70           C  
ANISOU  174  CA  PRO A  24    13300  18426  19072   2646   1327   -840       C  
ATOM    175  C   PRO A  24      13.229 -27.015  79.627  1.00154.17           C  
ANISOU  175  C   PRO A  24    15743  21415  21419   2678   1330  -1016       C  
ATOM    176  O   PRO A  24      12.123 -27.168  80.147  1.00158.46           O  
ANISOU  176  O   PRO A  24    16382  21834  21991   2591   1270  -1222       O  
ATOM    177  CB  PRO A  24      13.525 -24.989  78.175  1.00130.59           C  
ANISOU  177  CB  PRO A  24    12535  17967  19116   2311   1160  -1087       C  
ATOM    178  CG  PRO A  24      12.129 -24.500  78.062  1.00133.45           C  
ANISOU  178  CG  PRO A  24    13024  17844  19835   2082   1011  -1367       C  
ATOM    179  CD  PRO A  24      11.404 -25.507  77.206  1.00130.27           C  
ANISOU  179  CD  PRO A  24    13166  17035  19298   2266   1105  -1107       C  
ATOM    180  N   VAL A  25      14.363 -27.263  80.261  1.00166.89           N  
ANISOU  180  N   VAL A  25    17107  23516  22788   2780   1394   -922       N  
ATOM    181  CA  VAL A  25      14.341 -27.661  81.660  1.00161.10           C  
ANISOU  181  CA  VAL A  25    16191  23199  21820   2748   1375  -1080       C  
ATOM    182  C   VAL A  25      14.163 -26.420  82.530  1.00165.52           C  
ANISOU  182  C   VAL A  25    16346  23899  22645   2439   1260  -1498       C  
ATOM    183  O   VAL A  25      14.543 -25.303  82.153  1.00162.69           O  
ANISOU  183  O   VAL A  25    15763  23440  22611   2296   1180  -1592       O  
ATOM    184  CB  VAL A  25      15.624 -28.443  82.005  1.00146.77           C  
ANISOU  184  CB  VAL A  25    14283  21806  19677   2955   1459   -809       C  
ATOM    185  CG1 VAL A  25      16.835 -27.533  81.964  1.00149.14           C  
ANISOU  185  CG1 VAL A  25    14229  22306  20130   2886   1473   -785       C  
ATOM    186  CG2 VAL A  25      15.492 -29.129  83.344  1.00146.81           C  
ANISOU  186  CG2 VAL A  25    14193  22193  19394   2915   1413   -896       C  
ATOM    187  N   THR A  26      13.589 -26.617  83.718  1.00156.49           N  
ANISOU  187  N   THR A  26    15090  23013  21357   2327   1225  -1754       N  
ATOM    188  CA  THR A  26      13.270 -25.516  84.621  1.00174.14           C  
ANISOU  188  CA  THR A  26    16951  25397  23819   2049   1111  -2216       C  
ATOM    189  C   THR A  26      14.294 -25.357  85.743  1.00186.47           C  
ANISOU  189  C   THR A  26    18157  27493  25202   1994   1105  -2270       C  
ATOM    190  O   THR A  26      14.910 -24.295  85.877  1.00192.22           O  
ANISOU  190  O   THR A  26    18568  28287  26179   1880   1010  -2410       O  
ATOM    191  CB  THR A  26      11.857 -25.712  85.193  1.00181.97           C  
ANISOU  191  CB  THR A  26    18023  26329  24787   1926   1080  -2522       C  
ATOM    192  OG1 THR A  26      11.811 -26.906  85.985  1.00193.57           O  
ANISOU  192  OG1 THR A  26    19593  28164  25790   2008   1142  -2373       O  
ATOM    193  CG2 THR A  26      10.831 -25.822  84.065  1.00174.47           C  
ANISOU  193  CG2 THR A  26    17444  24782  24065   1968   1066  -2448       C  
ATOM    194  N   SER A  27      14.490 -26.397  86.554  1.00183.16           N  
ANISOU  194  N   SER A  27    17786  27438  24370   2056   1169  -2139       N  
ATOM    195  CA  SER A  27      15.353 -26.342  87.727  1.00176.60           C  
ANISOU  195  CA  SER A  27    16648  27098  23352   1958   1150  -2191       C  
ATOM    196  C   SER A  27      16.578 -27.228  87.536  1.00166.12           C  
ANISOU  196  C   SER A  27    15406  25927  21786   2165   1222  -1736       C  
ATOM    197  O   SER A  27      16.633 -28.086  86.649  1.00170.94           O  
ANISOU  197  O   SER A  27    16321  26334  22295   2399   1287  -1414       O  
ATOM    198  CB  SER A  27      14.580 -26.762  88.984  1.00181.92           C  
ANISOU  198  CB  SER A  27    17252  28118  23753   1775   1123  -2448       C  
ATOM    199  OG  SER A  27      15.446 -26.951  90.093  1.00190.55           O  
ANISOU  199  OG  SER A  27    18114  29681  24604   1672   1104  -2418       O  
ATOM    200  N   LEU A  28      17.572 -27.015  88.394  1.00155.40           N  
ANISOU  200  N   LEU A  28    13769  24922  20354   2079   1195  -1725       N  
ATOM    201  CA  LEU A  28      18.789 -27.808  88.302  1.00163.36           C  
ANISOU  201  CA  LEU A  28    14812  26076  21180   2252   1245  -1321       C  
ATOM    202  C   LEU A  28      18.656 -29.138  89.044  1.00194.25           C  
ANISOU  202  C   LEU A  28    18854  30242  24710   2247   1212  -1185       C  
ATOM    203  O   LEU A  28      19.190 -30.155  88.587  1.00196.59           O  
ANISOU  203  O   LEU A  28    19330  30504  24860   2465   1230   -840       O  
ATOM    204  CB  LEU A  28      19.972 -26.985  88.820  1.00151.16           C  
ANISOU  204  CB  LEU A  28    12925  24739  19768   2161   1207  -1313       C  
ATOM    205  CG  LEU A  28      21.402 -27.494  88.651  1.00144.02           C  
ANISOU  205  CG  LEU A  28    11984  23947  18791   2328   1257   -911       C  
ATOM    206  CD1 LEU A  28      22.342 -26.302  88.642  1.00136.00           C  
ANISOU  206  CD1 LEU A  28    10666  22958  18051   2274   1209   -898       C  
ATOM    207  CD2 LEU A  28      21.774 -28.451  89.763  1.00151.92           C  
ANISOU  207  CD2 LEU A  28    12961  25270  19492   2238   1209   -815       C  
ATOM    208  N   GLN A  29      17.936 -29.164  90.174  1.00199.87           N  
ANISOU  208  N   GLN A  29    19463  31220  25257   1990   1138  -1455       N  
ATOM    209  CA  GLN A  29      17.734 -30.426  90.887  1.00202.04           C  
ANISOU  209  CA  GLN A  29    19847  31755  25163   1929   1050  -1304       C  
ATOM    210  C   GLN A  29      16.899 -31.437  90.115  1.00201.30           C  
ANISOU  210  C   GLN A  29    20120  31415  24951   2130   1024  -1113       C  
ATOM    211  O   GLN A  29      16.820 -32.596  90.539  1.00199.71           O  
ANISOU  211  O   GLN A  29    20029  31390  24463   2122    894   -907       O  
ATOM    212  CB  GLN A  29      17.011 -30.194  92.217  1.00197.25           C  
ANISOU  212  CB  GLN A  29    19046  31522  24379   1578    980  -1650       C  
ATOM    213  CG  GLN A  29      17.701 -29.321  93.233  1.00190.95           C  
ANISOU  213  CG  GLN A  29    17895  31028  23628   1338    963  -1869       C  
ATOM    214  CD  GLN A  29      16.754 -28.922  94.350  1.00189.55           C  
ANISOU  214  CD  GLN A  29    17534  31182  23305   1016    925  -2307       C  
ATOM    215  OE1 GLN A  29      16.035 -29.757  94.904  1.00183.26           O  
ANISOU  215  OE1 GLN A  29    16817  30624  22190    872    865  -2299       O  
ATOM    216  NE2 GLN A  29      16.732 -27.635  94.672  1.00195.64           N  
ANISOU  216  NE2 GLN A  29    18042  31983  24310    902    937  -2696       N  
ATOM    217  N   SER A  30      16.252 -30.980  89.037  1.00212.18           N  
ANISOU  217  N   SER A  30    21692  32375  26554   2300   1107  -1146       N  
ATOM    218  CA  SER A  30      15.386 -31.852  88.200  1.00189.76           C  
ANISOU  218  CA  SER A  30    19233  29234  23633   2511   1075   -949       C  
ATOM    219  C   SER A  30      15.964 -31.953  86.785  1.00177.30           C  
ANISOU  219  C   SER A  30    17873  27352  22142   2857   1142   -619       C  
ATOM    220  O   SER A  30      15.332 -32.607  85.932  1.00170.09           O  
ANISOU  220  O   SER A  30    17216  26364  21047   3078   1057   -331       O  
ATOM    221  CB  SER A  30      13.967 -31.345  88.180  1.00169.71           C  
ANISOU  221  CB  SER A  30    16795  26407  21279   2421   1103  -1231       C  
ATOM    222  OG  SER A  30      13.817 -30.301  87.230  1.00147.61           O  
ANISOU  222  OG  SER A  30    13954  23279  18852   2459   1201  -1352       O  
ATOM    223  N   SER A  31      17.122 -31.324  86.557  1.00167.80           N  
ANISOU  223  N   SER A  31    16559  25981  21216   2901   1269   -666       N  
ATOM    224  CA  SER A  31      17.792 -31.359  85.231  1.00171.84           C  
ANISOU  224  CA  SER A  31    17205  26273  21813   3189   1367   -389       C  
ATOM    225  C   SER A  31      18.608 -32.651  85.110  1.00192.42           C  
ANISOU  225  C   SER A  31    19929  29013  24168   3437   1315    -64       C  
ATOM    226  O   SER A  31      18.985 -33.013  83.978  1.00202.76           O  
ANISOU  226  O   SER A  31    21511  30080  25447   3734   1345    156       O  
ATOM    227  CB  SER A  31      18.657 -30.142  85.029  1.00160.23           C  
ANISOU  227  CB  SER A  31    15423  24876  20580   3111   1453   -444       C  
ATOM    228  OG  SER A  31      19.850 -30.237  85.794  1.00154.55           O  
ANISOU  228  OG  SER A  31    14427  24539  19756   3036   1423   -391       O  
ATOM    229  N   THR A  32      18.863 -33.311  86.245  1.00191.67           N  
ANISOU  229  N   THR A  32    19626  29293  23906   3307   1213    -43       N  
ATOM    230  CA  THR A  32      19.636 -34.580  86.275  1.00198.07           C  
ANISOU  230  CA  THR A  32    20506  30222  24528   3504   1101    244       C  
ATOM    231  C   THR A  32      18.688 -35.760  86.030  1.00196.80           C  
ANISOU  231  C   THR A  32    20663  29950  24163   3624    906    371       C  
ATOM    232  O   THR A  32      19.179 -36.830  85.620  1.00195.67           O  
ANISOU  232  O   THR A  32    20648  29784  23913   3875    778    619       O  
ATOM    233  CB  THR A  32      20.393 -34.735  87.600  1.00203.06           C  
ANISOU  233  CB  THR A  32    20824  31252  25077   3269   1004    240       C  
ATOM    234  OG1 THR A  32      21.742 -35.097  87.301  1.00205.15           O  
ANISOU  234  OG1 THR A  32    21009  31562  25377   3477   1020    480       O  
ATOM    235  CG2 THR A  32      19.776 -35.771  88.514  1.00201.92           C  
ANISOU  235  CG2 THR A  32    20718  31332  24669   3072    752    252       C  
ATOM    236  N   GLY A  33      17.386 -35.568  86.273  1.00186.43           N  
ANISOU  236  N   GLY A  33    19471  28552  22813   3465    859    212       N  
ATOM    237  CA  GLY A  33      16.424 -36.634  86.065  1.00188.40           C  
ANISOU  237  CA  GLY A  33    20044  28647  22893   3595    661    371       C  
ATOM    238  C   GLY A  33      15.895 -36.762  84.651  1.00193.67           C  
ANISOU  238  C   GLY A  33    21087  28825  23675   3911    734    485       C  
ATOM    239  O   GLY A  33      15.130 -37.692  84.379  1.00196.92           O  
ANISOU  239  O   GLY A  33    21804  29056  23961   4066    545    661       O  
ATOM    240  N   PHE A  34      16.272 -35.852  83.750  1.00192.58           N  
ANISOU  240  N   PHE A  34    20937  28466  23770   3991    974    411       N  
ATOM    241  CA  PHE A  34      15.724 -35.824  82.390  1.00190.38           C  
ANISOU  241  CA  PHE A  34    21014  27706  23615   4222   1056    500       C  
ATOM    242  C   PHE A  34      16.692 -36.483  81.405  1.00188.44           C  
ANISOU  242  C   PHE A  34    20894  27382  23325   4597   1102    748       C  
ATOM    243  O   PHE A  34      17.323 -35.836  80.569  1.00187.10           O  
ANISOU  243  O   PHE A  34    20671  27117  23300   4672   1307    746       O  
ATOM    244  CB  PHE A  34      15.399 -34.389  81.974  1.00186.66           C  
ANISOU  244  CB  PHE A  34    20454  27025  23441   4019   1244    259       C  
ATOM    245  CG  PHE A  34      14.276 -33.753  82.756  1.00184.44           C  
ANISOU  245  CG  PHE A  34    20089  26742  23246   3696   1193    -29       C  
ATOM    246  CD1 PHE A  34      13.396 -34.526  83.500  1.00186.50           C  
ANISOU  246  CD1 PHE A  34    20458  27102  23302   3635   1018    -13       C  
ATOM    247  CD2 PHE A  34      14.101 -32.378  82.745  1.00182.62           C  
ANISOU  247  CD2 PHE A  34    19650  26426  23312   3448   1295   -323       C  
ATOM    248  CE1 PHE A  34      12.365 -33.936  84.218  1.00189.09           C  
ANISOU  248  CE1 PHE A  34    20680  27469  23696   3341    993   -303       C  
ATOM    249  CE2 PHE A  34      13.074 -31.782  83.460  1.00183.65           C  
ANISOU  249  CE2 PHE A  34    19674  26562  23544   3167   1244   -640       C  
ATOM    250  CZ  PHE A  34      12.206 -32.562  84.197  1.00187.38           C  
ANISOU  250  CZ  PHE A  34    20249  27159  23787   3118   1118   -640       C  
ATOM    251  N   GLN A  35      16.812 -37.794  81.527  1.00197.27           N  
ANISOU  251  N   GLN A  35    22153  28563  24237   4825    883    958       N  
ATOM    252  CA  GLN A  35      17.528 -38.633  80.580  1.00189.18           C  
ANISOU  252  CA  GLN A  35    21293  27433  23155   5233    868   1169       C  
ATOM    253  C   GLN A  35      16.543 -39.412  79.718  1.00173.90           C  
ANISOU  253  C   GLN A  35    19834  25079  21161   5503    722   1333       C  
ATOM    254  O   GLN A  35      15.342 -39.438  80.001  1.00161.56           O  
ANISOU  254  O   GLN A  35    18458  23341  19587   5366    595   1322       O  
ATOM    255  CB  GLN A  35      18.482 -39.583  81.317  1.00198.31           C  
ANISOU  255  CB  GLN A  35    22240  28937  24173   5316    662   1279       C  
ATOM    256  CG  GLN A  35      19.428 -38.884  82.267  1.00210.64           C  
ANISOU  256  CG  GLN A  35    23356  30884  25794   5031    770   1151       C  
ATOM    257  CD  GLN A  35      20.374 -39.848  82.935  1.00226.03           C  
ANISOU  257  CD  GLN A  35    25119  33112  27651   5092    544   1276       C  
ATOM    258  OE1 GLN A  35      20.234 -41.063  82.801  1.00231.99           O  
ANISOU  258  OE1 GLN A  35    26055  33795  28296   5320    254   1440       O  
ATOM    259  NE2 GLN A  35      21.362 -39.314  83.641  1.00232.36           N  
ANISOU  259  NE2 GLN A  35    25556  34205  28525   4887    639   1211       N  
ATOM    260  N   PRO A  36      17.004 -39.999  78.610  1.00173.06           N  
ANISOU  260  N   PRO A  36    19938  24791  21027   5892    748   1482       N  
ATOM    261  CA  PRO A  36      16.105 -40.813  77.779  1.00165.59           C  
ANISOU  261  CA  PRO A  36    19472  23423  20020   6182    572   1661       C  
ATOM    262  C   PRO A  36      15.359 -41.866  78.591  1.00176.40           C  
ANISOU  262  C   PRO A  36    20964  24820  21240   6192    155   1804       C  
ATOM    263  O   PRO A  36      15.830 -42.329  79.632  1.00182.21           O  
ANISOU  263  O   PRO A  36    21423  25931  21875   6080    -45   1810       O  
ATOM    264  CB  PRO A  36      17.053 -41.454  76.762  1.00150.88           C  
ANISOU  264  CB  PRO A  36    17691  21534  18101   6612    618   1765       C  
ATOM    265  CG  PRO A  36      18.137 -40.442  76.608  1.00148.92           C  
ANISOU  265  CG  PRO A  36    17088  21540  17955   6478    972   1620       C  
ATOM    266  CD  PRO A  36      18.320 -39.823  77.969  1.00161.10           C  
ANISOU  266  CD  PRO A  36    18238  23428  19546   6078    968   1480       C  
ATOM    267  N   TYR A  37      14.178 -42.239  78.093  1.00171.61           N  
ANISOU  267  N   TYR A  37    20780  23799  20626   6305      1   1944       N  
ATOM    268  CA  TYR A  37      13.347 -43.289  78.686  1.00180.45           C  
ANISOU  268  CA  TYR A  37    22106  24841  21616   6151   -412   2078       C  
ATOM    269  C   TYR A  37      12.963 -42.935  80.124  1.00196.40           C  
ANISOU  269  C   TYR A  37    23781  27281  23563   5893   -515   2028       C  
ATOM    270  O   TYR A  37      12.871 -43.806  80.991  1.00207.58           O  
ANISOU  270  O   TYR A  37    25108  28953  24812   5837   -887   2166       O  
ATOM    271  CB  TYR A  37      14.061 -44.647  78.653  1.00180.80           C  
ANISOU  271  CB  TYR A  37    22211  24912  21573   6152   -704   2137       C  
ATOM    272  CG  TYR A  37      14.413 -45.197  77.281  1.00187.41           C  
ANISOU  272  CG  TYR A  37    23368  25373  22465   6253   -639   2107       C  
ATOM    273  CD1 TYR A  37      15.351 -44.562  76.475  1.00190.90           C  
ANISOU  273  CD1 TYR A  37    23710  25886  22936   6509   -299   2031       C  
ATOM    274  CD2 TYR A  37      13.831 -46.367  76.807  1.00193.14           C  
ANISOU  274  CD2 TYR A  37    24430  25724  23230   6061   -920   2145       C  
ATOM    275  CE1 TYR A  37      15.689 -45.067  75.232  1.00198.72           C  
ANISOU  275  CE1 TYR A  37    24960  26620  23923   6614   -245   2002       C  
ATOM    276  CE2 TYR A  37      14.162 -46.880  75.562  1.00196.77           C  
ANISOU  276  CE2 TYR A  37    25115  25921  23727   6153   -868   2096       C  
ATOM    277  CZ  TYR A  37      15.091 -46.225  74.780  1.00204.91           C  
ANISOU  277  CZ  TYR A  37    26076  27064  24718   6451   -533   2026       C  
ATOM    278  OH  TYR A  37      15.425 -46.729  73.542  1.00217.33           O  
ANISOU  278  OH  TYR A  37    27862  28437  26278   6564   -481   1978       O  
ATOM    279  N   CYS A  38      12.725 -41.648  80.381  1.00184.93           N  
ANISOU  279  N   CYS A  38    22149  25868  22249   5553   -187   1765       N  
ATOM    280  CA  CYS A  38      12.351 -41.155  81.709  1.00187.06           C  
ANISOU  280  CA  CYS A  38    22103  26504  22468   5115   -204   1584       C  
ATOM    281  C   CYS A  38      10.917 -40.638  81.666  1.00170.35           C  
ANISOU  281  C   CYS A  38    20187  24091  20446   4935   -167   1508       C  
ATOM    282  O   CYS A  38      10.660 -39.541  81.165  1.00181.60           O  
ANISOU  282  O   CYS A  38    21625  25268  22106   4820    124   1300       O  
ATOM    283  CB  CYS A  38      13.309 -40.061  82.172  1.00201.56           C  
ANISOU  283  CB  CYS A  38    23508  28666  24408   4865    104   1299       C  
ATOM    284  SG  CYS A  38      14.750 -40.665  83.074  1.00216.41           S  
ANISOU  284  SG  CYS A  38    25007  31081  26138   4839    -37   1352       S  
ATOM    285  N   LEU A  39       9.985 -41.427  82.188  1.00182.56           N  
ANISOU  285  N   LEU A  39    21876  25659  21831   4896   -489   1687       N  
ATOM    286  CA  LEU A  39       8.590 -41.016  82.173  1.00164.61           C  
ANISOU  286  CA  LEU A  39    19790  23103  19653   4736   -472   1634       C  
ATOM    287  C   LEU A  39       8.366 -39.807  83.073  1.00145.91           C  
ANISOU  287  C   LEU A  39    17036  21030  17373   4293   -229   1227       C  
ATOM    288  O   LEU A  39       8.883 -39.734  84.192  1.00148.94           O  
ANISOU  288  O   LEU A  39    17031  21964  17596   4045   -252   1088       O  
ATOM    289  CB  LEU A  39       7.680 -42.163  82.606  1.00160.81           C  
ANISOU  289  CB  LEU A  39    19507  22642  18953   4780   -901   1950       C  
ATOM    290  CG  LEU A  39       7.653 -43.377  81.678  1.00148.52           C  
ANISOU  290  CG  LEU A  39    18395  20669  17368   5131  -1190   2311       C  
ATOM    291  CD1 LEU A  39       8.786 -44.325  82.022  1.00152.87           C  
ANISOU  291  CD1 LEU A  39    18789  21508  17785   5111  -1400   2372       C  
ATOM    292  CD2 LEU A  39       6.308 -44.079  81.734  1.00130.84           C  
ANISOU  292  CD2 LEU A  39    16473  18066  15174   4781  -1426   2414       C  
ATOM    293  N   VAL A  40       7.593 -38.850  82.567  1.00133.47           N  
ANISOU  293  N   VAL A  40    15571  19067  16075   4187    -17   1026       N  
ATOM    294  CA  VAL A  40       7.213 -37.659  83.309  1.00140.35           C  
ANISOU  294  CA  VAL A  40    16102  20135  17091   3795    178    601       C  
ATOM    295  C   VAL A  40       5.694 -37.624  83.420  1.00149.55           C  
ANISOU  295  C   VAL A  40    17450  21044  18329   3669     92    575       C  
ATOM    296  O   VAL A  40       4.971 -38.245  82.638  1.00148.55           O  
ANISOU  296  O   VAL A  40    17761  20437  18244   3892    -52    876       O  
ATOM    297  CB  VAL A  40       7.742 -36.365  82.662  1.00141.34           C  
ANISOU  297  CB  VAL A  40    16102  20044  17559   3731    482    318       C  
ATOM    298  CG1 VAL A  40       9.215 -36.180  82.984  1.00142.22           C  
ANISOU  298  CG1 VAL A  40    15877  20578  17583   3735    583    259       C  
ATOM    299  CG2 VAL A  40       7.518 -36.394  81.164  1.00148.89           C  
ANISOU  299  CG2 VAL A  40    17498  20338  18736   3989    529    518       C  
ATOM    300  N   VAL A  41       5.216 -36.887  84.414  1.00154.68           N  
ANISOU  300  N   VAL A  41    17753  22021  18997   3311    176    206       N  
ATOM    301  CA  VAL A  41       3.791 -36.725  84.663  1.00161.35           C  
ANISOU  301  CA  VAL A  41    18678  22702  19924   3145    127    103       C  
ATOM    302  C   VAL A  41       3.446 -35.256  84.469  1.00168.78           C  
ANISOU  302  C   VAL A  41    19444  23392  21292   2925    376   -378       C  
ATOM    303  O   VAL A  41       4.249 -34.367  84.770  1.00172.32           O  
ANISOU  303  O   VAL A  41    19539  24090  21844   2781    542   -704       O  
ATOM    304  CB  VAL A  41       3.399 -37.211  86.076  1.00170.41           C  
ANISOU  304  CB  VAL A  41    19540  24510  20698   2892    -31     63       C  
ATOM    305  CG1 VAL A  41       4.154 -36.425  87.136  1.00177.17           C  
ANISOU  305  CG1 VAL A  41    19864  25977  21475   2592    134   -359       C  
ATOM    306  CG2 VAL A  41       1.899 -37.118  86.289  1.00176.01           C  
ANISOU  306  CG2 VAL A  41    20335  25066  21476   2742    -83    -12       C  
ATOM    307  N   ARG A  42       2.246 -34.999  83.956  1.00171.66           N  
ANISOU  307  N   ARG A  42    20057  23232  21933   2897    365   -409       N  
ATOM    308  CA  ARG A  42       1.775 -33.637  83.751  1.00179.27           C  
ANISOU  308  CA  ARG A  42    20861  23889  23364   2668    530   -872       C  
ATOM    309  C   ARG A  42       0.401 -33.498  84.383  1.00182.81           C  
ANISOU  309  C   ARG A  42    21238  24350  23872   2455    483  -1085       C  
ATOM    310  O   ARG A  42      -0.505 -34.286  84.096  1.00183.71           O  
ANISOU  310  O   ARG A  42    21709  24168  23926   2573    333   -752       O  
ATOM    311  CB  ARG A  42       1.740 -33.268  82.262  1.00180.31           C  
ANISOU  311  CB  ARG A  42    21374  23231  23906   2815    573   -733       C  
ATOM    312  CG  ARG A  42       1.449 -31.797  82.014  1.00179.16           C  
ANISOU  312  CG  ARG A  42    21015  22770  24288   2545    685  -1211       C  
ATOM    313  CD  ARG A  42       0.766 -31.549  80.680  1.00178.77           C  
ANISOU  313  CD  ARG A  42    21406  21841  24676   2586    649  -1061       C  
ATOM    314  NE  ARG A  42       1.655 -30.831  79.771  1.00183.71           N  
ANISOU  314  NE  ARG A  42    22023  22219  25559   2581    726  -1083       N  
ATOM    315  CZ  ARG A  42       1.288 -30.317  78.602  1.00193.84           C  
ANISOU  315  CZ  ARG A  42    23590  22782  27276   2520    699  -1029       C  
ATOM    316  NH1 ARG A  42       0.036 -30.435  78.175  1.00193.94           N  
ANISOU  316  NH1 ARG A  42    23946  22189  27553   2474    604   -951       N  
ATOM    317  NH2 ARG A  42       2.181 -29.681  77.857  1.00200.40           N  
ANISOU  317  NH2 ARG A  42    24359  23502  28283   2483    753  -1034       N  
ATOM    318  N   LYS A  43       0.267 -32.489  85.243  1.00202.32           N  
ANISOU  318  N   LYS A  43    23235  27170  26465   2152    598  -1644       N  
ATOM    319  CA  LYS A  43      -0.964 -32.210  85.964  1.00204.42           C  
ANISOU  319  CA  LYS A  43    23325  27555  26792   1919    590  -1961       C  
ATOM    320  C   LYS A  43      -2.132 -31.953  85.012  1.00201.72           C  
ANISOU  320  C   LYS A  43    23338  26385  26920   1944    552  -1923       C  
ATOM    321  O   LYS A  43      -1.932 -31.626  83.838  1.00202.42           O  
ANISOU  321  O   LYS A  43    23719  25817  27376   2059    561  -1798       O  
ATOM    322  CB  LYS A  43      -0.747 -31.019  86.899  1.00210.45           C  
ANISOU  322  CB  LYS A  43    23508  28779  27676   1622    725  -2632       C  
ATOM    323  CG  LYS A  43      -0.866 -29.652  86.250  1.00206.62           C  
ANISOU  323  CG  LYS A  43    22919  27760  27826   1513    790  -3061       C  
ATOM    324  CD  LYS A  43      -0.767 -28.561  87.307  1.00203.25           C  
ANISOU  324  CD  LYS A  43    21897  27836  27493   1236    863  -3743       C  
ATOM    325  CE  LYS A  43       0.464 -28.762  88.185  1.00193.23           C  
ANISOU  325  CE  LYS A  43    20332  27315  25771   1224    911  -3731       C  
ATOM    326  NZ  LYS A  43       0.480 -27.860  89.370  1.00182.98           N  
ANISOU  326  NZ  LYS A  43    18471  26585  24468    958    968  -4370       N  
ATOM    327  N   PRO A  44      -3.366 -32.126  85.500  1.00202.56           N  
ANISOU  327  N   PRO A  44    23429  26519  27017   1821    499  -2008       N  
