CNRS Nantes University UFIP UFIP
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***  6pdb  ***

elNémo ID: 211018161858104671

Job options:

ID        	=	 211018161858104671
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  
ATOM   1404  N   THR A 284     -10.859 -19.986  74.642  1.00163.40           N  
ANISOU 1404  N   THR A 284    24600  21061  16426   2127   -938   3431       N  
ATOM   1405  CA  THR A 284     -11.039 -20.508  73.292  1.00180.17           C  
ANISOU 1405  CA  THR A 284    26655  23152  18649   1896   -754   3381       C  
ATOM   1406  C   THR A 284     -10.483 -19.548  72.250  1.00196.01           C  
ANISOU 1406  C   THR A 284    28574  25257  20644   1536   -522   3121       C  
ATOM   1407  O   THR A 284     -10.211 -19.928  71.110  1.00208.80           O  
ANISOU 1407  O   THR A 284    30041  26919  22376   1372   -380   2957       O  
ATOM   1408  CB  THR A 284     -12.519 -20.772  72.983  1.00189.55           C  
ANISOU 1408  CB  THR A 284    27755  24247  20018   1683   -672   3614       C  
ATOM   1409  OG1 THR A 284     -12.666 -21.139  71.606  1.00198.06           O  
ANISOU 1409  OG1 THR A 284    28905  25303  21046   1521   -498   3609       O  
ATOM   1410  CG2 THR A 284     -13.343 -19.529  73.266  1.00185.10           C  
ANISOU 1410  CG2 THR A 284    27076  23731  19522   1378   -569   3652       C  
ATOM   1411  N   GLU A 285     -10.295 -18.308  72.665  1.00190.88           N  
ANISOU 1411  N   GLU A 285    28002  24652  19872   1445   -501   3090       N  
ATOM   1412  CA  GLU A 285      -9.843 -17.232  71.808  1.00193.22           C  
ANISOU 1412  CA  GLU A 285    28190  25045  20182   1120   -296   2913       C  
ATOM   1413  C   GLU A 285      -8.365 -16.942  72.072  1.00193.63           C  
ANISOU 1413  C   GLU A 285    27964  25184  20421   1107   -442   2560       C  
ATOM   1414  O   GLU A 285      -7.642 -17.761  72.648  1.00192.85           O  
ANISOU 1414  O   GLU A 285    27727  25096  20451   1310   -640   2420       O  
ATOM   1415  CB  GLU A 285     -10.701 -15.978  72.026  1.00196.53           C  
ANISOU 1415  CB  GLU A 285    28885  25430  20356   1000   -167   3158       C  
ATOM   1416  CG  GLU A 285     -12.174 -16.217  72.260  1.00199.10           C  
ANISOU 1416  CG  GLU A 285    29164  25702  20784    955   -130   3416       C  
ATOM   1417  CD  GLU A 285     -12.912 -14.924  72.549  1.00198.20           C  
ANISOU 1417  CD  GLU A 285    28909  25632  20766    725    -42   3449       C  
ATOM   1418  OE1 GLU A 285     -12.331 -13.846  72.301  1.00196.77           O  
ANISOU 1418  OE1 GLU A 285    28858  25484  20423    623     68   3374       O  
ATOM   1419  OE2 GLU A 285     -14.065 -14.984  73.026  1.00196.63           O  
ANISOU 1419  OE2 GLU A 285    28462  25440  20808    639   -102   3554       O  
ATOM   1420  N   ASP A 286      -7.917 -15.783  71.619  1.00198.63           N  
ANISOU 1420  N   ASP A 286    28491  25889  21089    860   -335   2449       N  
ATOM   1421  CA  ASP A 286      -6.590 -15.197  71.684  1.00197.25           C  
ANISOU 1421  CA  ASP A 286    28047  25796  21104    770   -453   2189       C  
ATOM   1422  C   ASP A 286      -6.748 -13.993  72.606  1.00199.94           C  
ANISOU 1422  C   ASP A 286    28592  26047  21329    749   -584   2228       C  
ATOM   1423  O   ASP A 286      -7.743 -13.907  73.324  1.00201.93           O  
ANISOU 1423  O   ASP A 286    29181  26196  21347    896   -614   2437       O  
ATOM   1424  CB  ASP A 286      -6.052 -14.865  70.294  1.00200.05           C  
ANISOU 1424  CB  ASP A 286    28078  26308  21624    527   -231   2091       C  
ATOM   1425  CG  ASP A 286      -5.494 -16.088  69.589  1.00207.53           C  
ANISOU 1425  CG  ASP A 286    28801  27353  22698    630   -200   1972       C  
ATOM   1426  OD1 ASP A 286      -5.130 -17.056  70.294  1.00202.90           O  
ANISOU 1426  OD1 ASP A 286    28233  26717  22143    853   -392   1906       O  
ATOM   1427  OD2 ASP A 286      -5.421 -16.082  68.341  1.00213.93           O  
ANISOU 1427  OD2 ASP A 286    29409  28303  23573    509     22   1950       O  
ATOM   1428  N   PHE A 287      -5.771 -13.082  72.616  1.00205.01           N  
ANISOU 1428  N   PHE A 287    29037  26723  22134    596   -687   2051       N  
ATOM   1429  CA  PHE A 287      -5.739 -11.986  73.590  1.00207.53           C  
ANISOU 1429  CA  PHE A 287    29549  26927  22376    601   -891   2023       C  
ATOM   1430  C   PHE A 287      -7.116 -11.474  74.009  1.00214.18           C  
ANISOU 1430  C   PHE A 287    30815  27658  22907    665   -791   2272       C  
ATOM   1431  O   PHE A 287      -7.333 -11.213  75.196  1.00205.04           O  
ANISOU 1431  O   PHE A 287    29930  26399  21576    887  -1022   2293       O  
ATOM   1432  CB  PHE A 287      -4.929 -10.808  73.042  1.00205.33           C  
ANISOU 1432  CB  PHE A 287    29007  26681  22329    312   -894   1904       C  
ATOM   1433  CG  PHE A 287      -5.065  -9.552  73.859  1.00197.07           C  
ANISOU 1433  CG  PHE A 287    28190  25481  21208    274  -1076   1882       C  
ATOM   1434  CD1 PHE A 287      -4.369  -9.404  75.048  1.00185.52           C  
ANISOU 1434  CD1 PHE A 287    26805  23925  19759    431  -1467   1712       C  
ATOM   1435  CD2 PHE A 287      -5.896  -8.521  73.444  1.00196.24           C  
ANISOU 1435  CD2 PHE A 287    28227  25327  21009     90   -853   2030       C  
ATOM   1436  CE1 PHE A 287      -4.495  -8.253  75.803  1.00184.73           C  
ANISOU 1436  CE1 PHE A 287    26946  23663  19578    423  -1670   1661       C  
ATOM   1437  CE2 PHE A 287      -6.027  -7.369  74.196  1.00194.49           C  
ANISOU 1437  CE2 PHE A 287    28244  24942  20710     75  -1029   1999       C  
ATOM   1438  CZ  PHE A 287      -5.325  -7.235  75.377  1.00192.89           C  
ANISOU 1438  CZ  PHE A 287    28144  24625  20520    250  -1457   1800       C  
ATOM   1439  N   GLN A 288      -8.045 -11.303  73.065  1.00216.08           N  
ANISOU 1439  N   GLN A 288    31114  27932  23053    491   -447   2483       N  
ATOM   1440  CA  GLN A 288      -9.416 -10.980  73.453  1.00219.24           C  
ANISOU 1440  CA  GLN A 288    31934  28244  23122    576   -325   2805       C  
ATOM   1441  C   GLN A 288      -9.991 -12.042  74.391  1.00216.37           C  
ANISOU 1441  C   GLN A 288    31811  27825  22574    959   -499   2979       C  
ATOM   1442  O   GLN A 288     -10.680 -11.714  75.366  1.00214.15           O  
ANISOU 1442  O   GLN A 288    31750  27478  22141   1154   -604   3126       O  
ATOM   1443  CB  GLN A 288     -10.286 -10.833  72.205  1.00225.09           C  
ANISOU 1443  CB  GLN A 288    32654  29065  23804    317     99   3034       C  
ATOM   1444  CG  GLN A 288     -11.455  -9.878  72.363  1.00229.93           C  
ANISOU 1444  CG  GLN A 288    33358  29663  24342    219    280   3249       C  
ATOM   1445  CD  GLN A 288     -11.039  -8.420  72.281  1.00237.20           C  
ANISOU 1445  CD  GLN A 288    34430  30528  25168     19    341   3214       C  
ATOM   1446  OE1 GLN A 288      -9.850  -8.096  72.254  1.00238.74           O  
ANISOU 1446  OE1 GLN A 288    34356  30729  25625    -64    153   2911       O  
ATOM   1447  NE2 GLN A 288     -12.023  -7.531  72.235  1.00240.30           N  
ANISOU 1447  NE2 GLN A 288    34546  30992  25766    -96    522   3279       N  
ATOM   1448  N   GLY A 289      -9.723 -13.320  74.107  1.00214.52           N  
ANISOU 1448  N   GLY A 289    31381  27645  22483   1054   -527   2927       N  
ATOM   1449  CA  GLY A 289     -10.111 -14.388  75.022  1.00210.78           C  
ANISOU 1449  CA  GLY A 289    31032  27132  21922   1433   -723   3082       C  
ATOM   1450  C   GLY A 289      -9.393 -14.318  76.356  1.00211.06           C  
ANISOU 1450  C   GLY A 289    31067  27161  21964   1712  -1067   2910       C  
ATOM   1451  O   GLY A 289      -9.972 -14.628  77.400  1.00215.25           O  
ANISOU 1451  O   GLY A 289    31715  27672  22396   2029  -1215   3081       O  
ATOM   1452  N   LEU A 290      -8.109 -13.948  76.332  1.00228.05           N  
ANISOU 1452  N   LEU A 290    32965  29356  24327   1569  -1189   2553       N  
ATOM   1453  CA  LEU A 290      -7.365 -13.746  77.572  1.00202.28           C  
ANISOU 1453  CA  LEU A 290    29697  26092  21067   1790  -1520   2370       C  
ATOM   1454  C   LEU A 290      -8.075 -12.738  78.461  1.00204.84           C  
ANISOU 1454  C   LEU A 290    30407  26324  21099   1952  -1634   2503       C  
ATOM   1455  O   LEU A 290      -8.247 -12.963  79.664  1.00179.97           O  
ANISOU 1455  O   LEU A 290    27401  23186  17793   2340  -1868   2566       O  
ATOM   1456  CB  LEU A 290      -5.943 -13.275  77.255  1.00177.31           C  
ANISOU 1456  CB  LEU A 290    26226  22970  18172   1535  -1618   2031       C  
ATOM   1457  CG  LEU A 290      -5.037 -12.894  78.431  1.00155.79           C  
ANISOU 1457  CG  LEU A 290    23479  20238  15476   1679  -1974   1814       C  
ATOM   1458  CD1 LEU A 290      -4.812 -14.082  79.349  1.00152.76           C  
ANISOU 1458  CD1 LEU A 290    23001  19954  15089   2039  -2129   1816       C  
ATOM   1459  CD2 LEU A 290      -3.711 -12.315  77.953  1.00154.50           C  
ANISOU 1459  CD2 LEU A 290    23011  20095  15596   1370  -2061   1566       C  
ATOM   1460  N   ARG A 291      -8.477 -11.610  77.878  1.00202.04           N  
ANISOU 1460  N   ARG A 291    30206  25894  20666   1682  -1464   2555       N  
ATOM   1461  CA  ARG A 291      -9.267 -10.616  78.593  1.00220.50           C  
ANISOU 1461  CA  ARG A 291    32956  28132  22692   1828  -1522   2718       C  
ATOM   1462  C   ARG A 291     -10.498 -11.249  79.232  1.00235.91           C  
ANISOU 1462  C   ARG A 291    34706  30137  24793   1998  -1393   2920       C  
ATOM   1463  O   ARG A 291     -10.720 -11.141  80.442  1.00237.40           O  
ANISOU 1463  O   ARG A 291    34869  30325  25005   2250  -1559   2879       O  
ATOM   1464  CB  ARG A 291      -9.715  -9.524  77.621  1.00223.81           C  
ANISOU 1464  CB  ARG A 291    33454  28495  23087   1447  -1224   2803       C  
ATOM   1465  CG  ARG A 291     -10.347  -8.319  78.289  1.00228.26           C  
ANISOU 1465  CG  ARG A 291    34206  28966  23557   1478  -1235   2832       C  
ATOM   1466  CD  ARG A 291     -11.091  -7.450  77.284  1.00230.09           C  
ANISOU 1466  CD  ARG A 291    34309  29213  23903   1094   -829   2957       C  
ATOM   1467  NE  ARG A 291     -10.327  -7.185  76.067  1.00233.97           N  
ANISOU 1467  NE  ARG A 291    34806  29704  24387    756   -703   2917       N  
ATOM   1468  CZ  ARG A 291     -10.628  -6.228  75.196  1.00228.03           C  
ANISOU 1468  CZ  ARG A 291    33996  28959  23685    415   -396   3001       C  
ATOM   1469  NH1 ARG A 291      -9.895  -6.055  74.104  1.00219.95           N  
ANISOU 1469  NH1 ARG A 291    32512  28037  23022     73   -248   2837       N  
ATOM   1470  NH2 ARG A 291     -11.650  -5.423  75.434  1.00228.71           N  
ANISOU 1470  NH2 ARG A 291    33977  29057  23865    394   -218   3087       N  
ATOM   1471  N   ALA A 292     -11.310 -11.923  78.410  1.00228.94           N  
ANISOU 1471  N   ALA A 292    33553  29308  24124   1790  -1103   3090       N  
ATOM   1472  CA  ALA A 292     -12.568 -12.496  78.882  1.00224.86           C  
ANISOU 1472  CA  ALA A 292    32702  28836  23898   1782  -1016   3247       C  
ATOM   1473  C   ALA A 292     -12.343 -13.540  79.968  1.00226.66           C  
ANISOU 1473  C   ALA A 292    32828  29090  24204   2131  -1248   3236       C  
ATOM   1474  O   ALA A 292     -12.979 -13.494  81.025  1.00235.57           O  
ANISOU 1474  O   ALA A 292    33824  30229  25451   2252  -1315   3275       O  
ATOM   1475  CB  ALA A 292     -13.336 -13.097  77.706  1.00221.26           C  
ANISOU 1475  CB  ALA A 292    31995  28422  23651   1467   -772   3390       C  
ATOM   1476  N   GLU A 293     -11.445 -14.497  79.720  1.00237.14           N  
ANISOU 1476  N   GLU A 293    34181  30444  25478   2293  -1361   3183       N  
ATOM   1477  CA  GLU A 293     -11.209 -15.561  80.691  1.00211.30           C  
ANISOU 1477  CA  GLU A 293    30729  27228  22328   2620  -1553   3180       C  
ATOM   1478  C   GLU A 293     -10.729 -14.995  82.022  1.00214.11           C  
ANISOU 1478  C   GLU A 293    31166  27621  22565   2916  -1789   3036       C  
ATOM   1479  O   GLU A 293     -11.273 -15.324  83.084  1.00205.58           O  
ANISOU 1479  O   GLU A 293    29881  26578  21653   3076  -1833   3088       O  
ATOM   1480  CB  GLU A 293     -10.199 -16.563  80.131  1.00191.81           C  
ANISOU 1480  CB  GLU A 293    28269  24809  19802   2758  -1640   3125       C  
ATOM   1481  CG  GLU A 293      -9.748 -17.626  81.124  1.00170.81           C  
ANISOU 1481  CG  GLU A 293    25380  22246  17273   3118  -1838   3100       C  
ATOM   1482  CD  GLU A 293     -10.572 -18.903  81.041  1.00152.63           C  
ANISOU 1482  CD  GLU A 293    22773  19913  15305   3088  -1740   3283       C  
ATOM   1483  OE1 GLU A 293     -11.722 -18.850  80.554  1.00154.86           O  
ANISOU 1483  OE1 GLU A 293    22994  20101  15744   2790  -1573   3429       O  
ATOM   1484  OE2 GLU A 293     -10.066 -19.966  81.458  1.00139.37           O  
ANISOU 1484  OE2 GLU A 293    20891  18311  13751   3343  -1855   3273       O  
ATOM   1485  N   VAL A 294      -9.692 -14.157  81.983  1.00215.96           N  
ANISOU 1485  N   VAL A 294    31697  27843  22513   2976  -1974   2839       N  
ATOM   1486  CA  VAL A 294      -9.169 -13.542  83.201  1.00221.58           C  
ANISOU 1486  CA  VAL A 294    32519  28579  23095   3249  -2257   2657       C  
ATOM   1487  C   VAL A 294     -10.259 -12.746  83.911  1.00222.09           C  
ANISOU 1487  C   VAL A 294    32581  28584  23220   3229  -2140   2725       C  
ATOM   1488  O   VAL A 294     -10.429 -12.846  85.132  1.00218.42           O  
ANISOU 1488  O   VAL A 294    32005  28175  22810   3494  -2247   2689       O  
ATOM   1489  CB  VAL A 294      -7.952 -12.659  82.871  1.00224.97           C  
ANISOU 1489  CB  VAL A 294    33288  28960  23232   3204  -2542   2420       C  
ATOM   1490  CG1 VAL A 294      -7.633 -11.738  84.036  1.00222.65           C  
ANISOU 1490  CG1 VAL A 294    33159  28631  22805   3409  -2844   2215       C  
ATOM   1491  CG2 VAL A 294      -6.757 -13.524  82.521  1.00228.78           C  
ANISOU 1491  CG2 VAL A 294    33413  29545  23967   3097  -2601   2204       C  
ATOM   1492  N   GLU A 295     -11.009 -11.938  83.156  1.00220.90           N  
ANISOU 1492  N   GLU A 295    32525  28340  23065   2914  -1906   2821       N  
ATOM   1493  CA  GLU A 295     -12.086 -11.151  83.750  1.00225.89           C  
ANISOU 1493  CA  GLU A 295    33125  28937  23765   2873  -1787   2891       C  
ATOM   1494  C   GLU A 295     -13.118 -12.045  84.433  1.00254.99           C  
ANISOU 1494  C   GLU A 295    36439  32701  27746   2919  -1698   3062       C  
ATOM   1495  O   GLU A 295     -13.519 -11.787  85.574  1.00250.14           O  
ANISOU 1495  O   GLU A 295    35783  32106  27154   3114  -1765   3042       O  
ATOM   1496  CB  GLU A 295     -12.751 -10.280  82.684  1.00203.32           C  
ANISOU 1496  CB  GLU A 295    30318  26017  20917   2485  -1519   2987       C  
ATOM   1497  CG  GLU A 295     -12.965  -8.838  83.116  1.00190.69           C  
ANISOU 1497  CG  GLU A 295    28959  24326  19167   2498  -1539   2901       C  
ATOM   1498  CD  GLU A 295     -11.686  -8.022  83.071  1.00185.02           C  
ANISOU 1498  CD  GLU A 295    28678  23482  18139   2586  -1817   2663       C  
ATOM   1499  OE1 GLU A 295     -11.032  -8.002  82.007  1.00179.06           O  
ANISOU 1499  OE1 GLU A 295    28035  22694  17305   2363  -1797   2641       O  
ATOM   1500  OE2 GLU A 295     -11.333  -7.402  84.099  1.00185.93           O  
ANISOU 1500  OE2 GLU A 295    29021  23526  18097   2855  -2091   2485       O  
ATOM   1501  N   THR A 296     -13.573 -13.095  83.740  1.00232.29           N  
ANISOU 1501  N   THR A 296    33305  29852  25101   2722  -1569   3223       N  
ATOM   1502  CA  THR A 296     -14.557 -14.004  84.325  1.00240.77           C  
ANISOU 1502  CA  THR A 296    34073  30950  26460   2735  -1540   3369       C  
ATOM   1503  C   THR A 296     -14.040 -14.649  85.608  1.00235.30           C  
ANISOU 1503  C   THR A 296    33266  30334  25803   3104  -1733   3299       C  
ATOM   1504  O   THR A 296     -14.794 -14.809  86.576  1.00239.92           O  
ANISOU 1504  O   THR A 296    33844  30924  26389   3431  -1681   3317       O  
ATOM   1505  CB  THR A 296     -14.959 -15.075  83.307  1.00245.72           C  
ANISOU 1505  CB  THR A 296    34541  31546  27275   2531  -1431   3502       C  
ATOM   1506  OG1 THR A 296     -13.786 -15.717  82.783  1.00252.23           O  
ANISOU 1506  OG1 THR A 296    35391  32406  28039   2591  -1519   3437       O  
ATOM   1507  CG2 THR A 296     -15.764 -14.458  82.169  1.00245.09           C  
ANISOU 1507  CG2 THR A 296    34547  31404  27171   2223  -1200   3572       C  
ATOM   1508  N   ILE A 297     -12.764 -15.039  85.632  1.00260.58           N  
ANISOU 1508  N   ILE A 297    36545  33594  28871   3341  -1887   3162       N  
ATOM   1509  CA  ILE A 297     -12.182 -15.611  86.844  1.00214.96           C  
ANISOU 1509  CA  ILE A 297    30626  27929  23121   3713  -2061   3069       C  
ATOM   1510  C   ILE A 297     -12.025 -14.548  87.928  1.00227.92           C  
ANISOU 1510  C   ILE A 297    32445  29591  24562   3950  -2183   2911       C  
ATOM   1511  O   ILE A 297     -12.341 -14.787  89.099  1.00224.19           O  
ANISOU 1511  O   ILE A 297    31800  29194  24188   4156  -2215   2913       O  
ATOM   1512  CB  ILE A 297     -10.841 -16.295  86.512  1.00160.55           C  
ANISOU 1512  CB  ILE A 297    23735  21123  16144   3888  -2211   2948       C  
ATOM   1513  CG1 ILE A 297     -11.063 -17.549  85.660  1.00170.96           C  
ANISOU 1513  CG1 ILE A 297    24836  22425  17698   3736  -2096   3107       C  
ATOM   1514  CG2 ILE A 297     -10.078 -16.642  87.778  1.00 98.16           C  
ANISOU 1514  CG2 ILE A 297    15683  13380   8235   4270  -2406   2804       C  
ATOM   1515  CD1 ILE A 297     -11.978 -18.580  86.290  1.00172.24           C  
ANISOU 1515  CD1 ILE A 297    24642  22586  18215   3722  -2038   3270       C  
ATOM   1516  N   SER A 298     -11.564 -13.351  87.551  1.00230.14           N  
ANISOU 1516  N   SER A 298    33087  29791  24563   3915  -2258   2766       N  
ATOM   1517  CA  SER A 298     -11.319 -12.294  88.530  1.00228.53           C  
ANISOU 1517  CA  SER A 298    33117  29570  24145   4159  -2430   2575       C  
ATOM   1518  C   SER A 298     -12.605 -11.802  89.188  1.00223.46           C  
ANISOU 1518  C   SER A 298    32410  28898  23596   4132  -2264   2694       C  
ATOM   1519  O   SER A 298     -12.629 -11.558  90.401  1.00229.12           O  
ANISOU 1519  O   SER A 298    33132  29668  24256   4431  -2366   2595       O  
ATOM   1520  CB  SER A 298     -10.583 -11.133  87.862  1.00236.75           C  
ANISOU 1520  CB  SER A 298    34579  30478  24897   4059  -2584   2392       C  
ATOM   1521  OG  SER A 298      -9.438 -11.601  87.171  1.00241.03           O  
ANISOU 1521  OG  SER A 298    35161  31053  25364   4021  -2754   2290       O  
ATOM   1522  N   LYS A 299     -13.684 -11.662  88.416  1.00243.49           N  
ANISOU 1522  N   LYS A 299    34870  31367  26279   3780  -2017   2894       N  
ATOM   1523  CA  LYS A 299     -14.949 -11.186  88.969  1.00235.03           C  
ANISOU 1523  CA  LYS A 299    33956  30226  25118   4033  -1829   2930       C  
ATOM   1524  C   LYS A 299     -15.492 -12.105  90.060  1.00235.03           C  
ANISOU 1524  C   LYS A 299    33793  30336  25173   4462  -1777   2966       C  
ATOM   1525  O   LYS A 299     -16.276 -11.656  90.904  1.00241.30           O  
ANISOU 1525  O   LYS A 299    34716  31137  25831   4796  -1679   2944       O  
ATOM   1526  CB  LYS A 299     -15.973 -11.021  87.843  1.00217.58           C  
ANISOU 1526  CB  LYS A 299    31777  27921  22973   3741  -1556   3093       C  
ATOM   1527  CG  LYS A 299     -17.130 -10.089  88.172  1.00202.87           C  
ANISOU 1527  CG  LYS A 299    30132  25972  20977   3902  -1369   3111       C  
ATOM   1528  CD  LYS A 299     -17.963  -9.788  86.936  1.00190.15           C  
ANISOU 1528  CD  LYS A 299    28529  24279  19438   3549  -1121   3246       C  
ATOM   1529  CE  LYS A 299     -19.183  -8.955  87.281  1.00191.99           C  
ANISOU 1529  CE  LYS A 299    28941  24444  19563   3730   -918   3280       C  
ATOM   1530  NZ  LYS A 299     -20.038  -8.732  86.084  1.00199.01           N  
ANISOU 1530  NZ  LYS A 299    29787  25278  20551   3391   -673   3410       N  
ATOM   1531  N   GLU A 300     -15.081 -13.374  90.071  1.00226.70           N  
ANISOU 1531  N   GLU A 300    32446  29384  24305   4472  -1826   3021       N  
ATOM   1532  CA  GLU A 300     -15.452 -14.327  91.106  1.00228.80           C  
ANISOU 1532  CA  GLU A 300    32496  29800  24637   4861  -1773   3057       C  
ATOM   1533  C   GLU A 300     -14.541 -14.268  92.329  1.00235.85           C  
ANISOU 1533  C   GLU A 300    33349  30827  25435   5193  -1978   2867       C  
ATOM   1534  O   GLU A 300     -14.478 -15.241  93.088  1.00234.41           O  
ANISOU 1534  O   GLU A 300    32907  30815  25345   5457  -1959   2883       O  
ATOM   1535  CB  GLU A 300     -15.464 -15.748  90.541  1.00225.75           C  