ATOM    328  CA  PRO A  44      -4.545 -31.915  84.652  1.00212.69           C  
ANISOU  328  CA  PRO A  44    25055  26986  28773   1827    446  -1956       C  
ATOM    329  C   PRO A  44      -4.509 -30.563  83.953  1.00230.97           C  
ANISOU  329  C   PRO A  44    27281  28736  31741   1684    528  -2386       C  
ATOM    330  O   PRO A  44      -4.031 -29.567  84.502  1.00223.47           O  
ANISOU  330  O   PRO A  44    25853  28130  30927   1489    621  -2923       O  
ATOM    331  CB  PRO A  44      -5.709 -32.006  85.643  1.00204.08           C  
ANISOU  331  CB  PRO A  44    23731  26249  27560   1631    429  -2180       C  
ATOM    332  CG  PRO A  44      -5.203 -32.900  86.716  1.00196.80           C  
ANISOU  332  CG  PRO A  44    22599  26225  25951   1633    380  -1992       C  
ATOM    333  CD  PRO A  44      -3.741 -32.587  86.850  1.00200.51           C  
ANISOU  333  CD  PRO A  44    22843  27050  26290   1658    472  -2112       C  
ATOM    334  N   SER A  45      -4.999 -30.551  82.715  1.00224.15           N  
ANISOU  334  N   SER A  45    26892  26986  31291   1773    453  -2120       N  
ATOM    335  CA  SER A  45      -4.891 -29.376  81.860  1.00233.77           C  
ANISOU  335  CA  SER A  45    28095  27587  33138   1624    465  -2411       C  
ATOM    336  C   SER A  45      -5.520 -28.149  82.506  1.00233.90           C  
ANISOU  336  C   SER A  45    27620  27662  33591   1294    484  -3137       C  
ATOM    337  O   SER A  45      -6.726 -28.110  82.768  1.00234.82           O  
ANISOU  337  O   SER A  45    27737  27580  33906   1181    447  -3300       O  
ATOM    338  CB  SER A  45      -5.553 -29.665  80.513  1.00242.60           C  
ANISOU  338  CB  SER A  45    29836  27726  34616   1724    355  -1985       C  
ATOM    339  OG  SER A  45      -5.579 -28.516  79.683  1.00246.83           O  
ANISOU  339  OG  SER A  45    30358  27625  35802   1510    319  -2259       O  
ATOM    340  N   SER A  46      -4.683 -27.149  82.752  1.00233.15           N  
ANISOU  340  N   SER A  46    27093  27836  33655   1151    521  -3573       N  
ATOM    341  CA  SER A  46      -5.083 -25.853  83.280  1.00230.41           C  
ANISOU  341  CA  SER A  46    26240  27525  33780    854    488  -4310       C  
ATOM    342  C   SER A  46      -5.689 -25.031  82.155  1.00219.57           C  
ANISOU  342  C   SER A  46    25065  25176  33187    691    331  -4416       C  
ATOM    343  O   SER A  46      -6.124 -25.589  81.143  1.00222.36           O  
ANISOU  343  O   SER A  46    25969  24851  33668    790    277  -3929       O  
ATOM    344  CB  SER A  46      -3.898 -25.136  83.924  1.00236.68           C  
ANISOU  344  CB  SER A  46    26530  28944  34453    785    529  -4671       C  
ATOM    345  OG  SER A  46      -3.369 -25.901  84.991  1.00241.33           O  
ANISOU  345  OG  SER A  46    26944  30405  34345    893    656  -4571       O  
ATOM    346  N   SER A  47      -5.744 -23.713  82.338  1.00218.76           N  
ANISOU  346  N   SER A  47    24514  24982  33622    426    222  -5050       N  
ATOM    347  CA  SER A  47      -6.133 -22.800  81.269  1.00209.19           C  
ANISOU  347  CA  SER A  47    23425  23320  32738    165     -8  -4715       C  
ATOM    348  C   SER A  47      -5.426 -23.126  79.956  1.00211.13           C  
ANISOU  348  C   SER A  47    24161  23198  32861    247    -46  -4070       C  
ATOM    349  O   SER A  47      -4.349 -23.730  79.942  1.00204.98           O  
ANISOU  349  O   SER A  47    23470  22456  31957    496     82  -4047       O  
ATOM    350  CB  SER A  47      -5.832 -21.355  81.667  1.00198.99           C  
ANISOU  350  CB  SER A  47    21523  22293  31792    -19   -138  -5223       C  
ATOM    351  OG  SER A  47      -6.246 -20.459  80.652  1.00191.93           O  
ANISOU  351  OG  SER A  47    20745  21128  31051   -108   -315  -4807       O  
ATOM    352  N   TRP A  48      -6.021 -22.694  78.848  1.00214.63           N  
ANISOU  352  N   TRP A  48    24900  23394  33256    100   -191  -3564       N  
ATOM    353  CA  TRP A  48      -5.555 -22.998  77.506  1.00214.50           C  
ANISOU  353  CA  TRP A  48    25393  23130  32979    133   -222  -2959       C  
ATOM    354  C   TRP A  48      -4.325 -22.195  77.098  1.00205.33           C  
ANISOU  354  C   TRP A  48    23975  21971  32069     64   -297  -3088       C  
ATOM    355  O   TRP A  48      -3.856 -22.367  75.967  1.00211.01           O  
ANISOU  355  O   TRP A  48    25067  22521  32587     71   -315  -2643       O  
ATOM    356  CB  TRP A  48      -6.678 -22.708  76.509  1.00219.57           C  
ANISOU  356  CB  TRP A  48    26414  23677  33337     -4   -329  -2507       C  
ATOM    357  CG  TRP A  48      -7.704 -23.801  76.348  1.00225.38           C  
ANISOU  357  CG  TRP A  48    27675  24343  33614     91   -261  -2121       C  
ATOM    358  CD1 TRP A  48      -7.963 -24.818  77.224  1.00229.05           C  
ANISOU  358  CD1 TRP A  48    28182  24819  34026    266   -155  -2187       C  
ATOM    359  CD2 TRP A  48      -8.628 -23.958  75.263  1.00228.38           C  
ANISOU  359  CD2 TRP A  48    28298  24577  33901     35   -337  -1753       C  
ATOM    360  NE1 TRP A  48      -8.984 -25.607  76.742  1.00228.27           N  
ANISOU  360  NE1 TRP A  48    28630  24661  33443    313   -154  -1736       N  
ATOM    361  CE2 TRP A  48      -9.408 -25.100  75.540  1.00229.47           C  
ANISOU  361  CE2 TRP A  48    28767  24683  33738    164   -268  -1541       C  
ATOM    362  CE3 TRP A  48      -8.864 -23.251  74.084  1.00228.79           C  
ANISOU  362  CE3 TRP A  48    28233  24511  34184    -90   -477  -1625       C  
ATOM    363  CZ2 TRP A  48     -10.407 -25.549  74.677  1.00229.09           C  
ANISOU  363  CZ2 TRP A  48    28928  24505  33610    148   -329  -1224       C  
ATOM    364  CZ3 TRP A  48      -9.856 -23.700  73.226  1.00227.62           C  
ANISOU  364  CZ3 TRP A  48    28297  24236  33950    -94   -530  -1328       C  
ATOM    365  CH2 TRP A  48     -10.616 -24.836  73.529  1.00227.77           C  
ANISOU  365  CH2 TRP A  48    28637  24242  33665     15   -452  -1141       C  
ATOM    366  N   PHE A  49      -3.772 -21.349  77.969  1.00213.85           N  
ANISOU  366  N   PHE A  49    24441  23278  33534      2   -344  -3695       N  
ATOM    367  CA  PHE A  49      -2.738 -20.410  77.553  1.00186.40           C  
ANISOU  367  CA  PHE A  49    20699  19813  30312    -89   -479  -3792       C  
ATOM    368  C   PHE A  49      -1.383 -20.662  78.205  1.00190.99           C  
ANISOU  368  C   PHE A  49    20999  20543  31027     31   -377  -4214       C  
ATOM    369  O   PHE A  49      -0.476 -19.835  78.057  1.00191.51           O  
ANISOU  369  O   PHE A  49    20755  20671  31338    -74   -518  -4382       O  
ATOM    370  CB  PHE A  49      -3.187 -18.983  77.876  1.00167.06           C  
ANISOU  370  CB  PHE A  49    17812  17538  28125   -200   -665  -4088       C  
ATOM    371  CG  PHE A  49      -4.183 -18.412  76.905  1.00152.22           C  
ANISOU  371  CG  PHE A  49    16229  15501  26107   -275   -791  -3647       C  
ATOM    372  CD1 PHE A  49      -4.758 -19.191  75.913  1.00148.64           C  
ANISOU  372  CD1 PHE A  49    16367  14857  25252   -297   -735  -3088       C  
ATOM    373  CD2 PHE A  49      -4.559 -17.084  77.003  1.00144.13           C  
ANISOU  373  CD2 PHE A  49    14929  14553  25279   -295   -955  -3816       C  
ATOM    374  CE1 PHE A  49      -5.680 -18.646  75.035  1.00149.85           C  
ANISOU  374  CE1 PHE A  49    16643  14907  25387   -358   -857  -2828       C  
ATOM    375  CE2 PHE A  49      -5.473 -16.536  76.134  1.00140.09           C  
ANISOU  375  CE2 PHE A  49    14557  13885  24786   -325  -1079  -3532       C  
ATOM    376  CZ  PHE A  49      -6.035 -17.312  75.149  1.00149.56           C  
ANISOU  376  CZ  PHE A  49    16122  14883  25822   -352  -1048  -3105       C  
ATOM    377  N   TRP A  50      -1.217 -21.768  78.926  1.00179.60           N  
ANISOU  377  N   TRP A  50    19658  19358  29222    328   -121  -4263       N  
ATOM    378  CA  TRP A  50       0.096 -22.130  79.439  1.00188.73           C  
ANISOU  378  CA  TRP A  50    20630  21277  29804    539     40  -4095       C  
ATOM    379  C   TRP A  50       0.123 -23.630  79.683  1.00197.97           C  
ANISOU  379  C   TRP A  50    22162  22763  30295    880    284  -3636       C  
ATOM    380  O   TRP A  50      -0.841 -24.199  80.205  1.00179.96           O  
ANISOU  380  O   TRP A  50    19990  20498  27887    926    337  -3689       O  
ATOM    381  CB  TRP A  50       0.453 -21.347  80.711  1.00192.39           C  
ANISOU  381  CB  TRP A  50    20454  22385  30259    434     -1  -4668       C  
ATOM    382  CG  TRP A  50      -0.438 -21.595  81.873  1.00192.33           C  
ANISOU  382  CG  TRP A  50    20261  22720  30094    432     86  -5046       C  
ATOM    383  CD1 TRP A  50      -0.415 -22.669  82.713  1.00193.79           C  
ANISOU  383  CD1 TRP A  50    20509  23493  29628    639    308  -4874       C  
ATOM    384  CD2 TRP A  50      -1.499 -20.751  82.326  1.00185.18           C  
ANISOU  384  CD2 TRP A  50    19055  21613  29693    191    -66  -5669       C  
ATOM    385  NE1 TRP A  50      -1.396 -22.544  83.667  1.00189.49           N  
ANISOU  385  NE1 TRP A  50    19719  23166  29114    528    322  -5335       N  
ATOM    386  CE2 TRP A  50      -2.077 -21.374  83.449  1.00186.72           C  
ANISOU  386  CE2 TRP A  50    19138  22338  29468    271    112  -5848       C  
ATOM    387  CE3 TRP A  50      -2.017 -19.529  81.889  1.00180.62           C  
ANISOU  387  CE3 TRP A  50    18275  20495  29857    -86   -354  -6052       C  
ATOM    388  CZ2 TRP A  50      -3.148 -20.814  84.142  1.00190.48           C  
ANISOU  388  CZ2 TRP A  50    19299  22818  30256     92     46  -6461       C  
ATOM    389  CZ3 TRP A  50      -3.077 -18.976  82.576  1.00183.76           C  
ANISOU  389  CZ3 TRP A  50    18432  21085  30303   -101   -357  -6301       C  
ATOM    390  CH2 TRP A  50      -3.631 -19.615  83.692  1.00189.47           C  
ANISOU  390  CH2 TRP A  50    18993  22210  30789    -99   -194  -6730       C  
ATOM    391  N   LYS A  51       1.216 -24.266  79.284  1.00202.00           N  
ANISOU  391  N   LYS A  51    22844  23515  30391   1110    400  -3183       N  
ATOM    392  CA  LYS A  51       1.369 -25.695  79.493  1.00205.25           C  
ANISOU  392  CA  LYS A  51    23570  24235  30182   1440    567  -2743       C  
ATOM    393  C   LYS A  51       2.038 -25.912  80.839  1.00200.82           C  
ANISOU  393  C   LYS A  51    22597  24548  29159   1506    669  -2922       C  
ATOM    394  O   LYS A  51       3.193 -25.497  81.013  1.00205.42           O  
ANISOU  394  O   LYS A  51    22890  25508  29653   1506    695  -2965       O  
ATOM    395  CB  LYS A  51       2.211 -26.311  78.390  1.00211.69           C  
ANISOU  395  CB  LYS A  51    24763  24874  30795   1667    628  -2199       C  
ATOM    396  CG  LYS A  51       2.081 -25.610  77.052  1.00211.17           C  
ANISOU  396  CG  LYS A  51    24914  24086  31236   1491    510  -2111       C  
ATOM    397  CD  LYS A  51       3.083 -26.157  76.048  1.00211.32           C  
ANISOU  397  CD  LYS A  51    25221  24081  30990   1709    601  -1622       C  
ATOM    398  CE  LYS A  51       2.961 -25.453  74.706  1.00209.85           C  
ANISOU  398  CE  LYS A  51    25245  23213  31278   1481    474  -1518       C  
ATOM    399  NZ  LYS A  51       4.125 -25.742  73.820  1.00209.36           N  
ANISOU  399  NZ  LYS A  51    25315  23278  30954   1640    574  -1134       N  
ATOM    400  N   PRO A  52       1.368 -26.534  81.808  1.00201.64           N  
ANISOU  400  N   PRO A  52    22656  24994  28963   1538    713  -3012       N  
ATOM    401  CA  PRO A  52       2.006 -26.760  83.109  1.00189.76           C  
ANISOU  401  CA  PRO A  52    20767  24331  27003   1552    794  -3167       C  
ATOM    402  C   PRO A  52       3.269 -27.595  82.976  1.00182.57           C  
ANISOU  402  C   PRO A  52    19972  23762  25634   1804    872  -2712       C  
ATOM    403  O   PRO A  52       3.365 -28.487  82.129  1.00186.22           O  
ANISOU  403  O   PRO A  52    20876  23934  25945   2042    879  -2225       O  
ATOM    404  CB  PRO A  52       0.928 -27.492  83.918  1.00186.30           C  
ANISOU  404  CB  PRO A  52    20380  24106  26300   1541    803  -3206       C  
ATOM    405  CG  PRO A  52      -0.071 -27.975  82.917  1.00188.07           C  
ANISOU  405  CG  PRO A  52    21122  23601  26735   1633    738  -2890       C  
ATOM    406  CD  PRO A  52      -0.027 -27.001  81.783  1.00194.10           C  
ANISOU  406  CD  PRO A  52    21977  23680  28092   1524    672  -2979       C  
ATOM    407  N   ARG A  53       4.249 -27.268  83.817  1.00183.86           N  
ANISOU  407  N   ARG A  53    19725  24529  25605   1750    916  -2894       N  
ATOM    408  CA  ARG A  53       5.554 -27.915  83.802  1.00173.18           C  
ANISOU  408  CA  ARG A  53    18394  23533  23874   1954    983  -2530       C  
ATOM    409  C   ARG A  53       5.423 -29.432  83.883  1.00156.07           C  
ANISOU  409  C   ARG A  53    16564  21502  21233   2190    982  -2081       C  
ATOM    410  O   ARG A  53       4.538 -29.962  84.561  1.00155.76           O  
ANISOU  410  O   ARG A  53    16555  21625  21003   2134    936  -2123       O  
ATOM    411  CB  ARG A  53       6.382 -27.388  84.974  1.00180.20           C  
ANISOU  411  CB  ARG A  53    18777  25075  24616   1813   1008  -2833       C  
ATOM    412  CG  ARG A  53       6.686 -25.898  84.892  1.00184.22           C  
ANISOU  412  CG  ARG A  53    18930  25474  25591   1614    945  -3238       C  
ATOM    413  CD  ARG A  53       7.002 -25.317  86.266  1.00188.70           C  
ANISOU  413  CD  ARG A  53    18998  26646  26053   1432    932  -3666       C  
ATOM    414  NE  ARG A  53       8.115 -25.976  86.941  1.00194.75           N  
ANISOU  414  NE  ARG A  53    19667  27970  26358   1528   1005  -3421       N  
ATOM    415  CZ  ARG A  53       9.208 -25.350  87.365  1.00197.71           C  
ANISOU  415  CZ  ARG A  53    19717  28650  26755   1478    988  -3512       C  
ATOM    416  NH1 ARG A  53      10.169 -26.032  87.973  1.00196.85           N  
ANISOU  416  NH1 ARG A  53    19551  28999  26244   1553   1046  -3264       N  
ATOM    417  NH2 ARG A  53       9.340 -24.043  87.184  1.00199.70           N  
ANISOU  417  NH2 ARG A  53    19697  28727  27453   1343    875  -3838       N  
ATOM    418  N   TYR A  54       6.317 -30.131  83.186  1.00135.79           N  
ANISOU  418  N   TYR A  54    14229  18884  18481   2451   1007  -1650       N  
ATOM    419  CA  TYR A  54       6.356 -31.591  83.208  1.00152.64           C  
ANISOU  419  CA  TYR A  54    16663  21142  20192   2705    944  -1212       C  
ATOM    420  C   TYR A  54       7.200 -32.018  84.402  1.00165.43           C  
ANISOU  420  C   TYR A  54    17955  23482  21419   2664    933  -1224       C  
ATOM    421  O   TYR A  54       8.411 -31.777  84.435  1.00163.45           O  
ANISOU  421  O   TYR A  54    17503  23467  21133   2702   1001  -1203       O  
ATOM    422  CB  TYR A  54       6.923 -32.157  81.907  1.00162.26           C  
ANISOU  422  CB  TYR A  54    18267  21977  21409   3018    958   -789       C  
ATOM    423  CG  TYR A  54       5.984 -32.163  80.713  1.00168.67           C  
ANISOU  423  CG  TYR A  54    19532  22054  22501   3096    924   -639       C  
ATOM    424  CD1 TYR A  54       5.801 -31.029  79.934  1.00174.69           C  
ANISOU  424  CD1 TYR A  54    20287  22364  23724   2926    977   -835       C  
ATOM    425  CD2 TYR A  54       5.312 -33.324  80.344  1.00166.76           C  
ANISOU  425  CD2 TYR A  54    19735  21549  22077   3330    799   -270       C  
ATOM    426  CE1 TYR A  54       4.955 -31.043  78.834  1.00173.69           C  
ANISOU  426  CE1 TYR A  54    20594  21530  23870   2959    929   -678       C  
ATOM    427  CE2 TYR A  54       4.467 -33.347  79.244  1.00169.47           C  
ANISOU  427  CE2 TYR A  54    20526  21182  22682   3400    758   -104       C  
ATOM    428  CZ  TYR A  54       4.293 -32.206  78.492  1.00175.59           C  
ANISOU  428  CZ  TYR A  54    21297  21505  23915   3203    836   -311       C  
ATOM    429  OH  TYR A  54       3.453 -32.228  77.398  1.00181.70           O  
ANISOU  429  OH  TYR A  54    22530  21540  24967   3233    779   -131       O  
ATOM    430  N   LYS A  55       6.564 -32.647  85.381  1.00161.99           N  
ANISOU  430  N   LYS A  55    17464  23394  20692   2562    832  -1238       N  
ATOM    431  CA  LYS A  55       7.269 -33.118  86.560  1.00179.59           C  
ANISOU  431  CA  LYS A  55    19399  26299  22537   2464    782  -1227       C  
ATOM    432  C   LYS A  55       7.720 -34.556  86.362  1.00184.10           C  
ANISOU  432  C   LYS A  55    20234  26939  22776   2723    619   -720       C  
ATOM    433  O   LYS A  55       7.054 -35.351  85.694  1.00187.08           O  
ANISOU  433  O   LYS A  55    21004  26957  23121   2929    493   -412       O  
ATOM    434  CB  LYS A  55       6.373 -33.016  87.796  1.00185.65           C  
ANISOU  434  CB  LYS A  55    19917  27485  23138   2159    736  -1525       C  
ATOM    435  CG  LYS A  55       6.210 -31.599  88.319  1.00190.16           C  
ANISOU  435  CG  LYS A  55    20094  28176  23982   1885    869  -2106       C  
ATOM    436  CD  LYS A  55       5.135 -31.515  89.390  1.00193.76           C  
ANISOU  436  CD  LYS A  55    20337  28996  24287   1611    842  -2430       C  
ATOM    437  CE  LYS A  55       5.758 -31.406  90.770  1.00199.42           C  
ANISOU  437  CE  LYS A  55    20628  30461  24684   1361    850  -2650       C  
ATOM    438  NZ  LYS A  55       6.639 -30.204  90.872  1.00200.55           N  
ANISOU  438  NZ  LYS A  55    20456  30648  25097   1290    957  -2997       N  
ATOM    439  N   CYS A  56       8.858 -34.886  86.959  1.00197.87           N  
ANISOU  439  N   CYS A  56    21755  29127  24299   2711    589   -636       N  
ATOM    440  CA  CYS A  56       9.415 -36.222  86.838  1.00182.95           C  
ANISOU  440  CA  CYS A  56    20052  27327  22136   2942    390   -196       C  
ATOM    441  C   CYS A  56       8.978 -37.091  88.011  1.00170.72           C  
ANISOU  441  C   CYS A  56    18397  26255  20214   2740    140    -96       C  
ATOM    442  O   CYS A  56       8.725 -36.597  89.113  1.00168.71           O  
ANISOU  442  O   CYS A  56    17817  26433  19853   2392    177   -394       O  
ATOM    443  CB  CYS A  56      10.940 -36.155  86.775  1.00181.12           C  
ANISOU  443  CB  CYS A  56    19639  27272  21908   3038    466   -132       C  
ATOM    444  SG  CYS A  56      11.707 -37.697  86.267  1.00178.41           S  
ANISOU  444  SG  CYS A  56    19547  26884  21358   3406    229    367       S  
ATOM    445  N   VAL A  57       8.900 -38.401  87.765  1.00170.14           N  
ANISOU  445  N   VAL A  57    18591  26116  19938   2951   -146    330       N  
ATOM    446  CA  VAL A  57       8.531 -39.376  88.789  1.00169.84           C  
ANISOU  446  CA  VAL A  57    18471  26522  19539   2758   -472    518       C  
ATOM    447  C   VAL A  57       9.703 -40.252  89.196  1.00182.08           C  
ANISOU  447  C   VAL A  57    19901  28385  20897   2790   -704    767       C  
ATOM    448  O   VAL A  57       9.537 -41.149  90.037  1.00188.86           O  
ANISOU  448  O   VAL A  57    20677  29620  21460   2605  -1045    971       O  
ATOM    449  CB  VAL A  57       7.341 -40.245  88.341  1.00153.82           C  
ANISOU  449  CB  VAL A  57    16819  24195  17433   2919   -734    836       C  
ATOM    450  CG1 VAL A  57       6.541 -40.733  89.551  1.00141.86           C  
ANISOU  450  CG1 VAL A  57    15127  23191  15584   2569   -985    879       C  
ATOM    451  CG2 VAL A  57       6.449 -39.473  87.385  1.00152.58           C  
ANISOU  451  CG2 VAL A  57    16917  23457  17598   3046   -499    685       C  
ATOM    452  N   ASN A  58      10.884 -40.011  88.632  1.00177.83           N  
ANISOU  452  N   ASN A  58    19330  27706  20530   2995   -549    761       N  
ATOM    453  CA  ASN A  58      12.123 -40.702  88.979  1.00177.23           C  
ANISOU  453  CA  ASN A  58    19104  27886  20350   3026   -729    946       C  
ATOM    454  C   ASN A  58      11.993 -42.227  88.878  1.00172.06           C  
ANISOU  454  C   ASN A  58    18663  27200  19511   3206  -1204   1374       C  
ATOM    455  O   ASN A  58      12.165 -42.966  89.851  1.00177.86           O  
ANISOU  455  O   ASN A  58    19222  28339  20017   2958  -1544   1520       O  
ATOM    456  CB  ASN A  58      12.576 -40.267  90.377  1.00182.78           C  
ANISOU  456  CB  ASN A  58    19379  29162  20908   2568   -707    729       C  
ATOM    457  CG  ASN A  58      12.994 -38.798  90.422  1.00186.78           C  
ANISOU  457  CG  ASN A  58    19653  29679  21636   2453   -295    332       C  
ATOM    458  OD1 ASN A  58      13.409 -38.227  89.413  1.00189.03           O  
ANISOU  458  OD1 ASN A  58    20041  29595  22188   2721    -61    285       O  
ATOM    459  ND2 ASN A  58      12.867 -38.179  91.593  1.00188.74           N  
ANISOU  459  ND2 ASN A  58    19579  30364  21769   2041   -235     48       N  
ATOM    460  N   LEU A  59      11.711 -42.694  87.660  1.00171.19           N  
ANISOU  460  N   LEU A  59    18937  26590  19517   3636  -1259   1582       N  
ATOM    461  CA  LEU A  59      11.665 -44.124  87.369  1.00171.67           C  
ANISOU  461  CA  LEU A  59    19229  26536  19461   3899  -1739   1985       C  
ATOM    462  C   LEU A  59      11.710 -44.307  85.857  1.00179.27           C  
ANISOU  462  C   LEU A  59    20581  26917  20617   4419  -1649   2108       C  
ATOM    463  O   LEU A  59      11.411 -43.385  85.094  1.00178.44           O  
ANISOU  463  O   LEU A  59    20614  26484  20700   4509  -1264   1926       O  
ATOM    464  CB  LEU A  59      10.428 -44.798  87.978  1.00161.60           C  
ANISOU  464  CB  LEU A  59    18048  25398  17955   3708  -2120   2193       C  
ATOM    465  CG  LEU A  59       9.031 -44.281  87.645  1.00160.30           C  
ANISOU  465  CG  LEU A  59    18113  24959  17834   3690  -1959   2124       C  
ATOM    466  CD1 LEU A  59       8.409 -45.155  86.567  1.00169.13           C  
ANISOU  466  CD1 LEU A  59    19712  25544  19006   4127  -2234   2489       C  
ATOM    467  CD2 LEU A  59       8.160 -44.256  88.890  1.00156.57           C  
ANISOU  467  CD2 LEU A  59    17415  24965  17108   3223  -2100   2074       C  
ATOM    468  N   SER A  60      12.092 -45.507  85.433  1.00186.20           N  
ANISOU  468  N   SER A  60    21624  27671  21454   4747  -2036   2410       N  
ATOM    469  CA  SER A  60      12.266 -45.792  84.019  1.00186.70           C  
ANISOU  469  CA  SER A  60    22101  27100  21737   5064  -1899   2423       C  
ATOM    470  C   SER A  60      11.064 -46.556  83.469  1.00185.71           C  
ANISOU  470  C   SER A  60    22483  26347  21731   4868  -2064   2506       C  
ATOM    471  O   SER A  60      10.044 -46.724  84.142  1.00195.55           O  
ANISOU  471  O   SER A  60    23765  27636  22900   4572  -2243   2570       O  
ATOM    472  CB  SER A  60      13.565 -46.570  83.808  1.00194.84           C  
ANISOU  472  CB  SER A  60    23072  28103  22854   5155  -2022   2431       C  
ATOM    473  OG  SER A  60      13.648 -47.085  82.491  1.00198.43           O  
ANISOU  473  OG  SER A  60    23924  27974  23495   5331  -1953   2415       O  
ATOM    474  N   ILE A  61      11.189 -47.038  82.233  1.00190.71           N  
ANISOU  474  N   ILE A  61    23465  26427  22569   4986  -2005   2493       N  
ATOM    475  CA  ILE A  61      10.113 -47.757  81.560  1.00184.03           C  
ANISOU  475  CA  ILE A  61    23020  24991  21911   4740  -2147   2553       C  
ATOM    476  C   ILE A  61      10.436 -49.224  81.331  1.00187.69           C  
ANISOU  476  C   ILE A  61    23571  25187  22556   4531  -2505   2636       C  
ATOM    477  O   ILE A  61       9.519 -50.003  81.018  1.00187.37           O  
ANISOU  477  O   ILE A  61    23723  24752  22716   4206  -2706   2739       O  
ATOM    478  CB  ILE A  61       9.744 -47.088  80.218  1.00187.34           C  
ANISOU  478  CB  ILE A  61    23729  24989  22462   4914  -1799   2465       C  
ATOM    479  CG1 ILE A  61       8.340 -47.511  79.771  1.00189.64           C  
ANISOU  479  CG1 ILE A  61    24317  24794  22943   4569  -1916   2526       C  
ATOM    480  CG2 ILE A  61      10.784 -47.395  79.156  1.00187.84           C  
ANISOU  480  CG2 ILE A  61    23868  24904  22599   5144  -1681   2396       C  
ATOM    481  CD1 ILE A  61       7.814 -46.747  78.584  1.00183.30           C  
ANISOU  481  CD1 ILE A  61    23769  23599  22277   4631  -1605   2437       C  