ANISOU 1535  CB  GLU A 300    31801  29455  24517   4714  -1724   3207       C  
ATOM   1536  CG  GLU A 300     -16.559 -16.623  91.122  1.00228.89           C  
ANISOU 1536  CG  GLU A 300    32005  29966  24998   4983  -1528   3360       C  
ATOM   1537  CD  GLU A 300     -16.305 -18.092  90.883  1.00227.73           C  
ANISOU 1537  CD  GLU A 300    31530  29881  25115   4917  -1548   3461       C  
ATOM   1538  OE1 GLU A 300     -15.315 -18.620  91.433  1.00229.08           O  
ANISOU 1538  OE1 GLU A 300    31526  30162  25351   5042  -1692   3362       O  
ATOM   1539  OE2 GLU A 300     -17.086 -18.716  90.136  1.00223.66           O  
ANISOU 1539  OE2 GLU A 300    30931  29301  24750   4737  -1429   3634       O  
ATOM   1540  N   LEU A 301     -13.841 -13.155  92.544  1.00239.09           N  
ANISOU 1540  N   LEU A 301    33999  31179  25666   5183  -2173   2683       N  
ATOM   1541  CA  LEU A 301     -12.996 -13.036  93.723  1.00243.51           C  
ANISOU 1541  CA  LEU A 301    34531  31865  26126   5502  -2391   2480       C  
ATOM   1542  C   LEU A 301     -13.333 -11.848  94.605  1.00248.25           C  
ANISOU 1542  C   LEU A 301    35451  32421  26453   5817  -2436   2321       C  
ATOM   1543  O   LEU A 301     -13.107 -11.927  95.816  1.00246.11           O  
ANISOU 1543  O   LEU A 301    35137  32293  26080   6225  -2518   2179       O  
ATOM   1544  CB  LEU A 301     -11.515 -12.946  93.325  1.00239.64           C  
ANISOU 1544  CB  LEU A 301    34020  31386  25647   5290  -2680   2344       C  
ATOM   1545  CG  LEU A 301     -10.897 -14.206  92.720  1.00230.54           C  
ANISOU 1545  CG  LEU A 301    32593  30324  24677   5200  -2676   2416       C  
ATOM   1546  CD1 LEU A 301      -9.402 -14.019  92.500  1.00228.99           C  
ANISOU 1546  CD1 LEU A 301    32555  30179  24269   5343  -2966   2162       C  
ATOM   1547  CD2 LEU A 301     -11.171 -15.400  93.618  1.00228.81           C  
ANISOU 1547  CD2 LEU A 301    31961  30270  24707   5362  -2580   2514       C  
ATOM   1548  N   GLU A 302     -13.863 -10.751  94.062  1.00247.07           N  
ANISOU 1548  N   GLU A 302    35616  32084  26176   5658  -2377   2330       N  
ATOM   1549  CA  GLU A 302     -14.358  -9.726  94.971  1.00258.32           C  
ANISOU 1549  CA  GLU A 302    37348  33457  27345   6023  -2383   2191       C  
ATOM   1550  C   GLU A 302     -15.752 -10.191  95.385  1.00275.90           C  
ANISOU 1550  C   GLU A 302    39506  35773  29550   6331  -2047   2351       C  
ATOM   1551  O   GLU A 302     -16.718  -9.422  95.350  1.00281.16           O  
ANISOU 1551  O   GLU A 302    40410  36336  30080   6417  -1875   2392       O  
ATOM   1552  CB  GLU A 302     -14.367  -8.340  94.315  1.00248.31           C  
ANISOU 1552  CB  GLU A 302    36439  31960  25948   5759  -2448   2132       C  
ATOM   1553  CG  GLU A 302     -13.811  -7.243  95.223  1.00241.14           C  
ANISOU 1553  CG  GLU A 302    35833  30985  24806   6016  -2730   1859       C  
ATOM   1554  CD  GLU A 302     -13.734  -5.887  94.544  1.00231.38           C  
ANISOU 1554  CD  GLU A 302    34932  29523  23459   5720  -2814   1801       C  
ATOM   1555  OE1 GLU A 302     -14.791  -5.284  94.259  1.00230.19           O  
ANISOU 1555  OE1 GLU A 302    34982  29243  23236   5728  -2569   1896       O  
ATOM   1556  OE2 GLU A 302     -12.603  -5.464  94.222  1.00229.15           O  
ANISOU 1556  OE2 GLU A 302    34867  29147  23053   5657  -3126   1595       O  
ATOM   1557  N   LEU A 303     -15.846 -11.466  95.767  1.00269.88           N  
ANISOU 1557  N   LEU A 303    38394  35221  28928   6486  -1948   2451       N  
ATOM   1558  CA  LEU A 303     -17.047 -12.161  96.216  1.00273.07           C  
ANISOU 1558  CA  LEU A 303    38629  35788  29337   6768  -1641   2630       C  
ATOM   1559  C   LEU A 303     -17.124 -12.314  97.723  1.00281.94           C  
ANISOU 1559  C   LEU A 303    39696  37158  30271   7342  -1616   2519       C  
ATOM   1560  O   LEU A 303     -18.209 -12.189  98.301  1.00286.75           O  
ANISOU 1560  O   LEU A 303    40351  37876  30726   7678  -1375   2602       O  
ATOM   1561  CB  LEU A 303     -17.108 -13.551  95.581  1.00270.23           C  
ANISOU 1561  CB  LEU A 303    37891  35513  29269   6529  -1541   2838       C  
ATOM   1562  CG  LEU A 303     -18.297 -14.441  95.947  1.00272.24           C  
ANISOU 1562  CG  LEU A 303    37905  35959  29577   6752  -1244   3063       C  
ATOM   1563  CD1 LEU A 303     -19.624 -13.735  95.708  1.00274.90           C  
ANISOU 1563  CD1 LEU A 303    38438  36216  29797   6792  -1007   3188       C  
ATOM   1564  CD2 LEU A 303     -18.229 -15.750  95.178  1.00269.44           C  
ANISOU 1564  CD2 LEU A 303    37217  35625  29533   6451  -1210   3246       C  
ATOM   1565  N   LEU A 304     -15.994 -12.578  98.368  1.00283.83           N  
ANISOU 1565  N   LEU A 304    39821  37513  30510   7466  -1848   2335       N  
ATOM   1566  CA  LEU A 304     -15.947 -12.708  99.813  1.00275.28           C  
ANISOU 1566  CA  LEU A 304    38673  36693  29228   8010  -1834   2200       C  
ATOM   1567  C   LEU A 304     -15.682 -11.333 100.420  1.00314.19           C  
ANISOU 1567  C   LEU A 304    44016  41494  33869   8255  -2038   1926       C  
ATOM   1568  O   LEU A 304     -15.346 -10.368  99.729  1.00309.00           O  
ANISOU 1568  O   LEU A 304    43653  40553  33199   7963  -2224   1841       O  
ATOM   1569  CB  LEU A 304     -14.865 -13.716 100.226  1.00228.86           C  
ANISOU 1569  CB  LEU A 304    32431  31022  23504   8022  -1968   2135       C  
ATOM   1570  CG  LEU A 304     -15.014 -14.637 101.453  1.00196.75           C  
ANISOU 1570  CG  LEU A 304    28044  27346  19364   8468  -1798   2155       C  
ATOM   1571  CD1 LEU A 304     -14.677 -13.958 102.782  1.00194.05           C  
ANISOU 1571  CD1 LEU A 304    27865  27159  18707   8967  -1915   1878       C  
ATOM   1572  CD2 LEU A 304     -16.403 -15.261 101.513  1.00178.97           C  
ANISOU 1572  CD2 LEU A 304    25643  25254  17105   8607  -1416   2445       C  
ATOM   1573  N   ASP A 305     -15.827 -11.253 101.734  1.00291.07           N  
ANISOU 1573  N   ASP A 305    41107  38789  30696   8800  -2002   1787       N  
ATOM   1574  CA  ASP A 305     -15.688  -9.981 102.424  1.00294.71           C  
ANISOU 1574  CA  ASP A 305    41983  39133  30862   9112  -2192   1511       C  
ATOM   1575  C   ASP A 305     -14.222  -9.558 102.484  1.00290.36           C  
ANISOU 1575  C   ASP A 305    41502  38468  30354   8957  -2630   1242       C  
ATOM   1576  O   ASP A 305     -13.345 -10.344 102.857  1.00289.73           O  
ANISOU 1576  O   ASP A 305    41104  38588  30393   8968  -2743   1181       O  
ATOM   1577  CB  ASP A 305     -16.320 -10.081 103.810  1.00300.71           C  
ANISOU 1577  CB  ASP A 305    42732  40201  31323   9773  -2002   1446       C  
ATOM   1578  CG  ASP A 305     -17.761 -10.586 103.751  1.00303.32           C  
ANISOU 1578  CG  ASP A 305    42929  40696  31622   9908  -1557   1755       C  
ATOM   1579  OD1 ASP A 305     -18.262 -10.853 102.634  1.00300.90           O  
ANISOU 1579  OD1 ASP A 305    42543  40240  31545   9485  -1419   2001       O  
ATOM   1580  OD2 ASP A 305     -18.393 -10.714 104.820  1.00308.05           O  
ANISOU 1580  OD2 ASP A 305    43492  41591  31962  10439  -1345   1757       O  
ATOM   1581  N   ARG A 306     -13.974  -8.305 102.093  1.00298.22           N  
ANISOU 1581  N   ARG A 306    42900  39149  31259   8791  -2867   1097       N  
ATOM   1582  CA  ARG A 306     -12.658  -7.705 101.885  1.00288.07           C  
ANISOU 1582  CA  ARG A 306    41726  37704  30025   8523  -3301    881       C  
ATOM   1583  C   ARG A 306     -11.621  -8.020 102.957  1.00297.94           C  
ANISOU 1583  C   ARG A 306    42800  39168  31237   8808  -3559    635       C  
ATOM   1584  O   ARG A 306     -10.447  -8.224 102.632  1.00295.70           O  
ANISOU 1584  O   ARG A 306    42340  38888  31125   8484  -3828    571       O  
ATOM   1585  CB  ARG A 306     -12.802  -6.184 101.772  1.00277.49           C  
ANISOU 1585  CB  ARG A 306    40901  36047  28485   8514  -3486    721       C  
ATOM   1586  CG  ARG A 306     -11.476  -5.440 101.747  1.00266.88           C  
ANISOU 1586  CG  ARG A 306    39696  34561  27144   8293  -3971    467       C  
ATOM   1587  CD  ARG A 306     -11.538  -4.179 100.905  1.00254.49           C  
ANISOU 1587  CD  ARG A 306    38583  32640  25473   8027  -4113    412       C  
ATOM   1588  NE  ARG A 306     -12.494  -3.209 101.430  1.00243.86           N  
ANISOU 1588  NE  ARG A 306    37599  31142  23913   8328  -4012    360       N  
ATOM   1589  CZ  ARG A 306     -12.653  -1.985 100.939  1.00232.61           C  
ANISOU 1589  CZ  ARG A 306    36576  29416  22389   8147  -4119    303       C  
ATOM   1590  NH1 ARG A 306     -11.910  -1.581  99.917  1.00230.69           N  
ANISOU 1590  NH1 ARG A 306    36576  28947  22130   7845  -4366    207       N  
ATOM   1591  NH2 ARG A 306     -13.545  -1.161 101.473  1.00228.90           N  
ANISOU 1591  NH2 ARG A 306    36481  28804  21687   8529  -4014    231       N  
ATOM   1592  N   GLU A 307     -12.022  -8.043 104.229  1.00287.24           N  
ANISOU 1592  N   GLU A 307    41478  38015  29643   9409  -3471    494       N  
ATOM   1593  CA  GLU A 307     -11.060  -8.316 105.292  1.00294.67           C  
ANISOU 1593  CA  GLU A 307    42244  39186  30532   9700  -3698    245       C  
ATOM   1594  C   GLU A 307     -10.318  -9.628 105.039  1.00283.10           C  
ANISOU 1594  C   GLU A 307    40247  37957  29359   9437  -3649    383       C  
ATOM   1595  O   GLU A 307      -9.087  -9.688 105.141  1.00292.61           O  
ANISOU 1595  O   GLU A 307    41305  39196  30677   9274  -3957    231       O  
ATOM   1596  CB  GLU A 307     -11.776  -8.344 106.643  1.00302.12           C  
ANISOU 1596  CB  GLU A 307    43244  40392  31156  10402  -3504    127       C  
ATOM   1597  CG  GLU A 307     -12.288  -6.979 107.101  1.00309.13           C  
ANISOU 1597  CG  GLU A 307    44682  41050  31725  10749  -3626    -90       C  
ATOM   1598  CD  GLU A 307     -11.176  -6.014 107.470  1.00313.02           C  
ANISOU 1598  CD  GLU A 307    45436  41340  32158  10759  -4150   -451       C  
ATOM   1599  OE1 GLU A 307     -10.128  -6.468 107.974  1.00314.28           O  
ANISOU 1599  OE1 GLU A 307    45323  41687  32401  10778  -4366   -603       O  
ATOM   1600  OE2 GLU A 307     -11.357  -4.794 107.258  1.00314.31           O  
ANISOU 1600  OE2 GLU A 307    46070  41158  32194  10738  -4344   -576       O  
ATOM   1601  N   LEU A 308     -11.054 -10.690 104.701  1.00299.10           N  
ANISOU 1601  N   LEU A 308    41978  40149  31517   9382  -3266    676       N  
ATOM   1602  CA  LEU A 308     -10.417 -11.948 104.319  1.00264.71           C  
ANISOU 1602  CA  LEU A 308    37142  35970  27466   9096  -3204    830       C  
ATOM   1603  C   LEU A 308      -9.532 -11.777 103.087  1.00266.42           C  
ANISOU 1603  C   LEU A 308    37360  35934  27934   8487  -3456    873       C  
ATOM   1604  O   LEU A 308      -8.458 -12.386 102.998  1.00270.93           O  
ANISOU 1604  O   LEU A 308    37624  36618  28700   8285  -3603    848       O  
ATOM   1605  CB  LEU A 308     -11.476 -13.021 104.068  1.00237.66           C  
ANISOU 1605  CB  LEU A 308    33454  32710  24137   9110  -2770   1149       C  
ATOM   1606  CG  LEU A 308     -11.796 -13.987 105.212  1.00223.53           C  
ANISOU 1606  CG  LEU A 308    31330  31359  22242   9554  -2500   1193       C  
ATOM   1607  CD1 LEU A 308     -10.542 -14.724 105.655  1.00214.76           C  
ANISOU 1607  CD1 LEU A 308    29849  30471  21278   9521  -2641   1081       C  
ATOM   1608  CD2 LEU A 308     -12.443 -13.268 106.386  1.00226.40           C  
ANISOU 1608  CD2 LEU A 308    31956  31866  22200  10143  -2427   1029       C  
ATOM   1609  N   CYS A 309      -9.974 -10.967 102.120  1.00264.97           N  
ANISOU 1609  N   CYS A 309    37501  35440  27734   8186  -3483    950       N  
ATOM   1610  CA  CYS A 309      -9.181 -10.730 100.916  1.00256.42           C  
ANISOU 1610  CA  CYS A 309    36474  34165  26790   7673  -3697    972       C  
ATOM   1611  C   CYS A 309      -7.823 -10.132 101.264  1.00272.98           C  
ANISOU 1611  C   CYS A 309    38796  36263  28662   7909  -4160    568       C  
ATOM   1612  O   CYS A 309      -6.787 -10.567 100.749  1.00270.48           O  
ANISOU 1612  O   CYS A 309    38357  36008  28406   7775  -4348    488       O  
ATOM   1613  CB  CYS A 309      -9.939  -9.802  99.963  1.00237.62           C  
ANISOU 1613  CB  CYS A 309    34463  31482  24338   7409  -3631   1073       C  
ATOM   1614  SG  CYS A 309     -11.443 -10.494  99.235  1.00223.91           S  
ANISOU 1614  SG  CYS A 309    32606  29727  22741   7280  -3148   1442       S  
ATOM   1615  N   GLN A 310      -7.815  -9.122 102.138  1.00255.71           N  
ANISOU 1615  N   GLN A 310    36935  33997  26224   8243  -4374    300       N  
ATOM   1616  CA  GLN A 310      -6.564  -8.479 102.524  1.00269.44           C  
ANISOU 1616  CA  GLN A 310    38906  35695  27773   8437  -4882   -116       C  
ATOM   1617  C   GLN A 310      -5.659  -9.455 103.267  1.00269.96           C  
ANISOU 1617  C   GLN A 310    38520  36117  27937   8610  -4936   -205       C  
ATOM   1618  O   GLN A 310      -4.441  -9.478 103.049  1.00281.21           O  
ANISOU 1618  O   GLN A 310    39914  37575  29357   8525  -5286   -419       O  
ATOM   1619  CB  GLN A 310      -6.854  -7.247 103.378  1.00274.11           C  
ANISOU 1619  CB  GLN A 310    39940  36113  28095   8792  -5090   -385       C  
ATOM   1620  CG  GLN A 310      -7.477  -6.098 102.588  1.00275.88           C  
ANISOU 1620  CG  GLN A 310    40669  35951  28202   8602  -5130   -366       C  
ATOM   1621  CD  GLN A 310      -6.561  -5.498 101.535  1.00276.90           C  
ANISOU 1621  CD  GLN A 310    41096  35812  28300   8259  -5533   -542       C  
ATOM   1622  OE1 GLN A 310      -5.371  -5.804 101.474  1.00278.30           O  
ANISOU 1622  OE1 GLN A 310    41143  36076  28521   8177  -5863   -736       O  
ATOM   1623  NE2 GLN A 310      -7.127  -4.650 100.682  1.00275.15           N  
ANISOU 1623  NE2 GLN A 310    41247  35280  28019   8010  -5492   -463       N  
ATOM   1624  N   LEU A 311      -6.239 -10.264 104.160  1.00289.81           N  
ANISOU 1624  N   LEU A 311    40659  38904  30550   8813  -4589    -36       N  
ATOM   1625  CA  LEU A 311      -5.465 -11.280 104.867  1.00262.01           C  
ANISOU 1625  CA  LEU A 311    36661  35745  27148   8947  -4559    -74       C  
ATOM   1626  C   LEU A 311      -4.832 -12.265 103.893  1.00241.34           C  
ANISOU 1626  C   LEU A 311    33712  33213  24774   8598  -4501     92       C  
ATOM   1627  O   LEU A 311      -3.678 -12.670 104.072  1.00248.65           O  
ANISOU 1627  O   LEU A 311    34404  34338  25734   8625  -4694    -64       O  
ATOM   1628  CB  LEU A 311      -6.357 -12.020 105.864  1.00254.98           C  
ANISOU 1628  CB  LEU A 311    35429  35099  26351   9123  -4149    136       C  
ATOM   1629  CG  LEU A 311      -6.949 -11.204 107.012  1.00256.75           C  
ANISOU 1629  CG  LEU A 311    35951  35346  26256   9634  -4171    -73       C  
ATOM   1630  CD1 LEU A 311      -7.972 -12.022 107.786  1.00257.78           C  
ANISOU 1630  CD1 LEU A 311    35896  35811  26238  10098  -3723     47       C  
ATOM   1631  CD2 LEU A 311      -5.848 -10.712 107.936  1.00259.29           C  
ANISOU 1631  CD2 LEU A 311    36324  35772  26423   9910  -4553   -452       C  
ATOM   1632  N   LEU A 312      -5.581 -12.678 102.868  1.00256.24           N  
ANISOU 1632  N   LEU A 312    35559  34963  26837   8266  -4230    410       N  
ATOM   1633  CA  LEU A 312      -5.022 -13.569 101.856  1.00233.35           C  
ANISOU 1633  CA  LEU A 312    32395  32116  24152   7954  -4182    558       C  
ATOM   1634  C   LEU A 312      -3.872 -12.909 101.107  1.00230.58           C  
ANISOU 1634  C   LEU A 312    32309  31641  23659   7810  -4618    303       C  
ATOM   1635  O   LEU A 312      -2.837 -13.542 100.868  1.00212.91           O  
ANISOU 1635  O   LEU A 312    29795  29584  21518   7718  -4732    252       O  
ATOM   1636  CB  LEU A 312      -6.116 -14.009 100.884  1.00213.49           C  
ANISOU 1636  CB  LEU A 312    29848  29438  21831   7631  -3846    917       C  
ATOM   1637  CG  LEU A 312      -5.668 -14.934  99.756  1.00200.84           C  
ANISOU 1637  CG  LEU A 312    28011  27856  20443   7325  -3776   1078       C  
ATOM   1638  CD1 LEU A 312      -5.046 -16.196 100.316  1.00194.48           C  
ANISOU 1638  CD1 LEU A 312    26676  27365  19851   7414  -3660   1121       C  
ATOM   1639  CD2 LEU A 312      -6.852 -15.264  98.876  1.00190.40           C  
ANISOU 1639  CD2 LEU A 312    26694  26349  19301   7021  -3472   1405       C  
ATOM   1640  N   LEU A 313      -4.035 -11.637 100.728  1.00228.57           N  
ANISOU 1640  N   LEU A 313    32579  31076  23190   7751  -4869    144       N  
ATOM   1641  CA  LEU A 313      -2.990 -10.930  99.990  1.00232.77           C  
ANISOU 1641  CA  LEU A 313    33394  31442  23605   7520  -5324   -108       C  
ATOM   1642  C   LEU A 313      -1.679 -10.914 100.766  1.00265.27           C  
ANISOU 1642  C   LEU A 313    37363  35756  27670   7663  -5710   -431       C  
ATOM   1643  O   LEU A 313      -0.605 -11.162 100.206  1.00259.50           O  
ANISOU 1643  O   LEU A 313    36501  35098  26997   7409  -5949   -522       O  
ATOM   1644  CB  LEU A 313      -3.439  -9.498  99.695  1.00207.01           C  
ANISOU 1644  CB  LEU A 313    30725  27798  20132   7457  -5534   -252       C  
ATOM   1645  CG  LEU A 313      -4.395  -9.231  98.535  1.00176.08           C  
ANISOU 1645  CG  LEU A 313    27033  23631  16238   7154  -5274     10       C  
ATOM   1646  CD1 LEU A 313      -4.654  -7.736  98.403  1.00176.64           C  
ANISOU 1646  CD1 LEU A 313    27679  23343  16094   7117  -5524   -183       C  
ATOM   1647  CD2 LEU A 313      -3.815  -9.792  97.252  1.00160.16           C  
ANISOU 1647  CD2 LEU A 313    24889  21623  14342   6758  -5285    120       C  
ATOM   1648  N   GLU A 314      -1.749 -10.615 102.064  1.00242.69           N  
ANISOU 1648  N   GLU A 314    34512  32998  24702   8053  -5775   -607       N  
ATOM   1649  CA  GLU A 314      -0.540 -10.582 102.877  1.00245.50           C  
ANISOU 1649  CA  GLU A 314    34712  33556  25011   8190  -6131   -917       C  
ATOM   1650  C   GLU A 314       0.063 -11.973 103.026  1.00249.54           C  
ANISOU 1650  C   GLU A 314    34595  34482  25737   8172  -5891   -752       C  
ATOM   1651  O   GLU A 314       1.287 -12.134 102.959  1.00255.97           O  
ANISOU 1651  O   GLU A 314    35224  35448  26585   8018  -6174   -912       O  
ATOM   1652  CB  GLU A 314      -0.843  -9.964 104.240  1.00246.94           C  
ANISOU 1652  CB  GLU A 314    35054  33757  25014   8649  -6219  -1137       C  
ATOM   1653  CG  GLU A 314       0.397  -9.637 105.053  1.00252.44           C  
ANISOU 1653  CG  GLU A 314    35704  34584  25629   8768  -6678  -1516       C  
ATOM   1654  CD  GLU A 314       0.075  -9.342 106.502  1.00258.32           C  
ANISOU 1654  CD  GLU A 314    36484  35449  26216   9291  -6663  -1693       C  
ATOM   1655  OE1 GLU A 314      -1.124  -9.186 106.814  1.00258.65           O  
ANISOU 1655  OE1 GLU A 314    36676  35415  26183   9536  -6351  -1551       O  
ATOM   1656  OE2 GLU A 314       1.014  -9.252 107.323  1.00262.90           O  
ANISOU 1656  OE2 GLU A 314    36938  36206  26743   9441  -6959  -1972       O  
ATOM   1657  N   GLY A 315      -0.780 -12.983 103.252  1.00249.93           N  
ANISOU 1657  N   GLY A 315    34299  34710  25953   8289  -5370   -431       N  
ATOM   1658  CA  GLY A 315      -0.301 -14.358 103.240  1.00232.64           C  
ANISOU 1658  CA  GLY A 315    31523  32860  24010   8219  -5098   -237       C  
ATOM   1659  C   GLY A 315       0.414 -14.712 101.952  1.00214.86           C  
ANISOU 1659  C   GLY A 315    29193  30577  21867   7837  -5201   -164       C  
ATOM   1660  O   GLY A 315       1.487 -15.320 101.967  1.00205.52           O  
ANISOU 1660  O   GLY A 315    27648  29661  20779   7757  -5273   -207       O  
ATOM   1661  N   LEU A 316      -0.174 -14.339 100.814  1.00222.51           N  
ANISOU 1661  N   LEU A 316    30491  31237  22817   7588  -5188    -44       N  
ATOM   1662  CA  LEU A 316       0.466 -14.608  99.531  1.00217.15           C  
ANISOU 1662  CA  LEU A 316    29785  30516  22207   7223  -5291     14       C  
ATOM   1663  C   LEU A 316       1.811 -13.901  99.433  1.00217.15           C  
ANISOU 1663  C   LEU A 316    29915  30518  22074   7042  -5826   -317       C  
ATOM   1664  O   LEU A 316       2.807 -14.502  99.015  1.00218.60           O  
ANISOU 1664  O   LEU A 316    29791  30912  22356   6849  -5897   -309       O  
ATOM   1665  CB  LEU A 316      -0.453 -14.205  98.381  1.00213.09           C  
ANISOU 1665  CB  LEU A 316    29641  29660  21664   6990  -5182    181       C  
ATOM   1666  CG  LEU A 316      -1.767 -14.980  98.345  1.00207.00           C  
ANISOU 1666  CG  LEU A 316    28701  28874  21075   7054  -4668    534       C  
ATOM   1667  CD1 LEU A 316      -2.658 -14.422  97.259  1.00207.74           C  
ANISOU 1667  CD1 LEU A 316    29183  28635  21114   6806  -4582    678       C  
ATOM   1668  CD2 LEU A 316      -1.506 -16.464  98.125  1.00202.30           C  