ATOM    482  N   LYS A  62      11.695 -49.639  81.500  1.00186.51           N  
ANISOU  482  N   LYS A  62    23225  25253  22386   4677  -2602   2614       N  
ATOM    483  CA  LYS A  62      12.022 -51.047  81.321  1.00214.23           C  
ANISOU  483  CA  LYS A  62    26771  28512  26115   4474  -2967   2709       C  
ATOM    484  C   LYS A  62      11.415 -51.888  82.431  1.00250.07           C  
ANISOU  484  C   LYS A  62    31235  33052  30726   3982  -3426   2892       C  
ATOM    485  O   LYS A  62      11.069 -53.053  82.210  1.00255.92           O  
ANISOU  485  O   LYS A  62    32064  33585  31588   3840  -3678   3042       O  
ATOM    486  CB  LYS A  62      13.543 -51.216  81.260  1.00207.10           C  
ANISOU  486  CB  LYS A  62    25658  27840  25191   4766  -2959   2628       C  
ATOM    487  CG  LYS A  62      14.284 -50.371  82.287  1.00205.61           C  
ANISOU  487  CG  LYS A  62    25116  28226  24780   4901  -2861   2573       C  
ATOM    488  CD  LYS A  62      15.669 -50.902  82.614  1.00205.03           C  
ANISOU  488  CD  LYS A  62    24771  28365  24765   4989  -3040   2552       C  
ATOM    489  CE  LYS A  62      16.221 -50.229  83.860  1.00202.68           C  
ANISOU  489  CE  LYS A  62    24060  28665  24285   4932  -3032   2543       C  
ATOM    490  NZ  LYS A  62      17.544 -50.783  84.241  1.00203.17           N  
ANISOU  490  NZ  LYS A  62    23845  28896  24454   4950  -3246   2530       N  
ATOM    491  N   ASP A  63      11.272 -51.313  83.621  1.00229.23           N  
ANISOU  491  N   ASP A  63    28429  30815  27854   3894  -3472   2873       N  
ATOM    492  CA  ASP A  63      10.549 -51.912  84.733  1.00227.25           C  
ANISOU  492  CA  ASP A  63    28177  30567  27602   3423  -3884   2992       C  
ATOM    493  C   ASP A  63       9.029 -51.809  84.585  1.00221.51           C  
ANISOU  493  C   ASP A  63    27681  29560  26924   3191  -3870   3057       C  
ATOM    494  O   ASP A  63       8.308 -52.313  85.454  1.00229.95           O  
ANISOU  494  O   ASP A  63    28802  30672  27897   2925  -4176   3125       O  
ATOM    495  CB  ASP A  63      11.018 -51.298  86.059  1.00226.19           C  
ANISOU  495  CB  ASP A  63    27729  31066  27145   3411  -3889   2906       C  
ATOM    496  CG  ASP A  63      11.090 -49.787  86.020  1.00222.42           C  
ANISOU  496  CG  ASP A  63    27024  31087  26398   3744  -3377   2794       C  
ATOM    497  OD1 ASP A  63      10.837 -49.206  84.947  1.00220.69           O  
ANISOU  497  OD1 ASP A  63    26981  30626  26246   4047  -3043   2743       O  
ATOM    498  OD2 ASP A  63      11.429 -49.182  87.057  1.00222.84           O  
ANISOU  498  OD2 ASP A  63    26698  31771  26202   3658  -3324   2752       O  
ATOM    499  N   ILE A  64       8.516 -51.173  83.526  1.00234.85           N  
ANISOU  499  N   ILE A  64    29523  31043  28668   3405  -3495   3009       N  
ATOM    500  CA  ILE A  64       7.073 -50.967  83.403  1.00225.49           C  
ANISOU  500  CA  ILE A  64    28517  29680  27479   3275  -3428   3062       C  
ATOM    501  C   ILE A  64       6.385 -51.955  82.463  1.00222.57           C  
ANISOU  501  C   ILE A  64    28347  28995  27226   3327  -3451   3202       C  
ATOM    502  O   ILE A  64       5.164 -52.145  82.575  1.00225.55           O  
ANISOU  502  O   ILE A  64    28823  29266  27608   3161  -3508   3308       O  
ATOM    503  CB  ILE A  64       6.792 -49.518  82.945  1.00220.71           C  
ANISOU  503  CB  ILE A  64    27956  29123  26781   3555  -2972   2903       C  
ATOM    504  CG1 ILE A  64       7.256 -48.527  84.001  1.00221.18           C  
ANISOU  504  CG1 ILE A  64    27711  29850  26476   3766  -2822   2810       C  
ATOM    505  CG2 ILE A  64       5.314 -49.266  82.648  1.00218.36           C  
ANISOU  505  CG2 ILE A  64    27846  28510  26611   3348  -2913   2945       C  
ATOM    506  CD1 ILE A  64       7.020 -47.102  83.592  1.00218.66           C  
ANISOU  506  CD1 ILE A  64    27367  29650  26065   4105  -2379   2692       C  
ATOM    507  N   LEU A  65       7.128 -52.657  81.624  1.00241.93           N  
ANISOU  507  N   LEU A  65    30835  31334  29755   3545  -3433   3201       N  
ATOM    508  CA  LEU A  65       6.572 -53.736  80.825  1.00239.53           C  
ANISOU  508  CA  LEU A  65    30687  30807  29517   3612  -3486   3309       C  
ATOM    509  C   LEU A  65       7.059 -55.060  81.398  1.00250.85           C  
ANISOU  509  C   LEU A  65    31934  32400  30977   3502  -3869   3513       C  
ATOM    510  O   LEU A  65       7.741 -55.103  82.425  1.00254.87           O  
ANISOU  510  O   LEU A  65    32224  33149  31466   3323  -4118   3570       O  
ATOM    511  CB  LEU A  65       6.919 -53.584  79.343  1.00231.88           C  
ANISOU  511  CB  LEU A  65    29951  29580  28571   3955  -3184   3116       C  
ATOM    512  CG  LEU A  65       6.274 -52.399  78.619  1.00225.39           C  
ANISOU  512  CG  LEU A  65    29330  28555  27752   4018  -2814   2965       C  
ATOM    513  CD1 LEU A  65       7.135 -51.147  78.688  1.00223.42           C  
ANISOU  513  CD1 LEU A  65    28968  28425  27494   4121  -2580   2819       C  
ATOM    514  CD2 LEU A  65       5.944 -52.766  77.177  1.00224.51           C  
ANISOU  514  CD2 LEU A  65    29528  28131  27644   4211  -2653   2863       C  
ATOM    515  N   GLU A  66       6.689 -56.154  80.735  1.00262.65           N  
ANISOU  515  N   GLU A  66    33525  33763  32506   3608  -3924   3609       N  
ATOM    516  CA  GLU A  66       7.033 -57.467  81.279  1.00272.81           C  
ANISOU  516  CA  GLU A  66    34596  35261  33798   3527  -4243   3845       C  
ATOM    517  C   GLU A  66       8.538 -57.715  81.285  1.00306.59           C  
ANISOU  517  C   GLU A  66    38736  39636  38120   3671  -4357   3760       C  
ATOM    518  O   GLU A  66       9.071 -58.070  82.350  1.00308.34           O  
ANISOU  518  O   GLU A  66    38682  40149  38326   3433  -4565   3879       O  
ATOM    519  CB  GLU A  66       6.251 -58.558  80.533  1.00247.70           C  
ANISOU  519  CB  GLU A  66    31599  31918  30597   3684  -4250   3889       C  
ATOM    520  CG  GLU A  66       4.743 -58.554  80.822  1.00217.54           C  
ANISOU  520  CG  GLU A  66    27821  28114  26722   3513  -4182   4038       C  
ATOM    521  CD  GLU A  66       3.988 -59.660  80.096  1.00185.55           C  
ANISOU  521  CD  GLU A  66    24005  23854  22643   3686  -4239   4017       C  
ATOM    522  OE1 GLU A  66       4.370 -59.997  78.956  1.00168.61           O  
ANISOU  522  OE1 GLU A  66    22125  21389  20550   3924  -4230   3791       O  
ATOM    523  OE2 GLU A  66       3.014 -60.196  80.669  1.00169.04           O  
ANISOU  523  OE2 GLU A  66    21860  21924  20443   3601  -4299   4183       O  
ATOM    524  N   PRO A  67       9.280 -57.557  80.187  1.00273.85           N  
ANISOU  524  N   PRO A  67    34766  35287  33999   4017  -4176   3501       N  
ATOM    525  CA  PRO A  67      10.739 -57.680  80.288  1.00275.81           C  
ANISOU  525  CA  PRO A  67    34832  35663  34299   4149  -4269   3422       C  
ATOM    526  C   PRO A  67      11.336 -56.493  81.023  1.00257.90           C  
ANISOU  526  C   PRO A  67    32397  33567  32026   4032  -4190   3346       C  
ATOM    527  O   PRO A  67      10.917 -55.353  80.831  1.00264.75           O  
ANISOU  527  O   PRO A  67    33386  34374  32832   4059  -3903   3213       O  
ATOM    528  CB  PRO A  67      11.202 -57.726  78.824  1.00275.20           C  
ANISOU  528  CB  PRO A  67    35011  35341  34212   4560  -4046   3159       C  
ATOM    529  CG  PRO A  67       9.969 -57.971  78.026  1.00275.48           C  
ANISOU  529  CG  PRO A  67    35362  35116  34190   4601  -3938   3135       C  
ATOM    530  CD  PRO A  67       8.867 -57.326  78.794  1.00273.76           C  
ANISOU  530  CD  PRO A  67    35106  34953  33957   4294  -3890   3282       C  
ATOM    531  N   ASP A  68      12.336 -56.765  81.861  1.00266.63           N  
ANISOU  531  N   ASP A  68    33221  34895  33192   3911  -4443   3416       N  
ATOM    532  CA  ASP A  68      13.040 -55.687  82.546  1.00248.09           C  
ANISOU  532  CA  ASP A  68    30722  32713  30827   3841  -4385   3283       C  
ATOM    533  C   ASP A  68      14.393 -55.443  81.889  1.00251.39           C  
ANISOU  533  C   ASP A  68    31049  33145  31321   4178  -4207   3095       C  
ATOM    534  O   ASP A  68      15.444 -55.595  82.528  1.00250.73           O  
ANISOU  534  O   ASP A  68    30707  33232  31326   4112  -4402   3103       O  
ATOM    535  CB  ASP A  68      13.192 -56.002  84.040  1.00237.27           C  
ANISOU  535  CB  ASP A  68    29142  31553  29456   3418  -4789   3410       C  
ATOM    536  CG  ASP A  68      13.926 -57.313  84.297  1.00237.48           C  
ANISOU  536  CG  ASP A  68    28964  31678  29590   3319  -5045   3561       C  
ATOM    537  OD1 ASP A  68      14.242 -58.033  83.328  1.00238.33           O  
ANISOU  537  OD1 ASP A  68    29079  31717  29760   3639  -5001   3617       O  
ATOM    538  OD2 ASP A  68      14.188 -57.626  85.477  1.00239.17           O  
ANISOU  538  OD2 ASP A  68    29037  32023  29813   2938  -5308   3593       O  
ATOM    539  N   ALA A  69      14.386 -55.048  80.622  1.00247.34           N  
ANISOU  539  N   ALA A  69    30744  32454  30781   4519  -3848   2924       N  
ATOM    540  CA  ALA A  69      15.632 -54.784  79.909  1.00247.92           C  
ANISOU  540  CA  ALA A  69    30735  32547  30916   4848  -3652   2744       C  
ATOM    541  C   ALA A  69      15.961 -53.296  79.918  1.00248.53           C  
ANISOU  541  C   ALA A  69    30775  32853  30804   5108  -3256   2564       C  
ATOM    542  O   ALA A  69      16.994 -52.884  80.445  1.00251.83           O  
ANISOU  542  O   ALA A  69    30934  33623  31129   5309  -3211   2482       O  
ATOM    543  CB  ALA A  69      15.561 -55.305  78.474  1.00249.01           C  
ANISOU  543  CB  ALA A  69    31142  32449  31021   5175  -3499   2633       C  
ATOM    544  N   TYR A  83      18.408 -52.536  73.231  1.00220.69           N  
ANISOU  544  N   TYR A  83    27986  28910  26957   6879  -1810   1808       N  
ATOM    545  CA  TYR A  83      18.137 -51.132  72.945  1.00217.85           C  
ANISOU  545  CA  TYR A  83    27707  28627  26437   6969  -1386   1801       C  
ATOM    546  C   TYR A  83      19.386 -50.281  73.117  1.00216.04           C  
ANISOU  546  C   TYR A  83    27161  28813  26110   7305  -1087   1729       C  
ATOM    547  O   TYR A  83      20.387 -50.730  73.677  1.00215.13           O  
ANISOU  547  O   TYR A  83    26744  28941  26057   7427  -1235   1683       O  
ATOM    548  CB  TYR A  83      17.026 -50.600  73.853  1.00218.24           C  
ANISOU  548  CB  TYR A  83    27789  28608  26523   6632  -1439   1923       C  
ATOM    549  CG  TYR A  83      17.359 -50.697  75.324  1.00226.44           C  
ANISOU  549  CG  TYR A  83    28505  29931  27601   6528  -1669   1988       C  
ATOM    550  CD1 TYR A  83      18.062 -49.685  75.972  1.00230.37           C  
ANISOU  550  CD1 TYR A  83    28698  30828  28004   6704  -1438   1968       C  
ATOM    551  CD2 TYR A  83      16.974 -51.802  76.065  1.00230.26           C  
ANISOU  551  CD2 TYR A  83    28949  30300  28238   6211  -2120   2093       C  
ATOM    552  CE1 TYR A  83      18.371 -49.777  77.316  1.00232.56           C  
ANISOU  552  CE1 TYR A  83    28659  31402  28303   6577  -1662   2028       C  
ATOM    553  CE2 TYR A  83      17.277 -51.901  77.403  1.00232.70           C  
ANISOU  553  CE2 TYR A  83    28971  30875  28571   6071  -2360   2170       C  
ATOM    554  CZ  TYR A  83      17.973 -50.888  78.027  1.00235.48           C  
ANISOU  554  CZ  TYR A  83    29041  31641  28789   6261  -2136   2124       C  
ATOM    555  OH  TYR A  83      18.271 -50.994  79.366  1.00241.26           O  
ANISOU  555  OH  TYR A  83    29469  32671  29529   6081  -2390   2199       O  
ATOM    556  N   ASP A  84      19.304 -49.040  72.647  1.00222.44           N  
ANISOU  556  N   ASP A  84    28007  29690  26819   7404   -670   1732       N  
ATOM    557  CA  ASP A  84      20.382 -48.069  72.763  1.00210.67           C  
ANISOU  557  CA  ASP A  84    26163  28591  25289   7641   -321   1691       C  
ATOM    558  C   ASP A  84      19.838 -46.725  72.308  1.00190.73           C  
ANISOU  558  C   ASP A  84    23735  26006  22729   7593     67   1738       C  
ATOM    559  O   ASP A  84      18.809 -46.649  71.630  1.00176.12           O  
ANISOU  559  O   ASP A  84    22263  23794  20862   7451     77   1779       O  
ATOM    560  CB  ASP A  84      21.608 -48.471  71.929  1.00213.34           C  
ANISOU  560  CB  ASP A  84    26380  29095  25586   7971   -206   1567       C  
ATOM    561  CG  ASP A  84      22.819 -47.578  72.178  1.00208.11           C  
ANISOU  561  CG  ASP A  84    25261  28870  24943   8136    134   1521       C  
ATOM    562  OD1 ASP A  84      22.768 -46.707  73.075  1.00204.59           O  
ANISOU  562  OD1 ASP A  84    24565  28612  24558   7989    250   1582       O  
ATOM    563  OD2 ASP A  84      23.830 -47.749  71.466  1.00206.78           O  
ANISOU  563  OD2 ASP A  84    24957  28870  24739   8389    291   1415       O  
ATOM    564  N   ALA A  85      20.536 -45.666  72.703  1.00195.32           N  
ANISOU  564  N   ALA A  85    23940  26928  23347   7661    370   1728       N  
ATOM    565  CA  ALA A  85      20.237 -44.321  72.234  1.00200.93           C  
ANISOU  565  CA  ALA A  85    24648  27607  24088   7607    754   1751       C  
ATOM    566  C   ALA A  85      21.074 -44.036  70.991  1.00213.15           C  
ANISOU  566  C   ALA A  85    26171  29248  25568   7823   1073   1701       C  
ATOM    567  O   ALA A  85      22.309 -44.031  71.054  1.00217.30           O  
ANISOU  567  O   ALA A  85    26335  30138  26091   7979   1207   1632       O  
ATOM    568  CB  ALA A  85      20.513 -43.291  73.327  1.00196.99           C  
ANISOU  568  CB  ALA A  85    23702  27441  23706   7490    913   1744       C  
ATOM    569  N   MET A  86      20.400 -43.796  69.866  1.00215.70           N  
ANISOU  569  N   MET A  86    26867  29249  25841   7804   1191   1742       N  
ATOM    570  CA  MET A  86      21.055 -43.504  68.590  1.00218.70           C  
ANISOU  570  CA  MET A  86    27259  29714  26121   7998   1495   1718       C  
ATOM    571  C   MET A  86      21.666 -42.105  68.644  1.00216.06           C  
ANISOU  571  C   MET A  86    26519  29687  25886   7934   1894   1721       C  
ATOM    572  O   MET A  86      21.104 -41.117  68.164  1.00204.69           O  
ANISOU  572  O   MET A  86    25171  28078  24524   7791   2099   1781       O  
ATOM    573  CB  MET A  86      20.085 -43.662  67.425  1.00224.28           C  
ANISOU  573  CB  MET A  86    28490  29974  26753   7951   1473   1779       C  
ATOM    574  CG  MET A  86      20.350 -44.933  66.627  1.00230.04           C  
ANISOU  574  CG  MET A  86    29453  30641  27310   8163   1297   1713       C  
ATOM    575  SD  MET A  86      19.740 -44.919  64.930  1.00229.10           S  
ANISOU  575  SD  MET A  86    29822  30175  27049   8192   1426   1763       S  
ATOM    576  CE  MET A  86      20.257 -46.547  64.380  1.00223.05           C  
ANISOU  576  CE  MET A  86    29178  29460  26111   8468   1160   1625       C  
ATOM    577  N   ASP A  87      22.850 -42.037  69.242  1.00215.39           N  
ANISOU  577  N   ASP A  87    25962  30049  25826   7995   1983   1651       N  
ATOM    578  CA  ASP A  87      23.566 -40.787  69.455  1.00214.10           C  
ANISOU  578  CA  ASP A  87    25339  30240  25769   7849   2318   1647       C  
ATOM    579  C   ASP A  87      24.031 -40.177  68.129  1.00213.53           C  
ANISOU  579  C   ASP A  87    25243  30280  25606   7909   2666   1671       C  
ATOM    580  O   ASP A  87      23.711 -40.634  67.034  1.00216.95           O  
ANISOU  580  O   ASP A  87    26037  30500  25894   8077   2677   1688       O  
ATOM    581  CB  ASP A  87      24.740 -41.008  70.410  1.00217.49           C  
ANISOU  581  CB  ASP A  87    25308  31081  26248   7861   2283   1584       C  
ATOM    582  CG  ASP A  87      25.732 -42.028  69.893  1.00219.06           C  
ANISOU  582  CG  ASP A  87    25474  31436  26324   8146   2237   1506       C  
ATOM    583  OD1 ASP A  87      25.464 -43.235  70.052  1.00217.74           O  
ANISOU  583  OD1 ASP A  87    25540  31081  26108   8301   1902   1468       O  
ATOM    584  OD2 ASP A  87      26.778 -41.627  69.335  1.00220.73           O  
ANISOU  584  OD2 ASP A  87    25408  31961  26497   8195   2516   1479       O  
ATOM    585  N   GLY A  88      24.812 -39.110  68.252  1.00217.76           N  
ANISOU  585  N   GLY A  88    25332  31183  26225   7738   2942   1685       N  
ATOM    586  CA  GLY A  88      25.278 -38.295  67.154  1.00214.49           C  
ANISOU  586  CA  GLY A  88    24787  30967  25744   7697   3281   1743       C  
ATOM    587  C   GLY A  88      24.719 -36.898  67.282  1.00207.81           C  
ANISOU  587  C   GLY A  88    23860  30004  25096   7222   3349   1810       C  
ATOM    588  O   GLY A  88      24.549 -36.397  68.401  1.00206.98           O  
ANISOU  588  O   GLY A  88    23563  29900  25181   6954   3223   1779       O  
ATOM    589  N   GLN A  89      24.450 -36.273  66.137  1.00204.51           N  
ANISOU  589  N   GLN A  89    23603  29462  24640   7044   3494   1886       N  
ATOM    590  CA  GLN A  89      23.693 -35.011  66.137  1.00203.82           C  
ANISOU  590  CA  GLN A  89    23548  29106  24789   6513   3441   1932       C  
ATOM    591  C   GLN A  89      24.454 -33.890  66.843  1.00209.30           C  
ANISOU  591  C   GLN A  89    23704  30161  25658   6164   3477   1944       C  
ATOM    592  O   GLN A  89      23.862 -33.096  67.574  1.00204.03           O  
ANISOU  592  O   GLN A  89    22969  29306  25246   5808   3319   1898       O  
ATOM    593  CB  GLN A  89      22.309 -35.210  66.777  1.00199.48           C  
ANISOU  593  CB  GLN A  89    23361  28025  24406   6425   3182   1877       C  
ATOM    594  CG  GLN A  89      21.431 -36.183  66.030  1.00207.28           C  
ANISOU  594  CG  GLN A  89    24918  28576  25263   6722   3100   1917       C  
ATOM    595  CD  GLN A  89      20.640 -35.489  64.962  1.00221.33           C  
ANISOU  595  CD  GLN A  89    27018  29945  27133   6421   3134   2005       C  
ATOM    596  OE1 GLN A  89      20.402 -34.291  65.059  1.00223.86           O  
ANISOU  596  OE1 GLN A  89    27173  30188  27695   5942   3118   2005       O  
ATOM    597  NE2 GLN A  89      20.241 -36.223  63.924  1.00228.96           N  
ANISOU  597  NE2 GLN A  89    28438  30631  27926   6685   3150   2079       N  
ATOM    598  N   ILE A  90      25.768 -33.843  66.646  1.00202.48           N  
ANISOU  598  N   ILE A  90    22452  29816  24666   6283   3668   2000       N  
ATOM    599  CA  ILE A  90      26.570 -32.824  67.308  1.00205.94           C  
ANISOU  599  CA  ILE A  90    22380  30598  25269   5986   3678   2053       C  
ATOM    600  C   ILE A  90      26.058 -31.461  66.887  1.00204.25           C  
ANISOU  600  C   ILE A  90    22133  30209  25262   5466   3602   2131       C  
ATOM    601  O   ILE A  90      26.066 -31.122  65.699  1.00207.54           O  
ANISOU  601  O   ILE A  90    22637  30633  25588   5342   3704   2243       O  
ATOM    602  CB  ILE A  90      28.050 -32.969  66.962  1.00216.28           C  
ANISOU  602  CB  ILE A  90    23296  32477  26403   6191   3908   2142       C  
ATOM    603  CG1 ILE A  90      28.509 -34.395  67.227  1.00224.48           C  
ANISOU  603  CG1 ILE A  90    24390  33634  27268   6721   3947   2035       C  
ATOM    604  CG2 ILE A  90      28.872 -31.983  67.786  1.00216.21           C  
ANISOU  604  CG2 ILE A  90    22776  32784  26588   5912   3872   2229       C  
ATOM    605  CD1 ILE A  90      29.951 -34.607  66.918  1.00235.30           C  
ANISOU  605  CD1 ILE A  90    25396  35511  28498   6908   4144   2078       C  
ATOM    606  N   GLN A  91      25.529 -30.702  67.843  1.00199.40           N  
ANISOU  606  N   GLN A  91    21415  29411  24938   5147   3390   2056       N  
ATOM    607  CA  GLN A  91      25.016 -29.370  67.551  1.00193.66           C  
ANISOU  607  CA  GLN A  91    20618  28483  24479   4638   3240   2095       C  
ATOM    608  C   GLN A  91      25.971 -28.278  68.018  1.00196.48           C  
ANISOU  608  C   GLN A  91    20427  29230  24998   4370   3180   2191       C  
ATOM    609  O   GLN A  91      25.531 -27.171  68.345  1.00186.56           O  
ANISOU  609  O   GLN A  91    19029  27804  24052   3963   2947   2154       O  
ATOM    610  CB  GLN A  91      23.617 -29.185  68.150  1.00187.82           C  
ANISOU  610  CB  GLN A  91    20159  27210  23992   4444   3009   1916       C  
ATOM    611  CG  GLN A  91      22.742 -28.206  67.350  1.00190.11           C  
ANISOU  611  CG  GLN A  91    20606  27096  24533   3999   2857   1941       C  
ATOM    612  CD  GLN A  91      21.246 -28.490  67.455  1.00182.29           C  
ANISOU  612  CD  GLN A  91    20079  25491  23694   3950   2712   1794       C  
ATOM    613  OE1 GLN A  91      20.530 -27.844  68.223  1.00164.75           O  
ANISOU  613  OE1 GLN A  91    17789  23031  21779   3682   2502   1626       O  
ATOM    614  NE2 GLN A  91      20.766 -29.443  66.662  1.00190.37           N  
ANISOU  614  NE2 GLN A  91    21569  26253  24510   4212   2814   1856       N  
ATOM    615  N   GLY A  92      27.273 -28.573  68.045  1.00197.42           N  
ANISOU  615  N   GLY A  92    20227  29854  24930   4601   3362   2313       N  
ATOM    616  CA  GLY A  92      28.288 -27.592  68.366  1.00205.76           C  
ANISOU  616  CA  GLY A  92    20768  31299  26114   4381   3309   2469       C  
ATOM    617  C   GLY A  92      27.972 -26.692  69.540  1.00208.47           C  
ANISOU  617  C   GLY A  92    20906  31505  26796   4083   3026   2372       C  
ATOM    618  O   GLY A  92      27.339 -27.111  70.515  1.00218.04           O  
ANISOU  618  O   GLY A  92    22274  32490  28079   4167   2941   2163       O  
ATOM    619  N   SER A  93      28.448 -25.455  69.464  1.00226.64           N  
ANISOU  619  N   SER A  93    22835  33978  29298   3734   2860   2528       N  
ATOM    620  CA  SER A  93      28.179 -24.444  70.468  1.00211.58           C  
ANISOU  620  CA  SER A  93    20699  31949  27742   3428   2545   2432       C  
ATOM    621  C   SER A  93      27.073 -23.515  69.978  1.00198.61           C  
ANISOU  621  C   SER A  93    19185  29891  26385   3006   2270   2344       C  
ATOM    622  O   SER A  93      26.531 -23.671  68.881  1.00197.57           O  
ANISOU  622  O   SER A  93    19337  29552  26177   2933   2330   2386       O  
ATOM    623  CB  SER A  93      29.450 -23.659  70.790  1.00206.52           C  
ANISOU  623  CB  SER A  93    19541  31742  27187   3328   2462   2672       C  
ATOM    624  OG  SER A  93      29.726 -22.735  69.755  1.00200.10           O  
ANISOU  624  OG  SER A  93    18535  31052  26441   3016   2343   2917       O  
ATOM    625  N   VAL A  94      26.731 -22.540  70.817  1.00196.31           N  
ANISOU  625  N   VAL A  94    18682  29459  26449   2719   1945   2207       N  
ATOM    626  CA  VAL A  94      25.742 -21.516  70.498  1.00202.42           C  
ANISOU  626  CA  VAL A  94    19491  29830  27589   2284   1604   2091       C  
ATOM    627  C   VAL A  94      26.213 -20.226  71.160  1.00215.26           C  
ANISOU  627  C   VAL A  94    20634  31601  29556   1992   1234   2120       C  
ATOM    628  O   VAL A  94      26.249 -20.134  72.394  1.00221.67           O  
ANISOU  628  O   VAL A  94    21302  32452  30472   2068   1149   1934       O  
ATOM    629  CB  VAL A  94      24.330 -21.882  70.977  1.00194.87           C  
ANISOU  629  CB  VAL A  94    18907  28375  26758   2289   1555   1735       C  
ATOM    630  CG1 VAL A  94      23.598 -22.689  69.915  1.00189.51           C  
ANISOU  630  CG1 VAL A  94    18720  27390  25895   2389   1748   1761       C  
ATOM    631  CG2 VAL A  94      24.397 -22.662  72.280  1.00197.12           C  
ANISOU  631  CG2 VAL A  94    19213  28785  26898   2605   1690   1548       C  
ATOM    632  N   GLU A  95      26.581 -19.237  70.351  1.00207.13           N  
ANISOU  632  N   GLU A  95    19348  30658  28692   1651    988   2364       N  
ATOM    633  CA  GLU A  95      27.067 -17.965  70.866  1.00210.85           C  
ANISOU  633  CA  GLU A  95    19344  31262  29508   1368    562   2442       C  
ATOM    634  C   GLU A  95      26.174 -16.822  70.400  1.00218.89           C  
ANISOU  634  C   GLU A  95    20310  31878  30980    866     78   2340       C  
ATOM    635  O   GLU A  95      25.607 -16.094  71.215  1.00224.23           O  
ANISOU  635  O   GLU A  95    20849  32309  32040    694   -277   2055       O  
ATOM    636  CB  GLU A  95      28.510 -17.717  70.423  1.00210.46           C  
ANISOU  636  CB  GLU A  95    18928  31751  29284   1391    607   2892       C  
ATOM    637  CG  GLU A  95      29.380 -18.955  70.473  1.00213.57           C  
ANISOU  637  CG  GLU A  95    19415  32515  29217   1867   1121   3021       C  
ATOM    638  CD  GLU A  95      29.316 -19.751  69.188  1.00224.89           C  
ANISOU  638  CD  GLU A  95    21141  34000  30307   1977   1461   3140       C  
ATOM    639  OE1 GLU A  95      29.867 -19.277  68.174  1.00230.22           O  
ANISOU  639  OE1 GLU A  95    21628  34932  30914   1766   1413   3455       O  
ATOM    640  OE2 GLU A  95      28.700 -20.838  69.186  1.00228.36           O  
ANISOU  640  OE2 GLU A  95    21996  34229  30542   2262   1752   2924       O  
ATOM    641  N   SER A 117      30.695 -20.253  73.607  1.00220.62           N  
ANISOU  641  N   SER A 117    20110  33784  29931   2613   1442   2807       N  
ATOM    642  CA  SER A 117      31.796 -20.983  74.230  1.00228.87           C  
ANISOU  642  CA  SER A 117    21033  35154  30775   2938   1686   2951       C  
ATOM    643  C   SER A 117      31.287 -22.184  75.005  1.00235.96           C  
ANISOU  643  C   SER A 117    22254  35899  31503   3217   1907   2658       C  
ATOM    644  O   SER A 117      31.856 -22.566  76.031  1.00242.21           O  
ANISOU  644  O   SER A 117    22944  36816  32267   3369   1951   2652       O  
ATOM    645  CB  SER A 117      32.589 -20.067  75.164  1.00229.62           C  
ANISOU  645  CB  SER A 117    20720  35409  31117   2814   1398   3101       C  
ATOM    646  OG  SER A 117      31.820 -19.710  76.301  1.00227.50           O  
ANISOU  646  OG  SER A 117    20493  34873  31073   2693   1158   2767       O  
ATOM    647  N   MET A 118      30.206 -22.787  74.515  1.00226.60           N  
ANISOU  647  N   MET A 118    21460  34427  30209   3263   2018   2438       N  
ATOM    648  CA  MET A 118      29.589 -23.922  75.193  1.00225.72           C  
ANISOU  648  CA  MET A 118    21670  34154  29940   3497   2167   2179       C  
ATOM    649  C   MET A 118      29.060 -24.888  74.141  1.00209.11           C  
ANISOU  649  C   MET A 118    19954  31912  27587   3701   2405   2155       C  
ATOM    650  O   MET A 118      28.039 -24.615  73.502  1.00201.57           O  
ANISOU  650  O   MET A 118    19236  30641  26710   3533   2326   2044       O  
ATOM    651  CB  MET A 118      28.457 -23.463  76.121  1.00239.12           C  
ANISOU  651  CB  MET A 118    23452  35544  31860   3277   1921   1841       C  
ATOM    652  CG  MET A 118      28.849 -22.511  77.264  1.00249.58           C  
ANISOU  652  CG  MET A 118    24419  36974  33435   3082   1654   1797       C  
ATOM    653  SD  MET A 118      29.012 -20.777  76.776  1.00254.35           S  
ANISOU  653  SD  MET A 118    24662  37558  34421   2697   1268   1927       S  
ATOM    654  CE  MET A 118      27.993 -19.992  78.016  1.00247.75           C  
ANISOU  654  CE  MET A 118    23766  36464  33905   2450    922   1488       C  
ATOM    655  N   ASN A 119      29.727 -26.027  73.992  1.00219.32           N  
ANISOU  655  N   ASN A 119    21320  33409  28605   4064   2668   2246       N  
ATOM    656  CA  ASN A 119      29.308 -27.007  73.008  1.00211.86           C  
ANISOU  656  CA  ASN A 119    20736  32349  27410   4309   2875   2221       C  
ATOM    657  C   ASN A 119      28.220 -27.887  73.602  1.00203.30           C  
ANISOU  657  C   ASN A 119    20031  30942  26273   4434   2836   1963       C  
ATOM    658  O   ASN A 119      28.199 -28.168  74.804  1.00206.94           O  
ANISOU  658  O   ASN A 119    20435  31421  26773   4457   2748   1845       O  
ATOM    659  CB  ASN A 119      30.493 -27.855  72.537  1.00217.34           C  
ANISOU  659  CB  ASN A 119    21321  33408  27852   4666   3141   2398       C  
ATOM    660  CG  ASN A 119      31.326 -28.386  73.683  1.00224.03           C  
ANISOU  660  CG  ASN A 119    21962  34457  28704   4845   3150   2403       C  
ATOM    661  OD1 ASN A 119      30.899 -28.374  74.834  1.00225.85           O  
ANISOU  661  OD1 ASN A 119    22215  34542  29056   4745   2983   2254       O  
ATOM    662  ND2 ASN A 119      32.526 -28.858  73.370  1.00226.80           N  
ANISOU  662  ND2 ASN A 119    22107  35143  28924   5092   3339   2571       N  
ATOM    663  N   VAL A 120      27.299 -28.313  72.749  1.00194.54           N  
ANISOU  663  N   VAL A 120    19310  29537  25070   4494   2884   1898       N  
ATOM    664  CA  VAL A 120      26.160 -29.086  73.209  1.00189.20           C  
ANISOU  664  CA  VAL A 120    19009  28526  24354   4590   2813   1693       C  
ATOM    665  C   VAL A 120      26.119 -30.412  72.470  1.00206.93           C  
ANISOU  665  C   VAL A 120    21586  30722  26315   4991   2975   1736       C  
ATOM    666  O   VAL A 120      26.697 -30.580  71.392  1.00209.69           O  
ANISOU  666  O   VAL A 120    21938  31218  26515   5141   3151   1878       O  
ATOM    667  CB  VAL A 120      24.840 -28.322  73.012  1.00180.77           C  
ANISOU  667  CB  VAL A 120    18144  27032  23509   4264   2641   1548       C  
ATOM    668  CG1 VAL A 120      24.930 -26.944  73.646  1.00179.38           C  
ANISOU  668  CG1 VAL A 120    17603  26909  23646   3879   2438   1482       C  
ATOM    669  CG2 VAL A 120      24.522 -28.215  71.536  1.00190.61           C  
ANISOU  669  CG2 VAL A 120    19630  28080  24712   4231   2722   1664       C  
ATOM    670  N   TYR A 121      25.422 -31.367  73.078  1.00197.83           N  
ANISOU  670  N   TYR A 121    20703  29381  25083   5164   2889   1609       N  
ATOM    671  CA  TYR A 121      25.285 -32.698  72.519  1.00206.40           C  
ANISOU  671  CA  TYR A 121    22118  30378  25928   5566   2955   1634       C  
ATOM    672  C   TYR A 121      23.823 -33.102  72.644  1.00206.33           C  
ANISOU  672  C   TYR A 121    22539  29920  25937   5542   2793   1524       C  
ATOM    673  O   TYR A 121      23.035 -32.445  73.331  1.00206.74           O  
ANISOU  673  O   TYR A 121    22581  29797  26175   5236   2653   1402       O  
ATOM    674  CB  TYR A 121      26.198 -33.697  73.235  1.00219.95           C  
ANISOU  674  CB  TYR A 121    23663  32391  27518   5865   2953   1647       C  
ATOM    675  CG  TYR A 121      26.759 -34.744  72.312  1.00232.57           C  
ANISOU  675  CG  TYR A 121    25382  34089  28896   6298   3085   1712       C  
ATOM    676  CD1 TYR A 121      27.553 -34.366  71.238  1.00236.28           C  
ANISOU  676  CD1 TYR A 121    25703  34782  29289   6357   3318   1819       C  
ATOM    677  CD2 TYR A 121      26.507 -36.095  72.501  1.00235.42           C  
ANISOU  677  CD2 TYR A 121    25981  34342  29124   6642   2953   1663       C  
ATOM    678  CE1 TYR A 121      28.085 -35.294  70.388  1.00236.88           C  
ANISOU  678  CE1 TYR A 121    25862  34989  29154   6761   3454   1836       C  
ATOM    679  CE2 TYR A 121      27.038 -37.039  71.642  1.00236.95           C  
ANISOU  679  CE2 TYR A 121    26284  34607  29137   7031   3030   1679       C  
ATOM    680  CZ  TYR A 121      27.826 -36.628  70.585  1.00237.46           C  
ANISOU  680  CZ  TYR A 121    26220  34885  29120   7059   3282   1740       C  
ATOM    681  OH  TYR A 121      28.366 -37.545  69.716  1.00239.63           O  
ANISOU  681  OH  TYR A 121    26634  35211  29204   7358   3329   1704       O  
ATOM    682  N   SER A 122      23.449 -34.177  71.955  1.00211.64           N  
ANISOU  682  N   SER A 122    23587  30403  26425   5875   2802   1565       N  
ATOM    683  CA  SER A 122      22.080 -34.670  72.026  1.00213.63           C  
ANISOU  683  CA  SER A 122    24272  30215  26684   5893   2630   1512       C  
ATOM    684  C   SER A 122      22.078 -36.183  71.866  1.00208.89           C  
ANISOU  684  C   SER A 122    23939  29573  25856   6354   2545   1566       C  
ATOM    685  O   SER A 122      23.006 -36.773  71.305  1.00208.56           O  
ANISOU  685  O   SER A 122    23823  29761  25660   6670   2660   1623       O  
ATOM    686  CB  SER A 122      21.183 -34.012  70.969  1.00224.69           C  
ANISOU  686  CB  SER A 122    25973  31203  28197   5697   2664   1538       C  
ATOM    687  OG  SER A 122      21.510 -34.463  69.670  1.00234.35           O  
ANISOU  687  OG  SER A 122    27402  32397  29245   5951   2813   1660       O  
ATOM    688  N   LEU A 123      21.008 -36.803  72.365  1.00207.51           N  
ANISOU  688  N   LEU A 123    24063  29107  25674   6390   2317   1543       N  
ATOM    689  CA  LEU A 123      20.780 -38.233  72.225  1.00208.79           C  
ANISOU  689  CA  LEU A 123    24526  29150  25656   6804   2135   1616       C  
ATOM    690  C   LEU A 123      19.357 -38.449  71.739  1.00206.09           C  
ANISOU  690  C   LEU A 123    24693  28278  25336   6809   1999   1673       C  
ATOM    691  O   LEU A 123      18.417 -37.790  72.205  1.00202.48           O  
ANISOU  691  O   LEU A 123    24295  27601  25037   6476   1934   1615       O  
ATOM    692  CB  LEU A 123      21.001 -38.988  73.538  1.00214.33           C  
ANISOU  692  CB  LEU A 123    25040  30082  26312   6854   1893   1591       C  
ATOM    693  CG  LEU A 123      22.394 -38.891  74.161  1.00223.79           C  
ANISOU  693  CG  LEU A 123    25752  31760  27519   6843   1978   1553       C  
ATOM    694  CD1 LEU A 123      22.383 -39.484  75.559  1.00227.74           C  
ANISOU  694  CD1 LEU A 123    26099  32421  28010   6760   1699   1533       C  
ATOM    695  CD2 LEU A 123      23.441 -39.563  73.299  1.00226.30           C  
ANISOU  695  CD2 LEU A 123    26017  32248  27719   7249   2090   1597       C  
ATOM    696  N   SER A 124      19.213 -39.389  70.810  1.00220.26           N  
ANISOU  696  N   SER A 124    26857  29853  26978   7159   1933   1772       N  
ATOM    697  CA  SER A 124      17.958 -39.642  70.127  1.00224.05           C  
ANISOU  697  CA  SER A 124    27890  29773  27467   7075   1789   1847       C  
ATOM    698  C   SER A 124      17.657 -41.138  70.136  1.00222.48           C  
ANISOU  698  C   SER A 124    28033  29414  27083   7151   1436   1880       C  
ATOM    699  O   SER A 124      18.419 -41.962  70.661  1.00226.13           O  
ANISOU  699  O   SER A 124    28308  30172  27438   7304   1296   1844       O  
ATOM    700  CB  SER A 124      17.996 -39.088  68.693  1.00228.12           C  
ANISOU  700  CB  SER A 124    28594  30091  27990   7105   2039   1903       C  
ATOM    701  OG  SER A 124      18.018 -37.665  68.705  1.00226.78           O  
ANISOU  701  OG  SER A 124    28164  29967  28035   6752   2252   1849       O  
ATOM    702  N   VAL A 125      16.500 -41.490  69.596  1.00242.49           N  
ANISOU  702  N   VAL A 125    31047  31466  29624   6977   1267   1934       N  
ATOM    703  CA  VAL A 125      16.140 -42.893  69.469  1.00242.50           C  
ANISOU  703  CA  VAL A 125    31344  31304  29492   6955    935   1939       C  
ATOM    704  C   VAL A 125      15.217 -43.004  68.268  1.00258.82           C  
ANISOU  704  C   VAL A 125    33869  32900  31572   6765    912   1971       C  
ATOM    705  O   VAL A 125      14.169 -42.350  68.205  1.00255.25           O  
ANISOU  705  O   VAL A 125    33585  32114  31284   6470    917   1998       O  
ATOM    706  CB  VAL A 125      15.503 -43.439  70.764  1.00224.63           C  
ANISOU  706  CB  VAL A 125    29030  29049  27271   6775    614   1943       C  
ATOM    707  CG1 VAL A 125      14.440 -42.516  71.282  1.00217.36           C  
ANISOU  707  CG1 VAL A 125    28140  27928  26519   6516    647   1963       C  
ATOM    708  CG2 VAL A 125      14.916 -44.802  70.531  1.00215.07           C  
ANISOU  708  CG2 VAL A 125    28109  27594  26012   6634    269   1944       C  
ATOM    709  N   ASP A 126      15.611 -43.815  67.295  1.00246.85           N  
ANISOU  709  N   ASP A 126    32527  31364  29901   6921    885   1951       N  
ATOM    710  CA  ASP A 126      14.853 -43.872  66.062  1.00250.39           C  
ANISOU  710  CA  ASP A 126    33360  31423  30352   6745    893   1974       C  
ATOM    711  C   ASP A 126      13.503 -44.540  66.299  1.00251.63           C  
ANISOU  711  C   ASP A 126    33729  31231  30650   6327    559   1957       C  
ATOM    712  O   ASP A 126      13.377 -45.421  67.152  1.00255.14           O  
ANISOU  712  O   ASP A 126    34074  31757  31110   6272    287   1932       O  
ATOM    713  CB  ASP A 126      15.612 -44.634  64.981  1.00258.47           C  
ANISOU  713  CB  ASP A 126    34494  32553  31159   7043    940   1939       C  
ATOM    714  CG  ASP A 126      16.429 -45.775  65.537  1.00263.55           C  
ANISOU  714  CG  ASP A 126    34944  33494  31697   7288    738   1855       C  
ATOM    715  OD1 ASP A 126      16.357 -46.025  66.756  1.00263.34           O  
ANISOU  715  OD1 ASP A 126    34722  33573  31764   7195    543   1845       O  
ATOM    716  OD2 ASP A 126      17.110 -46.450  64.740  1.00268.87           O  
ANISOU  716  OD2 ASP A 126    35670  34283  32205   7565    754   1796       O  
ATOM    717  N   PRO A 127      12.472 -44.121  65.566  1.00261.67           N  
ANISOU  717  N   PRO A 127    35238  32124  32062   5992    565   1974       N  
ATOM    718  CA  PRO A 127      11.178 -44.812  65.661  1.00261.43           C  
ANISOU  718  CA  PRO A 127    35313  31809  32211   5557    252   1950       C  
ATOM    719  C   PRO A 127      11.259 -46.295  65.334  1.00275.44           C  
ANISOU  719  C   PRO A 127    37210  33636  33810   5694     58   1924       C  
ATOM    720  O   PRO A 127      10.377 -47.051  65.759  1.00272.39           O  
ANISOU  720  O   PRO A 127    36949  33174  33372   5597   -136   1934       O  
ATOM    721  CB  PRO A 127      10.305 -44.059  64.649  1.00247.43           C  
ANISOU  721  CB  PRO A 127    33735  29687  30590   5244    337   1961       C  
ATOM    722  CG  PRO A 127      10.898 -42.694  64.597  1.00243.59           C  
ANISOU  722  CG  PRO A 127    33201  29246  30106   5407    652   2003       C  
ATOM    723  CD  PRO A 127      12.383 -42.888  64.765  1.00253.43           C  
ANISOU  723  CD  PRO A 127    34296  30906  31092   5934    840   2023       C  
ATOM    724  N   ASN A 128      12.279 -46.735  64.585  1.00266.73           N  
ANISOU  724  N   ASN A 128    36105  32674  32565   5987    126   1887       N  
ATOM    725  CA  ASN A 128      12.371 -48.148  64.228  1.00268.59           C  
ANISOU  725  CA  ASN A 128    36511  32959  32581   6208    -48   1844       C  
ATOM    726  C   ASN A 128      12.546 -49.040  65.450  1.00267.04           C  
ANISOU  726  C   ASN A 128    36126  32935  32402   6259   -319   1833       C  
ATOM    727  O   ASN A 128      12.031 -50.163  65.471  1.00270.78           O  
ANISOU  727  O   ASN A 128    36768  33347  32771   6290   -544   1814       O  
ATOM    728  CB  ASN A 128      13.535 -48.375  63.261  1.00270.87           C  
ANISOU  728  CB  ASN A 128    36782  33399  32738   6536     76   1789       C  
ATOM    729  CG  ASN A 128      13.283 -47.787  61.884  1.00272.70           C  
ANISOU  729  CG  ASN A 128    37266  33441  32904   6501    296   1813       C  
ATOM    730  OD1 ASN A 128      12.253 -47.162  61.635  1.00273.49           O  
ANISOU  730  OD1 ASN A 128    37550  33283  33083   6209    352   1865       O  
ATOM    731  ND2 ASN A 128      14.235 -47.988  60.979  1.00276.08           N  
ANISOU  731  ND2 ASN A 128    37758  34033  33108   6884    449   1778       N  
ATOM    732  N   THR A 129      13.245 -48.568  66.484  1.00272.40           N  
ANISOU  732  N   THR A 129    36448  33824  33228   6253   -318   1843       N  
ATOM    733  CA  THR A 129      13.327 -49.361  67.704  1.00262.42           C  
ANISOU  733  CA  THR A 129    35001  32707  32001   6243   -597   1857       C  
ATOM    734  C   THR A 129      12.127 -49.133  68.610  1.00272.37           C  
ANISOU  734  C   THR A 129    36288  33844  33356   5932   -707   1932       C  
ATOM    735  O   THR A 129      11.958 -49.874  69.580  1.00272.63           O  
ANISOU  735  O   THR A 129    36215  33965  33409   5877   -966   1971       O  
ATOM    736  CB  THR A 129      14.631 -49.099  68.465  1.00241.91           C  
ANISOU  736  CB  THR A 129    32076  30475  29364   6524   -536   1830       C  
ATOM    737  OG1 THR A 129      14.631 -49.843  69.692  1.00233.41           O  
ANISOU  737  OG1 THR A 129    30793  29500  28394   6405   -855   1863       O  
ATOM    738  CG2 THR A 129      14.769 -47.660  68.781  1.00231.11           C  
ANISOU  738  CG2 THR A 129    30617  29240  27954   6599   -220   1863       C  
ATOM    739  N   TRP A 130      11.305 -48.119  68.325  1.00257.42           N  
ANISOU  739  N   TRP A 130    34514  31753  31540   5718   -531   1955       N  
ATOM    740  CA  TRP A 130      10.081 -47.922  69.095  1.00256.47           C  
ANISOU  740  CA  TRP A 130    34428  31508  31513   5434   -632   2010       C  
ATOM    741  C   TRP A 130       9.034 -48.964  68.731  1.00249.83           C  
ANISOU  741  C   TRP A 130    33872  30490  30564   5377   -802   2019       C  
ATOM    742  O   TRP A 130       8.453 -49.608  69.611  1.00246.92           O  
ANISOU  742  O   TRP A 130    33451  30150  30217   5270  -1029   2070       O  
ATOM    743  CB  TRP A 130       9.532 -46.511  68.869  1.00264.56           C  
ANISOU  743  CB  TRP A 130    35472  32352  32695   5222   -414   2008       C  
ATOM    744  CG  TRP A 130      10.281 -45.433  69.587  1.00275.76           C  
ANISOU  744  CG  TRP A 130    36613  33956  34206   5298   -269   1997       C  
ATOM    745  CD1 TRP A 130      11.094 -44.484  69.040  1.00282.42           C  
ANISOU  745  CD1 TRP A 130    37458  34889  34960   5567     50   1982       C  
ATOM    746  CD2 TRP A 130      10.247 -45.172  70.994  1.00280.40           C  
ANISOU  746  CD2 TRP A 130    36997  34756  34784   5327   -331   2026       C  
ATOM    747  NE1 TRP A 130      11.588 -43.661  70.025  1.00286.30           N  
ANISOU  747  NE1 TRP A 130    37706  35645  35430   5750    194   1992       N  
ATOM    748  CE2 TRP A 130      11.080 -44.062  71.233  1.00284.70           C  
ANISOU  748  CE2 TRP A 130    37385  35532  35256   5621    -37   2012       C  
ATOM    749  CE3 TRP A 130       9.599 -45.775  72.075  1.00278.09           C  
ANISOU  749  CE3 TRP A 130    36606  34510  34546   5127   -606   2076       C  
ATOM    750  CZ2 TRP A 130      11.283 -43.544  72.511  1.00284.02           C  
ANISOU  750  CZ2 TRP A 130    37024  35743  35148   5729    -13   2023       C  
ATOM    751  CZ3 TRP A 130       9.801 -45.260  73.342  1.00277.64           C  
ANISOU  751  CZ3 TRP A 130    36336  34741  34412   5253   -587   2099       C  
ATOM    752  CH2 TRP A 130      10.636 -44.156  73.550  1.00280.04           C  
ANISOU  752  CH2 TRP A 130    36464  35296  34641   5558   -293   2064       C  
ATOM    753  N   GLN A 131       8.772 -49.138  67.434  1.00275.83           N  
ANISOU  753  N   GLN A 131    37453  33603  33745   5439   -702   1974       N  
ATOM    754  CA  GLN A 131       7.783 -50.123  67.009  1.00258.55           C  
ANISOU  754  CA  GLN A 131    35532  31244  31460   5398   -864   1960       C  
ATOM    755  C   GLN A 131       8.255 -51.544  67.294  1.00255.83           C  
ANISOU  755  C   GLN A 131    35159  31028  31015   5601  -1138   1943       C  
ATOM    756  O   GLN A 131       7.468 -52.386  67.743  1.00254.28           O  
ANISOU  756  O   GLN A 131    35014  30769  30831   5507  -1374   1972       O  
ATOM    757  CB  GLN A 131       7.464 -49.949  65.526  1.00244.39           C  
ANISOU  757  CB  GLN A 131    34048  29246  29562   5422   -701   1908       C  
ATOM    758  CG  GLN A 131       6.379 -50.883  65.050  1.00230.60           C  
ANISOU  758  CG  GLN A 131    32577  27315  27725   5367   -865   1879       C  
ATOM    759  CD  GLN A 131       5.059 -50.606  65.736  1.00213.04           C  
ANISOU  759  CD  GLN A 131    30334  24963  25649   5059   -937   1928       C  
ATOM    760  OE1 GLN A 131       4.702 -49.452  65.974  1.00208.04           O  
ANISOU  760  OE1 GLN A 131    29610  24269  25168   4852   -784   1959       O  
ATOM    761  NE2 GLN A 131       4.335 -51.664  66.076  1.00205.27           N  
ANISOU  761  NE2 GLN A 131    29418  23938  24638   5031  -1185   1936       N  
ATOM    762  N   THR A 132       9.538 -51.831  67.046  1.00257.39           N  
ANISOU  762  N   THR A 132    35253  31404  31138   5876  -1126   1895       N  
ATOM    763  CA  THR A 132      10.053 -53.171  67.311  1.00259.55           C  
ANISOU  763  CA  THR A 132    35475  31789  31355   6067  -1415   1864       C  
ATOM    764  C   THR A 132      10.030 -53.490  68.801  1.00267.30           C  
ANISOU  764  C   THR A 132    36176  32910  32477   5927  -1657   1956       C  
ATOM    765  O   THR A 132       9.754 -54.631  69.190  1.00269.56           O  
ANISOU  765  O   THR A 132    36470  33181  32770   5922  -1961   1980       O  
ATOM    766  CB  THR A 132      11.472 -53.327  66.752  1.00254.98           C  
ANISOU  766  CB  THR A 132    34803  31385  30692   6393  -1346   1781       C  
ATOM    767  OG1 THR A 132      12.323 -52.302  67.281  1.00251.86           O  
ANISOU  767  OG1 THR A 132    34109  31181  30407   6389  -1164   1811       O  
ATOM    768  CG2 THR A 132      11.474 -53.262  65.223  1.00253.35           C  
ANISOU  768  CG2 THR A 132    34898  31052  30312   6553  -1159   1703       C  
ATOM    769  N   LEU A 133      10.323 -52.503  69.652  1.00255.27           N  
ANISOU  769  N   LEU A 133    34395  31526  31071   5803  -1542   2014       N  
ATOM    770  CA  LEU A 133      10.275 -52.752  71.089  1.00258.43           C  
ANISOU  770  CA  LEU A 133    34528  32079  31586   5645  -1775   2117       C  
ATOM    771  C   LEU A 133       8.838 -52.912  71.559  1.00264.43           C  
ANISOU  771  C   LEU A 133    35391  32687  32391   5373  -1892   2208       C  
ATOM    772  O   LEU A 133       8.547 -53.769  72.398  1.00263.71           O  
ANISOU  772  O   LEU A 133    35195  32656  32345   5271  -2185   2306       O  
ATOM    773  CB  LEU A 133      10.976 -51.626  71.853  1.00255.16           C  
ANISOU  773  CB  LEU A 133    33814  31865  31270   5595  -1627   2137       C  
ATOM    774  CG  LEU A 133      11.474 -51.904  73.275  1.00255.88           C  
ANISOU  774  CG  LEU A 133    33566  32206  31449   5505  -1873   2223       C  
ATOM    775  CD1 LEU A 133      12.567 -52.956  73.267  1.00258.25           C  
ANISOU  775  CD1 LEU A 133    33739  32644  31742   5713  -2086   2194       C  
ATOM    776  CD2 LEU A 133      11.981 -50.621  73.918  1.00255.07           C  
ANISOU  776  CD2 LEU A 133    33206  32276  31434   5442  -1690   2215       C  
ATOM    777  N   LEU A 134       7.920 -52.122  71.002  1.00271.29           N  
ANISOU  777  N   LEU A 134    36455  33359  33264   5244  -1677   2185       N  
ATOM    778  CA  LEU A 134       6.517 -52.240  71.380  1.00267.26           C  
ANISOU  778  CA  LEU A 134    36032  32704  32811   4996  -1771   2258       C  
ATOM    779  C   LEU A 134       5.980 -53.619  71.017  1.00275.67           C  
ANISOU  779  C   LEU A 134    37276  33652  33814   5039  -2016   2264       C  
ATOM    780  O   LEU A 134       5.168 -54.194  71.751  1.00266.63           O  
ANISOU  780  O   LEU A 134    36076  32498  32732   4870  -2229   2374       O  
ATOM    781  CB  LEU A 134       5.705 -51.128  70.708  1.00249.25           C  
ANISOU  781  CB  LEU A 134    33923  30215  30566   4859  -1500   2210       C  
ATOM    782  CG  LEU A 134       4.184 -51.039  70.868  1.00234.14           C  
ANISOU  782  CG  LEU A 134    32117  28118  28726   4606  -1537   2255       C  
ATOM    783  CD1 LEU A 134       3.439 -51.923  69.876  1.00231.91           C  
ANISOU  783  CD1 LEU A 134    32132  27629  28355   4637  -1616   2208       C  
ATOM    784  CD2 LEU A 134       3.792 -51.368  72.298  1.00229.05           C  
ANISOU  784  CD2 LEU A 134    31239  27628  28162   4450  -1758   2389       C  
ATOM    785  N   HIS A 135       6.431 -54.166  69.886  1.00265.66           N  
ANISOU  785  N   HIS A 135    36215  32302  32421   5269  -1997   2152       N  
ATOM    786  CA  HIS A 135       6.012 -55.495  69.458  1.00275.40           C  
ANISOU  786  CA  HIS A 135    37634  33415  33590   5346  -2247   2127       C  
ATOM    787  C   HIS A 135       6.742 -56.606  70.204  1.00284.47           C  
ANISOU  787  C   HIS A 135    38582  34727  34775   5445  -2572   2180       C  
ATOM    788  O   HIS A 135       6.186 -57.695  70.379  1.00288.78           O  
ANISOU  788  O   HIS A 135    39184  35196  35341   5404  -2852   2225       O  
ATOM    789  CB  HIS A 135       6.250 -55.644  67.955  1.00280.09           C  