ANISOU 1668  CD2 LEU A 316    27569  28534  20764   7005  -4377    756       C  
ATOM   1669  N   GLU A 317       1.852 -12.614  99.800  1.00216.36           N  
ANISOU 1669  N   GLU A 317    30268  30168  21771   7066  -6212   -609       N  
ATOM   1670  CA  GLU A 317       3.106 -11.860  99.803  1.00217.13           C  
ANISOU 1670  CA  GLU A 317    30503  30207  21789   6827  -6774   -952       C  
ATOM   1671  C   GLU A 317       4.219 -12.623 100.510  1.00204.10           C  
ANISOU 1671  C   GLU A 317    28340  28979  20232   6893  -6819  -1012       C  
ATOM   1672  O   GLU A 317       5.326 -12.764  99.978  1.00198.15           O  
ANISOU 1672  O   GLU A 317    27424  28316  19547   6549  -7058  -1075       O  
ATOM   1673  CB  GLU A 317       2.899 -10.504 100.478  1.00249.49           C  
ANISOU 1673  CB  GLU A 317    35090  34007  25697   6958  -7136  -1265       C  
ATOM   1674  CG  GLU A 317       4.195  -9.810 100.887  1.00144.07           C  
ANISOU 1674  CG  GLU A 317    21803  20620  12318   6768  -7720  -1643       C  
ATOM   1675  CD  GLU A 317       3.965  -8.406 101.416  1.00148.19           C  
ANISOU 1675  CD  GLU A 317    22859  20767  12680   6863  -8111  -1967       C  
ATOM   1676  OE1 GLU A 317       4.943  -7.769 101.857  1.00152.41           O  
ANISOU 1676  OE1 GLU A 317    23471  21219  13217   6716  -8607  -2291       O  
ATOM   1677  OE2 GLU A 317       2.806  -7.939 101.395  1.00147.32           O  
ANISOU 1677  OE2 GLU A 317    23084  20436  12457   7074  -7917  -1885       O  
ATOM   1678  N   GLY A 318       3.946 -13.105 101.723  1.00201.74           N  
ANISOU 1678  N   GLY A 318    27762  28947  19942   7313  -6575   -982       N  
ATOM   1679  CA  GLY A 318       4.923 -13.932 102.415  1.00208.34           C  
ANISOU 1679  CA  GLY A 318    28055  30225  20881   7386  -6520   -990       C  
ATOM   1680  C   GLY A 318       5.234 -15.221 101.675  1.00206.73           C  
ANISOU 1680  C   GLY A 318    27362  30290  20898   7214  -6167   -684       C  
ATOM   1681  O   GLY A 318       6.379 -15.681 101.663  1.00204.90           O  
ANISOU 1681  O   GLY A 318    26764  30351  20739   7046  -6253   -703       O  
ATOM   1682  N   VAL A 319       4.216 -15.825 101.054  1.00219.70           N  
ANISOU 1682  N   VAL A 319    28982  31835  22657   7244  -5756   -389       N  
ATOM   1683  CA  VAL A 319       4.413 -17.086 100.341  1.00201.86           C  
ANISOU 1683  CA  VAL A 319    26277  29792  20629   7109  -5402   -100       C  
ATOM   1684  C   VAL A 319       5.322 -16.884  99.138  1.00196.24           C  
ANISOU 1684  C   VAL A 319    25648  29032  19880   6704  -5692   -146       C  
ATOM   1685  O   VAL A 319       6.162 -17.737  98.827  1.00202.23           O  
ANISOU 1685  O   VAL A 319    25961  30021  20855   6465  -5464    -34       O  
ATOM   1686  CB  VAL A 319       3.056 -17.684  99.929  1.00190.27           C  
ANISOU 1686  CB  VAL A 319    24828  28157  19308   7183  -4952    203       C  
ATOM   1687  CG1 VAL A 319       3.249 -18.761  98.872  1.00175.98           C  
ANISOU 1687  CG1 VAL A 319    22708  26444  17711   6978  -4691    457       C  
ATOM   1688  CG2 VAL A 319       2.350 -18.253 101.137  1.00199.39           C  
ANISOU 1688  CG2 VAL A 319    25722  29458  20580   7498  -4592    303       C  
ATOM   1689  N   LEU A 320       5.169 -15.756  98.441  1.00183.34           N  
ANISOU 1689  N   LEU A 320    24553  26965  18144   6400  -5979   -310       N  
ATOM   1690  CA  LEU A 320       5.959 -15.511  97.238  1.00178.06           C  
ANISOU 1690  CA  LEU A 320    23914  25989  17752   5643  -5889   -343       C  
ATOM   1691  C   LEU A 320       7.449 -15.512  97.554  1.00184.65           C  
ANISOU 1691  C   LEU A 320    24448  26970  18742   5299  -6009   -469       C  
ATOM   1692  O   LEU A 320       8.261 -16.006  96.763  1.00193.65           O  
ANISOU 1692  O   LEU A 320    25316  28112  20151   4824  -5760   -336       O  
ATOM   1693  CB  LEU A 320       5.540 -14.190  96.594  1.00177.83           C  
ANISOU 1693  CB  LEU A 320    24465  25459  17644   5367  -6152   -503       C  
ATOM   1694  CG  LEU A 320       4.070 -14.128  96.170  1.00127.02           C  
ANISOU 1694  CG  LEU A 320    18358  18862  11044   5638  -6001   -330       C  
ATOM   1695  CD1 LEU A 320       3.724 -12.774  95.571  1.00128.36           C  
ANISOU 1695  CD1 LEU A 320    19071  18561  11139   5345  -6236   -488       C  
ATOM   1696  CD2 LEU A 320       3.736 -15.256  95.206  1.00123.13           C  
ANISOU 1696  CD2 LEU A 320    17585  18434  10766   5496  -5509    -18       C  
ATOM   1697  N   ARG A 321       7.829 -14.969  98.711  1.00175.28           N  
ANISOU 1697  N   ARG A 321    20142  27795  18660   -497    -60   1694       N  
ATOM   1698  CA  ARG A 321       9.238 -14.914  99.075  1.00174.04           C  
ANISOU 1698  CA  ARG A 321    19806  27890  18432   -547    -17   1573       C  
ATOM   1699  C   ARG A 321       9.828 -16.288  99.374  1.00190.48           C  
ANISOU 1699  C   ARG A 321    21768  30048  20557   -406   -321   1609       C  
ATOM   1700  O   ARG A 321      11.054 -16.400  99.481  1.00187.15           O  
ANISOU 1700  O   ARG A 321    21179  29809  20120   -405   -306   1553       O  
ATOM   1701  CB  ARG A 321       9.420 -13.985 100.276  1.00156.99           C  
ANISOU 1701  CB  ARG A 321    17576  25875  16199   -868    166   1555       C  
ATOM   1702  CG  ARG A 321       8.870 -12.582 100.045  1.00147.49           C  
ANISOU 1702  CG  ARG A 321    16477  24589  14973  -1019    517   1522       C  
ATOM   1703  CD  ARG A 321       9.235 -11.642 101.176  1.00151.55           C  
ANISOU 1703  CD  ARG A 321    16951  25250  15379  -1354    741   1478       C  
ATOM   1704  NE  ARG A 321      10.547 -11.038 100.970  1.00158.37           N  
ANISOU 1704  NE  ARG A 321    17703  26340  16129  -1414    882   1351       N  
ATOM   1705  CZ  ARG A 321      10.742  -9.888 100.334  1.00164.13           C  
ANISOU 1705  CZ  ARG A 321    18459  27087  16815  -1449   1186   1253       C  
ATOM   1706  NH1 ARG A 321       9.708  -9.220  99.842  1.00160.17           N  
ANISOU 1706  NH1 ARG A 321    18078  26388  16392  -1444   1388   1279       N  
ATOM   1707  NH2 ARG A 321      11.969  -9.404 100.187  1.00171.24           N  
ANISOU 1707  NH2 ARG A 321    19251  28203  17611  -1493   1284   1154       N  
ATOM   1708  N   ASP A 322       9.001 -17.328  99.500  1.00189.81           N  
ANISOU 1708  N   ASP A 322    21752  29826  20542   -287   -590   1721       N  
ATOM   1709  CA  ASP A 322       9.454 -18.672  99.854  1.00197.26           C  
ANISOU 1709  CA  ASP A 322    22569  30832  21549   -157   -879   1770       C  
ATOM   1710  C   ASP A 322       8.872 -19.702  98.892  1.00208.00           C  
ANISOU 1710  C   ASP A 322    24090  31983  22957    116  -1064   1819       C  
ATOM   1711  O   ASP A 322       7.670 -19.987  98.936  1.00213.75           O  
ANISOU 1711  O   ASP A 322    24966  32544  23704    140  -1208   1930       O  
ATOM   1712  CB  ASP A 322       9.075 -19.018 101.293  1.00195.80           C  
ANISOU 1712  CB  ASP A 322    22283  30728  21385   -336  -1063   1868       C  
ATOM   1713  CG  ASP A 322       9.782 -20.259 101.793  1.00192.12           C  
ANISOU 1713  CG  ASP A 322    21609  30389  21000   -256  -1334   1923       C  
ATOM   1714  OD1 ASP A 322      11.011 -20.211 102.000  1.00189.69           O  
ANISOU 1714  OD1 ASP A 322    21098  30272  20703   -321  -1280   1899       O  
ATOM   1715  OD2 ASP A 322       9.107 -21.296 101.954  1.00190.36           O  
ANISOU 1715  OD2 ASP A 322    21414  30070  20845   -125  -1603   2012       O  
ATOM   1716  N   GLN A 323       9.722 -20.258  98.023  1.00201.12           N  
ANISOU 1716  N   GLN A 323    23206  31104  22104    309  -1049   1750       N  
ATOM   1717  CA  GLN A 323       9.268 -21.286  97.088  1.00205.26           C  
ANISOU 1717  CA  GLN A 323    23922  31420  22647    542  -1203   1785       C  
ATOM   1718  C   GLN A 323       8.766 -22.527  97.819  1.00209.46           C  
ANISOU 1718  C   GLN A 323    24405  31931  23249    614  -1532   1909       C  
ATOM   1719  O   GLN A 323       7.752 -23.117  97.428  1.00208.32           O  
ANISOU 1719  O   GLN A 323    24466  31596  23090    712  -1709   2000       O  
ATOM   1720  CB  GLN A 323      10.397 -21.661  96.125  1.00206.65           C  
ANISOU 1720  CB  GLN A 323    24094  31583  22840    716  -1074   1680       C  
ATOM   1721  CG  GLN A 323       9.977 -22.572  94.968  1.00203.07           C  
ANISOU 1721  CG  GLN A 323    23915  30879  22362    917  -1155   1688       C  
ATOM   1722  CD  GLN A 323       9.419 -21.822  93.774  1.00195.07           C  
ANISOU 1722  CD  GLN A 323    23185  29696  21237    886  -1002   1643       C  
ATOM   1723  OE1 GLN A 323       9.202 -20.612  93.830  1.00192.06           O  
ANISOU 1723  OE1 GLN A 323    22781  29374  20818    730   -843   1619       O  
ATOM   1724  NE2 GLN A 323       9.179 -22.544  92.684  1.00192.09           N  
ANISOU 1724  NE2 GLN A 323    23082  29099  20805   1012  -1044   1643       N  
ATOM   1725  N   LEU A 324       9.475 -22.950  98.872  1.00213.35           N  
ANISOU 1725  N   LEU A 324    24622  32622  23821    556  -1634   1933       N  
ATOM   1726  CA  LEU A 324       9.097 -24.163  99.596  1.00207.50           C  
ANISOU 1726  CA  LEU A 324    23791  31886  23164    625  -1955   2047       C  
ATOM   1727  C   LEU A 324       7.678 -24.071 100.151  1.00202.32           C  
ANISOU 1727  C   LEU A 324    23266  31131  22473    542  -2124   2151       C  
ATOM   1728  O   LEU A 324       6.918 -25.045 100.091  1.00204.76           O  
ANISOU 1728  O   LEU A 324    23673  31317  22811    684  -2382   2247       O  
ATOM   1729  CB  LEU A 324      10.096 -24.429 100.723  1.00201.93           C  
ANISOU 1729  CB  LEU A 324    22736  31432  22554    502  -2024   2081       C  
ATOM   1730  CG  LEU A 324      11.456 -25.014 100.331  1.00203.13           C  
ANISOU 1730  CG  LEU A 324    22696  31658  22828    635  -1948   2069       C  
ATOM   1731  CD1 LEU A 324      12.437 -24.964 101.497  1.00202.70           C  
ANISOU 1731  CD1 LEU A 324    22278  31872  22866    426  -1993   2153       C  
ATOM   1732  CD2 LEU A 324      11.290 -26.436  99.831  1.00207.45           C  
ANISOU 1732  CD2 LEU A 324    23295  32054  23473    905  -2122   2116       C  
ATOM   1733  N   ALA A 325       7.305 -22.911 100.702  1.00201.44           N  
ANISOU 1733  N   ALA A 325    23166  31061  22311    313  -1968   2146       N  
ATOM   1734  CA  ALA A 325       5.935 -22.724 101.175  1.00179.64           C  
ANISOU 1734  CA  ALA A 325    20541  28164  19550    237  -2067   2268       C  
ATOM   1735  C   ALA A 325       4.944 -22.896 100.035  1.00186.09           C  
ANISOU 1735  C   ALA A 325    21637  28719  20350    400  -2113   2354       C  
ATOM   1736  O   ALA A 325       3.886 -23.514 100.204  1.00193.32           O  
ANISOU 1736  O   ALA A 325    22657  29494  21300    470  -2353   2509       O  
ATOM   1737  CB  ALA A 325       5.774 -21.345 101.812  1.00166.72           C  
ANISOU 1737  CB  ALA A 325    18898  26577  17872    -42  -1799   2241       C  
ATOM   1738  N   LEU A 326       5.268 -22.335  98.869  1.00188.70           N  
ANISOU 1738  N   LEU A 326    22092  28981  20624    442  -1894   2273       N  
ATOM   1739  CA  LEU A 326       4.426 -22.495  97.690  1.00187.96           C  
ANISOU 1739  CA  LEU A 326    22276  28643  20497    550  -1941   2369       C  
ATOM   1740  C   LEU A 326       4.237 -23.971  97.357  1.00192.54           C  
ANISOU 1740  C   LEU A 326    22954  29129  21073    758  -2249   2436       C  
ATOM   1741  O   LEU A 326       3.112 -24.434  97.143  1.00194.92           O  
ANISOU 1741  O   LEU A 326    23442  29249  21371    806  -2461   2616       O  
ATOM   1742  CB  LEU A 326       5.057 -21.744  96.519  1.00183.73           C  
ANISOU 1742  CB  LEU A 326    21829  28086  19893    546  -1660   2238       C  
ATOM   1743  CG  LEU A 326       4.439 -21.890  95.135  1.00189.32           C  
ANISOU 1743  CG  LEU A 326    22836  28558  20538    615  -1685   2315       C  
ATOM   1744  CD1 LEU A 326       3.021 -21.351  95.150  1.00189.56           C  
ANISOU 1744  CD1 LEU A 326    22994  28417  20612    496  -1729   2547       C  
ATOM   1745  CD2 LEU A 326       5.293 -21.177  94.104  1.00194.13           C  
ANISOU 1745  CD2 LEU A 326    23491  29189  21082    602  -1398   2144       C  
ATOM   1746  N   ARG A 327       5.338 -24.724  97.297  1.00194.68           N  
ANISOU 1746  N   ARG A 327    23101  29510  21356    881  -2266   2311       N  
ATOM   1747  CA  ARG A 327       5.269 -26.152  96.997  1.00192.29           C  
ANISOU 1747  CA  ARG A 327    22882  29117  21061   1080  -2514   2358       C  
ATOM   1748  C   ARG A 327       4.409 -26.902  98.012  1.00191.84           C  
ANISOU 1748  C   ARG A 327    22755  29070  21064   1100  -2849   2513       C  
ATOM   1749  O   ARG A 327       3.557 -27.716  97.636  1.00193.07           O  
ANISOU 1749  O   ARG A 327    23114  29059  21187   1212  -3087   2643       O  
ATOM   1750  CB  ARG A 327       6.678 -26.734  96.945  1.00193.18           C  
ANISOU 1750  CB  ARG A 327    22807  29355  21237   1190  -2420   2221       C  
ATOM   1751  CG  ARG A 327       7.410 -26.415  95.655  1.00197.34           C  
ANISOU 1751  CG  ARG A 327    23493  29786  21699   1249  -2138   2089       C  
ATOM   1752  CD  ARG A 327       8.889 -26.734  95.757  1.00204.83           C  
ANISOU 1752  CD  ARG A 327    24197  30872  22759   1331  -1981   1982       C  
ATOM   1753  NE  ARG A 327       9.628 -26.220  94.608  1.00212.03           N  
ANISOU 1753  NE  ARG A 327    25242  31701  23618   1369  -1672   1847       N  
ATOM   1754  CZ  ARG A 327      10.920 -26.440  94.394  1.00221.91           C  
ANISOU 1754  CZ  ARG A 327    26339  33006  24971   1464  -1476   1768       C  
ATOM   1755  NH1 ARG A 327      11.621 -27.167  95.254  1.00222.37           N  
ANISOU 1755  NH1 ARG A 327    26083  33204  25202   1517  -1564   1832       N  
ATOM   1756  NH2 ARG A 327      11.513 -25.932  93.321  1.00226.51           N  
ANISOU 1756  NH2 ARG A 327    27069  33495  25500   1499  -1192   1645       N  
ATOM   1757  N   ALA A 328       4.634 -26.655  99.309  1.00194.53           N  
ANISOU 1757  N   ALA A 328    22820  29608  21485    976  -2881   2507       N  
ATOM   1758  CA  ALA A 328       3.874 -27.346 100.353  1.00195.06           C  
ANISOU 1758  CA  ALA A 328    22801  29699  21616    981  -3195   2640       C  
ATOM   1759  C   ALA A 328       2.380 -27.073 100.216  1.00203.15           C  
ANISOU 1759  C   ALA A 328    24064  30511  22613    960  -3301   2825       C  
ATOM   1760  O   ALA A 328       1.560 -27.995 100.292  1.00209.95           O  
ANISOU 1760  O   ALA A 328    25016  31267  23487   1082  -3606   2972       O  
ATOM   1761  CB  ALA A 328       4.376 -26.928 101.736  1.00193.49           C  
ANISOU 1761  CB  ALA A 328    22302  29736  21480    781  -3166   2598       C  
ATOM   1762  N   LEU A 329       2.006 -25.808 100.012  1.00199.26           N  
ANISOU 1762  N   LEU A 329    23663  29947  22100    803  -3048   2844       N  
ATOM   1763  CA  LEU A 329       0.600 -25.471  99.808  1.00197.30           C  
ANISOU 1763  CA  LEU A 329    23622  29471  21871    771  -3109   3071       C  
ATOM   1764  C   LEU A 329       0.069 -26.186  98.570  1.00220.37           C  
ANISOU 1764  C   LEU A 329    26821  32188  24721    923  -3281   3194       C  
ATOM   1765  O   LEU A 329      -1.083 -26.637  98.535  1.00213.56           O  
ANISOU 1765  O   LEU A 329    26109  31155  23880    972  -3527   3436       O  
ATOM   1766  CB  LEU A 329       0.445 -23.960  99.665  1.00170.83           C  
ANISOU 1766  CB  LEU A 329    20299  26074  18536    576  -2750   3068       C  
ATOM   1767  CG  LEU A 329      -0.925 -23.425  99.250  1.00154.35           C  
ANISOU 1767  CG  LEU A 329    18408  23725  16511    522  -2732   3338       C  
ATOM   1768  CD1 LEU A 329      -1.938 -23.592 100.367  1.00163.58           C  
ANISOU 1768  CD1 LEU A 329    19537  24818  17799    489  -2888   3535       C  
ATOM   1769  CD2 LEU A 329      -0.808 -21.974  98.831  1.00138.38           C  
ANISOU 1769  CD2 LEU A 329    16397  21674  14507    350  -2334   3298       C  
ATOM   1770  N   GLU A 330       0.911 -26.294  97.535  1.00204.43           N  
ANISOU 1770  N   GLU A 330    24890  30174  22610    984  -3149   3042       N  
ATOM   1771  CA  GLU A 330       0.522 -26.952  96.293  1.00218.33           C  
ANISOU 1771  CA  GLU A 330    26959  31731  24263   1081  -3274   3134       C  
ATOM   1772  C   GLU A 330       0.214 -28.428  96.516  1.00220.31           C  
ANISOU 1772  C   GLU A 330    27261  31947  24499   1255  -3635   3218       C  
ATOM   1773  O   GLU A 330      -0.767 -28.947  95.975  1.00222.93           O  
ANISOU 1773  O   GLU A 330    27855  32083  24767   1288  -3862   3432       O  
ATOM   1774  CB  GLU A 330       1.648 -26.750  95.277  1.00232.04           C  
ANISOU 1774  CB  GLU A 330    28762  33492  25912   1098  -3010   2912       C  
ATOM   1775  CG  GLU A 330       1.424 -27.299  93.873  1.00241.51           C  
ANISOU 1775  CG  GLU A 330    30334  34460  26971   1088  -3003   2983       C  
ATOM   1776  CD  GLU A 330       2.572 -27.009  92.928  1.00253.72           C  
ANISOU 1776  CD  GLU A 330    32051  35930  28421   1248  -3115   2907       C  
ATOM   1777  OE1 GLU A 330       3.571 -26.406  93.379  1.00259.35           O  
ANISOU 1777  OE1 GLU A 330    32543  36794  29205   1380  -3098   2749       O  
ATOM   1778  OE2 GLU A 330       2.457 -27.349  91.731  1.00258.97           O  
ANISOU 1778  OE2 GLU A 330    33076  36377  28943   1221  -3200   3016       O  
ATOM   1779  N   GLU A 331       1.032 -29.119  97.316  1.00234.29           N  
ANISOU 1779  N   GLU A 331    28775  33908  26336   1353  -3701   3075       N  
ATOM   1780  CA  GLU A 331       0.825 -30.550  97.535  1.00227.88           C  
ANISOU 1780  CA  GLU A 331    27977  33079  25527   1528  -4028   3140       C  
ATOM   1781  C   GLU A 331      -0.432 -30.819  98.349  1.00234.97           C  
ANISOU 1781  C   GLU A 331    28871  33930  26479   1530  -4348   3374       C  
ATOM   1782  O   GLU A 331      -1.146 -31.796  98.088  1.00223.34           O  
ANISOU 1782  O   GLU A 331    27577  32329  24954   1650  -4644   3529       O  
ATOM   1783  CB  GLU A 331       2.042 -31.181  98.204  1.00219.41           C  
ANISOU 1783  CB  GLU A 331    26585  32227  24555   1614  -4006   2961       C  
ATOM   1784  CG  GLU A 331       3.121 -31.596  97.225  1.00214.04           C  
ANISOU 1784  CG  GLU A 331    25981  31508  23835   1715  -3799   2800       C  
ATOM   1785  CD  GLU A 331       4.066 -32.626  97.810  1.00212.64           C  
ANISOU 1785  CD  GLU A 331    25515  31483  23796   1847  -3863   2723       C  
ATOM   1786  OE1 GLU A 331       3.579 -33.650  98.336  1.00211.45           O  
ANISOU 1786  OE1 GLU A 331    25311  31341  23690   1953  -4172   2825       O  
ATOM   1787  OE2 GLU A 331       5.295 -32.421  97.735  1.00212.68           O  
ANISOU 1787  OE2 GLU A 331    25332  31594  23882   1845  -3605   2583       O  
ATOM   1788  N   ALA A 332      -0.698 -29.984  99.359  1.00235.61           N  
ANISOU 1788  N   ALA A 332    28757  34103  26660   1395  -4282   3403       N  
ATOM   1789  CA  ALA A 332      -1.862 -30.186 100.217  1.00243.56           C  
ANISOU 1789  CA  ALA A 332    29746  35051  27744   1394  -4548   3624       C  
ATOM   1790  C   ALA A 332      -3.145 -30.271  99.400  1.00245.70           C  
ANISOU 1790  C   ALA A 332    30345  35048  27964   1421  -4708   3915       C  
ATOM   1791  O   ALA A 332      -4.045 -31.051  99.726  1.00245.29           O  
ANISOU 1791  O   ALA A 332    30353  34912  27933   1520  -5045   4122       O  
ATOM   1792  CB  ALA A 332      -1.956 -29.062 101.254  1.00244.49           C  
ANISOU 1792  CB  ALA A 332    29679  35252  27964   1198  -4348   3607       C  
ATOM   1793  N   LEU A 333      -3.251 -29.477  98.335  1.00260.57           N  
ANISOU 1793  N   LEU A 333    32435  36788  29781   1319  -4486   3959       N  
ATOM   1794  CA  LEU A 333      -4.430 -29.494  97.464  1.00240.39           C  
ANISOU 1794  CA  LEU A 333    30192  33967  27177   1291  -4634   4281       C  
ATOM   1795  C   LEU A 333      -3.973 -29.318  96.021  1.00247.09           C  
ANISOU 1795  C   LEU A 333    31291  34722  27869   1235  -4467   4206       C  
ATOM   1796  O   LEU A 333      -3.908 -28.191  95.533  1.00252.59           O  
ANISOU 1796  O   LEU A 333    32014  35375  28585   1080  -4182   4202       O  
ATOM   1797  CB  LEU A 333      -5.406 -28.396  97.870  1.00213.10           C  
ANISOU 1797  CB  LEU A 333    26703  30390  23876   1142  -4520   4527       C  
ATOM   1798  CG  LEU A 333      -6.896 -28.566  97.601  1.00191.50           C  
ANISOU 1798  CG  LEU A 333    24171  27394  21195   1130  -4776   4974       C  
ATOM   1799  CD1 LEU A 333      -7.630 -27.466  98.336  1.00176.16           C  
ANISOU 1799  CD1 LEU A 333    22096  25363  19474   1003  -4581   5165       C  
ATOM   1800  CD2 LEU A 333      -7.207 -28.508  96.120  1.00193.61           C  
ANISOU 1800  CD2 LEU A 333    24757  27473  21334   1041  -4793   5149       C  
ATOM   1801  N   GLU A 334      -3.649 -30.416  95.342  1.00232.98           N  