ANISOU  789  CB  HIS A 135    38530  33873  34018   5564  -2119   1977       C  
ATOM    790  CG  HIS A 135       5.958 -57.012  67.424  1.00284.18           C  
ANISOU  790  CG  HIS A 135    39255  34269  34450   5688  -2388   1914       C  
ATOM    791  ND1 HIS A 135       6.832 -58.072  67.555  1.00288.38           N  
ANISOU  791  ND1 HIS A 135    39708  34904  34959   5905  -2643   1875       N  
ATOM    792  CD2 HIS A 135       4.884 -57.492  66.756  1.00285.42           C  
ANISOU  792  CD2 HIS A 135    39692  34202  34552   5623  -2462   1872       C  
ATOM    793  CE1 HIS A 135       6.308 -59.144  66.988  1.00289.94           C  
ANISOU  793  CE1 HIS A 135    40141  34937  35089   5974  -2867   1806       C  
ATOM    794  NE2 HIS A 135       5.126 -58.819  66.497  1.00288.70           N  
ANISOU  794  NE2 HIS A 135    40205  34582  34903   5806  -2759   1805       N  
ATOM    795  N   GLU A 136       7.973 -56.363  70.654  1.00294.73           N  
ANISOU  795  N   GLU A 136    39636  36247  36099   5562  -2556   2180       N  
ATOM    796  CA  GLU A 136       8.710 -57.400  71.369  1.00270.32           C  
ANISOU  796  CA  GLU A 136    36329  33311  33067   5632  -2885   2234       C  
ATOM    797  C   GLU A 136       8.249 -57.569  72.812  1.00256.83           C  
ANISOU  797  C   GLU A 136    34362  31728  31494   5347  -3102   2442       C  
ATOM    798  O   GLU A 136       8.380 -58.664  73.365  1.00262.29           O  
ANISOU  798  O   GLU A 136    34933  32482  32242   5322  -3434   2534       O  
ATOM    799  CB  GLU A 136      10.210 -57.089  71.326  1.00263.26           C  
ANISOU  799  CB  GLU A 136    35242  32619  32165   5852  -2800   2156       C  
ATOM    800  CG  GLU A 136      11.109 -58.037  72.105  1.00261.70           C  
ANISOU  800  CG  GLU A 136    34774  32597  32061   5910  -3136   2206       C  
ATOM    801  CD  GLU A 136      12.505 -57.458  72.312  1.00255.06           C  
ANISOU  801  CD  GLU A 136    33668  31985  31258   6057  -3021   2152       C  
ATOM    802  OE1 GLU A 136      13.160 -57.134  71.293  1.00252.71           O  
ANISOU  802  OE1 GLU A 136    33472  31681  30865   6319  -2798   1998       O  
ATOM    803  OE2 GLU A 136      12.937 -57.309  73.476  1.00251.53           O  
ANISOU  803  OE2 GLU A 136    32906  31735  30931   5902  -3149   2268       O  
ATOM    804  N   ARG A 137       7.698 -56.531  73.437  1.00273.92           N  
ANISOU  804  N   ARG A 137    36431  33940  33706   5124  -2936   2526       N  
ATOM    805  CA  ARG A 137       7.312 -56.626  74.838  1.00257.76           C  
ANISOU  805  CA  ARG A 137    34119  32062  31755   4849  -3136   2737       C  
ATOM    806  C   ARG A 137       5.913 -56.065  75.016  1.00256.36           C  
ANISOU  806  C   ARG A 137    34037  31768  31601   4617  -3023   2806       C  
ATOM    807  O   ARG A 137       5.544 -55.077  74.379  1.00257.21           O  
ANISOU  807  O   ARG A 137    34308  31737  31684   4629  -2729   2691       O  
ATOM    808  CB  ARG A 137       8.293 -55.905  75.766  1.00243.82           C  
ANISOU  808  CB  ARG A 137    32040  30568  30031   4799  -3116   2776       C  
ATOM    809  CG  ARG A 137       8.811 -54.613  75.232  1.00236.80           C  
ANISOU  809  CG  ARG A 137    31192  29675  29107   4927  -2758   2618       C  
ATOM    810  CD  ARG A 137       9.950 -54.112  76.077  1.00232.57           C  
ANISOU  810  CD  ARG A 137    30338  29417  28611   4928  -2779   2629       C  
ATOM    811  NE  ARG A 137      11.165 -54.861  75.772  1.00236.22           N  
ANISOU  811  NE  ARG A 137    30710  29961  29080   5159  -2904   2568       N  
ATOM    812  CZ  ARG A 137      12.323 -54.705  76.403  1.00241.25           C  
ANISOU  812  CZ  ARG A 137    31056  30833  29774   5195  -2975   2566       C  
ATOM    813  NH1 ARG A 137      12.429 -53.828  77.391  1.00237.31           N  
ANISOU  813  NH1 ARG A 137    30338  30522  29306   5011  -2941   2615       N  
ATOM    814  NH2 ARG A 137      13.374 -55.431  76.047  1.00249.14           N  
ANISOU  814  NH2 ARG A 137    31977  31882  30802   5416  -3091   2498       N  
ATOM    815  N   HIS A 138       5.136 -56.720  75.871  1.00249.27           N  
ANISOU  815  N   HIS A 138    33022  30937  30753   4403  -3260   3005       N  
ATOM    816  CA  HIS A 138       3.732 -56.408  76.069  1.00244.87           C  
ANISOU  816  CA  HIS A 138    32534  30281  30225   4192  -3196   3089       C  
ATOM    817  C   HIS A 138       3.517 -55.849  77.468  1.00246.55           C  
ANISOU  817  C   HIS A 138    32444  30756  30477   3926  -3259   3280       C  
ATOM    818  O   HIS A 138       4.300 -56.102  78.387  1.00245.48           O  
ANISOU  818  O   HIS A 138    32041  30891  30340   3854  -3454   3402       O  
ATOM    819  CB  HIS A 138       2.875 -57.654  75.837  1.00241.31           C  
ANISOU  819  CB  HIS A 138    32210  29704  29772   4175  -3405   3168       C  
ATOM    820  CG  HIS A 138       2.842 -58.090  74.406  1.00235.11           C  
ANISOU  820  CG  HIS A 138    31775  28632  28925   4398  -3351   2953       C  
ATOM    821  ND1 HIS A 138       1.972 -57.554  73.481  1.00233.40           N  
ANISOU  821  ND1 HIS A 138    31833  28168  28682   4389  -3136   2823       N  
ATOM    822  CD2 HIS A 138       3.598 -58.989  73.735  1.00236.63           C  
ANISOU  822  CD2 HIS A 138    32084  28763  29063   4631  -3497   2840       C  
ATOM    823  CE1 HIS A 138       2.185 -58.115  72.304  1.00234.07           C  
ANISOU  823  CE1 HIS A 138    32191  28068  28677   4594  -3152   2653       C  
ATOM    824  NE2 HIS A 138       3.166 -58.989  72.431  1.00237.53           N  
ANISOU  824  NE2 HIS A 138    32545  28612  29095   4757  -3369   2652       N  
ATOM    825  N   LEU A 139       2.452 -55.057  77.605  1.00240.50           N  
ANISOU  825  N   LEU A 139    31727  29912  29738   3767  -3104   3292       N  
ATOM    826  CA  LEU A 139       2.183 -54.322  78.835  1.00239.74           C  
ANISOU  826  CA  LEU A 139    31390  30048  29654   3520  -3141   3420       C  
ATOM    827  C   LEU A 139       2.208 -55.249  80.044  1.00243.29           C  
ANISOU  827  C   LEU A 139    31546  30820  30074   3317  -3477   3712       C  
ATOM    828  O   LEU A 139       1.611 -56.329  80.035  1.00246.00           O  
ANISOU  828  O   LEU A 139    31878  31191  30398   3310  -3599   3878       O  
ATOM    829  CB  LEU A 139       0.831 -53.607  78.733  1.00241.33           C  
ANISOU  829  CB  LEU A 139    31700  30092  29901   3390  -2968   3408       C  
ATOM    830  CG  LEU A 139      -0.487 -54.391  78.796  1.00246.26           C  
ANISOU  830  CG  LEU A 139    32356  30667  30547   3275  -3057   3578       C  
ATOM    831  CD1 LEU A 139      -1.653 -53.421  78.846  1.00245.37           C  
ANISOU  831  CD1 LEU A 139    32297  30437  30496   3138  -2874   3546       C  
ATOM    832  CD2 LEU A 139      -0.662 -55.371  77.643  1.00250.32           C  
ANISOU  832  CD2 LEU A 139    33137  30921  31051   3462  -3074   3486       C  
ATOM    833  N   ARG A 140       2.943 -54.833  81.074  1.00255.21           N  
ANISOU  833  N   ARG A 140    32827  32595  31547   3162  -3625   3755       N  
ATOM    834  CA  ARG A 140       2.998 -55.562  82.340  1.00254.43           C  
ANISOU  834  CA  ARG A 140    32463  32831  31378   2857  -3871   3910       C  
ATOM    835  C   ARG A 140       1.729 -55.258  83.124  1.00256.74           C  
ANISOU  835  C   ARG A 140    32711  33207  31632   2543  -3863   3976       C  
ATOM    836  O   ARG A 140       1.714 -54.443  84.048  1.00257.60           O  
ANISOU  836  O   ARG A 140    32898  33301  31677   2317  -4034   3785       O  
ATOM    837  CB  ARG A 140       4.273 -55.216  83.105  1.00244.51           C  
ANISOU  837  CB  ARG A 140    31084  31734  30085   2774  -4058   3796       C  
ATOM    838  CG  ARG A 140       4.633 -56.187  84.223  1.00238.19           C  
ANISOU  838  CG  ARG A 140    30056  31190  29256   2461  -4375   3935       C  
ATOM    839  CD  ARG A 140       5.665 -55.599  85.181  1.00230.50           C  
ANISOU  839  CD  ARG A 140    29174  30207  28198   2393  -4663   3616       C  
ATOM    840  NE  ARG A 140       6.230 -56.638  86.039  1.00227.99           N  
ANISOU  840  NE  ARG A 140    28923  29824  27879   2245  -5125   3501       N  
ATOM    841  CZ  ARG A 140       7.321 -56.496  86.785  1.00226.25           C  
ANISOU  841  CZ  ARG A 140    28787  29707  27472   2468  -5316   3128       C  
ATOM    842  NH1 ARG A 140       7.744 -57.508  87.530  1.00233.67           N  
ANISOU  842  NH1 ARG A 140    29943  30899  27942   3090  -5473   2601       N  
ATOM    843  NH2 ARG A 140       8.023 -55.371  86.742  1.00218.99           N  
ANISOU  843  NH2 ARG A 140    27620  29054  26530   2513  -5062   3169       N  
ATOM    844  N   GLN A 141       0.647 -55.908  82.690  1.00257.97           N  
ANISOU  844  N   GLN A 141    32875  33382  31760   2650  -3695   4132       N  
ATOM    845  CA  GLN A 141      -0.672 -55.704  83.277  1.00257.24           C  
ANISOU  845  CA  GLN A 141    32687  33472  31581   2493  -3552   4230       C  
ATOM    846  C   GLN A 141      -0.667 -55.696  84.800  1.00285.45           C  
ANISOU  846  C   GLN A 141    35866  37702  34888   2290  -3502   4353       C  
ATOM    847  O   GLN A 141      -1.350 -54.834  85.384  1.00286.92           O  
ANISOU  847  O   GLN A 141    37714  36488  34814   2537  -4425   2974       O  
ATOM    848  CB  GLN A 141      -1.635 -56.780  82.746  1.00238.81           C  
ANISOU  848  CB  GLN A 141    30522  31140  29075   2865  -3424   4274       C  
ATOM    849  CG  GLN A 141      -2.157 -56.514  81.345  1.00224.06           C  
ANISOU  849  CG  GLN A 141    28996  28684  27455   2942  -3387   4181       C  
ATOM    850  CD  GLN A 141      -3.224 -55.439  81.332  1.00212.07           C  
ANISOU  850  CD  GLN A 141    27533  27029  26016   2805  -3190   4125       C  
ATOM    851  OE1 GLN A 141      -2.951 -54.270  81.608  1.00204.18           O  
ANISOU  851  OE1 GLN A 141    26483  25996  25101   2635  -3151   4026       O  
ATOM    852  NE2 GLN A 141      -4.455 -55.833  81.030  1.00211.76           N  
ANISOU  852  NE2 GLN A 141    27653  26862  25946   2885  -3127   4149       N  
ATOM    853  N   PRO A 142       0.059 -56.582  85.504  1.00270.40           N  
ANISOU  853  N   PRO A 142    34832  35959  31951   3637  -3595   3280       N  
ATOM    854  CA  PRO A 142       0.143 -56.415  86.958  1.00270.01           C  
ANISOU  854  CA  PRO A 142    35091  35559  31940   3227  -4374   2978       C  
ATOM    855  C   PRO A 142       1.027 -55.240  87.338  1.00262.60           C  
ANISOU  855  C   PRO A 142    34126  34407  31242   2800  -4605   2900       C  
ATOM    856  O   PRO A 142       2.193 -55.420  87.703  1.00266.00           O  
ANISOU  856  O   PRO A 142    34392  35005  31672   2778  -4752   2884       O  
ATOM    857  CB  PRO A 142       0.734 -57.748  87.435  1.00272.78           C  
ANISOU  857  CB  PRO A 142    35129  36338  32177   3280  -4542   3204       C  
ATOM    858  CG  PRO A 142       1.506 -58.248  86.279  1.00272.84           C  
ANISOU  858  CG  PRO A 142    34936  36511  32219   3590  -4168   3369       C  
ATOM    859  CD  PRO A 142       0.714 -57.831  85.069  1.00272.04           C  
ANISOU  859  CD  PRO A 142    34507  36435  32421   3401  -3633   3888       C  
ATOM    860  N   GLU A 143       0.484 -54.026  87.258  1.00269.83           N  
ANISOU  860  N   GLU A 143    35000  35227  32295   2529  -4473   2974       N  
ATOM    861  CA  GLU A 143       1.226 -52.848  87.699  1.00256.39           C  
ANISOU  861  CA  GLU A 143    33007  33831  30579   2373  -4381   3008       C  
ATOM    862  C   GLU A 143       0.196 -51.797  88.101  1.00250.62           C  
ANISOU  862  C   GLU A 143    32212  33285  29726   2284  -4200   3000       C  
ATOM    863  O   GLU A 143      -0.426 -51.171  87.238  1.00250.37           O  
ANISOU  863  O   GLU A 143    32286  32933  29911   2259  -4004   3045       O  
ATOM    864  CB  GLU A 143       2.143 -52.341  86.593  1.00247.22           C  
ANISOU  864  CB  GLU A 143    31740  32455  29736   2354  -4226   3131       C  
ATOM    865  CG  GLU A 143       2.967 -51.116  86.957  1.00238.12           C  
ANISOU  865  CG  GLU A 143    30348  31652  28476   2412  -4074   3053       C  
ATOM    866  CD  GLU A 143       4.061 -51.425  87.962  1.00236.66           C  
ANISOU  866  CD  GLU A 143    29971  31845  28104   2385  -4278   2957       C  
ATOM    867  OE1 GLU A 143       3.741 -51.744  89.124  1.00237.82           O  
ANISOU  867  OE1 GLU A 143    30025  32342  27995   2270  -4405   2886       O  
ATOM    868  OE2 GLU A 143       5.250 -51.348  87.585  1.00236.74           O  
ANISOU  868  OE2 GLU A 143    29855  31861  28234   2474  -4239   2960       O  
ATOM    869  N   HIS A 144       0.021 -51.614  89.411  1.00251.45           N  
ANISOU  869  N   HIS A 144    32055  33957  29527   2159  -4240   2970       N  
ATOM    870  CA  HIS A 144      -0.923 -50.626  89.917  1.00249.94           C  
ANISOU  870  CA  HIS A 144    31710  34032  29225   1996  -4028   2926       C  
ATOM    871  C   HIS A 144      -0.350 -49.787  91.057  1.00253.17           C  
ANISOU  871  C   HIS A 144    31586  35235  29372   1756  -3876   2867       C  
ATOM    872  O   HIS A 144      -1.115 -49.093  91.737  1.00258.10           O  
ANISOU  872  O   HIS A 144    31871  36422  29774   1561  -3694   2891       O  
ATOM    873  CB  HIS A 144      -2.233 -51.298  90.354  1.00253.19           C  
ANISOU  873  CB  HIS A 144    32163  34514  29526   1932  -4084   3031       C  
ATOM    874  CG  HIS A 144      -3.218 -51.484  89.238  1.00252.33           C  
ANISOU  874  CG  HIS A 144    32461  33809  29602   2144  -4063   3071       C  
ATOM    875  ND1 HIS A 144      -2.836 -51.735  87.938  1.00254.16           N  
ANISOU  875  ND1 HIS A 144    32978  33458  30131   2285  -4015   3030       N  
ATOM    876  CD2 HIS A 144      -4.572 -51.465  89.233  1.00254.25           C  
ANISOU  876  CD2 HIS A 144    32791  33982  29831   2133  -3985   3123       C  
ATOM    877  CE1 HIS A 144      -3.911 -51.858  87.179  1.00250.17           C  
ANISOU  877  CE1 HIS A 144    32731  32552  29771   2342  -3908   3019       C  
ATOM    878  NE2 HIS A 144      -4.978 -51.697  87.941  1.00251.94           N  
ANISOU  878  NE2 HIS A 144    32856  33074  29794   2312  -3867   3072       N  
ATOM    879  N   LYS A 145       0.961 -49.831  91.301  1.00264.37           N  
ANISOU  879  N   LYS A 145    32772  36942  30735   1745  -3901   2859       N  
ATOM    880  CA  LYS A 145       1.531 -49.097  92.429  1.00242.88           C  
ANISOU  880  CA  LYS A 145    29419  35190  27675   1469  -3725   2837       C  
ATOM    881  C   LYS A 145       1.484 -47.587  92.206  1.00238.07           C  
ANISOU  881  C   LYS A 145    28427  35147  26881   1569  -3347   2748       C  
ATOM    882  O   LYS A 145       1.032 -46.837  93.080  1.00241.41           O  
ANISOU  882  O   LYS A 145    28416  36312  26996   1293  -3183   2615       O  
ATOM    883  CB  LYS A 145       2.958 -49.583  92.692  1.00228.95           C  
ANISOU  883  CB  LYS A 145    27552  33506  25934   1449  -3873   2820       C  
ATOM    884  CG  LYS A 145       3.808 -49.749  91.438  1.00211.68           C  
ANISOU  884  CG  LYS A 145    25650  30756  24022   1829  -3910   2835       C  
ATOM    885  CD  LYS A 145       4.844 -48.656  91.257  1.00192.38           C  
ANISOU  885  CD  LYS A 145    22791  28853  21453   1981  -3606   2793       C  
ATOM    886  CE  LYS A 145       5.586 -48.831  89.940  1.00162.12           C  
ANISOU  886  CE  LYS A 145    19238  24450  17910   2378  -3586   2829       C  
ATOM    887  NZ  LYS A 145       6.573 -47.742  89.721  1.00148.55           N  
ANISOU  887  NZ  LYS A 145    17135  23241  16066   2643  -3254   2743       N  
ATOM    888  N   VAL A 146       1.944 -47.123  91.048  1.00230.64           N  
ANISOU  888  N   VAL A 146    27634  33879  26119   1977  -3200   2749       N  
ATOM    889  CA  VAL A 146       1.814 -45.720  90.670  1.00224.06           C  
ANISOU  889  CA  VAL A 146    26519  33447  25167   2221  -2860   2597       C  
ATOM    890  C   VAL A 146       0.637 -45.588  89.715  1.00221.23           C  
ANISOU  890  C   VAL A 146    26572  32430  25057   2448  -2794   2689       C  
ATOM    891  O   VAL A 146      -0.028 -44.546  89.672  1.00215.27           O  
ANISOU  891  O   VAL A 146    25606  31986  24201   2557  -2590   2556       O  
ATOM    892  CB  VAL A 146       3.109 -45.160  90.050  1.00214.72           C  
ANISOU  892  CB  VAL A 146    25202  32348  24035   2585  -2691   2506       C  
ATOM    893  CG1 VAL A 146       4.242 -45.189  91.064  1.00208.45           C  
ANISOU  893  CG1 VAL A 146    23961  32231  23008   2304  -2752   2391       C  
ATOM    894  CG2 VAL A 146       3.489 -45.945  88.805  1.00212.12           C  
ANISOU  894  CG2 VAL A 146    25426  31076  24094   2890  -2763   2681       C  
ATOM    895  N   LEU A 147       0.369 -46.649  88.947  1.00220.08           N  
ANISOU  895  N   LEU A 147    23353  29983  30284   4951   -412   2622       N  
ATOM    896  CA  LEU A 147      -0.671 -46.587  87.923  1.00227.53           C  
ANISOU  896  CA  LEU A 147    24528  30606  31318   5045   -702   2665       C  
ATOM    897  C   LEU A 147      -2.042 -46.339  88.535  1.00237.61           C  
ANISOU  897  C   LEU A 147    25955  31769  32558   5031   -914   2799       C  
ATOM    898  O   LEU A 147      -2.819 -45.530  88.016  1.00238.86           O  
ANISOU  898  O   LEU A 147    26419  31718  32618   5042  -1171   2793       O  
ATOM    899  CB  LEU A 147      -0.682 -47.877  87.102  1.00223.09           C  
ANISOU  899  CB  LEU A 147    23870  29837  31055   5090   -732   2610       C  
ATOM    900  CG  LEU A 147       0.101 -47.887  85.788  1.00218.38           C  
ANISOU  900  CG  LEU A 147    23271  29252  30452   5255   -583   2668       C  
ATOM    901  CD1 LEU A 147      -0.610 -47.051  84.737  1.00216.28           C  
ANISOU  901  CD1 LEU A 147    23339  28771  30068   5391   -820   2764       C  
ATOM    902  CD2 LEU A 147       1.517 -47.382  86.001  1.00219.32           C  
ANISOU  902  CD2 LEU A 147    23231  29775  30325   5265   -199   2701       C  
ATOM    903  N   GLN A 148      -2.364 -47.033  89.629  1.00235.82           N  
ANISOU  903  N   GLN A 148    25501  31729  32372   5032   -745   3035       N  
ATOM    904  CA  GLN A 148      -3.639 -46.790  90.297  1.00239.28           C  
ANISOU  904  CA  GLN A 148    26023  32165  32729   5061   -833   3290       C  
ATOM    905  C   GLN A 148      -3.696 -45.368  90.841  1.00241.88           C  
ANISOU  905  C   GLN A 148    26530  32651  32721   5083   -840   3299       C  
ATOM    906  O   GLN A 148      -4.723 -44.689  90.724  1.00238.93           O  
ANISOU  906  O   GLN A 148    26401  32147  32233   5102  -1022   3384       O  
ATOM    907  CB  GLN A 148      -3.847 -47.808  91.421  1.00241.77           C  
ANISOU  907  CB  GLN A 148    26034  32681  33148   5061   -609   3576       C  
ATOM    908  CG  GLN A 148      -5.171 -47.700  92.164  1.00244.66           C  
ANISOU  908  CG  GLN A 148    26432  33076  33453   5097   -647   3889       C  
ATOM    909  CD  GLN A 148      -6.208 -48.678  91.645  1.00246.19           C  
ANISOU  909  CD  GLN A 148    26602  32995  33944   5077   -805   4037       C  
ATOM    910  OE1 GLN A 148      -6.019 -49.308  90.607  1.00245.30           O  
ANISOU  910  OE1 GLN A 148    26515  32632  34055   5061   -949   3860       O  
ATOM    911  NE2 GLN A 148      -7.309 -48.818  92.376  1.00248.44           N  
ANISOU  911  NE2 GLN A 148    26832  33336  34227   5088   -775   4372       N  
ATOM    912  N   GLN A 149      -2.595 -44.899  91.436  1.00234.83           N  
ANISOU  912  N   GLN A 149    25527  32042  31655   5078   -642   3216       N  
ATOM    913  CA  GLN A 149      -2.539 -43.530  91.942  1.00231.95           C  
ANISOU  913  CA  GLN A 149    25330  31830  30972   5116   -668   3190       C  
ATOM    914  C   GLN A 149      -2.704 -42.513  90.818  1.00224.84           C  
ANISOU  914  C   GLN A 149    24762  30659  30007   5088   -934   3018       C  
ATOM    915  O   GLN A 149      -3.333 -41.465  91.007  1.00228.86           O  
ANISOU  915  O   GLN A 149    25512  31148  30297   5117  -1059   3068       O  
ATOM    916  CB  GLN A 149      -1.229 -43.306  92.694  1.00235.18           C  
ANISOU  916  CB  GLN A 149    25551  32580  31228   5107   -429   3115       C  
ATOM    917  CG  GLN A 149      -1.047 -44.228  93.895  1.00240.77           C  
ANISOU  917  CG  GLN A 149    25972  33573  31937   5126   -162   3330       C  
ATOM    918  CD  GLN A 149      -2.189 -44.124  94.893  1.00243.63           C  
ANISOU  918  CD  GLN A 149    26358  34043  32166   5229   -161   3597       C  
ATOM    919  OE1 GLN A 149      -3.090 -44.964  94.914  1.00245.18           O  
ANISOU  919  OE1 GLN A 149    26489  34126  32544   5233   -173   3801       O  
ATOM    920  NE2 GLN A 149      -2.155 -43.090  95.727  1.00245.17           N  
ANISOU  920  NE2 GLN A 149    26644  34468  32043   5321   -141   3601       N  
ATOM    921  N   LEU A 150      -2.139 -42.798  89.643  1.00224.27           N  
ANISOU  921  N   LEU A 150    24721  30381  30109   5035  -1012   2832       N  
ATOM    922  CA  LEU A 150      -2.247 -41.866  88.526  1.00218.57           C  
ANISOU  922  CA  LEU A 150    24258  29618  29172   5148  -1102   2928       C  
ATOM    923  C   LEU A 150      -3.663 -41.849  87.960  1.00239.26           C  
ANISOU  923  C   LEU A 150    27180  31852  31874   5091  -1403   2983       C  
ATOM    924  O   LEU A 150      -4.243 -40.777  87.750  1.00240.93           O  
ANISOU  924  O   LEU A 150    27693  32005  31845   5094  -1531   3061       O  
ATOM    925  CB  LEU A 150      -1.228 -42.235  87.448  1.00205.41           C  
ANISOU  925  CB  LEU A 150    22470  28058  27516   5268   -929   2938       C  
ATOM    926  CG  LEU A 150       0.235 -42.027  87.848  1.00200.21           C  
ANISOU  926  CG  LEU A 150    21561  27823  26686   5317   -620   2904       C  
ATOM    927  CD1 LEU A 150       1.126 -41.997  86.631  1.00200.44           C  
ANISOU  927  CD1 LEU A 150    21575  27977  26604   5474   -470   2930       C  
ATOM    928  CD2 LEU A 150       0.395 -40.738  88.646  1.00197.03           C  
ANISOU  928  CD2 LEU A 150    21253  27667  25942   5346   -635   2908       C  
ATOM    929  N   ARG A 151      -4.233 -43.030  87.698  1.00226.05           N  
ANISOU  929  N   ARG A 151    25452  29919  30516   5032  -1526   2933       N  
ATOM    930  CA  ARG A 151      -5.595 -43.097  87.179  1.00241.49           C  
ANISOU  930  CA  ARG A 151    27685  31553  32518   4990  -1797   3015       C  
ATOM    931  C   ARG A 151      -6.612 -42.576  88.187  1.00257.93           C  
ANISOU  931  C   ARG A 151    29818  33779  34406   5003  -1749   3259       C  
ATOM    932  O   ARG A 151      -7.696 -42.143  87.785  1.00257.60           O  
ANISOU  932  O   ARG A 151    30063  33542  34273   4961  -1922   3368       O  
ATOM    933  CB  ARG A 151      -5.926 -44.528  86.729  1.00242.85           C  
ANISOU  933  CB  ARG A 151    27726  31555  32993   5024  -1858   3019       C  
ATOM    934  CG  ARG A 151      -5.942 -45.587  87.816  1.00242.64           C  
ANISOU  934  CG  ARG A 151    27311  31766  33114   5061  -1624   3184       C  
ATOM    935  CD  ARG A 151      -6.309 -46.960  87.247  1.00238.84           C  
ANISOU  935  CD  ARG A 151    26732  31081  32934   5090  -1720   3193       C  
ATOM    936  NE  ARG A 151      -7.304 -46.894  86.181  1.00235.10           N  
ANISOU  936  NE  ARG A 151    26607  30255  32464   5095  -2039   3183       N  
ATOM    937  CZ  ARG A 151      -7.467 -47.833  85.253  1.00230.02           C  
ANISOU  937  CZ  ARG A 151    26022  29368  32007   5156  -2206   3086       C  
ATOM    938  NH1 ARG A 151      -8.399 -47.690  84.320  1.00227.51           N  
ANISOU  938  NH1 ARG A 151    26072  28755  31615   5169  -2480   3098       N  
ATOM    939  NH2 ARG A 151      -6.690 -48.909  85.250  1.00227.59           N  
ANISOU  939  NH2 ARG A 151    25426  29121  31925   5210  -2080   2985       N  
ATOM    940  N   SER A 152      -6.282 -42.609  89.482  1.00258.14           N  
ANISOU  940  N   SER A 152    29581  34153  34347   5063  -1499   3355       N  
ATOM    941  CA  SER A 152      -7.133 -41.980  90.489  1.00255.87           C  
ANISOU  941  CA  SER A 152    29347  34042  33829   5113  -1428   3570       C  
ATOM    942  C   SER A 152      -7.054 -40.462  90.395  1.00250.21           C  
ANISOU  942  C   SER A 152    28934  33331  32805   5103  -1514   3481       C  
ATOM    943  O   SER A 152      -8.079 -39.770  90.441  1.00251.52           O  
ANISOU  943  O   SER A 152    29341  33430  32797   5098  -1593   3611       O  
ATOM    944  CB  SER A 152      -6.737 -42.445  91.892  1.00257.83           C  
ANISOU  944  CB  SER A 152    29252  34668  34043   5197  -1140   3700       C  
ATOM    945  OG  SER A 152      -5.425 -42.026  92.226  1.00256.57           O  
ANISOU  945  OG  SER A 152    28993  34723  33768   5213  -1016   3516       O  
ATOM    946  N   ARG A 153      -5.841 -39.926  90.269  1.00275.32           N  
ANISOU  946  N   ARG A 153    32097  36599  35912   5093  -1488   3274       N  
ATOM    947  CA  ARG A 153      -5.664 -38.484  90.163  1.00256.01           C  
ANISOU  947  CA  ARG A 153    29931  34154  33188   5073  -1586   3193       C  
ATOM    948  C   ARG A 153      -6.029 -37.979  88.773  1.00273.05           C  
ANISOU  948  C   ARG A 153    32438  35999  35310   4976  -1800   3182       C  
ATOM    949  O   ARG A 153      -6.427 -36.818  88.624  1.00277.90           O  
ANISOU  949  O   ARG A 153    33351  36600  35638   4968  -1868   3241       O  
ATOM    950  CB  ARG A 153      -4.225 -38.110  90.523  1.00229.75           C  
ANISOU  950  CB  ARG A 153    26435  31082  29777   5115  -1464   3031       C  
ATOM    951  CG  ARG A 153      -3.926 -38.236  92.010  1.00212.51           C  
ANISOU  951  CG  ARG A 153    23994  29256  27494   5220  -1251   3073       C  
ATOM    952  CD  ARG A 153      -2.650 -37.509  92.392  1.00197.71           C  
ANISOU  952  CD  ARG A 153    22045  27604  25471   5239  -1197   2905       C  
ATOM    953  NE  ARG A 153      -2.103 -38.003  93.652  1.00185.29           N  
ANISOU  953  NE  ARG A 153    20161  26388  23854   5323   -952   2941       N  
ATOM    954  CZ  ARG A 153      -1.243 -39.012  93.753  1.00174.29           C  
ANISOU  954  CZ  ARG A 153    18462  25126  22635   5277   -756   2917       C  
ATOM    955  NH1 ARG A 153      -0.831 -39.654  92.668  1.00171.56           N  
ANISOU  955  NH1 ARG A 153    18064  24580  22539   5170   -774   2824       N  
ATOM    956  NH2 ARG A 153      -0.802 -39.389  94.945  1.00170.06           N  
ANISOU  956  NH2 ARG A 153    17686  24928  22001   5341   -532   2994       N  
ATOM    957  N   GLY A 154      -5.895 -38.823  87.754  1.00250.57           N  
ANISOU  957  N   GLY A 154    29540  33013  32651   4989  -1819   3196       N  
ATOM    958  CA  GLY A 154      -6.287 -38.439  86.413  1.00248.33           C  
ANISOU  958  CA  GLY A 154    29571  32538  32247   4987  -1933   3293       C  
ATOM    959  C   GLY A 154      -5.246 -37.661  85.648  1.00242.97           C  
ANISOU  959  C   GLY A 154    28984  32094  31240   5164  -1805   3305       C  
ATOM    960  O   GLY A 154      -5.594 -36.890  84.747  1.00244.97           O  
ANISOU  960  O   GLY A 154    29598  32241  31239   5158  -1887   3374       O  
ATOM    961  N   ASP A 155      -3.972 -37.845  85.972  1.00249.63           N  
ANISOU  961  N   ASP A 155    29529  33263  32057   5311  -1607   3224       N  
ATOM    962  CA  ASP A 155      -2.914 -37.102  85.316  1.00224.53           C  
ANISOU  962  CA  ASP A 155    26431  30349  28530   5499  -1510   3196       C  
ATOM    963  C   ASP A 155      -2.656 -37.663  83.923  1.00199.06           C  
ANISOU  963  C   ASP A 155    23282  26999  25351   5603  -1494   3213       C  
ATOM    964  O   ASP A 155      -3.260 -38.648  83.490  1.00199.27           O  
ANISOU  964  O   ASP A 155    23279  26732  25703   5533  -1561   3249       O  
ATOM    965  CB  ASP A 155      -1.640 -37.161  86.152  1.00222.24           C  
ANISOU  965  CB  ASP A 155    25773  30463  28207   5592  -1305   3103       C  
ATOM    966  CG  ASP A 155      -1.897 -36.909  87.619  1.00227.16           C  
ANISOU  966  CG  ASP A 155    26283  31173  28854   5502  -1306   3067       C  
ATOM    967  OD1 ASP A 155      -2.947 -36.318  87.943  1.00229.77           O  
ANISOU  967  OD1 ASP A 155    26875  31313  29114   5413  -1468   3107       O  
ATOM    968  OD2 ASP A 155      -1.056 -37.309  88.449  1.00229.23           O  
ANISOU  968  OD2 ASP A 155    26208  31691  29198   5511  -1131   2999       O  
ATOM    969  N   ASN A 156      -1.740 -37.019  83.213  1.00193.32           N  
ANISOU  969  N   ASN A 156    22716  26443  24294   5663  -1409   3099       N  
ATOM    970  CA  ASN A 156      -1.217 -37.513  81.952  1.00171.49           C  
ANISOU  970  CA  ASN A 156    20133  23469  21555   5393  -1275   2840       C  
ATOM    971  C   ASN A 156       0.217 -37.974  82.154  1.00152.51           C  
ANISOU  971  C   ASN A 156    17417  21339  19191   5344   -997   2682       C  
ATOM    972  O   ASN A 156       0.952 -37.425  82.980  1.00152.86           O  
ANISOU  972  O   ASN A 156    17285  21706  19088   5348   -906   2666       O  
ATOM    973  CB  ASN A 156      -1.275 -36.452  80.848  1.00174.71           C  
ANISOU  973  CB  ASN A 156    21099  23683  21598   5036  -1298   2605       C  
ATOM    974  CG  ASN A 156      -2.561 -36.512  80.052  1.00183.59           C  
ANISOU  974  CG  ASN A 156    22554  24443  22758   5004  -1487   2708       C  
ATOM    975  OD1 ASN A 156      -3.245 -37.533  80.046  1.00189.08           O  
ANISOU  975  OD1 ASN A 156    23094  24966  23782   5198  -1599   2900       O  
ATOM    976  ND2 ASN A 156      -2.887 -35.425  79.357  1.00183.55           N  
ANISOU  976  ND2 ASN A 156    22987  24318  22434   4748  -1524   2599       N  
ATOM    977  N   VAL A 157       0.616 -38.983  81.387  1.00142.13           N  
ANISOU  977  N   VAL A 157    16050  19893  18060   5300   -867   2577       N  
ATOM    978  CA  VAL A 157       1.950 -39.553  81.504  1.00140.46           C  
ANISOU  978  CA  VAL A 157    15549  19931  17888   5269   -571   2483       C  
ATOM    979  C   VAL A 157       2.601 -39.515  80.130  1.00138.65           C  
ANISOU  979  C   VAL A 157    15687  19541  17453   5005   -452   2217       C  
ATOM    980  O   VAL A 157       1.966 -39.842  79.120  1.00160.67           O  
ANISOU  980  O   VAL A 157    18766  21993  20288   4970   -569   2125       O  
ATOM    981  CB  VAL A 157       1.935 -40.990  82.071  1.00148.84           C  
ANISOU  981  CB  VAL A 157    16082  21060  19410   5562   -478   2670       C  
ATOM    982  CG1 VAL A 157       1.024 -41.079  83.277  1.00154.79           C  
ANISOU  982  CG1 VAL A 157    16471  21931  20410   5891   -655   2991       C  
ATOM    983  CG2 VAL A 157       1.561 -42.020  81.029  1.00151.40           C  
ANISOU  983  CG2 VAL A 157    16542  21014  19971   5573   -527   2595       C  
ATOM    984  N   TYR A 158       3.838 -39.042  80.089  1.00135.42           N  
ANISOU  984  N   TYR A 158    15275  19384  16796   4831   -243   2117       N  
ATOM    985  CA  TYR A 158       4.587 -38.890  78.856  1.00129.35           C  
ANISOU  985  CA  TYR A 158    14813  18542  15793   4625   -120   1925       C  
ATOM    986  C   TYR A 158       5.907 -39.620  79.025  1.00131.21           C  
ANISOU  986  C   TYR A 158    14752  19045  16057   4656    197   1972       C  
ATOM    987  O   TYR A 158       6.344 -39.896  80.143  1.00142.44           O  
ANISOU  987  O   TYR A 158    15758  20757  17606   4757    328   2129       O  
ATOM    988  CB  TYR A 158       4.824 -37.405  78.508  1.00129.00           C  
ANISOU  988  CB  TYR A 158    15088  18541  15383   4361   -194   1829       C  
ATOM    989  CG  TYR A 158       3.562 -36.562  78.401  1.00127.37           C  
ANISOU  989  CG  TYR A 158    15177  18108  15108   4310   -464   1811       C  
ATOM    990  CD1 TYR A 158       2.818 -36.232  79.528  1.00133.73           C  
ANISOU  990  CD1 TYR A 158    15850  18969  15993   4443   -622   1965       C  
ATOM    991  CD2 TYR A 158       3.132 -36.076  77.171  1.00123.48           C  
ANISOU  991  CD2 TYR A 158    15087  17380  14451   4149   -542   1667       C  
ATOM    992  CE1 TYR A 158       1.675 -35.463  79.431  1.00136.53           C  
ANISOU  992  CE1 TYR A 158    16495  19129  16253   4410   -844   1998       C  
ATOM    993  CE2 TYR A 158       1.985 -35.304  77.064  1.00130.08           C  
ANISOU  993  CE2 TYR A 158    16187  18029  15210   4085   -747   1686       C  
ATOM    994  CZ  TYR A 158       1.262 -35.001  78.200  1.00135.51           C  
ANISOU  994  CZ  TYR A 158    16765  18756  15964   4211   -894   1863       C  
ATOM    995  OH  TYR A 158       0.121 -34.235  78.118  1.00140.52           O  
ANISOU  995  OH  TYR A 158    17680  19218  16494   4165  -1078   1932       O  
ATOM    996  N   VAL A 159       6.541 -39.941  77.903  1.00122.76           N  
ANISOU  996  N   VAL A 159    13891  17900  14852   4592    333   1857       N  
ATOM    997  CA  VAL A 159       7.832 -40.616  77.898  1.00126.01           C  
ANISOU  997  CA  VAL A 159    14089  18559  15231   4623    657   1937       C  
ATOM    998  C   VAL A 159       8.829 -39.725  77.174  1.00172.60           C  
ANISOU  998  C   VAL A 159    20233  24599  20748   4418    746   1917       C  
ATOM    999  O   VAL A 159       8.527 -39.197  76.096  1.00196.74           O  
ANISOU  999  O   VAL A 159    23664  27460  23627   4338    614   1771       O  
ATOM   1000  CB  VAL A 159       7.748 -41.999  77.229  1.00113.86           C  
ANISOU 1000  CB  VAL A 159    12548  16816  13896   4816    752   1875       C  
ATOM   1001  CG1 VAL A 159       8.896 -42.880  77.685  1.00118.62           C  
ANISOU 1001  CG1 VAL A 159    12789  17714  14567   4907   1116   2039       C  
ATOM   1002  CG2 VAL A 159       6.410 -42.655  77.527  1.00112.29           C  
ANISOU 1002  CG2 VAL A 159    12257  16327  14081   4988    516   1866       C  
ATOM   1003  N   VAL A 160      10.013 -39.560  77.763  1.00112.73           N  
ANISOU 1003  N   VAL A 160    12409  17372  13052   4340    969   2099       N  
ATOM   1004  CA  VAL A 160      11.069 -38.797  77.110  1.00176.91           C  
ANISOU 1004  CA  VAL A 160    20709  25657  20852   4168   1054   2171       C  
ATOM   1005  C   VAL A 160      11.619 -39.598  75.936  1.00186.67           C  
ANISOU 1005  C   VAL A 160    22106  26839  21982   4299   1240   2166       C  
ATOM   1006  O   VAL A 160      12.051 -40.749  76.093  1.00116.08           O  
ANISOU 1006  O   VAL A 160    12970  17978  13156   4462   1485   2255       O  
ATOM   1007  CB  VAL A 160      12.173 -38.432  78.113  1.00157.64           C  
ANISOU 1007  CB  VAL A 160    17957  23607  18332   4043   1219   2414       C  
ATOM   1008  CG1 VAL A 160      13.397 -37.903  77.383  1.00115.32           C  
ANISOU 1008  CG1 VAL A 160    12724  18421  12672   3906   1336   2587       C  
ATOM   1009  CG2 VAL A 160      11.667 -37.390  79.104  1.00140.75           C  
ANISOU 1009  CG2 VAL A 160    15756  21506  16218   3918    974   2377       C  
ATOM   1010  N   THR A 161      11.595 -38.991  74.747  1.00165.46           N  
ANISOU 1010  N   THR A 161    19767  24028  19071   4253   1129   2068       N  
ATOM   1011  CA  THR A 161      12.057 -39.624  73.520  1.00183.47           C  
ANISOU 1011  CA  THR A 161    22249  26263  21197   4428   1263   2048       C  
ATOM   1012  C   THR A 161      13.338 -39.011  72.964  1.00188.29           C  
ANISOU 1012  C   THR A 161    22898  27156  21487   4373   1404   2296       C  
ATOM   1013  O   THR A 161      13.935 -39.592  72.052  1.00199.88           O  
ANISOU 1013  O   THR A 161    24490  28668  22786   4573   1563   2361       O  
ATOM   1014  CB  THR A 161      10.955 -39.569  72.446  1.00200.59           C  
ANISOU 1014  CB  THR A 161    24770  28079  23368   4501   1026   1752       C  
ATOM   1015  OG1 THR A 161      11.487 -39.955  71.171  1.00211.11           O  
ANISOU 1015  OG1 THR A 161    26321  29412  24478   4690   1129   1728       O  
ATOM   1016  CG2 THR A 161      10.364 -38.168  72.342  1.00203.63           C  
ANISOU 1016  CG2 THR A 161    25299  28405  23667   4275    783   1680       C  
ATOM   1017  N   GLU A 162      13.777 -37.864  73.477  1.00183.32           N  
ANISOU 1017  N   GLU A 162    22167  26715  20772   4133   1330   2459       N  
ATOM   1018  CA  GLU A 162      15.007 -37.240  73.006  1.00181.74           C  
ANISOU 1018  CA  GLU A 162    21958  26783  20310   4073   1426   2769       C  
ATOM   1019  C   GLU A 162      15.536 -36.338  74.110  1.00181.56           C  
ANISOU 1019  C   GLU A 162    21703  26972  20307   3798   1369   2974       C  
ATOM   1020  O   GLU A 162      14.756 -35.707  74.827  1.00186.72           O  
ANISOU 1020  O   GLU A 162    22338  27507  21101   3643   1149   2796       O  
ATOM   1021  CB  GLU A 162      14.769 -36.450  71.711  1.00188.92           C  
ANISOU 1021  CB  GLU A 162    23137  27590  21055   4096   1253   2685       C  
ATOM   1022  CG  GLU A 162      16.025 -35.866  71.074  1.00188.86           C  
ANISOU 1022  CG  GLU A 162    23092  27868  20798   4105   1336   3065       C  
ATOM   1023  CD  GLU A 162      15.806 -35.451  69.629  1.00183.24           C  
ANISOU 1023  CD  GLU A 162    22600  27092  19930   4261   1236   2992       C  
ATOM   1024  OE1 GLU A 162      14.949 -36.062  68.956  1.00178.17           O  
ANISOU 1024  OE1 GLU A 162    22169  26220  19308   4448   1205   2672       O  
ATOM   1025  OE2 GLU A 162      16.488 -34.514  69.165  1.00182.26           O  
ANISOU 1025  OE2 GLU A 162    22413  27157  19679   4205   1178   3270       O  
ATOM   1026  N   VAL A 163      16.858 -36.284  74.246  1.00192.64           N  
ANISOU 1026  N   VAL A 163    22945  28690  21559   3753   1557   3365       N  
ATOM   1027  CA  VAL A 163      17.487 -35.517  75.312  1.00177.20           C  
ANISOU 1027  CA  VAL A 163    20759  26949  19618   3491   1504   3586       C  
ATOM   1028  C   VAL A 163      18.554 -34.605  74.723  1.00177.85           C  
ANISOU 1028  C   VAL A 163    20857  27216  19501   3376   1450   3957       C  
ATOM   1029  O   VAL A 163      19.134 -34.885  73.669  1.00177.66           O  
ANISOU 1029  O   VAL A 163    20930  27276  19297   3558   1583   4168       O  
ATOM   1030  CB  VAL A 163      18.095 -36.437  76.395  1.00160.71           C  
ANISOU 1030  CB  VAL A 163    18352  25111  17598   3512   1805   3778       C  
ATOM   1031  CG1 VAL A 163      19.328 -37.130  75.870  1.00146.13           C  
ANISOU 1031  CG1 VAL A 163    16453  23522  15549   3638   2147   4182       C  
ATOM   1032  CG2 VAL A 163      18.407 -35.660  77.660  1.00158.11           C  
ANISOU 1032  CG2 VAL A 163    17790  24957  17327   3254   1689   3883       C  
ATOM   1033  N   LEU A 164      18.799 -33.495  75.415  1.00164.52           N  
ANISOU 1033  N   LEU A 164    19066  25590  17853   3098   1228   4050       N  
ATOM   1034  CA  LEU A 164      19.829 -32.526  75.060  1.00172.66           C  
ANISOU 1034  CA  LEU A 164    20048  26791  18766   2944   1116   4452       C  
ATOM   1035  C   LEU A 164      20.768 -32.405  76.252  1.00197.06           C  
ANISOU 1035  C   LEU A 164    22869  30140  21862   2735   1174   4763       C  
ATOM   1036  O   LEU A 164      20.376 -31.892  77.305  1.00204.78           O  
ANISOU 1036  O   LEU A 164    23771  31066  22972   2547    983   4568       O  
ATOM   1037  CB  LEU A 164      19.219 -31.170  74.702  1.00165.85           C  
ANISOU 1037  CB  LEU A 164    19320  25718  17978   2778    734   4268       C  
ATOM   1038  CG  LEU A 164      20.010 -30.226  73.786  1.00173.61           C  
ANISOU 1038  CG  LEU A 164    20283  26802  18878   2724    595   4641       C  
ATOM   1039  CD1 LEU A 164      19.129 -29.073  73.338  1.00180.50           C  
ANISOU 1039  CD1 LEU A 164    21289  27430  19864   2606    271   4365       C  
ATOM   1040  CD2 LEU A 164      21.273 -29.690  74.455  1.00173.50           C  
ANISOU 1040  CD2 LEU A 164    20040  27032  18852   2501    534   5126       C  
ATOM   1041  N   GLN A 165      21.999 -32.870  76.083  1.00206.61           N  
ANISOU 1041  N   GLN A 165    23945  31643  22913   2782   1436   5263       N  
ATOM   1042  CA  GLN A 165      23.010 -32.880  77.128  1.00203.81           C  
ANISOU 1042  CA  GLN A 165    23322  31583  22533   2588   1552   5637       C  
ATOM   1043  C   GLN A 165      24.254 -32.158  76.622  1.00215.36           C  
ANISOU 1043  C   GLN A 165    24729  33241  23855   2474   1472   6240       C  
ATOM   1044  O   GLN A 165      24.272 -31.591  75.529  1.00221.65           O  
ANISOU 1044  O   GLN A 165    25662  33950  24604   2558   1308   6342       O  
ATOM   1045  CB  GLN A 165      23.351 -34.312  77.553  1.00193.90           C  
ANISOU 1045  CB  GLN A 165    21904  30543  21226   2754   2021   5755       C  
ATOM   1046  CG  GLN A 165      24.159 -35.087  76.519  1.00194.97           C  
ANISOU 1046  CG  GLN A 165    22107  30842  21131   3003   2348   6161       C  
ATOM   1047  CD  GLN A 165      24.374 -36.535  76.908  1.00194.47           C  
ANISOU 1047  CD  GLN A 165    21900  30949  21040   3180   2820   6226       C  
ATOM   1048  OE1 GLN A 165      23.639 -37.084  77.728  1.00195.24           O  
ANISOU 1048  OE1 GLN A 165    21869  30974  21338   3187   2888   5864       O  
ATOM   1049  NE2 GLN A 165      25.391 -37.161  76.325  1.00194.39           N  
ANISOU 1049  NE2 GLN A 165    21892  31180  20789   3346   3153   6723       N  
ATOM   1050  N   THR A 166      25.298 -32.164  77.440  1.00209.80           N  
ANISOU 1050  N   THR A 166    23791  32823  23099   2288   1582   6675       N  
ATOM   1051  CA  THR A 166      26.568 -31.552  77.089  1.00220.47           C  
ANISOU 1051  CA  THR A 166    25049  34388  24331   2167   1510   7352       C  
ATOM   1052  C   THR A 166      27.671 -32.596  77.151  1.00244.90           C  
ANISOU 1052  C   THR A 166    27996  37851  27206   2278   1988   7917       C  
ATOM   1053  O   THR A 166      27.651 -33.483  78.011  1.00245.74           O  
ANISOU 1053  O   THR A 166    27959  38096  27315   2275   2306   7818       O  
ATOM   1054  CB  THR A 166      26.904 -30.378  78.016  1.00209.04           C  
ANISOU 1054  CB  THR A 166    23468  32935  23024   1781   1126   7443       C  
ATOM   1055  OG1 THR A 166      26.721 -30.776  79.381  1.00213.57           O  
ANISOU 1055  OG1 THR A 166    23885  33599  23662   1651   1237   7204       O  
ATOM   1056  CG2 THR A 166      26.013 -29.178  77.714  1.00194.00           C  
ANISOU 1056  CG2 THR A 166    21727  30678  21306   1681    638   7026       C  
ATOM   1057  N   GLN A 167      28.627 -32.496  76.230  1.00243.82           N  
ANISOU 1057  N   GLN A 167    27873  37890  26878   2401   2052   8543       N  
ATOM   1058  CA  GLN A 167      29.871 -33.250  76.336  1.00252.13           C  
ANISOU 1058  CA  GLN A 167    28770  38994  28035   2395   2312   8722       C  
ATOM   1059  C   GLN A 167      30.987 -32.342  76.827  1.00256.00           C  
ANISOU 1059  C   GLN A 167    29058  39503  28707   2045   2041   9040       C  
ATOM   1060  O   GLN A 167      32.124 -32.390  76.345  1.00265.81           O  
ANISOU 1060  O   GLN A 167    30226  40697  30074   2063   2042   9241       O  
ATOM   1061  CB  GLN A 167      30.232 -33.880  74.994  1.00257.06           C  
ANISOU 1061  CB  GLN A 167    29535  39522  28614   2760   2465   8745       C  
ATOM   1062  CG  GLN A 167      31.236 -35.027  75.075  1.00255.81           C  
ANISOU 1062  CG  GLN A 167    29291  39336  28570   2845   2752   8723       C  
ATOM   1063  CD  GLN A 167      31.488 -35.678  73.727  1.00249.95           C  
ANISOU 1063  CD  GLN A 167    28714  38521  27737   3246   2891   8735       C  
ATOM   1064  OE1 GLN A 167      30.563 -35.897  72.945  1.00249.42           O  
ANISOU 1064  OE1 GLN A 167    28861  38426  27481   3547   2948   8585       O  
ATOM   1065  NE2 GLN A 167      32.750 -35.983  73.445  1.00249.16           N  
ANISOU 1065  NE2 GLN A 167    28522  38397  27752   3270   2934   8906       N  
ATOM   1066  N   LYS A 168      30.663 -31.489  77.796  1.00277.19           N  
ANISOU 1066  N   LYS A 168    31657  42263  31398   1734   1785   9088       N  
ATOM   1067  CA  LYS A 168      31.639 -30.605  78.410  1.00254.20           C  
ANISOU 1067  CA  LYS A 168    28560  39371  28654   1375   1497   9380       C  
ATOM   1068  C   LYS A 168      31.119 -30.162  79.768  1.00246.73           C  
ANISOU 1068  C   LYS A 168    27526  38563  27658   1092   1345   9310       C  
ATOM   1069  O   LYS A 168      29.908 -30.091  79.996  1.00239.88           O  
ANISOU 1069  O   LYS A 168    26779  37598  26769   1156   1260   8856       O  
ATOM   1070  CB  LYS A 168      31.922 -29.389  77.525  1.00239.04           C  
ANISOU 1070  CB  LYS A 168    26678  37322  26823   1318   1079   9677       C  
ATOM   1071  CG  LYS A 168      33.185 -28.626  77.876  1.00227.74           C  
ANISOU 1071  CG  LYS A 168    25041  35870  25620   1004    829  10008       C  
ATOM   1072  CD  LYS A 168      34.422 -29.445  77.558  1.00215.92           C  
ANISOU 1072  CD  LYS A 168    23433  34381  24226   1124   1128  10076       C  
ATOM   1073  CE  LYS A 168      35.684 -28.783  78.090  1.00210.02           C  
ANISOU 1073  CE  LYS A 168    22468  33639  23690    808    907  10374       C  
ATOM   1074  NZ  LYS A 168      35.612 -28.556  79.561  1.00205.22           N  
ANISOU 1074  NZ  LYS A 168    21754  33140  23080    472    800  10346       N  
ATOM   1075  N   GLU A 169      32.051 -29.855  80.658  1.00242.44           N  
ANISOU 1075  N   GLU A 169    26776  38088  27252    791   1242   9479       N  
ATOM   1076  CA  GLU A 169      31.745 -29.322  81.981  1.00247.65           C  
ANISOU 1076  CA  GLU A 169    27327  38909  27859    503   1041   9465       C  
ATOM   1077  C   GLU A 169      31.997 -27.825  81.882  1.00251.57           C  
ANISOU 1077  C   GLU A 169    27871  39289  28426    227    422   9790       C  
ATOM   1078  O   GLU A 169      33.138 -27.374  81.993  1.00255.07           O  
ANISOU 1078  O   GLU A 169    28173  39685  29057      3    266  10070       O  
ATOM   1079  CB  GLU A 169      32.617 -29.976  83.049  1.00250.41           C  
ANISOU 1079  CB  GLU A 169    27415  39399  28331    372   1291   9413       C  
ATOM   1080  CG  GLU A 169      32.220 -29.648  84.478  1.00249.93           C  
ANISOU 1080  CG  GLU A 169    27202  39575  28185    145   1184   9331       C  
ATOM   1081  CD  GLU A 169      33.030 -30.427  85.495  1.00246.26           C  
ANISOU 1081  CD  GLU A 169    26466  39238  27865     90   1452   9211       C  
ATOM   1082  OE1 GLU A 169      33.181 -31.655  85.320  1.00244.19           O  
ANISOU 1082  OE1 GLU A 169    26183  38898  27701    350   1827   8958       O  
ATOM   1083  OE2 GLU A 169      33.527 -29.806  86.459  1.00244.99           O  
ANISOU 1083  OE2 GLU A 169    26146  39220  27717   -204   1224   9368       O  
ATOM   1084  N   VAL A 170      30.939 -27.051  81.672  1.00253.32           N  
ANISOU 1084  N   VAL A 170    28286  39123  28842    247     18   9170       N  
ATOM   1085  CA  VAL A 170      31.082 -25.625  81.414  1.00255.47           C  
ANISOU 1085  CA  VAL A 170    28609  39138  29320     24   -596   9275       C  
ATOM   1086  C   VAL A 170      30.852 -24.859  82.707  1.00272.74           C  
ANISOU 1086  C   VAL A 170    30779  41193  31657   -270  -1003   8885       C  
ATOM   1087  O   VAL A 170      29.916 -25.148  83.463  1.00259.35           O  
ANISOU 1087  O   VAL A 170    29148  39422  29969   -189   -940   8221       O  
ATOM   1088  CB  VAL A 170      30.119 -25.157  80.308  1.00233.65           C  
ANISOU 1088  CB  VAL A 170    26057  36044  26676    222   -788   8894       C  
ATOM   1089  CG1 VAL A 170      30.447 -25.856  78.999  1.00225.06           C  
ANISOU 1089  CG1 VAL A 170    24979  35113  25420    542   -427   9320       C  
ATOM   1090  CG2 VAL A 170      28.674 -25.429  80.697  1.00221.46           C  
ANISOU 1090  CG2 VAL A 170    24697  34273  25175    359   -740   8007       C  
ATOM   1091  N   GLU A 171      31.737 -23.907  82.976  1.00264.86           N  
ANISOU 1091  N   GLU A 171    29680  40180  30775   -586  -1430   9336       N  
ATOM   1092  CA  GLU A 171      31.657 -23.047  84.147  1.00272.68           C  
ANISOU 1092  CA  GLU A 171    30672  41025  31908   -874  -1902   9021       C  
ATOM   1093  C   GLU A 171      31.922 -21.629  83.663  1.00279.11           C  
ANISOU 1093  C   GLU A 171    31536  41523  32989  -1095  -2552   9233       C  
ATOM   1094  O   GLU A 171      33.024 -21.323  83.198  1.00282.06           O  
ANISOU 1094  O   GLU A 171    31752  42008  33410  -1241  -2676  10017       O  
ATOM   1095  CB  GLU A 171      32.650 -23.524  85.212  1.00277.49           C  
ANISOU 1095  CB  GLU A 171    31044  42012  32376  -1071  -1709   9422       C  
ATOM   1096  CG  GLU A 171      34.062 -23.712  84.688  1.00283.41           C  
ANISOU 1096  CG  GLU A 171    31605  43046  33032  -1193  -1556  10433       C  
ATOM   1097  CD  GLU A 171      34.645 -25.049  85.090  1.00282.76           C  