ANISOU 1801  N   GLU A 334    29696  32896  25932   1350  -4623   4142       N  
ATOM   1802  CA  GLU A 334      -3.284 -30.237  93.942  1.00240.04           C  
ANISOU 1802  CA  GLU A 334    30877  33666  26662   1264  -4452   4082       C  
ATOM   1803  C   GLU A 334      -4.254 -30.979  93.034  1.00244.94           C  
ANISOU 1803  C   GLU A 334    31900  34041  27124   1231  -4743   4373       C  
ATOM   1804  O   GLU A 334      -5.073 -30.364  92.342  1.00236.87           O  
ANISOU 1804  O   GLU A 334    31083  32843  26075   1050  -4754   4641       O  
ATOM   1805  CB  GLU A 334      -1.857 -30.730  93.675  1.00244.20           C  
ANISOU 1805  CB  GLU A 334    31346  34316  27122   1375  -4261   3725       C  
ATOM   1806  CG  GLU A 334      -1.394 -30.572  92.221  1.00248.73           C  
ANISOU 1806  CG  GLU A 334    32239  34746  27522   1287  -4049   3630       C  
ATOM   1807  CD  GLU A 334      -0.061 -31.255  91.936  1.00251.21           C  
ANISOU 1807  CD  GLU A 334    32529  35126  27793   1426  -3867   3321       C  
ATOM   1808  OE1 GLU A 334       0.536 -30.977  90.870  1.00251.91           O  
ANISOU 1808  OE1 GLU A 334    32823  35122  27770   1357  -3612   3185       O  
ATOM   1809  OE2 GLU A 334       0.385 -32.069  92.775  1.00253.51           O  
ANISOU 1809  OE2 GLU A 334    32587  35553  28181   1597  -3969   3232       O  
ATOM   1810  N   GLN A 335      -4.163 -32.309  93.042  1.00234.09           N  
ANISOU 1810  N   GLN A 335    30636  32655  25651   1389  -4983   4342       N  
ATOM   1811  CA  GLN A 335      -5.118 -33.159  92.347  1.00231.68           C  
ANISOU 1811  CA  GLN A 335    30719  32133  25177   1360  -5310   4633       C  
ATOM   1812  C   GLN A 335      -5.734 -34.183  93.291  1.00221.75           C  
ANISOU 1812  C   GLN A 335    29357  30919  23979   1541  -5694   4776       C  
ATOM   1813  O   GLN A 335      -6.272 -35.195  92.835  1.00222.97           O  
ANISOU 1813  O   GLN A 335    29787  30896  24036   1608  -5833   4811       O  
ATOM   1814  CB  GLN A 335      -4.464 -33.858  91.153  1.00241.94           C  
ANISOU 1814  CB  GLN A 335    32377  33315  26235   1340  -5213   4471       C  
ATOM   1815  CG  GLN A 335      -3.285 -33.110  90.547  1.00256.51           C  
ANISOU 1815  CG  GLN A 335    34188  35210  28063   1273  -4772   4152       C  
ATOM   1816  CD  GLN A 335      -2.115 -34.019  90.233  1.00270.71           C  
ANISOU 1816  CD  GLN A 335    36046  37029  29782   1421  -4608   3838       C  
ATOM   1817  OE1 GLN A 335      -2.214 -35.238  90.354  1.00274.06           O  
ANISOU 1817  OE1 GLN A 335    36576  37410  30143   1556  -4814   3860       O  
ATOM   1818  NE2 GLN A 335      -0.995 -33.428  89.835  1.00277.16           N  
ANISOU 1818  NE2 GLN A 335    36785  37903  30620   1402  -4219   3556       N  
ATOM   1819  N   GLY A 336      -5.676 -33.935  94.596  1.00242.76           N  
ANISOU 1819  N   GLY A 336    31618  33766  26854   1640  -5708   4716       N  
ATOM   1820  CA  GLY A 336      -6.231 -34.873  95.548  1.00229.22           C  
ANISOU 1820  CA  GLY A 336    29800  31978  25316   1856  -5805   4559       C  
ATOM   1821  C   GLY A 336      -7.672 -34.484  95.776  1.00222.41           C  
ANISOU 1821  C   GLY A 336    29017  30846  24642   1833  -5694   4643       C  
ATOM   1822  O   GLY A 336      -8.595 -35.272  95.537  1.00219.03           O  
ANISOU 1822  O   GLY A 336    28766  30227  24228   1936  -5668   4613       O  
ATOM   1823  N   GLN A 337      -7.843 -33.235  96.213  1.00231.82           N  
ANISOU 1823  N   GLN A 337    30041  32069  25970   1682  -5595   4788       N  
ATOM   1824  CA  GLN A 337      -9.134 -32.644  96.567  1.00236.80           C  
ANISOU 1824  CA  GLN A 337    30687  32462  26826   1628  -5469   4923       C  
ATOM   1825  C   GLN A 337     -10.052 -33.676  97.206  1.00261.42           C  
ANISOU 1825  C   GLN A 337    33832  35428  30069   1840  -5468   4744       C  
ATOM   1826  O   GLN A 337     -11.211 -33.845  96.833  1.00254.09           O  
ANISOU 1826  O   GLN A 337    33070  34267  29205   1840  -5383   4837       O  
ATOM   1827  CB  GLN A 337      -9.764 -31.947  95.351  1.00220.76           C  
ANISOU 1827  CB  GLN A 337    28903  30222  24752   1421  -5378   5205       C  
ATOM   1828  CG  GLN A 337     -10.019 -32.776  94.091  1.00202.30           C  
ANISOU 1828  CG  GLN A 337    26910  27734  22221   1414  -5428   5218       C  
ATOM   1829  CD  GLN A 337     -11.477 -32.760  93.672  1.00194.89           C  
ANISOU 1829  CD  GLN A 337    26124  26497  21429   1347  -5323   5372       C  
ATOM   1830  OE1 GLN A 337     -11.828 -32.239  92.619  1.00200.34           O  
ANISOU 1830  OE1 GLN A 337    26743  27095  22283   1495  -5279   5284       O  
ATOM   1831  NE2 GLN A 337     -12.336 -33.365  94.495  1.00190.98           N  
ANISOU 1831  NE2 GLN A 337    25826  25860  20876   1102  -5273   5607       N  
ATOM   1832  N   SER A 338      -9.486 -34.385  98.186  1.00261.86           N  
ANISOU 1832  N   SER A 338    33692  35651  30152   2010  -5549   4483       N  
ATOM   1833  CA  SER A 338     -10.174 -35.461  98.875  1.00267.85           C  
ANISOU 1833  CA  SER A 338    34437  36345  30988   2232  -5532   4273       C  
ATOM   1834  C   SER A 338     -11.365 -34.910  99.649  1.00270.94           C  
ANISOU 1834  C   SER A 338    34787  36557  31603   2198  -5400   4349       C  
ATOM   1835  O   SER A 338     -11.431 -33.722  99.982  1.00276.77           O  
ANISOU 1835  O   SER A 338    35427  37264  32470   2018  -5343   4530       O  
ATOM   1836  CB  SER A 338      -9.220 -36.192  99.824  1.00269.32           C  
ANISOU 1836  CB  SER A 338    34393  36750  31185   2378  -5644   3988       C  
ATOM   1837  OG  SER A 338      -8.088 -36.693  99.133  1.00271.43           O  
ANISOU 1837  OG  SER A 338    34681  37172  31276   2402  -5765   3945       O  
ATOM   1838  N   LEU A 339     -12.326 -35.797  99.915  1.00288.86           N  
ANISOU 1838  N   LEU A 339    37119  38727  33907   2367  -5327   4237       N  
ATOM   1839  CA  LEU A 339     -13.531 -35.401 100.635  1.00274.91           C  
ANISOU 1839  CA  LEU A 339    35336  36775  32343   2347  -5195   4304       C  
ATOM   1840  C   LEU A 339     -13.208 -34.786 101.992  1.00260.59           C  
ANISOU 1840  C   LEU A 339    33294  35032  30688   2294  -5206   4243       C  
ATOM   1841  O   LEU A 339     -13.968 -33.946 102.483  1.00256.85           O  
ANISOU 1841  O   LEU A 339    32793  34402  30398   2174  -5099   4417       O  
ATOM   1842  CB  LEU A 339     -14.465 -36.605 100.801  1.00272.72           C  
ANISOU 1842  CB  LEU A 339    35116  36456  32051   2536  -5123   4169       C  
ATOM   1843  CG  LEU A 339     -15.901 -36.426 100.295  1.00270.63           C  
ANISOU 1843  CG  LEU A 339    34970  35908  31950   2333  -5086   4483       C  
ATOM   1844  CD1 LEU A 339     -16.795 -37.560 100.774  1.00267.95           C  
ANISOU 1844  CD1 LEU A 339    34572  35507  31729   2307  -5167   4501       C  
ATOM   1845  CD2 LEU A 339     -16.468 -35.074 100.717  1.00268.86           C  
ANISOU 1845  CD2 LEU A 339    34720  35507  31928   2199  -4961   4657       C  
ATOM   1846  N   GLY A 340     -12.091 -35.176 102.605  1.00253.82           N  
ANISOU 1846  N   GLY A 340    32260  34405  29773   2355  -5328   4023       N  
ATOM   1847  CA  GLY A 340     -11.718 -34.677 103.907  1.00263.09           C  
ANISOU 1847  CA  GLY A 340    33201  35678  31082   2267  -5347   3963       C  
ATOM   1848  C   GLY A 340     -11.035 -33.323 103.885  1.00270.48           C  
ANISOU 1848  C   GLY A 340    33995  36725  32050   2006  -5344   4206       C  
ATOM   1849  O   GLY A 340     -10.294 -32.984 102.962  1.00269.08           O  
ANISOU 1849  O   GLY A 340    33835  36660  31743   1926  -5385   4310       O  
ATOM   1850  N   PRO A 341     -11.313 -32.511 104.907  1.00267.77           N  
ANISOU 1850  N   PRO A 341    33502  36379  31858   1863  -5264   4327       N  
ATOM   1851  CA  PRO A 341     -10.680 -31.188 105.016  1.00260.46           C  
ANISOU 1851  CA  PRO A 341    32391  35640  30931   1611  -5203   4587       C  
ATOM   1852  C   PRO A 341      -9.168 -31.301 105.096  1.00255.20           C  
ANISOU 1852  C   PRO A 341    31502  35357  30106   1561  -5314   4436       C  
ATOM   1853  O   PRO A 341      -8.630 -32.049 105.912  1.00258.77           O  
ANISOU 1853  O   PRO A 341    31813  35941  30566   1622  -5417   4166       O  
ATOM   1854  CB  PRO A 341     -11.270 -30.618 106.310  1.00260.54           C  
ANISOU 1854  CB  PRO A 341    32282  35596  31117   1499  -5103   4697       C  
ATOM   1855  CG  PRO A 341     -12.569 -31.339 106.485  1.00261.51           C  
ANISOU 1855  CG  PRO A 341    32601  35394  31367   1673  -5062   4607       C  
ATOM   1856  CD  PRO A 341     -12.373 -32.711 105.913  1.00263.47           C  
ANISOU 1856  CD  PRO A 341    32975  35656  31475   1919  -5182   4283       C  
ATOM   1857  N   VAL A 342      -8.486 -30.539 104.240  1.00255.80           N  
ANISOU 1857  N   VAL A 342    31532  35622  30039   1441  -5269   4619       N  
ATOM   1858  CA  VAL A 342      -7.029 -30.568 104.190  1.00240.07           C  
ANISOU 1858  CA  VAL A 342    29302  34046  27866   1393  -5327   4498       C  
ATOM   1859  C   VAL A 342      -6.452 -29.999 105.479  1.00230.63           C  
ANISOU 1859  C   VAL A 342    27786  33166  26675   1215  -5273   4469       C  
ATOM   1860  O   VAL A 342      -6.920 -28.978 105.997  1.00232.82           O  
ANISOU 1860  O   VAL A 342    28078  33330  27054   1044  -5008   4548       O  
ATOM   1861  CB  VAL A 342      -6.518 -29.799 102.961  1.00234.39           C  
ANISOU 1861  CB  VAL A 342    28654  33410  26994   1312  -5161   4602       C  
ATOM   1862  CG1 VAL A 342      -5.004 -29.889 102.887  1.00234.12           C  
ANISOU 1862  CG1 VAL A 342    28457  33636  26863   1292  -5005   4234       C  
ATOM   1863  CG2 VAL A 342      -7.147 -30.357 101.698  1.00230.73           C  
ANISOU 1863  CG2 VAL A 342    28506  32690  26472   1431  -5301   4745       C  
ATOM   1864  N   GLU A 343      -5.433 -30.669 106.003  1.00226.79           N  
ANISOU 1864  N   GLU A 343    27083  32943  26145   1232  -5380   4214       N  
ATOM   1865  CA  GLU A 343      -4.816 -30.241 107.255  1.00217.33           C  
ANISOU 1865  CA  GLU A 343    25647  31946  24983   1018  -5246   4040       C  
ATOM   1866  C   GLU A 343      -3.992 -28.983 107.019  1.00206.58           C  
ANISOU 1866  C   GLU A 343    24277  30642  23573    799  -4785   3862       C  
ATOM   1867  O   GLU A 343      -3.131 -28.974 106.131  1.00208.14           O  
ANISOU 1867  O   GLU A 343    24476  30920  23687    847  -4675   3725       O  
ATOM   1868  CB  GLU A 343      -3.932 -31.348 107.817  1.00223.48           C  
ANISOU 1868  CB  GLU A 343    26183  32966  25763   1080  -5489   3845       C  
ATOM   1869  CG  GLU A 343      -4.215 -32.723 107.233  1.00230.20           C  
ANISOU 1869  CG  GLU A 343    27246  33500  26721   1375  -5628   3663       C  
ATOM   1870  CD  GLU A 343      -5.476 -33.374 107.790  1.00234.85           C  
ANISOU 1870  CD  GLU A 343    28063  33684  27483   1514  -5674   3561       C  
ATOM   1871  OE1 GLU A 343      -6.372 -32.661 108.292  1.00235.76           O  
ANISOU 1871  OE1 GLU A 343    28245  33680  27653   1416  -5581   3716       O  
ATOM   1872  OE2 GLU A 343      -5.573 -34.617 107.717  1.00237.09           O  
ANISOU 1872  OE2 GLU A 343    28454  33792  27838   1733  -5783   3331       O  
ATOM   1873  N   PRO A 344      -4.224 -27.912 107.777  1.00197.42           N  
ANISOU 1873  N   PRO A 344    23121  29430  22461    555  -4494   3860       N  
ATOM   1874  CA  PRO A 344      -3.463 -26.677 107.562  1.00189.49           C  
ANISOU 1874  CA  PRO A 344    22119  28481  21400    339  -4049   3695       C  
ATOM   1875  C   PRO A 344      -1.981 -26.882 107.832  1.00183.25           C  
ANISOU 1875  C   PRO A 344    21102  28006  20518    243  -4033   3434       C  
ATOM   1876  O   PRO A 344      -1.582 -27.728 108.634  1.00191.06           O  
ANISOU 1876  O   PRO A 344    21895  29182  21518    233  -4299   3381       O  
ATOM   1877  CB  PRO A 344      -4.082 -25.694 108.566  1.00194.46           C  
ANISOU 1877  CB  PRO A 344    22799  28984  22102     87  -3780   3756       C  
ATOM   1878  CG  PRO A 344      -4.703 -26.558 109.608  1.00202.38           C  
ANISOU 1878  CG  PRO A 344    23737  29985  23175    124  -4113   3855       C  
ATOM   1879  CD  PRO A 344      -5.181 -27.786 108.889  1.00198.86           C  
ANISOU 1879  CD  PRO A 344    23319  29489  22749    459  -4539   4005       C  
ATOM   1880  N   LEU A 345      -1.166 -26.098 107.139  1.00184.52           N  
ANISOU 1880  N   LEU A 345    21276  28225  20607    169  -3723   3296       N  
ATOM   1881  CA  LEU A 345       0.280 -26.127 107.279  1.00179.24           C  
ANISOU 1881  CA  LEU A 345    20399  27832  19870     69  -3654   3087       C  
ATOM   1882  C   LEU A 345       0.723 -24.840 107.962  1.00175.69           C  
ANISOU 1882  C   LEU A 345    19928  27460  19366   -276  -3286   2980       C  
ATOM   1883  O   LEU A 345      -0.045 -23.884 108.078  1.00166.77           O  
ANISOU 1883  O   LEU A 345    18967  26145  18254   -400  -3029   3046       O  
ATOM   1884  CB  LEU A 345       0.963 -26.306 105.918  1.00174.54           C  
ANISOU 1884  CB  LEU A 345    19843  27246  19229    264  -3593   3010       C  
ATOM   1885  CG  LEU A 345       0.522 -27.580 105.189  1.00164.06           C  
ANISOU 1885  CG  LEU A 345    18593  25817  17924    576  -3927   3113       C  
ATOM   1886  CD1 LEU A 345       1.237 -27.737 103.856  1.00168.31           C  
ANISOU 1886  CD1 LEU A 345    19210  26338  18402    732  -3821   3021       C  
ATOM   1887  CD2 LEU A 345       0.731 -28.809 106.069  1.00150.21           C  
ANISOU 1887  CD2 LEU A 345    16617  24224  16232    640  -4287   3123       C  
ATOM   1888  N   ASP A 346       1.953 -24.829 108.455  1.00169.88           N  
ANISOU 1888  N   ASP A 346    18984  26988  18574   -449  -3256   2839       N  
ATOM   1889  CA  ASP A 346       2.409 -23.647 109.165  1.00179.94           C  
ANISOU 1889  CA  ASP A 346    20259  28347  19764   -814  -2927   2747       C  
ATOM   1890  C   ASP A 346       2.915 -22.583 108.193  1.00177.00           C  
ANISOU 1890  C   ASP A 346    19976  27951  19324   -825  -2556   2650       C  
ATOM   1891  O   ASP A 346       3.085 -22.816 106.994  1.00171.41           O  
ANISOU 1891  O   ASP A 346    19303  27193  18631   -568  -2566   2637       O  
ATOM   1892  CB  ASP A 346       3.484 -24.022 110.178  1.00194.35           C  
ANISOU 1892  CB  ASP A 346    21826  30467  21550  -1055  -3067   2684       C  
ATOM   1893  CG  ASP A 346       2.989 -25.016 111.202  1.00198.69           C  
ANISOU 1893  CG  ASP A 346    22270  31054  22167  -1081  -3432   2775       C  
ATOM   1894  OD1 ASP A 346       1.909 -24.770 111.784  1.00199.95           O  
ANISOU 1894  OD1 ASP A 346    22592  31036  22342  -1160  -3407   2845       O  
ATOM   1895  OD2 ASP A 346       3.667 -26.041 111.420  1.00200.34           O  
ANISOU 1895  OD2 ASP A 346    22227  31461  22433  -1019  -3733   2789       O  
ATOM   1896  N   GLY A 347       3.151 -21.390 108.735  1.00178.99           N  
ANISOU 1896  N   GLY A 347    20282  28235  19493  -1147  -2216   2577       N  
ATOM   1897  CA  GLY A 347       3.658 -20.285 107.962  1.00178.80           C  
ANISOU 1897  CA  GLY A 347    20325  28211  19399  -1196  -1850   2477       C  
ATOM   1898  C   GLY A 347       2.568 -19.606 107.156  1.00179.48           C  
ANISOU 1898  C   GLY A 347    20632  28008  19554  -1075  -1628   2561       C  
ATOM   1899  O   GLY A 347       1.373 -19.850 107.353  1.00186.87           O  
ANISOU 1899  O   GLY A 347    21682  28727  20593  -1003  -1716   2719       O  
ATOM   1900  N   PRO A 348       2.967 -18.723 106.236  1.00167.60           N  
ANISOU 1900  N   PRO A 348    19177  26495  18009  -1061  -1337   2480       N  
ATOM   1901  CA  PRO A 348       1.974 -18.021 105.407  1.00178.85           C  
ANISOU 1901  CA  PRO A 348    20781  27652  19521   -974  -1118   2588       C  
ATOM   1902  C   PRO A 348       1.149 -18.937 104.521  1.00213.94           C  
ANISOU 1902  C   PRO A 348    25304  31918  24067   -661  -1408   2754       C  
ATOM   1903  O   PRO A 348       0.070 -18.527 104.076  1.00222.26           O  
ANISOU 1903  O   PRO A 348    26500  32719  25230   -620  -1302   2933       O  
ATOM   1904  CB  PRO A 348       2.832 -17.057 104.576  1.00161.96           C  
ANISOU 1904  CB  PRO A 348    18627  25608  17300  -1015   -811   2439       C  
ATOM   1905  CG  PRO A 348       4.068 -16.856 105.394  1.00148.57           C  
ANISOU 1905  CG  PRO A 348    16789  24194  15469  -1243   -755   2275       C  
ATOM   1906  CD  PRO A 348       4.323 -18.188 106.040  1.00151.38           C  
ANISOU 1906  CD  PRO A 348    17008  24674  15836  -1175  -1166   2308       C  
ATOM   1907  N   ALA A 349       1.619 -20.154 104.239  1.00203.36           N  
ANISOU 1907  N   ALA A 349    23879  30689  22699   -455  -1758   2724       N  
ATOM   1908  CA  ALA A 349       0.812 -21.093 103.468  1.00201.45           C  
ANISOU 1908  CA  ALA A 349    23747  30272  22521   -186  -2050   2888       C  
ATOM   1909  C   ALA A 349      -0.460 -21.459 104.222  1.00197.62           C  
ANISOU 1909  C   ALA A 349    23330  29611  22146   -185  -2225   3104       C  
ATOM   1910  O   ALA A 349      -1.561 -21.443 103.657  1.00197.46           O  
ANISOU 1910  O   ALA A 349    23466  29343  22218    -86  -2265   3326       O  
ATOM   1911  CB  ALA A 349       1.628 -22.345 103.146  1.00202.43           C  
ANISOU 1911  CB  ALA A 349    23768  30549  22597     14  -2353   2800       C  
ATOM   1912  N   GLY A 350      -0.328 -21.800 105.506  1.00206.71           N  
ANISOU 1912  N   GLY A 350    24363  30882  23296   -309  -2339   3066       N  
ATOM   1913  CA  GLY A 350      -1.507 -22.001 106.328  1.00186.36           C  
ANISOU 1913  CA  GLY A 350    21852  28129  20828   -337  -2450   3257       C  
ATOM   1914  C   GLY A 350      -2.280 -20.723 106.561  1.00177.57           C  
ANISOU 1914  C   GLY A 350    20870  26796  19801   -528  -2049   3362       C  
ATOM   1915  O   GLY A 350      -3.503 -20.757 106.720  1.00178.57           O  
ANISOU 1915  O   GLY A 350    21106  26668  20073   -479  -2082   3605       O  
ATOM   1916  N   ALA A 351      -1.586 -19.582 106.585  1.00200.42           N  
ANISOU 1916  N   ALA A 351    23753  29774  22623   -747  -1653   3199       N  
ATOM   1917  CA  ALA A 351      -2.286 -18.305 106.632  1.00191.41           C  
ANISOU 1917  CA  ALA A 351    22739  28407  21583   -915  -1214   3301       C  
ATOM   1918  C   ALA A 351      -3.160 -18.127 105.400  1.00189.88           C  
ANISOU 1918  C   ALA A 351    22649  27966  21530   -727  -1189   3533       C  
ATOM   1919  O   ALA A 351      -4.201 -17.465 105.465  1.00178.38           O  
ANISOU 1919  O   ALA A 351    21289  26233  20253   -789   -954   3760       O  
ATOM   1920  CB  ALA A 351      -1.288 -17.153 106.758  1.00182.35           C  
ANISOU 1920  CB  ALA A 351    21559  27417  20308  -1170   -810   3072       C  
ATOM   1921  N   VAL A 352      -2.753 -18.712 104.273  1.00192.55           N  
ANISOU 1921  N   VAL A 352    22975  28386  21800   -519  -1417   3501       N  
ATOM   1922  CA  VAL A 352      -3.614 -18.741 103.098  1.00191.60           C  
ANISOU 1922  CA  VAL A 352    22974  28036  21788   -367  -1480   3754       C  
ATOM   1923  C   VAL A 352      -4.715 -19.782 103.263  1.00194.99           C  
ANISOU 1923  C   VAL A 352    23475  28289  22322   -200  -1863   4036       C  
ATOM   1924  O   VAL A 352      -5.886 -19.510 102.978  1.00196.07           O  
ANISOU 1924  O   VAL A 352    23711  28146  22640   -187  -1822   4364       O  
ATOM   1925  CB  VAL A 352      -2.769 -19.004 101.836  1.00189.86           C  
ANISOU 1925  CB  VAL A 352    22759  27949  21429   -238  -1571   3608       C  
ATOM   1926  CG1 VAL A 352      -3.652 -19.438 100.673  1.00188.13           C  
ANISOU 1926  CG1 VAL A 352    22696  27512  21274    -88  -1778   3883       C  
ATOM   1927  CG2 VAL A 352      -1.951 -17.775 101.471  1.00189.38           C  
ANISOU 1927  CG2 VAL A 352    22651  27995  21311   -393  -1158   3409       C  
ATOM   1928  N   LEU A 353      -4.364 -20.983 103.740  1.00178.00           N  
ANISOU 1928  N   LEU A 353    21260  26296  20077    -76  -2241   3939       N  
ATOM   1929  CA  LEU A 353      -5.361 -22.043 103.882  1.00188.36           C  
ANISOU 1929  CA  LEU A 353    22636  27463  21470    100  -2637   4195       C  
ATOM   1930  C   LEU A 353      -6.395 -21.724 104.955  1.00219.26           C  
ANISOU 1930  C   LEU A 353    26567  31180  25562      2  -2546   4403       C  
ATOM   1931  O   LEU A 353      -7.554 -22.139 104.836  1.00204.80           O  
ANISOU 1931  O   LEU A 353    24828  29115  23872    121  -2745   4734       O  
ATOM   1932  CB  LEU A 353      -4.674 -23.376 104.183  1.00175.49           C  
ANISOU 1932  CB  LEU A 353    20905  26064  19710    249  -3036   4026       C  
ATOM   1933  CG  LEU A 353      -5.578 -24.610 104.205  1.00167.64           C  
ANISOU 1933  CG  LEU A 353    19977  24956  18764    461  -3492   4261       C  
ATOM   1934  CD1 LEU A 353      -6.486 -24.625 102.992  1.00112.12           C  