ANISOU 1097  CD  GLU A 171    31326  43366  32745  -1102   -859  10631       C  
ATOM   1098  OE1 GLU A 171      33.867 -25.920  85.530  1.00279.44           O  
ANISOU 1098  OE1 GLU A 171    30907  43111  32157   -897   -476  10229       O  
ATOM   1099  OE2 GLU A 171      35.871 -25.238  84.953  1.00284.29           O  
ANISOU 1099  OE2 GLU A 171    31345  43538  33135  -1188   -690  10830       O  
ATOM   1100  N   VAL A 172      30.910 -20.771  83.749  1.00293.51           N  
ANISOU 1100  N   VAL A 172    33562  42960  34998  -1105  -2962   8577       N  
ATOM   1101  CA  VAL A 172      31.020 -19.399  83.275  1.00260.33           C  
ANISOU 1101  CA  VAL A 172    29397  38423  31095  -1300  -3578   8701       C  
ATOM   1102  C   VAL A 172      30.279 -18.478  84.232  1.00256.77           C  
ANISOU 1102  C   VAL A 172    29132  37640  30790  -1449  -4079   8011       C  
ATOM   1103  O   VAL A 172      29.330 -18.883  84.911  1.00260.85           O  
ANISOU 1103  O   VAL A 172    29801  38134  31177  -1289  -3917   7342       O  
ATOM   1104  CB  VAL A 172      30.476 -19.229  81.836  1.00228.56           C  
ANISOU 1104  CB  VAL A 172    25436  34243  27164  -1074  -3516   8706       C  
ATOM   1105  CG1 VAL A 172      31.400 -19.895  80.819  1.00214.79           C  
ANISOU 1105  CG1 VAL A 172    23497  32816  25297   -919  -3152   9513       C  
ATOM   1106  CG2 VAL A 172      29.069 -19.788  81.732  1.00217.82           C  
ANISOU 1106  CG2 VAL A 172    24306  32771  25686   -789  -3212   7928       C  
ATOM   1107  N   THR A 173      30.724 -17.227  84.277  1.00251.45           N  
ANISOU 1107  N   THR A 173    28439  36707  30395  -1734  -4707   8205       N  
ATOM   1108  CA  THR A 173      30.099 -16.212  85.110  1.00249.11           C  
ANISOU 1108  CA  THR A 173    28344  36054  30252  -1876  -5256   7590       C  
ATOM   1109  C   THR A 173      28.695 -15.896  84.611  1.00242.76           C  
ANISOU 1109  C   THR A 173    27792  34947  29499  -1661  -5260   6925       C  
ATOM   1110  O   THR A 173      28.429 -15.958  83.411  1.00235.42           O  
ANISOU 1110  O   THR A 173    26835  33981  28633  -1520  -5074   7076       O  
ATOM   1111  CB  THR A 173      30.930 -14.919  85.133  1.00253.71           C  
ANISOU 1111  CB  THR A 173    28837  36388  31173  -2234  -5959   8000       C  
ATOM   1112  OG1 THR A 173      31.132 -14.459  83.792  1.00256.01           O  
ANISOU 1112  OG1 THR A 173    28997  36572  31702  -2218  -6044   8467       O  
ATOM   1113  CG2 THR A 173      32.280 -15.166  85.787  1.00253.36           C  
ANISOU 1113  CG2 THR A 173    28568  36626  31070  -2483  -6010   8644       C  
ATOM   1114  N   THR A 205      30.896 -18.044  90.458  1.00261.13           N  
ANISOU 1114  N   THR A 205    29621  38584  31011  -1964  -4910   6838       N  
ATOM   1115  CA  THR A 205      30.707 -18.920  89.308  1.00254.64           C  
ANISOU 1115  CA  THR A 205    28742  37885  30125  -1762  -4337   7087       C  
ATOM   1116  C   THR A 205      29.967 -20.192  89.713  1.00256.55           C  
ANISOU 1116  C   THR A 205    28918  38428  30133  -1407  -3707   6711       C  
ATOM   1117  O   THR A 205      29.835 -20.494  90.899  1.00252.13           O  
ANISOU 1117  O   THR A 205    28265  38082  29453  -1334  -3647   6415       O  
ATOM   1118  CB  THR A 205      32.050 -19.296  88.656  1.00252.13           C  
ANISOU 1118  CB  THR A 205    28172  37832  29795  -1956  -4112   8028       C  
ATOM   1119  OG1 THR A 205      31.811 -20.087  87.486  1.00249.96           O  
ANISOU 1119  OG1 THR A 205    27883  37647  29444  -1709  -3600   8223       O  
ATOM   1120  CG2 THR A 205      32.913 -20.085  89.629  1.00252.15           C  
ANISOU 1120  CG2 THR A 205    27905  38308  29591  -2057  -3779   8363       C  
ATOM   1121  N   VAL A 206      29.487 -20.932  88.719  1.00255.50           N  
ANISOU 1121  N   VAL A 206    28811  38316  29953  -1170  -3255   6736       N  
ATOM   1122  CA  VAL A 206      28.723 -22.147  88.948  1.00261.14           C  
ANISOU 1122  CA  VAL A 206    29460  39259  30503   -823  -2682   6404       C  
ATOM   1123  C   VAL A 206      29.566 -23.349  88.536  1.00269.25           C  
ANISOU 1123  C   VAL A 206    30223  40692  31386   -792  -2056   7008       C  
ATOM   1124  O   VAL A 206      30.640 -23.216  87.948  1.00274.08           O  
ANISOU 1124  O   VAL A 206    30745  41390  32003   -999  -2059   7682       O  
ATOM   1125  CB  VAL A 206      27.378 -22.134  88.198  1.00256.87           C  
ANISOU 1125  CB  VAL A 206    29182  38404  30014   -548  -2653   5893       C  
ATOM   1126  CG1 VAL A 206      26.618 -20.856  88.499  1.00257.86           C  
ANISOU 1126  CG1 VAL A 206    29589  38116  30270   -599  -3270   5381       C  
ATOM   1127  CG2 VAL A 206      27.608 -22.285  86.704  1.00254.28           C  
ANISOU 1127  CG2 VAL A 206    28896  37993  29727   -535  -2474   6286       C  
ATOM   1128  N   THR A 207      29.060 -24.544  88.851  1.00267.77           N  
ANISOU 1128  N   THR A 207    29904  40761  31077   -507  -1514   6790       N  
ATOM   1129  CA  THR A 207      29.749 -25.801  88.552  1.00254.34           C  
ANISOU 1129  CA  THR A 207    27954  39453  29229   -434   -863   7295       C  
ATOM   1130  C   THR A 207      28.766 -26.699  87.805  1.00251.18           C  
ANISOU 1130  C   THR A 207    27651  38971  28815    -73   -471   6984       C  
ATOM   1131  O   THR A 207      28.168 -27.610  88.384  1.00252.24           O  
ANISOU 1131  O   THR A 207    27639  39282  28920    168   -115   6678       O  
ATOM   1132  CB  THR A 207      30.272 -26.464  89.831  1.00253.09           C  
ANISOU 1132  CB  THR A 207    27446  39753  28963   -472   -556   7407       C  
ATOM   1133  OG1 THR A 207      30.964 -25.494  90.625  1.00258.66           O  
ANISOU 1133  OG1 THR A 207    28113  40467  29698   -794  -1032   7543       O  
ATOM   1134  CG2 THR A 207      31.225 -27.601  89.491  1.00250.49           C  
ANISOU 1134  CG2 THR A 207    26859  39835  28479   -476     87   8068       C  
ATOM   1135  N   ILE A 208      28.604 -26.440  86.510  1.00250.22           N  
ANISOU 1135  N   ILE A 208    27752  38588  28732    -27   -551   7085       N  
ATOM   1136  CA  ILE A 208      27.687 -27.200  85.665  1.00248.05           C  
ANISOU 1136  CA  ILE A 208    27611  38191  28446    297   -243   6800       C  
ATOM   1137  C   ILE A 208      28.433 -28.430  85.158  1.00257.12           C  
ANISOU 1137  C   ILE A 208    28587  39668  29436    415    357   7311       C  
ATOM   1138  O   ILE A 208      29.369 -28.282  84.354  1.00260.78           O  
ANISOU 1138  O   ILE A 208    29058  40204  29824    321    384   7905       O  
ATOM   1139  CB  ILE A 208      27.156 -26.355  84.503  1.00241.50           C  
ANISOU 1139  CB  ILE A 208    27080  36962  27716    313   -589   6663       C  
ATOM   1140  CG1 ILE A 208      26.266 -25.238  85.039  1.00239.34           C  
ANISOU 1140  CG1 ILE A 208    26996  36354  27587    235  -1124   6103       C  
ATOM   1141  CG2 ILE A 208      26.400 -27.238  83.511  1.00240.35           C  
ANISOU 1141  CG2 ILE A 208    27059  36736  27526    636   -233   6476       C  
ATOM   1142  CD1 ILE A 208      25.708 -24.353  83.969  1.00239.32           C  
ANISOU 1142  CD1 ILE A 208    27252  35977  27702    229  -1447   5960       C  
ATOM   1143  N   PRO A 209      28.052 -29.631  85.567  1.00250.87           N  
ANISOU 1143  N   PRO A 209    27637  39080  28602    642    832   7132       N  
ATOM   1144  CA  PRO A 209      28.832 -30.824  85.231  1.00247.48           C  
ANISOU 1144  CA  PRO A 209    27026  38989  28018    744   1425   7631       C  
ATOM   1145  C   PRO A 209      28.622 -31.257  83.786  1.00242.22           C  
ANISOU 1145  C   PRO A 209    26587  38157  27288    980   1591   7711       C  
ATOM   1146  O   PRO A 209      27.729 -30.786  83.082  1.00238.76           O  
ANISOU 1146  O   PRO A 209    26416  37361  26941   1089   1308   7316       O  
ATOM   1147  CB  PRO A 209      28.290 -31.873  86.206  1.00244.45           C  
ANISOU 1147  CB  PRO A 209    26376  38824  27681    929   1811   7309       C  
ATOM   1148  CG  PRO A 209      26.865 -31.469  86.400  1.00243.84           C  
ANISOU 1148  CG  PRO A 209    26475  38400  27774   1085   1471   6587       C  
ATOM   1149  CD  PRO A 209      26.835 -29.961  86.331  1.00247.22           C  
ANISOU 1149  CD  PRO A 209    27145  38540  28249    850    842   6482       C  
ATOM   1150  N   SER A 210      29.487 -32.170  83.353  1.00231.76           N  
ANISOU 1150  N   SER A 210    25154  37121  25785   1069   2070   8252       N  
ATOM   1151  CA  SER A 210      29.302 -32.814  82.063  1.00234.74           C  
ANISOU 1151  CA  SER A 210    25730  37397  26064   1367   2302   8312       C  
ATOM   1152  C   SER A 210      28.019 -33.638  82.071  1.00242.64           C  
ANISOU 1152  C   SER A 210    26794  38211  27185   1650   2464   7654       C  
ATOM   1153  O   SER A 210      27.596 -34.164  83.105  1.00234.74           O  
ANISOU 1153  O   SER A 210    25573  37320  26296   1669   2626   7370       O  
ATOM   1154  CB  SER A 210      30.501 -33.707  81.738  1.00230.39           C  
ANISOU 1154  CB  SER A 210    25127  36721  25689   1447   2508   8378       C  
ATOM   1155  OG  SER A 210      30.561 -34.825  82.609  1.00224.76           O  
ANISOU 1155  OG  SER A 210    24243  36024  25130   1513   2781   8082       O  
ATOM   1156  N   GLY A 211      27.402 -33.759  80.897  1.00230.37           N  
ANISOU 1156  N   GLY A 211    25521  36388  25621   1887   2411   7444       N  
ATOM   1157  CA  GLY A 211      26.154 -34.487  80.782  1.00230.46           C  
ANISOU 1157  CA  GLY A 211    25627  36175  25764   2146   2503   6851       C  
ATOM   1158  C   GLY A 211      24.918 -33.762  81.267  1.00234.25           C  
ANISOU 1158  C   GLY A 211    26201  36346  26456   2091   2086   6231       C  
ATOM   1159  O   GLY A 211      23.855 -34.386  81.355  1.00233.74           O  
ANISOU 1159  O   GLY A 211    26169  36117  26524   2295   2153   5782       O  
ATOM   1160  N   SER A 212      25.018 -32.472  81.590  1.00229.71           N  
ANISOU 1160  N   SER A 212    25674  35682  25923   1834   1649   6220       N  
ATOM   1161  CA  SER A 212      23.868 -31.715  82.074  1.00221.79           C  
ANISOU 1161  CA  SER A 212    24791  34392  25088   1795   1250   5660       C  
ATOM   1162  C   SER A 212      22.800 -31.560  80.994  1.00216.10           C  
ANISOU 1162  C   SER A 212    24388  33305  24417   1966   1092   5294       C  
ATOM   1163  O   SER A 212      23.088 -31.127  79.874  1.00225.01           O  
ANISOU 1163  O   SER A 212    25686  34337  25469   1963    996   5482       O  
ATOM   1164  CB  SER A 212      24.320 -30.338  82.558  1.00221.35           C  
ANISOU 1164  CB  SER A 212    24742  34304  25055   1481    805   5764       C  
ATOM   1165  OG  SER A 212      23.238 -29.597  83.094  1.00218.87           O  
ANISOU 1165  OG  SER A 212    24560  33727  24873   1464    429   5238       O  
ATOM   1166  N   THR A 213      21.563 -31.920  81.340  1.00228.66           N  
ANISOU 1166  N   THR A 213    26031  34713  26136   2128   1067   4803       N  
ATOM   1167  CA  THR A 213      20.435 -31.892  80.414  1.00197.41           C  
ANISOU 1167  CA  THR A 213    22363  30414  22230   2290    945   4443       C  
ATOM   1168  C   THR A 213      19.801 -30.502  80.389  1.00179.35           C  
ANISOU 1168  C   THR A 213    20285  27861  20001   2126    476   4190       C  
ATOM   1169  O   THR A 213      19.406 -29.976  81.435  1.00181.26           O  
ANISOU 1169  O   THR A 213    20479  28076  20316   2040    256   3985       O  
ATOM   1170  CB  THR A 213      19.401 -32.947  80.804  1.00178.46           C  
ANISOU 1170  CB  THR A 213    19907  27938  19961   2540   1123   4107       C  
ATOM   1171  OG1 THR A 213      19.919 -34.254  80.521  1.00175.57           O  
ANISOU 1171  OG1 THR A 213    19398  27754  19558   2715   1558   4322       O  
ATOM   1172  CG2 THR A 213      18.105 -32.738  80.033  1.00164.32           C  
ANISOU 1172  CG2 THR A 213    18424  25771  18237   2658    918   3718       C  
ATOM   1173  N   LEU A 214      19.710 -29.904  79.199  1.00178.88           N  
ANISOU 1173  N   LEU A 214    20442  27621  19902   2105    330   4214       N  
ATOM   1174  CA  LEU A 214      19.104 -28.585  79.044  1.00177.51           C  
ANISOU 1174  CA  LEU A 214    20457  27192  19798   1948    -81   3996       C  
ATOM   1175  C   LEU A 214      17.704 -28.602  78.437  1.00175.07           C  
ANISOU 1175  C   LEU A 214    20400  26582  19539   2094   -146   3582       C  
ATOM   1176  O   LEU A 214      16.905 -27.713  78.749  1.00183.87           O  
ANISOU 1176  O   LEU A 214    21655  27489  20719   1999   -438   3313       O  
ATOM   1177  CB  LEU A 214      20.007 -27.669  78.211  1.00179.77           C  
ANISOU 1177  CB  LEU A 214    20743  27510  20050   1785   -246   4364       C  
ATOM   1178  CG  LEU A 214      21.356 -27.337  78.854  1.00177.18           C  
ANISOU 1178  CG  LEU A 214    20189  27434  19697   1572   -299   4816       C  
ATOM   1179  CD1 LEU A 214      22.434 -28.313  78.409  1.00176.73           C  
ANISOU 1179  CD1 LEU A 214    19979  27678  19495   1694     86   5301       C  
ATOM   1180  CD2 LEU A 214      21.753 -25.901  78.553  1.00181.67           C  
ANISOU 1180  CD2 LEU A 214    20778  27892  20358   1328   -711   4992       C  
ATOM   1181  N   ALA A 215      17.376 -29.571  77.583  1.00164.41           N  
ANISOU 1181  N   ALA A 215    19124  25195  18151   2323    108   3532       N  
ATOM   1182  CA  ALA A 215      16.056 -29.625  76.958  1.00144.68           C  
ANISOU 1182  CA  ALA A 215    16865  22411  15696   2448     43   3171       C  
ATOM   1183  C   ALA A 215      15.767 -31.066  76.551  1.00140.82           C  
ANISOU 1183  C   ALA A 215    16384  21919  15201   2722    347   3103       C  
ATOM   1184  O   ALA A 215      16.620 -31.947  76.681  1.00142.04           O  
ANISOU 1184  O   ALA A 215    16367  22295  15307   2815    619   3341       O  
ATOM   1185  CB  ALA A 215      15.974 -28.676  75.762  1.00145.31           C  
ANISOU 1185  CB  ALA A 215    17106  22367  15739   2373   -121   3196       C  
ATOM   1186  N   PHE A 216      14.565 -31.294  76.019  1.00138.55           N  
ANISOU 1186  N   PHE A 216    16305  21373  14966   2847    297   2796       N  
ATOM   1187  CA  PHE A 216      14.085 -32.650  75.751  1.00150.99           C  
ANISOU 1187  CA  PHE A 216    17902  22874  16592   3102    511   2674       C  
ATOM   1188  C   PHE A 216      12.810 -32.590  74.910  1.00175.31           C  
ANISOU 1188  C   PHE A 216    21261  25645  19705   3181    381   2377       C  
ATOM   1189  O   PHE A 216      12.308 -31.512  74.576  1.00191.00           O  
ANISOU 1189  O   PHE A 216    23403  27505  21665   3037    169   2279       O  
ATOM   1190  CB  PHE A 216      13.839 -33.394  77.063  1.00132.89           C  
ANISOU 1190  CB  PHE A 216    15387  20652  14453   3174    596   2631       C  
ATOM   1191  CG  PHE A 216      12.848 -32.709  77.953  1.00137.53           C  
ANISOU 1191  CG  PHE A 216    16007  21106  15142   3105    334   2432       C  
ATOM   1192  CD1 PHE A 216      13.250 -31.684  78.793  1.00143.72           C  
ANISOU 1192  CD1 PHE A 216    16710  22008  15887   2913    160   2499       C  
ATOM   1193  CD2 PHE A 216      11.513 -33.076  77.944  1.00150.55           C  
ANISOU 1193  CD2 PHE A 216    17780  22506  16915   3248    243   2201       C  
ATOM   1194  CE1 PHE A 216      12.346 -31.039  79.605  1.00156.38           C  
ANISOU 1194  CE1 PHE A 216    18374  23495  17546   2895    -86   2319       C  
ATOM   1195  CE2 PHE A 216      10.602 -32.436  78.757  1.00162.24           C  
ANISOU 1195  CE2 PHE A 216    19305  23885  18454   3227     10   2076       C  
ATOM   1196  CZ  PHE A 216      11.019 -31.416  79.589  1.00164.74           C  
ANISOU 1196  CZ  PHE A 216    19559  24333  18704   3066   -149   2124       C  
ATOM   1197  N   ARG A 217      12.292 -33.774  74.572  1.00165.88           N  
ANISOU 1197  N   ARG A 217    20119  24329  18580   3405    514   2248       N  
ATOM   1198  CA  ARG A 217      11.068 -33.940  73.798  1.00171.24           C  
ANISOU 1198  CA  ARG A 217    21052  24709  19303   3496    403   1985       C  
ATOM   1199  C   ARG A 217      10.284 -35.123  74.358  1.00186.41           C  
ANISOU 1199  C   ARG A 217    22909  26482  21434   3675    442   1863       C  
ATOM   1200  O   ARG A 217      10.873 -36.078  74.872  1.00188.08           O  
ANISOU 1200  O   ARG A 217    22898  26838  21727   3796    641   1978       O  
ATOM   1201  CB  ARG A 217      11.418 -34.111  72.309  1.00170.93           C  
ANISOU 1201  CB  ARG A 217    21180  24665  19100   3618    491   1990       C  
ATOM   1202  CG  ARG A 217      10.262 -34.092  71.328  1.00167.32           C  
ANISOU 1202  CG  ARG A 217    20997  23934  18644   3682    368   1730       C  
ATOM   1203  CD  ARG A 217      10.790 -33.740  69.943  1.00155.57           C  
ANISOU 1203  CD  ARG A 217    19614  22545  16951   3762    420   1786       C  
ATOM   1204  NE  ARG A 217      11.886 -34.599  69.510  1.00149.28           N  
ANISOU 1204  NE  ARG A 217    18749  21939  16031   3992    640   1962       N  
ATOM   1205  CZ  ARG A 217      11.846 -35.366  68.428  1.00161.38           C  
ANISOU 1205  CZ  ARG A 217    20443  23416  17458   4266    720   1861       C  
ATOM   1206  NH1 ARG A 217      12.889 -36.117  68.105  1.00158.84           N  
ANISOU 1206  NH1 ARG A 217    20072  23285  16996   4498    930   2056       N  
ATOM   1207  NH2 ARG A 217      10.770 -35.365  67.655  1.00176.85           N  
ANISOU 1207  NH2 ARG A 217    22625  25138  19432   4318    590   1579       N  
ATOM   1208  N   VAL A 218       8.951 -35.058  74.268  1.00182.04           N  
ANISOU 1208  N   VAL A 218    22529  25652  20987   3694    256   1670       N  
ATOM   1209  CA  VAL A 218       8.091 -36.056  74.899  1.00173.99           C  
ANISOU 1209  CA  VAL A 218    21412  24478  20217   3862    228   1612       C  
ATOM   1210  C   VAL A 218       7.214 -36.765  73.872  1.00164.69           C  
ANISOU 1210  C   VAL A 218    20473  22995  19106   3996    163   1438       C  
ATOM   1211  O   VAL A 218       6.994 -36.286  72.757  1.00164.80           O  
ANISOU 1211  O   VAL A 218    20755  22901  18959   3940    103   1325       O  
ATOM   1212  CB  VAL A 218       7.195 -35.440  75.999  1.00179.14           C  
ANISOU 1212  CB  VAL A 218    22008  25082  20974   3806     27   1622       C  
ATOM   1213  CG1 VAL A 218       8.036 -34.811  77.096  1.00182.10           C  
ANISOU 1213  CG1 VAL A 218    22145  25753  21293   3701     61   1762       C  
ATOM   1214  CG2 VAL A 218       6.215 -34.427  75.402  1.00182.65           C  
ANISOU 1214  CG2 VAL A 218    22779  25310  21311   3669   -185   1506       C  
ATOM   1215  N   ALA A 219       6.712 -37.933  74.278  1.00152.22           N  
ANISOU 1215  N   ALA A 219    18763  21285  17790   4184    168   1430       N  
ATOM   1216  CA  ALA A 219       5.693 -38.673  73.536  1.00149.92           C  
ANISOU 1216  CA  ALA A 219    18673  20651  17638   4310     33   1280       C  
ATOM   1217  C   ALA A 219       4.762 -39.318  74.555  1.00153.04           C  
ANISOU 1217  C   ALA A 219    18855  20915  18378   4433    -95   1371       C  
ATOM   1218  O   ALA A 219       5.168 -40.244  75.263  1.00107.00           O  
ANISOU 1218  O   ALA A 219    12697  15192  12766   4585     36   1477       O  
ATOM   1219  CB  ALA A 219       6.314 -39.724  72.616  1.00151.68           C  
ANISOU 1219  CB  ALA A 219    18963  20831  17838   4485    186   1189       C  
ATOM   1220  N   GLN A 220       3.522 -38.840  74.622  1.00112.78           N  
ANISOU 1220  N   GLN A 220    13915  15605  13333   4384   -338   1373       N  
ATOM   1221  CA  GLN A 220       2.543 -39.365  75.565  1.00111.49           C  
ANISOU 1221  CA  GLN A 220    13545  15324  13492   4536   -498   1535       C  
ATOM   1222  C   GLN A 220       2.162 -40.799  75.213  1.00158.14           C  
ANISOU 1222  C   GLN A 220    19383  20979  19724   4737   -547   1511       C  
ATOM   1223  O   GLN A 220       2.184 -41.201  74.049  1.00171.67           O  
ANISOU 1223  O   GLN A 220    21362  22492  21372   4735   -558   1319       O  
ATOM   1224  CB  GLN A 220       1.298 -38.473  75.565  1.00114.74           C  
ANISOU 1224  CB  GLN A 220    14202  15560  13832   4440   -743   1589       C  
ATOM   1225  CG  GLN A 220       0.065 -39.019  76.269  1.00125.23           C  
ANISOU 1225  CG  GLN A 220    15394  16708  15481   4627   -962   1813       C  
ATOM   1226  CD  GLN A 220      -1.044 -37.986  76.400  1.00149.61           C  
ANISOU 1226  CD  GLN A 220    18725  19694  18425   4536  -1161   1937       C  
ATOM   1227  OE1 GLN A 220      -1.108 -37.021  75.634  1.00146.71           O  
ANISOU 1227  OE1 GLN A 220    18695  19288  17760   4310  -1153   1802       O  
ATOM   1228  NE2 GLN A 220      -1.915 -38.178  77.384  1.00162.39           N  
ANISOU 1228  NE2 GLN A 220    20152  21292  20256   4735  -1326   2229       N  
ATOM   1229  N   LEU A 221       1.819 -41.582  76.235  1.00142.47           N  
ANISOU 1229  N   LEU A 221    17017  19011  18104   4935   -588   1713       N  
ATOM   1230  CA  LEU A 221       1.178 -42.873  76.030  1.00148.32           C  
ANISOU 1230  CA  LEU A 221    17663  19452  19240   5128   -723   1746       C  
ATOM   1231  C   LEU A 221      -0.055 -42.955  76.918  1.00173.31           C  
ANISOU 1231  C   LEU A 221    20624  22510  22716   5268   -982   2040       C  
ATOM   1232  O   LEU A 221      -0.192 -42.217  77.897  1.00180.92           O  
ANISOU 1232  O   LEU A 221    21422  23710  23610   5285   -989   2224       O  
ATOM   1233  CB  LEU A 221       2.110 -44.072  76.299  1.00131.11           C  
ANISOU 1233  CB  LEU A 221    15125  17398  17295   5296   -485   1753       C  
ATOM   1234  CG  LEU A 221       3.013 -44.240  77.520  1.00120.49           C  
ANISOU 1234  CG  LEU A 221    13268  16474  16039   5381   -210   1937       C  
ATOM   1235  CD1 LEU A 221       2.199 -44.611  78.746  1.00111.03           C  
ANISOU 1235  CD1 LEU A 221    11614  15321  15252   5593   -350   2237       C  
ATOM   1236  CD2 LEU A 221       4.045 -45.313  77.230  1.00107.57           C  
ANISOU 1236  CD2 LEU A 221    11470  14911  14492   5473     74   1871       C  
ATOM   1237  N   VAL A 222      -0.962 -43.854  76.545  1.00170.56           N  
ANISOU 1237  N   VAL A 222    20300  21798  22706   5389  -1219   2100       N  
ATOM   1238  CA  VAL A 222      -2.207 -44.076  77.267  1.00186.50           C  
ANISOU 1238  CA  VAL A 222    22119  23675  25069   5560  -1505   2453       C  
ATOM   1239  C   VAL A 222      -2.304 -45.557  77.606  1.00200.87           C  
ANISOU 1239  C   VAL A 222    23508  25363  27450   5819  -1566   2601       C  
ATOM   1240  O   VAL A 222      -1.909 -46.416  76.808  1.00206.76           O  
ANISOU 1240  O   VAL A 222    24348  25903  28308   5818  -1528   2371       O  
ATOM   1241  CB  VAL A 222      -3.431 -43.614  76.450  1.00189.86           C  
ANISOU 1241  CB  VAL A 222    23010  23741  25388   5428  -1805   2475       C  
ATOM   1242  CG1 VAL A 222      -3.276 -42.156  76.068  1.00190.48           C  
ANISOU 1242  CG1 VAL A 222    23478  23963  24932   5165  -1707   2321       C  
ATOM   1243  CG2 VAL A 222      -3.609 -44.468  75.203  1.00192.59           C  
ANISOU 1243  CG2 VAL A 222    23628  23692  25856   5388  -1932   2237       C  
ATOM   1244  N   ILE A 223      -2.808 -45.859  78.799  1.00207.99           N  
ANISOU 1244  N   ILE A 223    23917  26399  28712   6070  -1660   2995       N  
ATOM   1245  CA  ILE A 223      -2.924 -47.233  79.266  1.00214.80           C  
ANISOU 1245  CA  ILE A 223    24435  27109  30070   5978  -1728   2931       C  
ATOM   1246  C   ILE A 223      -4.331 -47.367  79.833  1.00253.20           C  
ANISOU 1246  C   ILE A 223    29400  31749  35057   5745  -2099   2953       C  
ATOM   1247  O   ILE A 223      -4.608 -46.898  80.943  1.00251.29           O  
ANISOU 1247  O   ILE A 223    29071  31718  34691   5580  -2082   2961       O  
ATOM   1248  CB  ILE A 223      -1.876 -47.582  80.331  1.00189.08           C  
ANISOU 1248  CB  ILE A 223    20726  24257  26859   5925  -1388   2860       C  
ATOM   1249  CG1 ILE A 223      -0.477 -47.097  79.929  1.00164.31           C  
ANISOU 1249  CG1 ILE A 223    17551  21478  23402   6143   -984   2840       C  
ATOM   1250  CG2 ILE A 223      -1.849 -49.087  80.563  1.00192.67           C  
ANISOU 1250  CG2 ILE A 223    20906  24573  27727   5894  -1418   2743       C  