ANISOU 1934  CD1 LEU A 353    13151  17671  11778    565  -3572   4563       C  
ATOM   1935  CD2 LEU A 353      -4.745 -25.875 104.246  1.00159.36           C  
ANISOU 1935  CD2 LEU A 353    18821  24141  17588    617  -3831   4073       C  
ATOM   1936  N   GLU A 354      -6.002 -21.003 106.008  1.00208.45           N  
ANISOU 1936  N   GLU A 354    25128  29886  24187   -225  -2242   4230       N  
ATOM   1937  CA  GLU A 354      -6.977 -20.583 107.008  1.00216.29           C  
ANISOU 1937  CA  GLU A 354    26174  30650  25356   -347  -2069   4418       C  
ATOM   1938  C   GLU A 354      -7.972 -19.592 106.414  1.00219.35           C  
ANISOU 1938  C   GLU A 354    26673  30704  25966   -384  -1732   4727       C  
ATOM   1939  O   GLU A 354      -9.097 -19.462 106.911  1.00220.83           O  
ANISOU 1939  O   GLU A 354    26926  30608  26372   -391  -1661   5021       O  
ATOM   1940  CB  GLU A 354      -6.262 -19.999 108.230  1.00221.69           C  
ANISOU 1940  CB  GLU A 354    26803  31485  25946   -635  -1789   4149       C  
ATOM   1941  CG  GLU A 354      -5.567 -21.060 109.092  1.00224.33           C  
ANISOU 1941  CG  GLU A 354    27007  32097  26131   -636  -2161   3950       C  
ATOM   1942  CD  GLU A 354      -4.761 -20.469 110.239  1.00226.45           C  
ANISOU 1942  CD  GLU A 354    27231  32536  26274   -982  -1906   3701       C  
ATOM   1943  OE1 GLU A 354      -5.226 -19.489 110.857  1.00227.43           O  
ANISOU 1943  OE1 GLU A 354    27476  32467  26468  -1216  -1496   3744       O  
ATOM   1944  OE2 GLU A 354      -3.660 -20.989 110.525  1.00225.93           O  
ANISOU 1944  OE2 GLU A 354    27015  32785  26044  -1039  -2105   3481       O  
ATOM   1945  N   CYS A 355      -7.570 -18.885 105.357  1.00235.22           N  
ANISOU 1945  N   CYS A 355    28690  32735  27946   -411  -1516   4683       N  
ATOM   1946  CA  CYS A 355      -8.455 -17.959 104.665  1.00207.69           C  
ANISOU 1946  CA  CYS A 355    25273  28951  24690   -456  -1214   5000       C  
ATOM   1947  C   CYS A 355      -9.410 -18.674 103.721  1.00193.39           C  
ANISOU 1947  C   CYS A 355    23537  26951  22991   -255  -1577   5386       C  
ATOM   1948  O   CYS A 355     -10.444 -18.105 103.357  1.00194.15           O  
ANISOU 1948  O   CYS A 355    23679  26743  23347   -289  -1406   5776       O  
ATOM   1949  CB  CYS A 355      -7.646 -16.924 103.878  1.00203.34           C  
ANISOU 1949  CB  CYS A 355    24688  28511  24061   -578   -861   4806       C  
ATOM   1950  SG  CYS A 355      -6.709 -15.748 104.882  1.00207.29           S  
ANISOU 1950  SG  CYS A 355    25136  29163  24461   -875   -331   4444       S  
ATOM   1951  N   LEU A 356      -9.090 -19.905 103.323  1.00201.89           N  
ANISOU 1951  N   LEU A 356    24632  28189  23887    -65  -2063   5312       N  
ATOM   1952  CA  LEU A 356      -9.844 -20.610 102.299  1.00209.04           C  
ANISOU 1952  CA  LEU A 356    25651  28945  24830     92  -2422   5647       C  
ATOM   1953  C   LEU A 356     -10.845 -21.612 102.868  1.00212.81           C  
ANISOU 1953  C   LEU A 356    26174  29277  25406    243  -2810   5938       C  
ATOM   1954  O   LEU A 356     -11.568 -22.247 102.093  1.00209.52           O  
ANISOU 1954  O   LEU A 356    25871  28720  25016    359  -3139   6263       O  
ATOM   1955  CB  LEU A 356      -8.866 -21.341 101.371  1.00213.98           C  
ANISOU 1955  CB  LEU A 356    26312  29809  25179    199  -2684   5388       C  
ATOM   1956  CG  LEU A 356      -7.787 -20.498 100.677  1.00216.36           C  
ANISOU 1956  CG  LEU A 356    26576  30273  25358     86  -2360   5090       C  
ATOM   1957  CD1 LEU A 356      -6.784 -21.380  99.934  1.00215.37           C  
ANISOU 1957  CD1 LEU A 356    26488  30367  24974    216  -2619   4822       C  
ATOM   1958  CD2 LEU A 356      -8.372 -19.438  99.758  1.00217.19           C  
ANISOU 1958  CD2 LEU A 356    26735  30165  25622    -43  -2080   5356       C  
ATOM   1959  N   VAL A 357     -10.907 -21.774 104.191  1.00231.18           N  
ANISOU 1959  N   VAL A 357    28427  31634  27778    227  -2790   5839       N  
ATOM   1960  CA  VAL A 357     -11.802 -22.722 104.845  1.00225.09           C  
ANISOU 1960  CA  VAL A 357    27680  30744  27100    376  -3157   6083       C  
ATOM   1961  C   VAL A 357     -12.641 -21.989 105.889  1.00226.42           C  
ANISOU 1961  C   VAL A 357    27837  30653  27539    258  -2827   6285       C  
ATOM   1962  O   VAL A 357     -12.492 -20.787 106.107  1.00221.20           O  
ANISOU 1962  O   VAL A 357    27158  29911  26976     56  -2313   6218       O  
ATOM   1963  CB  VAL A 357     -11.037 -23.898 105.488  1.00215.25           C  
ANISOU 1963  CB  VAL A 357    26350  29801  25634    493  -3534   5757       C  
ATOM   1964  CG1 VAL A 357     -10.188 -24.615 104.448  1.00211.17           C  
ANISOU 1964  CG1 VAL A 357    25855  29502  24877    612  -3795   5565       C  
ATOM   1965  CG2 VAL A 357     -10.177 -23.406 106.644  1.00211.07           C  
ANISOU 1965  CG2 VAL A 357    25695  29463  25038    304  -3250   5384       C  
ATOM   1966  N   LEU A 358     -13.540 -22.736 106.528  1.00221.04           N  
ANISOU 1966  N   LEU A 358    27178  29827  26980    388  -3118   6537       N  
ATOM   1967  CA  LEU A 358     -14.384 -22.267 107.616  1.00228.48           C  
ANISOU 1967  CA  LEU A 358    28128  30502  28180    307  -2857   6736       C  
ATOM   1968  C   LEU A 358     -13.878 -22.834 108.942  1.00248.73           C  
ANISOU 1968  C   LEU A 358    30628  33273  30606    275  -2983   6400       C  
ATOM   1969  O   LEU A 358     -12.809 -23.452 109.014  1.00251.68           O  
ANISOU 1969  O   LEU A 358    30919  34002  30707    292  -3219   6019       O  
ATOM   1970  CB  LEU A 358     -15.854 -22.614 107.371  1.00214.77           C  
ANISOU 1970  CB  LEU A 358    26464  28412  26726    463  -3069   7328       C  
ATOM   1971  CG  LEU A 358     -16.594 -21.707 106.391  1.00205.68           C  
ANISOU 1971  CG  LEU A 358    25358  26954  25837    395  -2788   7770       C  
ATOM   1972  CD1 LEU A 358     -18.006 -22.206 106.185  1.00200.31           C  
ANISOU 1972  CD1 LEU A 358    24781  25901  25427    495  -2812   7677       C  
ATOM   1973  CD2 LEU A 358     -16.612 -20.287 106.939  1.00202.53           C  
ANISOU 1973  CD2 LEU A 358    24931  26369  25651    160  -2089   7734       C  
ATOM   1974  N   SER A 359     -14.656 -22.604 110.003  1.00240.12           N  
ANISOU 1974  N   SER A 359    29572  31942  29722    211  -2807   6562       N  
ATOM   1975  CA  SER A 359     -14.290 -23.093 111.330  1.00248.69           C  
ANISOU 1975  CA  SER A 359    30611  33188  30693    136  -2915   6281       C  
ATOM   1976  C   SER A 359     -14.089 -24.604 111.345  1.00255.93           C  
ANISOU 1976  C   SER A 359    31441  34362  31440    371  -3584   6204       C  
ATOM   1977  O   SER A 359     -13.186 -25.107 112.025  1.00256.09           O  
ANISOU 1977  O   SER A 359    31354  34695  31252    298  -3748   5837       O  
ATOM   1978  CB  SER A 359     -15.359 -22.689 112.344  1.00249.24           C  
ANISOU 1978  CB  SER A 359    30768  32890  31042     59  -2643   6542       C  
ATOM   1979  OG  SER A 359     -15.381 -21.286 112.539  1.00252.28           O  
ANISOU 1979  OG  SER A 359    31233  33059  31562   -202  -1961   6535       O  
ATOM   1980  N   SER A 360     -14.921 -25.349 110.614  1.00261.21           N  
ANISOU 1980  N   SER A 360    32152  34894  32201    636  -3965   6546       N  
ATOM   1981  CA  SER A 360     -14.741 -26.797 110.575  1.00258.83           C  
ANISOU 1981  CA  SER A 360    31876  34684  31783    839  -4289   6032       C  
ATOM   1982  C   SER A 360     -13.480 -27.185 109.811  1.00258.12           C  
ANISOU 1982  C   SER A 360    31706  34955  31414    872  -4488   5784       C  
ATOM   1983  O   SER A 360     -12.906 -28.250 110.065  1.00253.46           O  
ANISOU 1983  O   SER A 360    31072  34535  30695    982  -4710   5377       O  
ATOM   1984  CB  SER A 360     -15.965 -27.464 109.948  1.00257.18           C  
ANISOU 1984  CB  SER A 360    31878  34097  31739   1050  -4260   5921       C  
ATOM   1985  OG  SER A 360     -16.102 -27.096 108.587  1.00259.82           O  
ANISOU 1985  OG  SER A 360    32307  34331  32081   1062  -4181   6067       O  
ATOM   1986  N   GLY A 361     -13.036 -26.343 108.879  1.00259.28           N  
ANISOU 1986  N   GLY A 361    31832  35205  31478    783  -4377   6024       N  
ATOM   1987  CA  GLY A 361     -11.889 -26.645 108.048  1.00254.95           C  
ANISOU 1987  CA  GLY A 361    31224  34971  30676    815  -4521   5798       C  
ATOM   1988  C   GLY A 361     -12.206 -27.129 106.651  1.00245.22           C  
ANISOU 1988  C   GLY A 361    30189  33539  29444    979  -4579   5742       C  
ATOM   1989  O   GLY A 361     -11.274 -27.390 105.881  1.00237.92           O  
ANISOU 1989  O   GLY A 361    29240  32847  28310   1011  -4693   5596       O  
ATOM   1990  N   MET A 362     -13.480 -27.258 106.298  1.00259.05           N  
ANISOU 1990  N   MET A 362    32139  34882  31407   1062  -4486   5841       N  
ATOM   1991  CA  MET A 362     -13.842 -27.739 104.973  1.00254.87           C  
ANISOU 1991  CA  MET A 362    31821  34178  30840   1170  -4533   5780       C  
ATOM   1992  C   MET A 362     -13.562 -26.692 103.898  1.00254.77           C  
ANISOU 1992  C   MET A 362    31812  34194  30795   1018  -4399   6095       C  
ATOM   1993  O   MET A 362     -13.693 -25.485 104.122  1.00256.53           O  
ANISOU 1993  O   MET A 362    31931  34393  31144    852  -4162   6448       O  
ATOM   1994  CB  MET A 362     -15.318 -28.129 104.950  1.00251.39           C  
ANISOU 1994  CB  MET A 362    31560  33353  30603   1261  -4449   5794       C  
ATOM   1995  CG  MET A 362     -15.709 -29.029 103.802  1.00248.15           C  
ANISOU 1995  CG  MET A 362    31377  32823  30086   1399  -4540   5631       C  
ATOM   1996  SD  MET A 362     -14.755 -30.552 103.782  1.00244.15           S  
ANISOU 1996  SD  MET A 362    30902  32567  29296   1631  -4795   5158       S  
ATOM   1997  CE  MET A 362     -16.002 -31.681 103.177  1.00242.78           C  
ANISOU 1997  CE  MET A 362    30982  32155  29107   1823  -4770   5019       C  
ATOM   1998  N   LEU A 363     -13.173 -27.174 102.718  1.00256.96           N  
ANISOU 1998  N   LEU A 363    32224  34514  30896   1075  -4522   5975       N  
ATOM   1999  CA  LEU A 363     -12.869 -26.338 101.564  1.00243.22           C  
ANISOU 1999  CA  LEU A 363    30520  32806  29087    936  -4424   6224       C  
ATOM   2000  C   LEU A 363     -14.075 -26.248 100.630  1.00238.56           C  
ANISOU 2000  C   LEU A 363    30141  31834  28668    896  -4326   6396       C  
ATOM   2001  O   LEU A 363     -14.916 -27.152 100.581  1.00243.01           O  
ANISOU 2001  O   LEU A 363    30860  32189  29285   1021  -4401   6232       O  
ATOM   2002  CB  LEU A 363     -11.647 -26.886 100.819  1.00238.63           C  
ANISOU 2002  CB  LEU A 363    29960  32521  28188    987  -4613   6004       C  
ATOM   2003  CG  LEU A 363     -11.646 -28.359 100.371  1.00237.56           C  
ANISOU 2003  CG  LEU A 363    30023  32313  27927   1186  -4834   5667       C  
ATOM   2004  CD1 LEU A 363     -12.444 -28.628  99.078  1.00237.98           C  
ANISOU 2004  CD1 LEU A 363    30367  32079  27975   1176  -4825   5760       C  
ATOM   2005  CD2 LEU A 363     -10.231 -28.909 100.266  1.00239.12           C  
ANISOU 2005  CD2 LEU A 363    30125  32867  27862   1253  -4997   5421       C  
ATOM   2006  N   VAL A 364     -14.157 -25.142  99.895  1.00236.65           N  
ANISOU 2006  N   VAL A 364    29884  31530  28503    712  -4135   6724       N  
ATOM   2007  CA  VAL A 364     -15.220 -24.912  98.915  1.00229.28           C  
ANISOU 2007  CA  VAL A 364    29105  30271  27739    615  -4031   6907       C  
ATOM   2008  C   VAL A 364     -14.618 -24.804  97.516  1.00229.73           C  
ANISOU 2008  C   VAL A 364    29289  30418  27581    512  -4099   6948       C  
ATOM   2009  O   VAL A 364     -13.860 -23.861  97.247  1.00231.79           O  
ANISOU 2009  O   VAL A 364    29440  30860  27771    381  -3976   7129       O  
ATOM   2010  CB  VAL A 364     -16.045 -23.664  99.263  1.00231.90           C  
ANISOU 2010  CB  VAL A 364    29302  30381  28430    459  -3695   7270       C  
ATOM   2011  CG1 VAL A 364     -17.203 -23.516  98.290  1.00234.10           C  
ANISOU 2011  CG1 VAL A 364    29698  30348  28903    351  -3609   7413       C  
ATOM   2012  CG2 VAL A 364     -16.558 -23.755 100.693  1.00233.45           C  
ANISOU 2012  CG2 VAL A 364    29394  30493  28814    546  -3617   7237       C  
ATOM   2013  N   PRO A 365     -14.895 -25.749  96.610  1.00217.64           N  
ANISOU 2013  N   PRO A 365    27995  28786  25914    562  -4270   6790       N  
ATOM   2014  CA  PRO A 365     -14.330 -25.661  95.250  1.00221.52           C  
ANISOU 2014  CA  PRO A 365    28642  29342  26183    435  -4334   6842       C  
ATOM   2015  C   PRO A 365     -14.603 -24.348  94.524  1.00239.90           C  
ANISOU 2015  C   PRO A 365    30916  31566  28671    174  -4111   7196       C  
ATOM   2016  O   PRO A 365     -13.749 -23.920  93.737  1.00240.46           O  
ANISOU 2016  O   PRO A 365    31025  31803  28538     53  -4111   7259       O  
ATOM   2017  CB  PRO A 365     -14.986 -26.847  94.530  1.00217.34           C  
ANISOU 2017  CB  PRO A 365    28376  28640  25563    509  -4484   6682       C  
ATOM   2018  CG  PRO A 365     -15.274 -27.826  95.609  1.00218.19           C  
ANISOU 2018  CG  PRO A 365    28448  28753  25701    758  -4566   6420       C  
ATOM   2019  CD  PRO A 365     -15.655 -26.996  96.811  1.00220.43           C  
ANISOU 2019  CD  PRO A 365    28492  28995  26266    741  -4398   6551       C  
ATOM   2020  N   GLU A 366     -15.758 -23.703  94.738  1.00228.81           N  
ANISOU 2020  N   GLU A 366    29417  29896  27624     80  -3904   7419       N  
ATOM   2021  CA  GLU A 366     -16.010 -22.413  94.090  1.00245.21           C  
ANISOU 2021  CA  GLU A 366    31396  31872  29900   -166  -3653   7748       C  
ATOM   2022  C   GLU A 366     -14.918 -21.399  94.409  1.00241.69           C  
ANISOU 2022  C   GLU A 366    30768  31682  29381   -226  -3470   7884       C  
ATOM   2023  O   GLU A 366     -14.538 -20.598  93.546  1.00248.48           O  
ANISOU 2023  O   GLU A 366    31617  32593  30199   -414  -3338   8056       O  
ATOM   2024  CB  GLU A 366     -17.379 -21.855  94.488  1.00256.19           C  
ANISOU 2024  CB  GLU A 366    32655  32963  31722   -230  -3425   7940       C  
ATOM   2025  CG  GLU A 366     -18.567 -22.503  93.798  1.00269.58           C  
ANISOU 2025  CG  GLU A 366    34498  34431  33501   -267  -3533   7903       C  
ATOM   2026  CD  GLU A 366     -18.843 -21.873  92.435  1.00280.68           C  
ANISOU 2026  CD  GLU A 366    35932  35746  34967   -530  -3472   8106       C  
ATOM   2027  OE1 GLU A 366     -19.843 -22.252  91.788  1.00284.26           O  
ANISOU 2027  OE1 GLU A 366    36469  36034  35502   -608  -3539   8124       O  
ATOM   2028  OE2 GLU A 366     -18.062 -20.990  92.014  1.00285.81           O  
ANISOU 2028  OE2 GLU A 366    36511  36508  35577   -668  -3350   8248       O  
ATOM   2029  N   LEU A 367     -14.410 -21.410  95.639  1.00255.12           N  
ANISOU 2029  N   LEU A 367    32319  33567  31050    -84  -3439   7812       N  
ATOM   2030  CA  LEU A 367     -13.288 -20.552  95.994  1.00224.26           C  
ANISOU 2030  CA  LEU A 367    28242  29923  27044   -125  -3129   7607       C  
ATOM   2031  C   LEU A 367     -11.951 -21.204  95.680  1.00200.42           C  
ANISOU 2031  C   LEU A 367    25295  27214  23641    -30  -3249   7048       C  
ATOM   2032  O   LEU A 367     -10.959 -20.494  95.484  1.00192.69           O  
ANISOU 2032  O   LEU A 367    24231  26406  22576    -98  -2926   6672       O  
ATOM   2033  CB  LEU A 367     -13.351 -20.163  97.481  1.00225.51           C  
ANISOU 2033  CB  LEU A 367    28211  30081  27390    -62  -2860   7483       C  
ATOM   2034  CG  LEU A 367     -12.907 -21.121  98.597  1.00224.45           C  
ANISOU 2034  CG  LEU A 367    28049  30134  27099    132  -3078   7153       C  
ATOM   2035  CD1 LEU A 367     -11.423 -20.991  98.899  1.00220.76           C  
ANISOU 2035  CD1 LEU A 367    27490  30001  26386    140  -2891   6527       C  
ATOM   2036  CD2 LEU A 367     -13.718 -20.905  99.871  1.00221.13           C  
ANISOU 2036  CD2 LEU A 367    27527  29537  26956    156  -2949   7359       C  
ATOM   2037  N   ALA A 368     -11.907 -22.536  95.634  1.00214.72           N  
ANISOU 2037  N   ALA A 368    27256  29089  25239    128  -3691   7003       N  
ATOM   2038  CA  ALA A 368     -10.655 -23.244  95.392  1.00209.95           C  
ANISOU 2038  CA  ALA A 368    26710  28750  24313    236  -3786   6503       C  
ATOM   2039  C   ALA A 368     -10.188 -23.065  93.951  1.00210.52           C  
ANISOU 2039  C   ALA A 368    26961  28824  24202    105  -3745   6444       C  
ATOM   2040  O   ALA A 368      -9.006 -22.801  93.704  1.00208.95           O  
ANISOU 2040  O   ALA A 368    26716  28823  23852    108  -3525   6008       O  
ATOM   2041  CB  ALA A 368     -10.818 -24.726  95.725  1.00208.35           C  
ANISOU 2041  CB  ALA A 368    26615  28585  23963    437  -4250   6509       C  
ATOM   2042  N   ILE A 369     -11.100 -23.244  92.986  1.00215.46           N  
ANISOU 2042  N   ILE A 369    27805  29227  24834    -24  -3971   6895       N  
ATOM   2043  CA  ILE A 369     -10.726 -23.193  91.568  1.00207.75           C  
ANISOU 2043  CA  ILE A 369    27054  28231  23651   -186  -3978   6863       C  
ATOM   2044  C   ILE A 369      -9.911 -21.944  91.224  1.00201.80           C  
ANISOU 2044  C   ILE A 369    26149  27588  22939   -311  -3520   6583       C  
ATOM   2045  O   ILE A 369      -8.865 -22.080  90.574  1.00192.60           O  
ANISOU 2045  O   ILE A 369    25078  26565  21535   -306  -3441   6204       O  
ATOM   2046  CB  ILE A 369     -11.966 -23.363  90.684  1.00201.49           C  
ANISOU 2046  CB  ILE A 369    26483  27133  22940   -367  -4196   7356       C  
ATOM   2047  CG1 ILE A 369     -12.592 -24.750  90.882  1.00205.37           C  
ANISOU 2047  CG1 ILE A 369    27145  27453  23432   -178  -4407   7129       C  
ATOM   2048  CG2 ILE A 369     -11.621 -23.149  89.218  1.00194.23           C  
ANISOU 2048  CG2 ILE A 369    25803  26198  21797   -612  -4214   7426       C  
ATOM   2049  CD1 ILE A 369     -11.589 -25.891  90.922  1.00203.92           C  
ANISOU 2049  CD1 ILE A 369    27102  27483  22893      7  -4634   6810       C  
ATOM   2050  N   PRO A 370     -10.322 -20.725  91.596  1.00190.53           N  
ANISOU 2050  N   PRO A 370    24495  26090  21806   -424  -3196   6754       N  
ATOM   2051  CA  PRO A 370      -9.449 -19.569  91.326  1.00197.40           C  
ANISOU 2051  CA  PRO A 370    25214  27096  22693   -523  -2759   6439       C  
ATOM   2052  C   PRO A 370      -8.080 -19.655  91.993  1.00221.87           C  
ANISOU 2052  C   PRO A 370    28185  30486  25628   -355  -2580   5836       C  
ATOM   2053  O   PRO A 370      -7.100 -19.156  91.425  1.00221.00           O  
ANISOU 2053  O   PRO A 370    28056  30521  25394   -401  -2353   5509       O  
ATOM   2054  CB  PRO A 370     -10.265 -18.383  91.861  1.00181.18           C  
ANISOU 2054  CB  PRO A 370    22933  24889  21019   -644  -2448   6763       C  
ATOM   2055  CG  PRO A 370     -11.680 -18.842  91.803  1.00176.49           C  
ANISOU 2055  CG  PRO A 370    22437  24016  20604   -690  -2755   7376       C  
ATOM   2056  CD  PRO A 370     -11.616 -20.297  92.163  1.00185.40           C  
ANISOU 2056  CD  PRO A 370    23732  25208  21504   -482  -3183   7271       C  
ATOM   2057  N   VAL A 371      -7.981 -20.262  93.179  1.00210.66           N  
ANISOU 2057  N   VAL A 371    26669  29157  24214   -176  -2682   5700       N  
ATOM   2058  CA  VAL A 371      -6.699 -20.326  93.883  1.00215.72           C  
ANISOU 2058  CA  VAL A 371    27162  30076  24727    -54  -2525   5185       C  
ATOM   2059  C   VAL A 371      -5.713 -21.240  93.157  1.00216.75           C  
ANISOU 2059  C   VAL A 371    27443  30340  24570     53  -2694   4881       C  
ATOM   2060  O   VAL A 371      -4.551 -20.874  92.943  1.00223.76           O  
ANISOU 2060  O   VAL A 371    28258  31409  25350     61  -2462   4512       O  
ATOM   2061  CB  VAL A 371      -6.918 -20.778  95.339  1.00214.47           C  
ANISOU 2061  CB  VAL A 371    26864  29968  24657     68  -2620   5163       C  
ATOM   2062  CG1 VAL A 371      -5.594 -20.855  96.086  1.00216.22           C  
ANISOU 2062  CG1 VAL A 371    26920  30482  24752    147  -2485   4680       C  
ATOM   2063  CG2 VAL A 371      -7.879 -19.833  96.045  1.00213.04           C  
ANISOU 2063  CG2 VAL A 371    26561  29614  24772    -47  -2388   5459       C  
ATOM   2064  N   VAL A 372      -6.156 -22.437  92.758  1.00222.14           N  
ANISOU 2064  N   VAL A 372    28350  30922  25133    136  -3081   5043       N  
ATOM   2065  CA  VAL A 372      -5.278 -23.346  92.018  1.00211.91           C  
ANISOU 2065  CA  VAL A 372    27237  29704  23577    228  -3204   4778       C  
ATOM   2066  C   VAL A 372      -4.876 -22.733  90.679  1.00205.92           C  
ANISOU 2066  C   VAL A 372    26634  28899  22709     66  -3012   4714       C  