ATOM   1251  CD1 ILE A 223       0.127 -47.846  78.777  1.00154.88           C  
ANISOU 1251  CD1 ILE A 223    16561  20071  22217   6175   -875   2595       C  
ATOM   1252  N   ASP A 224      -5.214 -48.008  79.092  1.00243.68           N  
ANISOU 1252  N   ASP A 224    28427  30151  34009   5775  -2409   2938       N  
ATOM   1253  CA  ASP A 224      -6.465 -48.514  79.643  1.00258.09           C  
ANISOU 1253  CA  ASP A 224    30356  31890  35815   5669  -2658   2911       C  
ATOM   1254  C   ASP A 224      -6.747 -49.950  79.225  1.00268.75           C  
ANISOU 1254  C   ASP A 224    31670  33065  37378   5802  -2735   2866       C  
ATOM   1255  O   ASP A 224      -7.251 -50.731  80.038  1.00267.88           O  
ANISOU 1255  O   ASP A 224    31409  33074  37300   5749  -2745   2836       O  
ATOM   1256  CB  ASP A 224      -7.628 -47.578  79.263  1.00266.79           C  
ANISOU 1256  CB  ASP A 224    31918  32823  36630   5565  -2882   3031       C  
ATOM   1257  CG  ASP A 224      -7.767 -47.389  77.767  1.00274.35           C  
ANISOU 1257  CG  ASP A 224    33233  33455  37551   5669  -2992   3117       C  
ATOM   1258  OD1 ASP A 224      -6.772 -47.590  77.039  1.00279.61           O  
ANISOU 1258  OD1 ASP A 224    33801  34028  38409   5821  -2884   3080       O  
ATOM   1259  OD2 ASP A 224      -8.874 -47.029  77.320  1.00276.41           O  
ANISOU 1259  OD2 ASP A 224    33882  33573  37571   5600  -3123   3238       O  
ATOM   1260  N   SER A 225      -6.443 -50.314  77.978  1.00266.70           N  
ANISOU 1260  N   SER A 225    31547  32511  37274   5963  -2763   2885       N  
ATOM   1261  CA  SER A 225      -6.481 -51.707  77.551  1.00270.39           C  
ANISOU 1261  CA  SER A 225    31916  32778  38042   6062  -2780   2871       C  
ATOM   1262  C   SER A 225      -5.199 -52.098  76.820  1.00271.54           C  
ANISOU 1262  C   SER A 225    31930  32772  38473   6249  -2639   2726       C  
ATOM   1263  O   SER A 225      -4.740 -53.240  76.922  1.00272.54           O  
ANISOU 1263  O   SER A 225    31807  32883  38864   6327  -2547   2635       O  
ATOM   1264  CB  SER A 225      -7.695 -51.955  76.648  1.00275.79           C  
ANISOU 1264  CB  SER A 225    32943  33074  38771   5979  -3010   3042       C  
ATOM   1265  OG  SER A 225      -7.615 -51.193  75.454  1.00278.45           O  
ANISOU 1265  OG  SER A 225    33618  33061  39121   5958  -3143   3032       O  
ATOM   1266  N   ASP A 226      -4.615 -51.148  76.087  1.00274.81           N  
ANISOU 1266  N   ASP A 226    32521  33069  38826   6325  -2606   2690       N  
ATOM   1267  CA  ASP A 226      -3.381 -51.362  75.339  1.00268.48           C  
ANISOU 1267  CA  ASP A 226    31811  32230  37970   6379  -2362   2358       C  
ATOM   1268  C   ASP A 226      -2.385 -50.244  75.618  1.00260.41           C  
ANISOU 1268  C   ASP A 226    30858  31719  36366   6236  -1940   2235       C  
ATOM   1269  O   ASP A 226      -2.623 -49.394  76.482  1.00263.25           O  
ANISOU 1269  O   ASP A 226    31040  32371  36612   6220  -1898   2494       O  
ATOM   1270  CB  ASP A 226      -3.675 -51.451  73.839  1.00271.28           C  
ANISOU 1270  CB  ASP A 226    32821  32144  38108   6239  -2590   1972       C  
ATOM   1271  CG  ASP A 226      -2.794 -52.458  73.130  1.00275.77           C  
ANISOU 1271  CG  ASP A 226    33483  32569  38729   6337  -2458   1606       C  
ATOM   1272  OD1 ASP A 226      -1.662 -52.694  73.600  1.00276.26           O  
ANISOU 1272  OD1 ASP A 226    33252  32979  38735   6417  -2054   1571       O  
ATOM   1273  OD2 ASP A 226      -3.235 -53.018  72.104  1.00278.81           O  
ANISOU 1273  OD2 ASP A 226    34243  32495  39198   6343  -2760   1366       O  
ATOM   1274  N   LEU A 227      -1.271 -50.230  74.892  1.00280.65           N  
ANISOU 1274  N   LEU A 227    33685  34389  38558   6153  -1647   1863       N  
ATOM   1275  CA  LEU A 227      -0.291 -49.165  75.020  1.00240.08           C  
ANISOU 1275  CA  LEU A 227    28647  29698  32874   5999  -1285   1759       C  
ATOM   1276  C   LEU A 227       0.161 -48.757  73.627  1.00243.00           C  
ANISOU 1276  C   LEU A 227    29618  29961  32750   5851  -1233   1361       C  
ATOM   1277  O   LEU A 227       0.224 -49.582  72.712  1.00248.12           O  
ANISOU 1277  O   LEU A 227    30497  30308  33471   5937  -1322   1122       O  
ATOM   1278  CB  LEU A 227       0.910 -49.591  75.875  1.00205.35           C  
ANISOU 1278  CB  LEU A 227    23759  25717  28550   6105   -870   1852       C  
ATOM   1279  CG  LEU A 227       1.999 -50.443  75.230  1.00185.43           C  
ANISOU 1279  CG  LEU A 227    21303  23190  25962   6175   -602   1615       C  
ATOM   1280  CD1 LEU A 227       3.257 -50.379  76.068  1.00178.16           C  
ANISOU 1280  CD1 LEU A 227    19983  22792  24918   6185   -131   1748       C  
ATOM   1281  CD2 LEU A 227       1.539 -51.886  75.076  1.00181.62           C  
ANISOU 1281  CD2 LEU A 227    20641  22318  26049   6386   -798   1623       C  
ATOM   1282  N   ASP A 228       0.462 -47.470  73.470  1.00222.39           N  
ANISOU 1282  N   ASP A 228    27246  27605  29646   5653  -1103   1299       N  
ATOM   1283  CA  ASP A 228       0.959 -46.945  72.206  1.00213.77           C  
ANISOU 1283  CA  ASP A 228    26649  26502  28072   5537  -1022    977       C  
ATOM   1284  C   ASP A 228       1.634 -45.608  72.465  1.00201.62           C  
ANISOU 1284  C   ASP A 228    25141  25374  26092   5351   -787   1015       C  
ATOM   1285  O   ASP A 228       1.337 -44.929  73.450  1.00199.93           O  
ANISOU 1285  O   ASP A 228    24710  25340  25913   5274   -798   1240       O  
ATOM   1286  CB  ASP A 228      -0.174 -46.785  71.184  1.00216.75           C  
ANISOU 1286  CB  ASP A 228    27468  26477  28410   5463  -1374    828       C  
ATOM   1287  CG  ASP A 228      -1.373 -46.047  71.755  1.00213.31           C  
ANISOU 1287  CG  ASP A 228    27009  25973  28067   5337  -1610   1091       C  
ATOM   1288  OD1 ASP A 228      -1.408 -45.822  72.983  1.00210.42           O  
ANISOU 1288  OD1 ASP A 228    26263  25831  27858   5368  -1547   1384       O  
ATOM   1289  OD2 ASP A 228      -2.279 -45.682  70.977  1.00213.15           O  
ANISOU 1289  OD2 ASP A 228    27351  25695  27943   5223  -1847   1021       O  
ATOM   1290  N   VAL A 229       2.536 -45.231  71.568  1.00205.38           N  
ANISOU 1290  N   VAL A 229    25885  25993  26159   5303   -596    809       N  
ATOM   1291  CA  VAL A 229       3.235 -43.957  71.681  1.00181.92           C  
ANISOU 1291  CA  VAL A 229    22950  23384  22789   5121   -404    852       C  
ATOM   1292  C   VAL A 229       2.503 -42.913  70.850  1.00169.86           C  
ANISOU 1292  C   VAL A 229    21807  21734  21000   4946   -584    733       C  
ATOM   1293  O   VAL A 229       1.850 -43.220  69.846  1.00172.02           O  
ANISOU 1293  O   VAL A 229    22383  21708  21268   4984   -768    549       O  
ATOM   1294  CB  VAL A 229       4.714 -44.083  71.260  1.00176.88           C  
ANISOU 1294  CB  VAL A 229    22312  23029  21866   5185    -78    799       C  
ATOM   1295  CG1 VAL A 229       5.474 -44.940  72.260  1.00166.69           C  
ANISOU 1295  CG1 VAL A 229    20589  21938  20808   5307    162    982       C  
ATOM   1296  CG2 VAL A 229       4.817 -44.681  69.868  1.00185.86           C  
ANISOU 1296  CG2 VAL A 229    23804  23953  22861   5343   -120    540       C  
ATOM   1297  N   LEU A 230       2.629 -41.655  71.269  1.00161.42           N  
ANISOU 1297  N   LEU A 230    20715  20905  19711   4751   -525    838       N  
ATOM   1298  CA  LEU A 230       1.897 -40.533  70.684  1.00171.62           C  
ANISOU 1298  CA  LEU A 230    22303  22124  20781   4558   -662    782       C  
ATOM   1299  C   LEU A 230       2.875 -39.429  70.279  1.00189.27           C  
ANISOU 1299  C   LEU A 230    24601  24674  22638   4419   -469    748       C  
ATOM   1300  O   LEU A 230       2.787 -38.292  70.741  1.00193.35           O  
ANISOU 1300  O   LEU A 230    25096  25336  23034   4232   -476    849       O  
ATOM   1301  CB  LEU A 230       0.828 -40.000  71.641  1.00163.27           C  
ANISOU 1301  CB  LEU A 230    21164  20997  19874   4462   -842    990       C  
ATOM   1302  CG  LEU A 230      -0.627 -40.448  71.474  1.00153.75           C  
ANISOU 1302  CG  LEU A 230    20098  19414  18905   4498  -1134   1051       C  
ATOM   1303  CD1 LEU A 230      -1.226 -39.819  70.229  1.00160.34           C  
ANISOU 1303  CD1 LEU A 230    21336  20096  19489   4343  -1219    891       C  
ATOM   1304  CD2 LEU A 230      -0.746 -41.963  71.401  1.00139.51           C  
ANISOU 1304  CD2 LEU A 230    18178  17367  17464   4722  -1231   1019       C  
ATOM   1305  N   LEU A 231       3.832 -39.781  69.414  1.00186.54           N  
ANISOU 1305  N   LEU A 231    24327  24435  22113   4537   -309    630       N  
ATOM   1306  CA  LEU A 231       4.728 -38.790  68.823  1.00194.14           C  
ANISOU 1306  CA  LEU A 231    25347  25683  22736   4448   -158    639       C  
ATOM   1307  C   LEU A 231       3.977 -37.584  68.264  1.00192.79           C  
ANISOU 1307  C   LEU A 231    25374  25471  22408   4247   -276    588       C  
ATOM   1308  O   LEU A 231       4.578 -36.518  68.081  1.00200.38           O  
ANISOU 1308  O   LEU A 231    26301  26675  23159   4117   -186    660       O  
ATOM   1309  CB  LEU A 231       5.562 -39.440  67.720  1.00196.80           C  
ANISOU 1309  CB  LEU A 231    25799  26083  22893   4681    -24    527       C  
ATOM   1310  CG  LEU A 231       6.471 -40.579  68.176  1.00196.73           C  
ANISOU 1310  CG  LEU A 231    25604  26159  22984   4883    156    607       C  
ATOM   1311  CD1 LEU A 231       7.048 -41.304  66.976  1.00202.74           C  
ANISOU 1311  CD1 LEU A 231    26564  26913  23555   5167    242    470       C  
ATOM   1312  CD2 LEU A 231       7.579 -40.038  69.061  1.00193.76           C  
ANISOU 1312  CD2 LEU A 231    24943  26151  22526   4772    366    873       C  
ATOM   1313  N   PHE A 232       2.689 -37.737  67.971  1.00198.46           N  
ANISOU 1313  N   PHE A 232    26283  25888  23235   4215   -473    495       N  
ATOM   1314  CA  PHE A 232       1.803 -36.638  67.616  1.00180.26           C  
ANISOU 1314  CA  PHE A 232    24146  23530  20813   4001   -568    494       C  
ATOM   1315  C   PHE A 232       0.979 -36.275  68.846  1.00164.21           C  
ANISOU 1315  C   PHE A 232    22030  21411  18950   3869   -693    680       C  
ATOM   1316  O   PHE A 232      -0.077 -36.871  69.089  1.00135.64           O  
ANISOU 1316  O   PHE A 232    18477  17523  15539   3914   -870    726       O  
ATOM   1317  CB  PHE A 232       0.909 -36.998  66.417  1.00185.53           C  
ANISOU 1317  CB  PHE A 232    25097  23950  21448   4051   -690    309       C  
ATOM   1318  CG  PHE A 232       0.065 -38.243  66.604  1.00186.42           C  
ANISOU 1318  CG  PHE A 232    25275  23706  21849   4181   -891    274       C  
ATOM   1319  CD1 PHE A 232       0.655 -39.494  66.691  1.00188.50           C  
ANISOU 1319  CD1 PHE A 232    25449  23901  22271   4421   -875    198       C  
ATOM   1320  CD2 PHE A 232      -1.322 -38.161  66.644  1.00180.08           C  
ANISOU 1320  CD2 PHE A 232    24622  22632  21168   4065  -1102    347       C  
ATOM   1321  CE1 PHE A 232      -0.108 -40.632  66.847  1.00186.75           C  
ANISOU 1321  CE1 PHE A 232    25258  23334  22366   4540  -1086    178       C  
ATOM   1322  CE2 PHE A 232      -2.095 -39.301  66.798  1.00177.67           C  
ANISOU 1322  CE2 PHE A 232    24354  21985  21169   4185  -1327    364       C  
ATOM   1323  CZ  PHE A 232      -1.484 -40.539  66.896  1.00182.06           C  
ANISOU 1323  CZ  PHE A 232    24794  22460  21921   4423  -1331    267       C  
ATOM   1324  N   PRO A 233       1.434 -35.321  69.661  1.00175.72           N  
ANISOU 1324  N   PRO A 233    23341  23094  20332   3731   -628    815       N  
ATOM   1325  CA  PRO A 233       0.737 -35.067  70.929  1.00185.78           C  
ANISOU 1325  CA  PRO A 233    24522  24318  21748   3686   -749    999       C  
ATOM   1326  C   PRO A 233      -0.612 -34.403  70.725  1.00187.82           C  
ANISOU 1326  C   PRO A 233    25017  24387  21959   3550   -893   1062       C  
ATOM   1327  O   PRO A 233      -0.705 -33.189  70.512  1.00181.52           O  
ANISOU 1327  O   PRO A 233    24325  23683  20962   3355   -858   1073       O  
ATOM   1328  CB  PRO A 233       1.702 -34.146  71.692  1.00189.67           C  
ANISOU 1328  CB  PRO A 233    24835  25109  22122   3578   -649   1080       C  
ATOM   1329  CG  PRO A 233       2.997 -34.163  70.912  1.00189.37           C  
ANISOU 1329  CG  PRO A 233    24743  25273  21936   3590   -470    992       C  
ATOM   1330  CD  PRO A 233       2.632 -34.484  69.502  1.00183.63           C  
ANISOU 1330  CD  PRO A 233    24241  24403  21128   3643   -467    829       C  
ATOM   1331  N   ASP A 234      -1.667 -35.211  70.788  1.00191.95           N  
ANISOU 1331  N   ASP A 234    25611  24639  22681   3653  -1058   1138       N  
ATOM   1332  CA  ASP A 234      -3.027 -34.704  70.731  1.00204.84           C  
ANISOU 1332  CA  ASP A 234    27458  26086  24286   3544  -1201   1291       C  
ATOM   1333  C   ASP A 234      -3.427 -34.190  72.109  1.00221.34           C  
ANISOU 1333  C   ASP A 234    29430  28249  26419   3571  -1279   1558       C  
ATOM   1334  O   ASP A 234      -3.207 -34.869  73.117  1.00225.54           O  
ANISOU 1334  O   ASP A 234    29701  28828  27166   3768  -1327   1675       O  
ATOM   1335  CB  ASP A 234      -3.973 -35.813  70.265  1.00205.79           C  
ANISOU 1335  CB  ASP A 234    27689  25879  24622   3655  -1382   1320       C  
ATOM   1336  CG  ASP A 234      -5.353 -35.300  69.897  1.00208.19           C  
ANISOU 1336  CG  ASP A 234    28260  25992  24851   3510  -1506   1490       C  
ATOM   1337  OD1 ASP A 234      -5.747 -34.221  70.386  1.00207.57           O  
ANISOU 1337  OD1 ASP A 234    28240  26016  24612   3382  -1476   1667       O  
ATOM   1338  OD2 ASP A 234      -6.044 -35.981  69.108  1.00210.20           O  
ANISOU 1338  OD2 ASP A 234    28678  25989  25199   3524  -1637   1455       O  
ATOM   1339  N   LYS A 235      -4.010 -32.990  72.155  1.00224.62           N  
ANISOU 1339  N   LYS A 235    30025  28693  26627   3397  -1283   1661       N  
ATOM   1340  CA  LYS A 235      -4.429 -32.437  73.439  1.00226.93           C  
ANISOU 1340  CA  LYS A 235    30253  29059  26912   3464  -1372   1914       C  
ATOM   1341  C   LYS A 235      -5.614 -33.199  74.016  1.00226.55           C  
ANISOU 1341  C   LYS A 235    30186  28811  27081   3669  -1574   2231       C  
ATOM   1342  O   LYS A 235      -5.702 -33.387  75.235  1.00226.35           O  
ANISOU 1342  O   LYS A 235    29946  28876  27180   3888  -1663   2446       O  
ATOM   1343  CB  LYS A 235      -4.769 -30.955  73.311  1.00228.82           C  
ANISOU 1343  CB  LYS A 235    30715  29361  26864   3239  -1323   1950       C  
ATOM   1344  CG  LYS A 235      -4.912 -30.261  74.662  1.00234.67           C  
ANISOU 1344  CG  LYS A 235    31399  30224  27541   3334  -1404   2144       C  
ATOM   1345  CD  LYS A 235      -3.684 -30.470  75.534  1.00240.36           C  
ANISOU 1345  CD  LYS A 235    31810  31171  28344   3454  -1375   2033       C  
ATOM   1346  CE  LYS A 235      -4.005 -30.274  77.008  1.00239.68           C  
ANISOU 1346  CE  LYS A 235    31605  31187  28274   3684  -1508   2261       C  
ATOM   1347  NZ  LYS A 235      -4.100 -28.840  77.384  1.00239.23           N  
ANISOU 1347  NZ  LYS A 235    31738  31207  27951   3560  -1535   2270       N  
ATOM   1348  N   LYS A 236      -6.540 -33.630  73.159  1.00226.69           N  
ANISOU 1348  N   LYS A 236    30406  28570  27154   3618  -1662   2296       N  
ATOM   1349  CA  LYS A 236      -7.742 -34.308  73.632  1.00218.75           C  
ANISOU 1349  CA  LYS A 236    29391  27353  26373   3798  -1889   2671       C  
ATOM   1350  C   LYS A 236      -7.399 -35.583  74.394  1.00205.66           C  
ANISOU 1350  C   LYS A 236    27363  25685  25095   4096  -1993   2744       C  
ATOM   1351  O   LYS A 236      -7.752 -35.735  75.569  1.00205.66           O  
ANISOU 1351  O   LYS A 236    27138  25760  25242   4338  -2106   3066       O  
ATOM   1352  CB  LYS A 236      -8.652 -34.626  72.444  1.00224.17           C  
ANISOU 1352  CB  LYS A 236    30355  27752  27067   3657  -1974   2690       C  
ATOM   1353  CG  LYS A 236      -9.844 -35.502  72.788  1.00225.13           C  
ANISOU 1353  CG  LYS A 236    30449  27608  27481   3835  -2251   3102       C  
ATOM   1354  CD  LYS A 236     -10.569 -35.967  71.533  1.00226.22           C  
ANISOU 1354  CD  LYS A 236    30849  27447  27658   3684  -2356   3057       C  
ATOM   1355  CE  LYS A 236      -9.642 -36.780  70.640  1.00227.66           C  
ANISOU 1355  CE  LYS A 236    30989  27571  27940   3682  -2303   2585       C  
ATOM   1356  NZ  LYS A 236     -10.191 -36.993  69.271  1.00227.38           N  
ANISOU 1356  NZ  LYS A 236    31251  27305  27838   3515  -2364   2435       N  
ATOM   1357  N   GLN A 237      -6.730 -36.525  73.729  1.00217.52           N  
ANISOU 1357  N   GLN A 237    28781  27107  26761   4111  -1952   2465       N  
ATOM   1358  CA  GLN A 237      -6.473 -37.827  74.334  1.00213.16           C  
ANISOU 1358  CA  GLN A 237    27872  26512  26609   4382  -2038   2541       C  
ATOM   1359  C   GLN A 237      -5.670 -37.678  75.622  1.00207.45           C  
ANISOU 1359  C   GLN A 237    26781  26120  25920   4547  -1923   2608       C  
ATOM   1360  O   GLN A 237      -4.593 -37.074  75.628  1.00208.87           O  
ANISOU 1360  O   GLN A 237    26943  26547  25871   4430  -1713   2363       O  
ATOM   1361  CB  GLN A 237      -5.741 -38.729  73.342  1.00212.10           C  
ANISOU 1361  CB  GLN A 237    27757  26262  26570   4362  -1969   2184       C  
ATOM   1362  CG  GLN A 237      -6.624 -39.274  72.222  1.00209.66           C  
ANISOU 1362  CG  GLN A 237    27732  25580  26347   4296  -2160   2144       C  
ATOM   1363  CD  GLN A 237      -7.836 -40.037  72.733  1.00202.92           C  
ANISOU 1363  CD  GLN A 237    26771  24453  25875   4462  -2474   2553       C  
ATOM   1364  OE1 GLN A 237      -8.931 -39.485  72.846  1.00197.70           O  
ANISOU 1364  OE1 GLN A 237    26277  23700  25141   4398  -2612   2876       O  
ATOM   1365  NE2 GLN A 237      -7.646 -41.317  73.030  1.00201.29           N  
ANISOU 1365  NE2 GLN A 237    26273  24118  26090   4685  -2589   2581       N  
ATOM   1366  N   ARG A 238      -6.201 -38.229  76.706  1.00202.42           N  
ANISOU 1366  N   ARG A 238    25829  25502  25579   4832  -2073   2967       N  
ATOM   1367  CA  ARG A 238      -5.528 -38.323  77.992  1.00190.02           C  
ANISOU 1367  CA  ARG A 238    23831  24257  24112   5056  -1984   3065       C  
ATOM   1368  C   ARG A 238      -5.099 -39.762  78.241  1.00188.89           C  
ANISOU 1368  C   ARG A 238    23266  24094  24409   5274  -1971   3079       C  
ATOM   1369  O   ARG A 238      -5.579 -40.694  77.592  1.00197.75           O  
ANISOU 1369  O   ARG A 238    24426  24906  25805   5303  -2112   3096       O  
ATOM   1370  CB  ARG A 238      -6.423 -37.826  79.133  1.00183.67           C  
ANISOU 1370  CB  ARG A 238    22918  23562  23304   5289  -2144   3499       C  
ATOM   1371  CG  ARG A 238      -6.231 -36.354  79.472  1.00174.48           C  
ANISOU 1371  CG  ARG A 238    21984  22611  21699   5157  -2060   3429       C  
ATOM   1372  CD  ARG A 238      -7.164 -35.905  80.586  1.00165.96           C  
ANISOU 1372  CD  ARG A 238    20843  21528  20688   5016  -2152   3601       C  
ATOM   1373  NE  ARG A 238      -8.553 -35.798  80.145  1.00164.43           N  
ANISOU 1373  NE  ARG A 238    20920  21001  20555   4726  -2301   3731       N  
ATOM   1374  CZ  ARG A 238      -9.476 -36.735  80.335  1.00178.53           C  
ANISOU 1374  CZ  ARG A 238    22574  22515  22744   4552  -2474   3788       C  
ATOM   1375  NH1 ARG A 238      -9.164 -37.863  80.959  1.00183.89           N  
ANISOU 1375  NH1 ARG A 238    22873  23202  23796   4647  -2506   3711       N  
ATOM   1376  NH2 ARG A 238     -10.714 -36.545  79.900  1.00190.14           N  
ANISOU 1376  NH2 ARG A 238    24315  23708  24220   4276  -2628   3887       N  
ATOM   1377  N   THR A 239      -4.194 -39.936  79.206  1.00188.29           N  
ANISOU 1377  N   THR A 239    22779  24354  24409   5427  -1802   3078       N  
ATOM   1378  CA  THR A 239      -3.722 -41.276  79.546  1.00174.17           C  
ANISOU 1378  CA  THR A 239    20528  22601  23046   5640  -1736   3118       C  
ATOM   1379  C   THR A 239      -4.841 -42.173  80.054  1.00163.13           C  
ANISOU 1379  C   THR A 239    18934  20930  22116   5587  -1980   3304       C  
ATOM   1380  O   THR A 239      -4.771 -43.397  79.892  1.00142.86           O  
ANISOU 1380  O   THR A 239    16155  18193  19934   5621  -2016   3248       O  
ATOM   1381  CB  THR A 239      -2.601 -41.207  80.580  1.00175.69           C  
ANISOU 1381  CB  THR A 239    20302  23238  23213   5745  -1483   3095       C  
ATOM   1382  OG1 THR A 239      -1.780 -40.059  80.334  1.00172.57           O  
ANISOU 1382  OG1 THR A 239    20192  23024  22351   5474  -1314   2823       O  
ATOM   1383  CG2 THR A 239      -1.785 -42.478  80.562  1.00177.98           C  
ANISOU 1383  CG2 THR A 239    20218  23577  23831   5845  -1298   3014       C  
ATOM   1384  N   PHE A 240      -5.883 -41.596  80.645  1.00187.53           N  
ANISOU 1384  N   PHE A 240    22171  23925  25156   5350  -2153   3385       N  
ATOM   1385  CA  PHE A 240      -6.947 -42.379  81.253  1.00200.98           C  
ANISOU 1385  CA  PHE A 240    23799  25378  27187   5156  -2389   3362       C  
ATOM   1386  C   PHE A 240      -8.290 -41.728  80.956  1.00220.23           C  
ANISOU 1386  C   PHE A 240    26650  27557  29469   4955  -2632   3459       C  
ATOM   1387  O   PHE A 240      -8.381 -40.524  80.709  1.00214.32           O  
ANISOU 1387  O   PHE A 240    26163  26890  28378   4898  -2572   3559       O  
ATOM   1388  CB  PHE A 240      -6.751 -42.509  82.769  1.00193.65           C  
ANISOU 1388  CB  PHE A 240    22556  24695  26328   5094  -2285   3269       C  
ATOM   1389  CG  PHE A 240      -5.518 -43.273  83.158  1.00176.98           C  
ANISOU 1389  CG  PHE A 240    20024  22833  24389   5222  -2036   3168       C  
ATOM   1390  CD1 PHE A 240      -5.539 -44.653  83.234  1.00172.17           C  
ANISOU 1390  CD1 PHE A 240    19190  22101  24125   5235  -2082   3058       C  
ATOM   1391  CD2 PHE A 240      -4.335 -42.609  83.445  1.00156.72           C  
ANISOU 1391  CD2 PHE A 240    17310  20647  21591   5329  -1750   3166       C  
ATOM   1392  CE1 PHE A 240      -4.407 -45.360  83.589  1.00166.00           C  
ANISOU 1392  CE1 PHE A 240    18031  21549  23491   5308  -1820   2971       C  
ATOM   1393  CE2 PHE A 240      -3.198 -43.313  83.800  1.00144.07           C  
ANISOU 1393  CE2 PHE A 240    15331  19287  20123   5406  -1492   3077       C  
ATOM   1394  CZ  PHE A 240      -3.236 -44.690  83.871  1.00156.41           C  
ANISOU 1394  CZ  PHE A 240    16664  20702  22061   5375  -1513   2989       C  
ATOM   1395  N   GLN A 241      -9.334 -42.551  80.979  1.00205.37           N  
ANISOU 1395  N   GLN A 241    24861  25399  27770   4874  -2885   3395       N  
ATOM   1396  CA  GLN A 241     -10.694 -42.094  80.719  1.00210.84           C  
ANISOU 1396  CA  GLN A 241    25971  25859  28279   4699  -3100   3443       C  
ATOM   1397  C   GLN A 241     -11.639 -42.604  81.798  1.00212.01           C  
ANISOU 1397  C   GLN A 241    26077  26029  28446   4668  -3173   3351       C  
ATOM   1398  O   GLN A 241     -12.477 -41.859  82.308  1.00213.02           O  
ANISOU 1398  O   GLN A 241    26293  26245  28399   4564  -3100   3555       O  
ATOM   1399  CB  GLN A 241     -11.176 -42.577  79.348  1.00217.84           C  
ANISOU 1399  CB  GLN A 241    27164  26441  29166   4739  -3260   3472       C  
ATOM   1400  CG  GLN A 241     -10.307 -42.161  78.177  1.00225.38           C  
ANISOU 1400  CG  GLN A 241    28159  27351  30124   4797  -3170   3609       C  
ATOM   1401  CD  GLN A 241     -10.032 -43.307  77.222  1.00232.24           C  
ANISOU 1401  CD  GLN A 241    29018  27993  31230   4996  -3250   3540       C  
ATOM   1402  OE1 GLN A 241     -10.280 -43.202  76.022  1.00237.17           O  
ANISOU 1402  OE1 GLN A 241    29921  28382  31811   4948  -3308   3620       O  
ATOM   1403  NE2 GLN A 241      -9.509 -44.407  77.752  1.00233.01           N  
ANISOU 1403  NE2 GLN A 241    28774  28179  31580   5191  -3205   3396       N  



If you find results from this site helpful for your research, please cite one of our papers:

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