ATOM   2067  O   VAL A 372      -3.750 -22.921  90.203  1.00212.97           O  
ANISOU 2067  O   VAL A 372    27572  29908  23438    124  -2887   4364       O  
ATOM   2068  CB  VAL A 372      -5.940 -24.729  91.854  1.00208.30           C  
ANISOU 2068  CB  VAL A 372    27019  29120  23007    324  -3644   4994       C  
ATOM   2069  CG1 VAL A 372      -6.500 -25.203  93.187  1.00199.97           C  
ANISOU 2069  CG1 VAL A 372    25790  28095  22095    466  -3838   5108       C  
ATOM   2070  CG2 VAL A 372      -7.028 -24.721  90.784  1.00214.29           C  
ANISOU 2070  CG2 VAL A 372    28068  29617  23736    134  -3830   5436       C  
ATOM   2071  N   TYR A 373      -5.794 -21.987  90.057  1.00212.82           N  
ANISOU 2071  N   TYR A 373    27579  29590  23691   -146  -2981   5073       N  
ATOM   2072  CA  TYR A 373      -5.520 -21.328  88.785  1.00197.91           C  
ANISOU 2072  CA  TYR A 373    25826  27653  21720   -341  -2813   5054       C  
ATOM   2073  C   TYR A 373      -4.308 -20.406  88.909  1.00198.81           C  
ANISOU 2073  C   TYR A 373    25717  27982  21840   -314  -2409   4629       C  
ATOM   2074  O   TYR A 373      -3.339 -20.529  88.151  1.00209.55           O  
ANISOU 2074  O   TYR A 373    27189  29416  23015   -300  -2309   4331       O  
ATOM   2075  CB  TYR A 373      -6.781 -20.570  88.364  1.00183.06           C  
ANISOU 2075  CB  TYR A 373    23959  25556  20037   -584  -2833   5566       C  
ATOM   2076  CG  TYR A 373      -6.909 -20.173  86.912  1.00169.60           C  
ANISOU 2076  CG  TYR A 373    22470  23731  18239   -849  -2817   5720       C  
ATOM   2077  CD1 TYR A 373      -6.360 -18.995  86.432  1.00162.63           C  
ANISOU 2077  CD1 TYR A 373    21447  22929  17415   -978  -2466   5557       C  
ATOM   2078  CD2 TYR A 373      -7.641 -20.962  86.031  1.00161.44           C  
ANISOU 2078  CD2 TYR A 373    21786  22497  17058  -1001  -3168   6060       C  
ATOM   2079  CE1 TYR A 373      -6.510 -18.631  85.107  1.00166.24           C  
ANISOU 2079  CE1 TYR A 373    22093  23278  17793  -1246  -2469   5712       C  
ATOM   2080  CE2 TYR A 373      -7.796 -20.610  84.709  1.00156.10           C  
ANISOU 2080  CE2 TYR A 373    21325  21702  16283  -1296  -3173   6228       C  
ATOM   2081  CZ  TYR A 373      -7.227 -19.443  84.250  1.00170.09           C  
ANISOU 2081  CZ  TYR A 373    22938  23562  18125  -1418  -2824   6050       C  
ATOM   2082  OH  TYR A 373      -7.381 -19.082  82.931  1.00186.11           O  
ANISOU 2082  OH  TYR A 373    25172  25480  20060  -1734  -2839   6220       O  
ATOM   2083  N   LEU A 374      -4.344 -19.476  89.875  1.00194.44           N  
ANISOU 2083  N   LEU A 374    24861  27519  21497   -313  -2162   4604       N  
ATOM   2084  CA  LEU A 374      -3.207 -18.586  90.114  1.00177.82           C  
ANISOU 2084  CA  LEU A 374    22541  25632  19391   -297  -1791   4219       C  
ATOM   2085  C   LEU A 374      -1.970 -19.356  90.555  1.00166.96           C  
ANISOU 2085  C   LEU A 374    21121  24465  17852    -91  -1814   3811       C  
ATOM   2086  O   LEU A 374      -0.846 -18.965  90.221  1.00165.14           O  
ANISOU 2086  O   LEU A 374    20829  24385  17531    -70  -1588   3490       O  
ATOM   2087  CB  LEU A 374      -3.568 -17.526  91.158  1.00175.06           C  
ANISOU 2087  CB  LEU A 374    21918  25314  19282   -361  -1526   4295       C  
ATOM   2088  CG  LEU A 374      -2.451 -16.564  91.584  1.00178.21           C  
ANISOU 2088  CG  LEU A 374    22094  25943  19673   -367  -1145   3921       C  
ATOM   2089  CD1 LEU A 374      -1.863 -15.854  90.378  1.00178.91           C  
ANISOU 2089  CD1 LEU A 374    22225  26068  19683   -466   -949   3788       C  
ATOM   2090  CD2 LEU A 374      -2.956 -15.552  92.600  1.00176.72           C  
ANISOU 2090  CD2 LEU A 374    21699  25736  19711   -468   -871   4035       C  
ATOM   2091  N   LEU A 375      -2.156 -20.436  91.314  1.00173.41           N  
ANISOU 2091  N   LEU A 375    21948  25290  18650     60  -2083   3840       N  
ATOM   2092  CA  LEU A 375      -1.033 -21.282  91.703  1.00179.27           C  
ANISOU 2092  CA  LEU A 375    22632  26211  19271    248  -2130   3511       C  
ATOM   2093  C   LEU A 375      -0.297 -21.778  90.468  1.00176.20           C  
ANISOU 2093  C   LEU A 375    22470  25788  18691    284  -2123   3341       C  
ATOM   2094  O   LEU A 375       0.935 -21.680  90.378  1.00181.36           O  
ANISOU 2094  O   LEU A 375    23028  26595  19285    361  -1924   3023       O  
ATOM   2095  CB  LEU A 375      -1.543 -22.452  92.552  1.00179.23           C  
ANISOU 2095  CB  LEU A 375    22629  26185  19285    387  -2467   3633       C  
ATOM   2096  CG  LEU A 375      -0.698 -23.678  92.928  1.00175.09           C  
ANISOU 2096  CG  LEU A 375    22072  25788  18667    589  -2626   3410       C  
ATOM   2097  CD1 LEU A 375      -0.669 -24.741  91.823  1.00182.12           C  
ANISOU 2097  CD1 LEU A 375    23281  26532  19383    659  -2812   3428       C  
ATOM   2098  CD2 LEU A 375       0.706 -23.271  93.328  1.00168.72           C  
ANISOU 2098  CD2 LEU A 375    21023  25223  17861    629  -2356   3064       C  
ATOM   2099  N   GLY A 376      -1.043 -22.314  89.500  1.00154.83           N  
ANISOU 2099  N   GLY A 376    20080  22863  15884    213  -2332   3568       N  
ATOM   2100  CA  GLY A 376      -0.449 -22.630  88.213  1.00163.35           C  
ANISOU 2100  CA  GLY A 376    21432  23863  16770    182  -2278   3426       C  
ATOM   2101  C   GLY A 376       0.200 -21.421  87.569  1.00169.03           C  
ANISOU 2101  C   GLY A 376    22077  24652  17494     63  -1935   3254       C  
ATOM   2102  O   GLY A 376       1.296 -21.516  87.013  1.00169.50           O  
ANISOU 2102  O   GLY A 376    22189  24770  17443    128  -1760   2961       O  
ATOM   2103  N   ALA A 377      -0.476 -20.269  87.625  1.00171.58           N  
ANISOU 2103  N   ALA A 377    22273  24956  17963   -110  -1822   3447       N  
ATOM   2104  CA  ALA A 377       0.108 -19.033  87.113  1.00168.03           C  
ANISOU 2104  CA  ALA A 377    21708  24595  17541   -221  -1489   3288       C  
ATOM   2105  C   ALA A 377       1.392 -18.678  87.848  1.00167.23           C  
ANISOU 2105  C   ALA A 377    21330  24750  17459    -68  -1237   2915       C  
ATOM   2106  O   ALA A 377       2.296 -18.073  87.262  1.00165.21           O  
ANISOU 2106  O   ALA A 377    21040  24585  17148    -82   -993   2678       O  
ATOM   2107  CB  ALA A 377      -0.889 -17.881  87.227  1.00168.24           C  
ANISOU 2107  CB  ALA A 377    21598  24556  17770   -420  -1394   3588       C  
ATOM   2108  N   LEU A 378       1.482 -19.013  89.135  1.00171.13           N  
ANISOU 2108  N   LEU A 378    21622  25366  18034     58  -1300   2878       N  
ATOM   2109  CA  LEU A 378       2.694 -18.707  89.882  1.00154.61           C  
ANISOU 2109  CA  LEU A 378    19269  23521  15956    160  -1091   2572       C  
ATOM   2110  C   LEU A 378       3.764 -19.782  89.719  1.00149.21           C  
ANISOU 2110  C   LEU A 378    18637  22895  15161    352  -1153   2346       C  
ATOM   2111  O   LEU A 378       4.957 -19.462  89.735  1.00142.38           O  
ANISOU 2111  O   LEU A 378    17627  22191  14279    414   -938   2096       O  
ATOM   2112  CB  LEU A 378       2.358 -18.500  91.354  1.00144.06           C  
ANISOU 2112  CB  LEU A 378    17693  22290  14752    154  -1108   2640       C  
ATOM   2113  CG  LEU A 378       1.437 -17.309  91.625  1.00148.31           C  
ANISOU 2113  CG  LEU A 378    18149  22764  15439    -32   -946   2841       C  
ATOM   2114  CD1 LEU A 378       1.244 -17.162  93.118  1.00152.43           C  
ANISOU 2114  CD1 LEU A 378    18470  23379  16068    -47   -922   2864       C  
ATOM   2115  CD2 LEU A 378       1.987 -16.025  91.009  1.00142.49           C  
ANISOU 2115  CD2 LEU A 378    17332  22104  14702   -147   -603   2700       C  
ATOM   2116  N   THR A 379       3.371 -21.052  89.559  1.00154.21           N  
ANISOU 2116  N   THR A 379    19469  23391  15730    446  -1429   2449       N  
ATOM   2117  CA  THR A 379       4.364 -22.099  89.322  1.00155.16           C  
ANISOU 2117  CA  THR A 379    19652  23528  15773    627  -1445   2255       C  
ATOM   2118  C   THR A 379       5.052 -21.936  87.971  1.00161.15           C  
ANISOU 2118  C   THR A 379    20626  24194  16409    607  -1240   2094       C  
ATOM   2119  O   THR A 379       6.194 -22.378  87.803  1.00162.97           O  
ANISOU 2119  O   THR A 379    20825  24473  16624    751  -1102   1881       O  
ATOM   2120  CB  THR A 379       3.723 -23.484  89.420  1.00164.83           C  
ANISOU 2120  CB  THR A 379    21064  24612  16953    721  -1773   2408       C  
ATOM   2121  OG1 THR A 379       2.588 -23.559  88.547  1.00175.80           O  
ANISOU 2121  OG1 THR A 379    22781  25767  18248    579  -1932   2650       O  
ATOM   2122  CG2 THR A 379       3.291 -23.779  90.848  1.00164.88           C  
ANISOU 2122  CG2 THR A 379    20821  24739  17087    778  -1967   2515       C  
ATOM   2123  N   MET A 380       4.378 -21.318  86.998  1.00165.15           N  
ANISOU 2123  N   MET A 380    21348  24555  16846    421  -1213   2211       N  
ATOM   2124  CA  MET A 380       5.013 -21.059  85.709  1.00151.75           C  
ANISOU 2124  CA  MET A 380    19860  22772  15027    367  -1009   2051       C  
ATOM   2125  C   MET A 380       6.076 -19.973  85.818  1.00155.73           C  
ANISOU 2125  C   MET A 380    20091  23482  15599    393   -687   1814       C  
ATOM   2126  O   MET A 380       7.062 -19.994  85.072  1.00158.12           O  
ANISOU 2126  O   MET A 380    20477  23769  15833    456   -486   1600       O  
ATOM   2127  CB  MET A 380       3.956 -20.673  84.674  1.00133.26           C  
ANISOU 2127  CB  MET A 380    17804  20230  12598    114  -1097   2279       C  
ATOM   2128  CG  MET A 380       3.005 -21.793  84.264  1.00130.86           C  
ANISOU 2128  CG  MET A 380    17860  19689  12172     52  -1413   2520       C  
ATOM   2129  SD  MET A 380       3.855 -23.245  83.620  1.00133.13           S  
ANISOU 2129  SD  MET A 380    18481  19830  12272    206  -1401   2309       S  
ATOM   2130  CE  MET A 380       4.253 -22.669  81.969  1.00205.20           C  
ANISOU 2130  CE  MET A 380    27941  28803  21223     -9  -1164   2188       C  
ATOM   2131  N   LEU A 381       5.897 -19.031  86.744  1.00147.98           N  
ANISOU 2131  N   LEU A 381    18800  22680  14746    342   -622   1853       N  
ATOM   2132  CA  LEU A 381       6.783 -17.896  86.944  1.00154.41           C  
ANISOU 2132  CA  LEU A 381    19353  23702  15614    334   -331   1662       C  
ATOM   2133  C   LEU A 381       8.053 -18.322  87.676  1.00153.22           C  
ANISOU 2133  C   LEU A 381    18983  23731  15501    524   -251   1465       C  
ATOM   2134  O   LEU A 381       8.159 -19.429  88.211  1.00154.83           O  
ANISOU 2134  O   LEU A 381    19182  23920  15726    655   -421   1494       O  
ATOM   2135  CB  LEU A 381       6.078 -16.791  87.734  1.00127.08           C  
ANISOU 2135  CB  LEU A 381    15672  20341  12271    186   -274   1793       C  
ATOM   2136  CG  LEU A 381       4.911 -16.051  87.080  1.00147.66           C  
ANISOU 2136  CG  LEU A 381    18395  22796  14913    -27   -279   2022       C  
ATOM   2137  CD1 LEU A 381       4.197 -15.159  88.090  1.00124.89           C  
ANISOU 2137  CD1 LEU A 381    15282  19981  12191   -140   -204   2177       C  
ATOM   2138  CD2 LEU A 381       5.404 -15.240  85.894  1.00145.89           C  
ANISOU 2138  CD2 LEU A 381    18235  22570  14626   -115    -62   1889       C  
ATOM   2139  N   SER A 382       9.032 -17.424  87.687  1.00151.12           N  
ANISOU 2139  N   SER A 382    18523  23640  15255    529      7   1286       N  
ATOM   2140  CA  SER A 382      10.314 -17.677  88.323  1.00156.39           C  
ANISOU 2140  CA  SER A 382    18958  24487  15976    676    101   1142       C  
ATOM   2141  C   SER A 382      10.338 -17.179  89.768  1.00166.07           C  
ANISOU 2141  C   SER A 382    19874  25941  17283    602     84   1188       C  
ATOM   2142  O   SER A 382       9.433 -16.487  90.240  1.00174.41           O  
ANISOU 2142  O   SER A 382    20896  27013  18358    445     66   1296       O  
ATOM   2143  CB  SER A 382      11.441 -17.026  87.526  1.00155.18           C  
ANISOU 2143  CB  SER A 382    18775  24392  15793    722    381    943       C  
ATOM   2144  OG  SER A 382      11.592 -15.668  87.897  1.00154.44           O  
ANISOU 2144  OG  SER A 382    18470  24494  15716    597    549    897       O  
ATOM   2145  N   GLU A 383      11.410 -17.553  90.469  1.00170.38           N  
ANISOU 2145  N   GLU A 383    20201  26650  17887    699    106   1122       N  
ATOM   2146  CA  GLU A 383      11.579 -17.169  91.867  1.00163.08           C  
ANISOU 2146  CA  GLU A 383    19002  25948  17014    591     82   1166       C  
ATOM   2147  C   GLU A 383      11.734 -15.659  92.022  1.00155.97           C  
ANISOU 2147  C   GLU A 383    17988  25198  16076    421    319   1096       C  
ATOM   2148  O   GLU A 383      11.075 -15.040  92.865  1.00146.49           O  
ANISOU 2148  O   GLU A 383    16721  24060  14880    246    323   1169       O  
ATOM   2149  CB  GLU A 383      12.786 -17.902  92.450  1.00168.49           C  
ANISOU 2149  CB  GLU A 383    19471  26770  17779    704     51   1147       C  
ATOM   2150  CG  GLU A 383      13.155 -17.508  93.863  1.00177.62           C  
ANISOU 2150  CG  GLU A 383    20346  28174  18968    547     25   1199       C  
ATOM   2151  CD  GLU A 383      13.981 -18.575  94.545  1.00185.31           C  
ANISOU 2151  CD  GLU A 383    21115  29238  20057    636   -117   1274       C  
ATOM   2152  OE1 GLU A 383      14.943 -19.068  93.916  1.00188.15           O  
ANISOU 2152  OE1 GLU A 383    21440  29561  20489    810    -29   1237       O  
ATOM   2153  OE2 GLU A 383      13.689 -18.902  95.715  1.00187.38           O  
ANISOU 2153  OE2 GLU A 383    21241  29602  20353    521   -302   1382       O  
ATOM   2154  N   THR A 384      12.625 -15.053  91.232  1.00158.76           N  
ANISOU 2154  N   THR A 384    18322  25603  16395    468    537    953       N  
ATOM   2155  CA  THR A 384      12.799 -13.602  91.272  1.00149.55           C  
ANISOU 2155  CA  THR A 384    17056  24580  15186    317    773    875       C  
ATOM   2156  C   THR A 384      11.496 -12.873  90.969  1.00149.25           C  
ANISOU 2156  C   THR A 384    17150  24417  15139    170    813    948       C  
ATOM   2157  O   THR A 384      11.201 -11.833  91.571  1.00144.63           O  
ANISOU 2157  O   THR A 384    16464  23932  14557     -7    957    964       O  
ATOM   2158  CB  THR A 384      13.888 -13.175  90.290  1.00139.04           C  
ANISOU 2158  CB  THR A 384    15712  23293  13825    423    975    715       C  
ATOM   2159  OG1 THR A 384      15.108 -13.854  90.611  1.00140.73           O  
ANISOU 2159  OG1 THR A 384    15776  23604  14092    559    956    699       O  
ATOM   2160  CG2 THR A 384      14.117 -11.676  90.379  1.00133.36           C  
ANISOU 2160  CG2 THR A 384    14870  22745  13057    271   1211    633       C  
ATOM   2161  N   GLN A 385      10.708 -13.397  90.029  1.00150.86           N  
ANISOU 2161  N   GLN A 385    17587  24392  15343    221    700   1017       N  
ATOM   2162  CA  GLN A 385       9.407 -12.805  89.739  1.00151.02           C  
ANISOU 2162  CA  GLN A 385    17715  24271  15395     69    707   1160       C  
ATOM   2163  C   GLN A 385       8.475 -12.902  90.943  1.00149.22           C  
ANISOU 2163  C   GLN A 385    17428  24027  15240    -35    595   1337       C  
ATOM   2164  O   GLN A 385       7.645 -12.012  91.165  1.00142.28           O  
ANISOU 2164  O   GLN A 385    16524  23107  14428   -198    716   1448       O  
ATOM   2165  CB  GLN A 385       8.797 -13.470  88.508  1.00160.48           C  
ANISOU 2165  CB  GLN A 385    19192  25222  16559    113    567   1238       C  
ATOM   2166  CG  GLN A 385       9.623 -13.266  87.243  1.00166.78           C  
ANISOU 2166  CG  GLN A 385    20088  26003  17279    176    714   1059       C  
ATOM   2167  CD  GLN A 385       9.230 -14.213  86.129  1.00169.01           C  
ANISOU 2167  CD  GLN A 385    20695  26035  17488    214    560   1113       C  
ATOM   2168  OE1 GLN A 385       8.920 -15.378  86.371  1.00177.08           O  
ANISOU 2168  OE1 GLN A 385    21841  26944  18498    297    344   1203       O  
ATOM   2169  NE2 GLN A 385       9.243 -13.716  84.898  1.00164.52           N  
ANISOU 2169  NE2 GLN A 385    20276  25376  16857    135    671   1058       N  
ATOM   2170  N   HIS A 386       8.581 -13.984  91.720  1.00159.63           N  
ANISOU 2170  N   HIS A 386    18722  25364  16565     55    376   1378       N  
ATOM   2171  CA  HIS A 386       7.821 -14.079  92.965  1.00158.49           C  
ANISOU 2171  CA  HIS A 386    18509  25225  16485    -47    275   1523       C  
ATOM   2172  C   HIS A 386       8.187 -12.942  93.909  1.00165.77           C  
ANISOU 2172  C   HIS A 386    19247  26335  17404   -227    519   1454       C  
ATOM   2173  O   HIS A 386       7.311 -12.275  94.471  1.00165.11           O  
ANISOU 2173  O   HIS A 386    19162  26190  17382   -390    623   1568       O  
ATOM   2174  CB  HIS A 386       8.074 -15.426  93.642  1.00144.70           C  
ANISOU 2174  CB  HIS A 386    16730  23506  14742     79      1   1551       C  
ATOM   2175  CG  HIS A 386       7.470 -16.589  92.926  1.00134.11           C  
ANISOU 2175  CG  HIS A 386    15599  21956  13400    225   -252   1655       C  
ATOM   2176  ND1 HIS A 386       7.875 -17.888  93.148  1.00137.35           N  
ANISOU 2176  ND1 HIS A 386    16005  22371  13812    385   -469   1648       N  
ATOM   2177  CD2 HIS A 386       6.471 -16.656  92.016  1.00125.36           C  
ANISOU 2177  CD2 HIS A 386    14718  20624  12288    210   -325   1792       C  
ATOM   2178  CE1 HIS A 386       7.165 -18.704  92.391  1.00126.66           C  
ANISOU 2178  CE1 HIS A 386    14889  20802  12433    470   -652   1751       C  
ATOM   2179  NE2 HIS A 386       6.305 -17.982  91.696  1.00125.92           N  
ANISOU 2179  NE2 HIS A 386    14948  20570  12328    355   -583   1849       N  
ATOM   2180  N   LYS A 387       9.487 -12.721  94.103  1.00167.87           N  
ANISOU 2180  N   LYS A 387    19366  26815  17601   -211    625   1287       N  
ATOM   2181  CA  LYS A 387       9.960 -11.663  94.990  1.00171.83           C  
ANISOU 2181  CA  LYS A 387    19718  27510  18059   -410    850   1219       C  
ATOM   2182  C   LYS A 387       9.483 -10.292  94.514  1.00174.95           C  
ANISOU 2182  C   LYS A 387    20144  27861  18468   -542   1148   1201       C  
ATOM   2183  O   LYS A 387       9.027  -9.465  95.314  1.00176.79           O  
ANISOU 2183  O   LYS A 387    20347  28110  18715   -748   1330   1244       O  
ATOM   2184  CB  LYS A 387      11.488 -11.704  95.046  1.00171.29           C  
ANISOU 2184  CB  LYS A 387    19496  27665  17920   -355    888   1081       C  
ATOM   2185  CG  LYS A 387      12.070 -12.968  95.668  1.00164.11           C  
ANISOU 2185  CG  LYS A 387    18494  26823  17036   -260    629   1130       C  
ATOM   2186  CD  LYS A 387      13.370 -12.687  96.396  1.00160.23           C  
ANISOU 2186  CD  LYS A 387    17793  26590  16495   -362    693   1088       C  
ATOM   2187  CE  LYS A 387      14.220 -13.942  96.482  1.00160.82           C  
ANISOU 2187  CE  LYS A 387    17747  26710  16647   -195    483   1140       C  
ATOM   2188  NZ  LYS A 387      13.378 -15.162  96.580  1.00154.96           N  
ANISOU 2188  NZ  LYS A 387    17093  25800  15983    -77    220   1238       N  
ATOM   2189  N   LEU A 388       9.587 -10.035  93.205  1.00180.85           N  
ANISOU 2189  N   LEU A 388    20956  28543  19217   -439   1217   1141       N  
ATOM   2190  CA  LEU A 388       9.161  -8.755  92.642  1.00163.37           C  
ANISOU 2190  CA  LEU A 388    18742  26293  17040   -560   1490   1136       C  
ATOM   2191  C   LEU A 388       7.666  -8.522  92.828  1.00169.33           C  
ANISOU 2191  C   LEU A 388    19574  26831  17932   -683   1510   1362       C  
ATOM   2192  O   LEU A 388       7.233  -7.384  93.048  1.00170.48           O  
ANISOU 2192  O   LEU A 388    19664  26963  18146   -854   1789   1402       O  
ATOM   2193  CB  LEU A 388       9.526  -8.694  91.158  1.00141.38           C  
ANISOU 2193  CB  LEU A 388    16023  23465  14231   -434   1508   1044       C  
ATOM   2194  CG  LEU A 388      11.000  -8.491  90.805  1.00138.58           C  
ANISOU 2194  CG  LEU A 388    15571  23311  13774   -331   1604    822       C  
ATOM   2195  CD1 LEU A 388      11.196  -8.385  89.300  1.00151.93           C  
ANISOU 2195  CD1 LEU A 388    17361  24916  15449   -230   1643    738       C  
ATOM   2196  CD2 LEU A 388      11.534  -7.253  91.498  1.00141.34           C  
ANISOU 2196  CD2 LEU A 388    15752  23872  14076   -488   1871    732       C  
ATOM   2197  N   LEU A 389       6.858  -9.582  92.725  1.00169.56           N  
ANISOU 2197  N   LEU A 389    19730  26675  18019   -599   1232   1533       N  
ATOM   2198  CA  LEU A 389       5.420  -9.431  92.938  1.00169.49           C  
ANISOU 2198  CA  LEU A 389    19787  26444  18168   -707   1231   1799       C  
ATOM   2199  C   LEU A 389       5.109  -9.104  94.391  1.00186.78           C  
ANISOU 2199  C   LEU A 389    21905  28662  20402   -853   1353   1849       C  
ATOM   2200  O   LEU A 389       4.242  -8.268  94.672  1.00182.52           O  
ANISOU 2200  O   LEU A 389    21354  27993  20002  -1008   1584   2000       O  
ATOM   2201  CB  LEU A 389       4.676 -10.699  92.514  1.00148.54           C  
ANISOU 2201  CB  LEU A 389    17298  23596  15544   -583    874   1983       C  
ATOM   2202  CG  LEU A 389       4.343 -10.857  91.030  1.00123.24           C  
ANISOU 2202  CG  LEU A 389    14243  20242  12341   -545    782   2065       C  
ATOM   2203  CD1 LEU A 389       3.586 -12.155  90.760  1.00122.34           C  
ANISOU 2203  CD1 LEU A 389    14323  19935  12227   -455    420   2263       C  
ATOM   2204  CD2 LEU A 389       3.546  -9.659  90.562  1.00121.57           C  
ANISOU 2204  CD2 LEU A 389    13989  19920  12283   -724   1021   2234       C  
ATOM   2205  N   ALA A 390       5.806  -9.750  95.328  1.00173.97           N  
ANISOU 2205  N   ALA A 390    20236  27194  18672   -825   1217   1739       N  
ATOM   2206  CA  ALA A 390       5.620  -9.423  96.737  1.00184.72           C  
ANISOU 2206  CA  ALA A 390    21554  28595  20038  -1010   1339   1763       C  
ATOM   2207  C   ALA A 390       5.996  -7.973  97.017  1.00187.00           C  
ANISOU 2207  C   ALA A 390    21772  28988  20291  -1217   1754   1651       C  
ATOM   2208  O   ALA A 390       5.322  -7.287  97.795  1.00195.00           O  
ANISOU 2208  O   ALA A 390    22810  29902  21380  -1413   1997   1741       O  
ATOM   2209  CB  ALA A 390       6.445 -10.369  97.607  1.00189.63           C  
ANISOU 2209  CB  ALA A 390    22116  29395  20541   -973   1099   1668       C  
ATOM   2210  N   GLU A 391       7.074  -7.490  96.396  1.00200.31           N  
ANISOU 2210  N   GLU A 391    23380  30862  21866  -1179   1857   1458       N  
ATOM   2211  CA  GLU A 391       7.424  -6.079  96.515  1.00186.65           C  
ANISOU 2211  CA  GLU A 391    21588  29233  20096  -1362   2249   1353       C  
ATOM   2212  C   GLU A 391       6.354  -5.190  95.890  1.00186.41           C  
ANISOU 2212  C   GLU A 391    21581  28993  20254  -1425   2504   1496       C  
ATOM   2213  O   GLU A 391       5.991  -4.153  96.458  1.00191.37           O  
ANISOU 2213  O   GLU A 391    22198  29576  20937  -1632   2857   1524       O  
ATOM   2214  CB  GLU A 391       8.795  -5.823  95.891  1.00177.49           C  
ANISOU 2214  CB  GLU A 391    20334  28314  18791  -1275   2269   1137       C  
ATOM   2215  CG  GLU A 391       9.945  -6.365  96.737  1.00184.75           C  
ANISOU 2215  CG  GLU A 391    21186  29462  19549  -1298   2117   1036       C  
ATOM   2216  CD  GLU A 391      11.310  -5.894  96.268  1.00196.64           C  
ANISOU 2216  CD  GLU A 391    22582  31203  20929  -1251   2201    861       C  
ATOM   2217  OE1 GLU A 391      11.368  -5.003  95.396  1.00198.97           O  
ANISOU 2217  OE1 GLU A 391    22858  31503  21240  -1226   2413    783       O  
ATOM   2218  OE2 GLU A 391      12.329  -6.413  96.775  1.00204.53           O  
ANISOU 2218  OE2 GLU A 391    23501  32382  21830  -1244   2051    822       O  
ATOM   2219  N   ALA A 392       5.853  -5.565  94.709  1.00196.44           N  
ANISOU 2219  N   ALA A 392    22886  30123  21630  -1273   2347   1603       N  
ATOM   2220  CA  ALA A 392       4.808  -4.770  94.070  1.00194.12           C  
ANISOU 2220  CA  ALA A 392    22586  29624  21548  -1355   2557   1799       C  
ATOM   2221  C   ALA A 392       3.513  -4.784  94.872  1.00195.55           C  
ANISOU 2221  C   ALA A 392    22819  29556  21927  -1470   2633   2074       C  
ATOM   2222  O   ALA A 392       2.742  -3.820  94.815  1.00185.21           O  
ANISOU 2222  O   ALA A 392    21465  28089  20817  -1610   2953   2237       O  
ATOM   2223  CB  ALA A 392       4.556  -5.272  92.647  1.00196.98           C  
ANISOU 2223  CB  ALA A 392    22999  29887  21957  -1212   2324   1885       C  
ATOM   2224  N   LEU A 393       3.253  -5.856  95.622  1.00191.80           N  
ANISOU 2224  N   LEU A 393    22426  29031  21420  -1411   2358   2142       N  
ATOM   2225  CA  LEU A 393       2.078  -5.881  96.487  1.00209.02           C  
ANISOU 2225  CA  LEU A 393    24661  30974  23784  -1515   2438   2394       C  
ATOM   2226  C   LEU A 393       2.273  -4.997  97.715  1.00240.39           C  
ANISOU 2226  C   LEU A 393    28622  34994  27719  -1744   2821   2293       C  
ATOM   2227  O   LEU A 393       1.366  -4.251  98.102  1.00233.47           O  
ANISOU 2227  O   LEU A 393    27760  33899  27048  -1894   3154   2478       O  
ATOM   2228  CB  LEU A 393       1.765  -7.316  96.901  1.00193.11           C  
ANISOU 2228  CB  LEU A 393    22734  28902  21736  -1378   2009   2487       C  
ATOM   2229  CG  LEU A 393       1.147  -8.197  95.816  1.00179.95           C  
ANISOU 2229  CG  LEU A 393    21139  27086  20147  -1203   1661   2687       C  
ATOM   2230  CD1 LEU A 393       1.229  -9.656  96.220  1.00174.58           C  
ANISOU 2230  CD1 LEU A 393    20535  26434  19363  -1046   1232   2680       C  
ATOM   2231  CD2 LEU A 393      -0.293  -7.793  95.558  1.00176.00           C  
ANISOU 2231  CD2 LEU A 393    20661  26274  19937  -1283   1775   3070       C  
ATOM   2232  N   GLU A 394       3.451  -5.077  98.341  1.00221.62           N  
ANISOU 2232  N   GLU A 394    26230  32885  25088  -1792   2791   2022       N  
ATOM   2233  CA  GLU A 394       3.744  -4.278  99.528  1.00228.25           C  
ANISOU 2233  CA  GLU A 394    27101  33789  25833  -2058   3133   1914       C  
ATOM   2234  C   GLU A 394       3.844  -2.794  99.192  1.00230.26           C  
ANISOU 2234  C   GLU A 394    27307  34048  26134  -2208   3614   1855       C  
ATOM   2235  O   GLU A 394       3.514  -1.946 100.030  1.00232.43           O  
ANISOU 2235  O   GLU A 394    27646  34223  26444  -2450   4014   1875       O  
ATOM   2236  CB  GLU A 394       5.036  -4.782 100.179  1.00225.35           C  
ANISOU 2236  CB  GLU A 394    26717  33724  25180  -2094   2929   1684       C  
ATOM   2237  CG  GLU A 394       5.192  -4.468 101.667  1.00225.96           C  
ANISOU 2237  CG  GLU A 394    26886  33842  25129  -2400   3118   1631       C  
ATOM   2238  CD  GLU A 394       5.578  -3.027 101.942  1.00226.89           C  
ANISOU 2238  CD  GLU A 394    27030  34022  25155  -2664   3608   1509       C  
ATOM   2239  OE1 GLU A 394       6.362  -2.460 101.155  1.00226.52           O  
ANISOU 2239  OE1 GLU A 394    26886  34152  25031  -2602   3683   1372       O  
ATOM   2240  OE2 GLU A 394       5.104  -2.464 102.954  1.00227.80           O  
ANISOU 2240  OE2 GLU A 394    27279  34003  25273  -2940   3929   1548       O  
ATOM   2241  N   SER A 395       4.281  -2.463  97.976  1.00249.73           N  
ANISOU 2241  N   SER A 395    29668  36615  28602  -2076   3597   1781       N  
ATOM   2242  CA  SER A 395       4.400  -1.085  97.517  1.00220.54           C  
ANISOU 2242  CA  SER A 395    25891  32942  24961  -2191   4020   1724       C  
ATOM   2243  C   SER A 395       3.193  -0.649  96.701  1.00215.10           C  
ANISOU 2243  C   SER A 395    25148  31976  24605  -2167   4176   2002       C  
ATOM   2244  O   SER A 395       3.131   0.509  96.273  1.00220.07           O  
ANISOU 2244  O   SER A 395    25683  32591  25343  -2265   4543   2001       O  
ATOM   2245  CB  SER A 395       5.676  -0.907  96.681  1.00193.70           C  
ANISOU 2245  CB  SER A 395    22393  29837  21367  -2077   3920   1474       C  
ATOM   2246  OG  SER A 395       5.664  -1.728  95.523  1.00174.09           O  
ANISOU 2246  OG  SER A 395    19881  27339  18927  -1830   3562   1517       O  
ATOM   2247  N   GLN A 396       2.244  -1.556  96.468  1.00226.63           N  
ANISOU 2247  N   GLN A 396    26654  33220  26237  -2050   3894   2261       N  
ATOM   2248  CA  GLN A 396       0.999  -1.279  95.760  1.00212.07           C  
ANISOU 2248  CA  GLN A 396    24759  31086  24733  -2053   3986   2610       C  
ATOM   2249  C   GLN A 396       1.254  -0.873  94.313  1.00203.17           C  
ANISOU 2249  C   GLN A 396    23513  30037  23645  -1984   3950   2595       C  
ATOM   2250  O   GLN A 396       0.373  -0.310  93.656  1.00202.39           O  
ANISOU 2250  O   GLN A 396    23325  29739  23836  -2049   4111   2875       O  
ATOM   2251  CB  GLN A 396       0.160  -0.222  96.488  1.00212.03           C  
ANISOU 2251  CB  GLN A 396    24736  30844  24980  -2269   4516   2793       C  
ATOM   2252  CG  GLN A 396      -0.023  -0.536  97.964  1.00215.06           C  
ANISOU 2252  CG  GLN A 396    25268  31147  25296  -2378   4599   2774       C  
ATOM   2253  CD  GLN A 396      -1.242   0.131  98.567  1.00217.60           C  
ANISOU 2253  CD  GLN A 396    25614  31108  25957  -2542   5044   3079       C  
ATOM   2254  OE1 GLN A 396      -2.370  -0.072  98.121  1.00216.85           O  
ANISOU 2254  OE1 GLN A 396    25473  30734  26187  -2481   4994   3456       O  
ATOM   2255  NE2 GLN A 396      -1.017   0.924  99.608  1.00219.12           N  
ANISOU 2255  NE2 GLN A 396    25892  31287  26076  -2768   5495   2938       N  
ATOM   2256  N   THR A 397       2.456  -1.151  93.808  1.00207.65           N  
ANISOU 2256  N   THR A 397    24073  30885  23940  -1865   3743   2290       N  
ATOM   2257  CA  THR A 397       2.797  -0.876  92.413  1.00204.59           C  
ANISOU 2257  CA  THR A 397    23601  30580  23552  -1794   3674   2241       C  
ATOM   2258  C   THR A 397       2.555  -2.120  91.556  1.00196.55           C  
ANISOU 2258  C   THR A 397    22689  29485  22507  -1631   3198   2354       C  
ATOM   2259  O   THR A 397       3.460  -2.680  90.939  1.00178.57           O  
ANISOU 2259  O   THR A 397    20455  27374  20018  -1489   2957   2136       O  
ATOM   2260  CB  THR A 397       4.244  -0.408  92.307  1.00204.07           C  
ANISOU 2260  CB  THR A 397    23476  30838  23222  -1758   3760   1859       C  
ATOM   2261  OG1 THR A 397       5.124  -1.498  92.610  1.00204.58           O  
ANISOU 2261  OG1 THR A 397    23632  31064  23034  -1607   3420   1667       O  
ATOM   2262  CG2 THR A 397       4.512   0.732  93.281  1.00202.56           C  
ANISOU 2262  CG2 THR A 397    23229  30727  23007  -1946   4210   1745       C  
ATOM   2263  N   LEU A 398       1.294  -2.547  91.524  1.00197.90           N  
ANISOU 2263  N   LEU A 398    22912  29378  22902  -1664   3082   2720       N  
ATOM   2264  CA  LEU A 398       0.897  -3.761  90.822  1.00200.98           C  
ANISOU 2264  CA  LEU A 398    23441  29657  23264  -1547   2632   2878       C  
ATOM   2265  C   LEU A 398       0.070  -3.468  89.577  1.00209.88           C  
ANISOU 2265  C   LEU A 398    24542  30605  24597  -1643   2592   3190       C  
ATOM   2266  O   LEU A 398      -0.433  -4.402  88.942  1.00211.98           O  
ANISOU 2266  O   LEU A 398    24950  30739  24855  -1602   2233   3388       O  
ATOM   2267  CB  LEU A 398       0.142  -4.706  91.764  1.00193.78           C  
ANISOU 2267  CB  LEU A 398    22639  28581  22406  -1503   2429   3075       C  
ATOM   2268  CG  LEU A 398      -1.129  -4.309  92.517  1.00191.49           C  
ANISOU 2268  CG  LEU A 398    22313  28021  22423  -1632   2642   3434       C  
ATOM   2269  CD1 LEU A 398      -1.679  -5.542  93.150  1.00195.47           C  
ANISOU 2269  CD1 LEU A 398    22955  28404  22911  -1529   2301   3582       C  
ATOM   2270  CD2 LEU A 398      -0.875  -3.301  93.602  1.00191.87           C  
ANISOU 2270  CD2 LEU A 398    22276  28123  22504  -1759   3103   3290       C  
ATOM   2271  N   LEU A 399      -0.085  -2.194  89.218  1.00205.90           N  
ANISOU 2271  N   LEU A 399    23861  30094  24278  -1792   2951   3254       N  
ATOM   2272  CA  LEU A 399      -0.872  -1.775  88.065  1.00200.35           C  
ANISOU 2272  CA  LEU A 399    23086  29230  23807  -1933   2944   3585       C  
ATOM   2273  C   LEU A 399      -0.035  -1.259  86.907  1.00227.90           C  
ANISOU 2273  C   LEU A 399    26514  32910  27169  -1950   2967   3352       C  
ATOM   2274  O   LEU A 399      -0.450  -1.402  85.756  1.00227.38           O  
ANISOU 2274  O   LEU A 399    26482  32747  27166  -2042   2776   3561       O  
ATOM   2275  CB  LEU A 399      -1.874  -0.686  88.473  1.00177.70           C  
ANISOU 2275  CB  LEU A 399    20024  26159  21335  -2116   3356   3928       C  
ATOM   2276  CG  LEU A 399      -3.023  -1.106  89.389  1.00157.15           C  
ANISOU 2276  CG  LEU A 399    17471  23275  18963  -2138   3355   4297       C  
ATOM   2277  CD1 LEU A 399      -3.633   0.099  90.076  1.00147.15           C  
ANISOU 2277  CD1 LEU A 399    16021  21851  18039  -2290   3900   4490       C  
ATOM   2278  CD2 LEU A 399      -4.079  -1.808  88.562  1.00150.46           C  
ANISOU 2278  CD2 LEU A 399    16694  22190  18284  -2192   2996   4767       C  
ATOM   2279  N   GLY A 400       1.123  -0.662  87.182  1.00213.95           N  
ANISOU 2279  N   GLY A 400    24666  31405  25219  -1883   3187   2943       N  
ATOM   2280  CA  GLY A 400       1.997  -0.150  86.151  1.00217.96           C  
ANISOU 2280  CA  GLY A 400    25110  32105  25600  -1875   3221   2696       C  
ATOM   2281  C   GLY A 400       2.459  -1.225  85.188  1.00217.50           C  
ANISOU 2281  C   GLY A 400    25259  32073  25310  -1766   2816   2585       C  
ATOM   2282  O   GLY A 400       2.211  -1.156  83.978  1.00222.37           O  
ANISOU 2282  O   GLY A 400    25901  32623  25967  -1870   2701   2709       O  
ATOM   2283  N   PRO A 401       3.156  -2.239  85.707  1.00221.39           N  
ANISOU 2283  N   PRO A 401    25909  32652  25555  -1573   2607   2355       N  
ATOM   2284  CA  PRO A 401       3.522  -3.377  84.850  1.00196.45           C  
ANISOU 2284  CA  PRO A 401    22982  29467  22194  -1466   2249   2273       C  
ATOM   2285  C   PRO A 401       2.312  -4.102  84.292  1.00190.57           C  
ANISOU 2285  C   PRO A 401    22403  28448  21558  -1580   1965   2669       C  
ATOM   2286  O   PRO A 401       2.414  -4.736  83.235  1.00188.14           O  
ANISOU 2286  O   PRO A 401    22293  28075  21116  -1594   1725   2668       O  
ATOM   2287  CB  PRO A 401       4.348  -4.274  85.785  1.00190.14           C  
ANISOU 2287  CB  PRO A 401    22267  28790  21188  -1252   2130   2022       C  
ATOM   2288  CG  PRO A 401       3.983  -3.830  87.177  1.00191.49           C  
ANISOU 2288  CG  PRO A 401    22305  28974  21479  -1296   2332   2094       C  
ATOM   2289  CD  PRO A 401       3.726  -2.362  87.058  1.00201.12           C  
ANISOU 2289  CD  PRO A 401    23317  30218  22882  -1465   2707   2153       C  
ATOM   2290  N   LEU A 402       1.170  -4.038  84.985  1.00190.57           N  
ANISOU 2290  N   LEU A 402    22346  28269  21792  -1672   1991   3022       N  
ATOM   2291  CA  LEU A 402      -0.048  -4.681  84.501  1.00200.17           C  
ANISOU 2291  CA  LEU A 402    23705  29216  23137  -1797   1713   3463       C  
ATOM   2292  C   LEU A 402      -0.480  -4.121  83.146  1.00216.61           C  
ANISOU 2292  C   LEU A 402    25764  31210  25329  -2031   1700   3688       C  
ATOM   2293  O   LEU A 402      -0.580  -4.861  82.161  1.00226.21           O  
ANISOU 2293  O   LEU A 402    27213  32336  26400  -2097   1397   3767       O  
ATOM   2294  CB  LEU A 402      -1.163  -4.524  85.539  1.00200.09           C  
ANISOU 2294  CB  LEU A 402    23592  29027  23407  -1852   1811   3816       C  
ATOM   2295  CG  LEU A 402      -2.573  -4.943  85.110  1.00200.79           C  
ANISOU 2295  CG  LEU A 402    23762  28816  23712  -2012   1576   4373       C  
ATOM   2296  CD1 LEU A 402      -2.628  -6.420  84.743  1.00202.31           C  
ANISOU 2296  CD1 LEU A 402    24269  28936  23665  -1926   1109   4399       C  
ATOM   2297  CD2 LEU A 402      -3.589  -4.630  86.198  1.00198.28           C  
ANISOU 2297  CD2 LEU A 402    23308  28316  23711  -2048   1756   4709       C  
ATOM   2298  N   GLU A 403      -0.767  -2.814  83.083  1.00222.72           N  
ANISOU 2298  N   GLU A 403    26265  31999  26362  -2184   2033   3812       N  
ATOM   2299  CA  GLU A 403      -1.163  -2.204  81.813  1.00217.69           C  
ANISOU 2299  CA  GLU A 403    25559  31295  25857  -2434   2029   4044       C  
ATOM   2300  C   GLU A 403      -0.097  -2.405  80.744  1.00215.33           C  
ANISOU 2300  C   GLU A 403    25409  31158  25251  -2401   1908   3677       C  
ATOM   2301  O   GLU A 403      -0.418  -2.604  79.566  1.00220.59           O  
ANISOU 2301  O   GLU A 403    26208  31721  25886  -2602   1699   3861       O  
ATOM   2302  CB  GLU A 403      -1.463  -0.716  81.994  1.00215.17           C  
ANISOU 2302  CB  GLU A 403    24884  31000  25870  -2573   2458   4175       C  
ATOM   2303  CG  GLU A 403      -2.586  -0.217  81.089  1.00217.92           C  
ANISOU 2303  CG  GLU A 403    25107  31145  26548  -2890   2429   4715       C  
ATOM   2304  CD  GLU A 403      -2.504   1.267  80.800  1.00222.35           C  
ANISOU 2304  CD  GLU A 403    25321  31799  27363  -3032   2829   4727       C  
ATOM   2305  OE1 GLU A 403      -1.377   1.791  80.684  1.00223.55           O  
ANISOU 2305  OE1 GLU A 403    25409  32210  27320  -2920   3001   4258       O  
ATOM   2306  OE2 GLU A 403      -3.570   1.910  80.685  1.00225.61           O  
ANISOU 2306  OE2 GLU A 403    25516  32020  28187  -3256   2976   5228       O  
ATOM   2307  N   LEU A 404       1.178  -2.327  81.133  1.00220.02           N  
ANISOU 2307  N   LEU A 404    25984  31992  25620  -2171   2047   3178       N  
ATOM   2308  CA  LEU A 404       2.271  -2.511  80.183  1.00208.18           C  
ANISOU 2308  CA  LEU A 404    24621  30633  23846  -2105   1973   2817       C  
ATOM   2309  C   LEU A 404       2.200  -3.881  79.519  1.00221.03           C  
ANISOU 2309  C   LEU A 404    26626  32108  25248  -2100   1592   2855       C  
ATOM   2310  O   LEU A 404       2.157  -3.987  78.288  1.00230.04           O  
ANISOU 2310  O   LEU A 404    27928  33173  26302  -2275   1456   2909       O  
ATOM   2311  CB  LEU A 404       3.613  -2.327  80.894  1.00191.23           C  
ANISOU 2311  CB  LEU A 404    22390  28749  21521  -1838   2167   2336       C  
ATOM   2312  CG  LEU A 404       4.859  -2.690  80.083  1.00182.80           C  
ANISOU 2312  CG  LEU A 404    21477  27808  20172  -1704   2099   1951       C  
ATOM   2313  CD1 LEU A 404       5.010  -1.771  78.883  1.00175.40           C  
ANISOU 2313  CD1 LEU A 404    20448  26922  19274  -1877   2208   1920       C  
ATOM   2314  CD2 LEU A 404       6.102  -2.658  80.958  1.00188.36           C  
ANISOU 2314  CD2 LEU A 404    22092  28746  20730  -1439   2251   1565       C  
ATOM   2315  N   VAL A 405       2.192  -4.945  80.325  1.00196.42           N  
ANISOU 2315  N   VAL A 405    23664  28939  22026  -1917   1423   2827       N  
ATOM   2316  CA  VAL A 405       2.139  -6.298  79.775  1.00204.88           C  
ANISOU 2316  CA  VAL A 405    25107  29859  22878  -1897   1084   2854       C  
ATOM   2317  C   VAL A 405       0.870  -6.493  78.952  1.00228.96           C  
ANISOU 2317  C   VAL A 405    28307  32657  26028  -2210    848   3338       C  
ATOM   2318  O   VAL A 405       0.889  -7.145  77.900  1.00225.48           O  
ANISOU 2318  O   VAL A 405    28180  32101  25394  -2339    632   3360       O  
ATOM   2319  CB  VAL A 405       2.258  -7.337  80.906  1.00197.13           C  
ANISOU 2319  CB  VAL A 405    24209  28875  21815  -1651    955   2778       C  
ATOM   2320  CG1 VAL A 405       1.966  -8.736  80.385  1.00194.76           C  
ANISOU 2320  CG1 VAL A 405    24289  28382  21328  -1657    604   2883       C  
ATOM   2321  CG2 VAL A 405       3.647  -7.280  81.527  1.00195.84           C  
ANISOU 2321  CG2 VAL A 405    23937  28956  21516  -1381   1139   2316       C  
ATOM   2322  N   GLY A 406      -0.248  -5.918  79.403  1.00219.96           N  
ANISOU 2322  N   GLY A 406    26959  31417  25199  -2360    899   3755       N  
ATOM   2323  CA  GLY A 406      -1.483  -6.028  78.638  1.00221.60           C  
ANISOU 2323  CA  GLY A 406    27269  31384  25545  -2685    673   4287       C  
ATOM   2324  C   GLY A 406      -1.363  -5.432  77.248  1.00225.34           C  
ANISOU 2324  C   GLY A 406    27770  31861  25988  -2969    681   4323       C  
ATOM   2325  O   GLY A 406      -1.710  -6.072  76.252  1.00228.69           O  
ANISOU 2325  O   GLY A 406    28502  32129  26259  -3197    395   4510       O  
ATOM   2326  N   SER A 407      -0.877  -4.189  77.166  1.00258.61           N  
ANISOU 2326  N   SER A 407    31669  36252  30338  -2980   1007   4147       N  
ATOM   2327  CA  SER A 407      -0.702  -3.536  75.872  1.00232.25           C  
ANISOU 2327  CA  SER A 407    28316  32944  26984  -3246   1030   4153       C  
ATOM   2328  C   SER A 407       0.361  -4.231  75.028  1.00212.51           C  
ANISOU 2328  C   SER A 407    26162  30497  24084  -3176    911   3730       C  
ATOM   2329  O   SER A 407       0.248  -4.261  73.796  1.00215.99           O  
ANISOU 2329  O   SER A 407    26793  30853  24422  -3467    768   3830       O  
ATOM   2330  CB  SER A 407      -0.354  -2.060  76.070  1.00226.83           C  
ANISOU 2330  CB  SER A 407    27199  32454  26531  -3232   1423   4024       C  
ATOM   2331  OG  SER A 407      -1.381  -1.373  76.765  1.00225.30           O  
ANISOU 2331  OG  SER A 407    26698  32168  26738  -3329   1585   4445       O  
ATOM   2332  N   LEU A 408       1.399  -4.781  75.664  1.00237.19           N  
ANISOU 2332  N   LEU A 408    29375  33750  26996  -2815    981   3275       N  
ATOM   2333  CA  LEU A 408       2.412  -5.529  74.923  1.00219.17           C  
ANISOU 2333  CA  LEU A 408    27430  31478  24368  -2721    904   2896       C  
ATOM   2334  C   LEU A 408       1.810  -6.792  74.319  1.00199.92           C  
ANISOU 2334  C   LEU A 408    25447  28778  21737  -2893    554   3126       C  
ATOM   2335  O   LEU A 408       2.030  -7.097  73.143  1.00195.06           O  
ANISOU 2335  O   LEU A 408    25142  28062  20909  -3095    453   3068       O  
ATOM   2336  CB  LEU A 408       3.594  -5.869  75.838  1.00228.72           C  
ANISOU 2336  CB  LEU A 408    28592  32863  25448  -2300   1058   2438       C  
ATOM   2337  CG  LEU A 408       5.001  -6.055  75.250  1.00129.91           C  
ANISOU 2337  CG  LEU A 408    16223  20451  12685  -2125   1171   1960       C  
ATOM   2338  CD1 LEU A 408       5.133  -7.328  74.414  1.00131.81           C  
ANISOU 2338  CD1 LEU A 408    16955  20476  12653  -2177    956   1916       C  
ATOM   2339  CD2 LEU A 408       5.404  -4.830  74.445  1.00136.15           C  
ANISOU 2339  CD2 LEU A 408    16820  21378  13533  -2261   1371   1838       C  
ATOM   2340  N   LEU A 409       1.037  -7.538  75.108  1.00196.25           N  
ANISOU 2340  N   LEU A 409    25045  28191  21331  -2832    369   3392       N  
ATOM   2341  CA  LEU A 409       0.395  -8.738  74.583  1.00197.39           C  
ANISOU 2341  CA  LEU A 409    25624  28085  21290  -3006     23   3644       C  
ATOM   2342  C   LEU A 409      -0.637  -8.397  73.516  1.00219.46           C  
ANISOU 2342  C   LEU A 409    28516  30709  24160  -3491   -160   4124       C  
ATOM   2343  O   LEU A 409      -0.855  -9.190  72.592  1.00228.67           O  
ANISOU 2343  O   LEU A 409    30115  31689  25079  -3736   -405   4237       O  
ATOM   2344  CB  LEU A 409      -0.248  -9.529  75.720  1.00185.32           C  
ANISOU 2344  CB  LEU A 409    24095  26480  19836  -2827   -140   3846       C  
ATOM   2345  CG  LEU A 409       0.753 -10.130  76.706  1.00179.83           C  
ANISOU 2345  CG  LEU A 409    23373  25927  19026  -2393    -32   3408       C  
ATOM   2346  CD1 LEU A 409       0.046 -10.889  77.822  1.00178.21           C  
ANISOU 2346  CD1 LEU A 409    23155  25649  18906  -2247   -213   3629       C  
ATOM   2347  CD2 LEU A 409       1.732 -11.028  75.970  1.00175.61           C  
ANISOU 2347  CD2 LEU A 409    23216  25350  18156  -2307    -65   3049       C  
ATOM   2348  N   GLU A 410      -1.295  -7.241  73.639  1.00209.00           N  
ANISOU 2348  N   GLU A 410    26799  29431  23178  -3659    -40   4434       N  
ATOM   2349  CA  GLU A 410      -2.253  -6.816  72.622  1.00213.41           C  
ANISOU 2349  CA  GLU A 410    27385  29842  23860  -4149   -204   4935       C  
ATOM   2350  C   GLU A 410      -1.565  -6.560  71.289  1.00214.73           C  
ANISOU 2350  C   GLU A 410    27746  30042  23800  -4380   -179   4696       C  
ATOM   2351  O   GLU A 410      -2.071  -6.957  70.233  1.00220.04           O  
ANISOU 2351  O   GLU A 410    28750  30532  24323  -4788   -439   4978       O  
ATOM   2352  CB  GLU A 410      -2.985  -5.554  73.083  1.00217.05           C  
ANISOU 2352  CB  GLU A 410    27328  30353  24786  -4245     -8   5293       C  
ATOM   2353  CG  GLU A 410      -4.132  -5.123  72.176  1.00222.41           C  
ANISOU 2353  CG  GLU A 410    27964  30859  25681  -4764   -190   5933       C  
ATOM   2354  CD  GLU A 410      -4.782  -3.827  72.629  1.00225.97           C  
ANISOU 2354  CD  GLU A 410    27869  31349  26640  -4840     71   6280       C  
ATOM   2355  OE1 GLU A 410      -4.241  -3.179  73.550  1.00224.19           O  
ANISOU 2355  OE1 GLU A 410    27330  31301  26553  -4509    420   5958       O  
ATOM   2356  OE2 GLU A 410      -5.834  -3.456  72.067  1.00230.20           O  
ANISOU 2356  OE2 GLU A 410    28295  31728  27443  -5249    -63   6895       O  
ATOM   2357  N   GLN A 411      -0.407  -5.900  71.320  1.00221.84           N  
ANISOU 2357  N   GLN A 411    28459  31169  24662  -4143    128   4187       N  
ATOM   2358  CA  GLN A 411       0.346  -5.596  70.112  1.00218.20           C  
ANISOU 2358  CA  GLN A 411    28156  30752  23997  -4318    189   3911       C  
ATOM   2359  C   GLN A 411       1.145  -6.784  69.592  1.00215.83           C  
ANISOU 2359  C   GLN A 411    28390  30344  23269  -4225     97   3548       C  
ATOM   2360  O   GLN A 411       1.660  -6.717  68.470  1.00218.59           O  
ANISOU 2360  O   GLN A 411    28981  30661  23413  -4429    116   3364       O  
ATOM   2361  CB  GLN A 411       1.294  -4.424  70.380  1.00217.70           C  
ANISOU 2361  CB  GLN A 411    27677  30974  24066  -4075    556   3516       C  
ATOM   2362  CG  GLN A 411       0.665  -3.048  70.370  1.00216.12           C  
ANISOU 2362  CG  GLN A 411    26995  30870  24252  -4285    699   3827       C  
ATOM   2363  CD  GLN A 411       1.681  -1.960  70.667  1.00213.50           C  
ANISOU 2363  CD  GLN A 411    26290  30825  24004  -4023   1064   3396       C  
ATOM   2364  OE1 GLN A 411       2.773  -2.235  71.169  1.00210.92           O  
ANISOU 2364  OE1 GLN A 411    26013  30634  23495  -3639   1208   2914       O  
ATOM   2365  NE2 GLN A 411       1.328  -0.719  70.358  1.00215.70           N  
ANISOU 2365  NE2 GLN A 411    26187  31197  24573  -4238   1212   3592       N  
ATOM   2366  N   SER A 412       1.264  -7.859  70.371  1.00203.77           N  
ANISOU 2366  N   SER A 412    27053  28751  21618  -3932     19   3445       N  
ATOM   2367  CA  SER A 412       2.057  -9.020  69.990  1.00197.06           C  
ANISOU 2367  CA  SER A 412    26686  27786  20403  -3802    -15   3100       C  
ATOM   2368  C   SER A 412       1.193 -10.153  69.454  1.00201.37           C  
ANISOU 2368  C   SER A 412    27736  28038  20738  -4113   -359   3445       C  
ATOM   2369  O   SER A 412       1.683 -11.274  69.296  1.00196.97           O  
ANISOU 2369  O   SER A 412    27600  27346  19893  -3996   -397   3215       O  
ATOM   2370  CB  SER A 412       2.894  -9.516  71.173  1.00195.59           C  
ANISOU 2370  CB  SER A 412    26377  27726  20211  -3267    140   2733       C  
ATOM   2371  OG  SER A 412       2.087 -10.110  72.176  1.00201.54           O  
ANISOU 2371  OG  SER A 412    27080  28423  21074  -3161    -41   3015       O  
ATOM   2372  N   ALA A 413      -0.083  -9.883  69.173  1.00208.33           N  
ANISOU 2372  N   ALA A 413    28581  28809  21767  -4517   -602   4014       N  
ATOM   2373  CA  ALA A 413      -0.969 -10.878  68.594  1.00208.71           C  
ANISOU 2373  CA  ALA A 413    29115  28579  21607  -4879   -959   4405       C  
ATOM   2374  C   ALA A 413      -0.767 -10.934  67.080  1.00217.13           C  
ANISOU 2374  C   ALA A 413    30619  29503  22379  -5337  -1017   4371       C  
ATOM   2375  O   ALA A 413      -0.660  -9.893  66.426  1.00212.53           O  
ANISOU 2375  O   ALA A 413    29830  29015  21906  -5572   -911   4385       O  
ATOM   2376  CB  ALA A 413      -2.429 -10.555  68.911  1.00202.72           C  
ANISOU 2376  CB  ALA A 413    28126  27748  21150  -5144  -1205   5089       C  
ATOM   2377  N   PRO A 414      -0.708 -12.137  66.495  1.00215.87           N  
ANISOU 2377  N   PRO A 414    31080  29106  21836  -5488  -1174   4322       N  
ATOM   2378  CA  PRO A 414      -0.776 -13.420  67.201  1.00208.17           C  
ANISOU 2378  CA  PRO A 414    30367  28015  20713  -5211  -1291   4281       C  
ATOM   2379  C   PRO A 414       0.552 -13.816  67.819  1.00199.83           C  
ANISOU 2379  C   PRO A 414    29269  27072  19587  -4645   -979   3658       C  
ATOM   2380  O   PRO A 414       1.595 -13.355  67.357  1.00198.15           O  
ANISOU 2380  O   PRO A 414    29031  26945  19313  -4550   -695   3238       O  
ATOM   2381  CB  PRO A 414      -1.157 -14.398  66.094  1.00215.94           C  
ANISOU 2381  CB  PRO A 414    32064  28691  21294  -5682  -1535   4461       C  
ATOM   2382  CG  PRO A 414      -0.531 -13.810  64.873  1.00222.56           C  
ANISOU 2382  CG  PRO A 414    33081  29511  21972  -5992  -1367   4233       C  
ATOM   2383  CD  PRO A 414      -0.609 -12.317  65.035  1.00220.11           C  
ANISOU 2383  CD  PRO A 414    32133  29455  22044  -5993  -1245   4323       C  
ATOM   2384  N   TRP A 415       0.526 -14.657  68.848  1.00204.59           N  
ANISOU 2384  N   TRP A 415    29848  27674  20211  -4280  -1035   3617       N  
ATOM   2385  CA  TRP A 415       1.778 -15.029  69.478  1.00194.18           C  
ANISOU 2385  CA  TRP A 415    28446  26467  18865  -3762   -750   3081       C  
ATOM   2386  C   TRP A 415       2.427 -16.136  68.654  1.00193.31           C  
ANISOU 2386  C   TRP A 415    28954  26115  18379  -3816   -686   2810       C  
ATOM   2387  O   TRP A 415       1.823 -16.684  67.728  1.00198.67           O  
ANISOU 2387  O   TRP A 415    30144  26543  18799  -4249   -888   3046       O  
ATOM   2388  CB  TRP A 415       1.554 -15.468  70.925  1.00185.50           C  
ANISOU 2388  CB  TRP A 415    27052  25475  17953  -3362   -822   3136       C  
ATOM   2389  CG  TRP A 415       1.010 -14.376  71.803  1.00177.49           C  
ANISOU 2389  CG  TRP A 415    25451  24676  17311  -3286   -811   3357       C  
ATOM   2390  CD1 TRP A 415       1.690 -13.296  72.284  1.00175.04           C  
ANISOU 2390  CD1 TRP A 415    24669  24622  17217  -3059   -524   3105       C  
ATOM   2391  CD2 TRP A 415      -0.327 -14.261  72.303  1.00172.17           C  
ANISOU 2391  CD2 TRP A 415    24620  23957  16841  -3444  -1074   3888       C  
ATOM   2392  NE1 TRP A 415       0.861 -12.514  73.049  1.00170.66           N  
ANISOU 2392  NE1 TRP A 415    23691  24174  16979  -3077   -565   3427       N  
ATOM   2393  CE2 TRP A 415      -0.384 -13.085  73.076  1.00167.17           C  
ANISOU 2393  CE2 TRP A 415    23422  23543  16553  -3303   -893   3916       C  
ATOM   2394  CE3 TRP A 415      -1.482 -15.036  72.170  1.00168.29           C  
ANISOU 2394  CE3 TRP A 415    24416  23249  16276  -3696  -1436   4359       C  
ATOM   2395  CZ2 TRP A 415      -1.546 -12.667  73.713  1.00161.92           C  
ANISOU 2395  CZ2 TRP A 415    22476  22865  16183  -3396  -1027   4393       C  
ATOM   2396  CZ3 TRP A 415      -2.634 -14.618  72.802  1.00162.88           C  
ANISOU 2396  CZ3 TRP A 415    23431  22566  15891  -3778  -1601   4850       C  
ATOM   2397  CH2 TRP A 415      -2.657 -13.446  73.566  1.00159.85           C  
ANISOU 2397  CH2 TRP A 415    22485  22381  15870  -3624  -1381   4862       C  
ATOM   2398  N   GLN A 416       3.681 -16.442  68.984  1.00175.88           N  
ANISOU 2398  N   GLN A 416    26705  23973  16150  -3393   -383   2328       N  
ATOM   2399  CA  GLN A 416       4.510 -17.417  68.279  1.00174.55           C  
ANISOU 2399  CA  GLN A 416    27066  23571  15683  -3366   -207   2009       C  
ATOM   2400  C   GLN A 416       5.055 -16.870  66.960  1.00168.00           C  
ANISOU 2400  C   GLN A 416    26499  22648  14686  -3662     -9   1815       C  
ATOM   2401  O   GLN A 416       5.501 -17.645  66.107  1.00173.36           O  
ANISOU 2401  O   GLN A 416    27738  23057  15073  -3797    115   1633       O  
ATOM   2402  CB  GLN A 416       3.771 -18.742  68.042  1.00184.41           C  
ANISOU 2402  CB  GLN A 416    28868  24529  16671  -3576   -464   2248       C  
ATOM   2403  CG  GLN A 416       4.664 -19.959  67.921  1.00203.04           C  
ANISOU 2403  CG  GLN A 416    31636  26684  18827  -3344   -244   1907       C  
ATOM   2404  CD  GLN A 416       3.911 -21.175  67.425  1.00218.15           C  
ANISOU 2404  CD  GLN A 416    34185  28279  20424  -3654   -480   2143       C  
ATOM   2405  OE1 GLN A 416       2.684 -21.164  67.330  1.00221.42           O  
ANISOU 2405  OE1 GLN A 416    34691  28649  20789  -4003   -854   2595       O  
ATOM   2406  NE2 GLN A 416       4.646 -22.231  67.098  1.00228.94           N  
ANISOU 2406  NE2 GLN A 416    35998  29407  21581  -3537   -250   1859       N  
ATOM   2407  N   GLU A 417       5.059 -15.549  66.769  1.00159.52           N  
ANISOU 2407  N   GLU A 417    25040  21781  13790  -3768     46   1837       N  
ATOM   2408  CA  GLU A 417       5.588 -14.929  65.555  1.00160.90           C  
ANISOU 2408  CA  GLU A 417    25402  21900  13830  -4041    225   1646       C  
ATOM   2409  C   GLU A 417       6.465 -13.748  65.940  1.00145.93           C  
ANISOU 2409  C   GLU A 417    22937  20316  12195  -3717    495   1358       C  
ATOM   2410  O   GLU A 417       5.986 -12.799  66.567  1.00143.57           O  
ANISOU 2410  O   GLU A 417    22116  20265  12170  -3680    413   1550       O  
ATOM   2411  CB  GLU A 417       4.449 -14.463  64.638  1.00182.85           C  
ANISOU 2411  CB  GLU A 417    28359  24587  16527  -4679    -64   2080       C  
ATOM   2412  CG  GLU A 417       4.867 -13.550  63.483  1.00188.18           C  
ANISOU 2412  CG  GLU A 417    29089  25277  17133  -4993     81   1937       C  
ATOM   2413  CD  GLU A 417       5.628 -14.267  62.381  1.00184.45           C  
ANISOU 2413  CD  GLU A 417    29277  24512  16291  -5157    279   1616       C  
ATOM   2414  OE1 GLU A 417       6.825 -13.959  62.178  1.00182.67           O  
ANISOU 2414  OE1 GLU A 417    28984  24342  16079  -4882    630   1168       O  
ATOM   2415  OE2 GLU A 417       5.023 -15.125  61.706  1.00183.18           O  
ANISOU 2415  OE2 GLU A 417    29720  24055  15827  -5577     93   1826       O  
ATOM   2416  N   ARG A 418       7.743 -13.803  65.563  1.00148.57           N  
ANISOU 2416  N   ARG A 418    23379  20622  12447  -3488    832    914       N  
ATOM   2417  CA  ARG A 418       8.659 -12.701  65.840  1.00154.93           C  
ANISOU 2417  CA  ARG A 418    23684  21715  13468  -3191   1089    634       C  
ATOM   2418  C   ARG A 418       8.193 -11.378  65.240  1.00176.57           C  
ANISOU 2418  C   ARG A 418    26175  24609  16304  -3537   1019    786       C  
ATOM   2419  O   ARG A 418       8.157 -11.230  64.014  1.00185.11           O  
ANISOU 2419  O   ARG A 418    27602  25536  17196  -3932   1020    774       O  
ATOM   2420  CB  ARG A 418      10.057 -13.001  65.300  1.00160.84           C  
ANISOU 2420  CB  ARG A 418    24664  22351  14096  -2962   1453    181       C  
ATOM   2421  CG  ARG A 418      10.801 -14.145  65.943  1.00164.03           C  
ANISOU 2421  CG  ARG A 418    25196  22640  14489  -2541   1618    -14       C  
ATOM   2422  CD  ARG A 418      12.173 -14.237  65.298  1.00174.27           C  
ANISOU 2422  CD  ARG A 418    26677  23816  15721  -2347   2013   -418       C  
ATOM   2423  NE  ARG A 418      13.021 -15.254  65.907  1.00174.23           N  
ANISOU 2423  NE  ARG A 418    26729  23701  15767  -1920   2226   -595       N  
ATOM   2424  CZ  ARG A 418      14.344 -15.276  65.793  1.00168.53           C  
ANISOU 2424  CZ  ARG A 418    25966  22948  15122  -1593   2594   -909       C  
ATOM   2425  NH1 ARG A 418      14.964 -14.331  65.099  1.00151.32           N  
ANISOU 2425  NH1 ARG A 418    23698  20844  12951  -1634   2778  -1103       N  
ATOM   2426  NH2 ARG A 418      15.048 -16.236  66.376  1.00153.05           N  
ANISOU 2426  NH2 ARG A 418    24029  20876  13246  -1226   2778  -1008       N  
ATOM   2427  N   SER A 419       7.851 -10.411  66.092  1.00172.11           N  
ANISOU 2427  N   SER A 419    25017  24339  16037  -3407    975    928       N  
ATOM   2428  CA  SER A 419       7.526  -9.064  65.636  1.00181.92           C  
ANISOU 2428  CA  SER A 419    25932  25759  17431  -3670    966   1049       C  
ATOM   2429  C   SER A 419       7.987  -8.085  66.707  1.00183.82           C  
ANISOU 2429  C   SER A 419    25530  26345  17970  -3274   1142    916       C  
ATOM   2430  O   SER A 419       7.592  -8.213  67.870  1.00197.66           O  
ANISOU 2430  O   SER A 419    27018  28195  19888  -3059   1075   1064       O  
ATOM   2431  CB  SER A 419       6.025  -8.895  65.354  1.00184.85           C  
ANISOU 2431  CB  SER A 419    26333  26043  17858  -4167    634   1595       C  
ATOM   2432  OG  SER A 419       5.269  -8.752  66.545  1.00176.12           O  
ANISOU 2432  OG  SER A 419    24842  25062  17013  -4010    514   1884       O  
ATOM   2433  N   THR A 420       8.800  -7.104  66.318  1.00172.98           N  
ANISOU 2433  N   THR A 420    23919  25152  16652  -3199   1365    646       N  
ATOM   2434  CA  THR A 420       9.287  -6.131  67.286  1.00180.48           C  
ANISOU 2434  CA  THR A 420    24290  26431  17853  -2855   1544    512       C  
ATOM   2435  C   THR A 420       8.127  -5.263  67.755  1.00223.00           C  
ANISOU 2435  C   THR A 420    29283  31947  23500  -3064   1414    907       C  
ATOM   2436  O   THR A 420       7.230  -4.925  66.978  1.00213.95           O  
ANISOU 2436  O   THR A 420    28202  30709  22380  -3507   1251   1217       O  
ATOM   2437  CB  THR A 420      10.409  -5.268  66.693  1.00147.57           C  
ANISOU 2437  CB  THR A 420    19974  22422  13673  -2742   1800    148       C  
ATOM   2438  OG1 THR A 420       9.886  -4.403  65.678  1.00132.57           O  
ANISOU 2438  OG1 THR A 420    18035  20536  11799  -3166   1733    294       O  
ATOM   2439  CG2 THR A 420      11.514  -6.144  66.101  1.00134.97           C  
ANISOU 2439  CG2 THR A 420    18804  20638  11839  -2567   1957   -204       C  
ATOM   2440  N   MET A 421       8.141  -4.908  69.034  1.00217.93           N  
ANISOU 2440  N   MET A 421    28237  31502  23063  -2767   1498    918       N  
ATOM   2441  CA  MET A 421       7.083  -4.097  69.612  1.00228.04           C  
ANISOU 2441  CA  MET A 421    29138  32881  24624  -2921   1440   1284       C  
ATOM   2442  C   MET A 421       7.548  -2.650  69.657  1.00232.91           C  
ANISOU 2442  C   MET A 421    29293  33777  25424  -2863   1685   1134       C  
ATOM   2443  O   MET A 421       8.712  -2.336  69.402  1.00236.31           O  
ANISOU 2443  O   MET A 421    29683  34346  25758  -2655   1875    745       O  
ATOM   2444  CB  MET A 421       6.746  -4.581  71.024  1.00227.33           C  
ANISOU 2444  CB  MET A 421    28915  32815  24644  -2664   1403   1398       C  
ATOM   2445  CG  MET A 421       6.777  -6.088  71.167  1.00232.20           C  
ANISOU 2445  CG  MET A 421    29956  33220  25050  -2555   1232   1378       C  
ATOM   2446  SD  MET A 421       5.420  -6.883  70.318  1.00238.19           S  
ANISOU 2446  SD  MET A 421    31145  33651  25707  -3024    877   1842       S  
ATOM   2447  CE  MET A 421       4.082  -6.116  71.194  1.00236.39           C  
ANISOU 2447  CE  MET A 421    30484  33488  25845  -3155    798   2335       C  
ATOM   2448  N   SER A 422       6.617  -1.759  69.978  1.00254.20           N  
ANISOU 2448  N   SER A 422    31639  36547  28401  -3050   1691   1467       N  
ATOM   2449  CA  SER A 422       6.877  -0.330  69.915  1.00249.04           C  
ANISOU 2449  CA  SER A 422    30548  36134  27941  -3066   1919   1386       C  
ATOM   2450  C   SER A 422       6.813   0.310  71.293  1.00236.49           C  
ANISOU 2450  C   SER A 422    28551  34727  26578  -2827   2120   1404       C  
ATOM   2451  O   SER A 422       7.768   0.965  71.721  1.00240.59           O  
ANISOU 2451  O   SER A 422    28837  35483  27093  -2566   2357   1075       O  
ATOM   2452  CB  SER A 422       5.880   0.348  68.970  1.00255.61           C  
ANISOU 2452  CB  SER A 422    31282  36892  28946  -3545   1814   1772       C  
ATOM   2453  OG  SER A 422       4.560   0.248  69.478  1.00257.55           O  
ANISOU 2453  OG  SER A 422    31435  36999  29424  -3738   1684   2278       O  
ATOM   2454  N   LEU A 423       5.694   0.132  71.986  1.00249.07           N  
ANISOU 2454  N   LEU A 423    30074  36200  28361  -2930   2032   1796       N  
ATOM   2455  CA  LEU A 423       5.281   0.902  73.149  1.00235.99           C  
ANISOU 2455  CA  LEU A 423    28032  34654  26979  -2839   2237   1934       C  
ATOM   2456  C   LEU A 423       6.428   1.097  74.132  1.00245.31           C  
ANISOU 2456  C   LEU A 423    29079  36066  28062  -2448   2465   1514       C  
ATOM   2457  O   LEU A 423       7.054   0.115  74.552  1.00241.70           O  
ANISOU 2457  O   LEU A 423    28854  35591  27392  -2202   2378   1301       O  
ATOM   2458  CB  LEU A 423       4.110   0.205  73.837  1.00221.83           C  
ANISOU 2458  CB  LEU A 423    26326  32645  25315  -2917   2068   2348       C  
ATOM   2459  CG  LEU A 423       3.145   1.150  74.545  1.00210.71           C  
ANISOU 2459  CG  LEU A 423    24537  31231  24291  -3037   2256   2709       C  
ATOM   2460  CD1 LEU A 423       2.510   2.124  73.556  1.00208.64           C  
ANISOU 2460  CD1 LEU A 423    24056  30943  24274  -3404   2296   3013       C  
ATOM   2461  CD2 LEU A 423       2.097   0.346  75.272  1.00209.85           C  
ANISOU 2461  CD2 LEU A 423    24546  30899  24288  -3064   2084   3087       C  
ATOM   2462  N   PRO A 424       6.737   2.329  74.524  1.00232.42           N  
ANISOU 2462  N   PRO A 424    27078  34651  26582  -2397   2757   1407       N  
ATOM   2463  CA  PRO A 424       7.784   2.529  75.519  1.00257.00           C  
ANISOU 2463  CA  PRO A 424    30074  37982  29590  -2071   2957   1056       C  
ATOM   2464  C   PRO A 424       7.194   2.486  76.916  1.00307.14           C  
ANISOU 2464  C   PRO A 424    36317  44302  36082  -2014   3047   1234       C  
ATOM   2465  O   PRO A 424       6.111   3.038  77.164  1.00301.95           O  
ANISOU 2465  O   PRO A 424    35482  43546  35699  -2215   3137   1580       O  
ATOM   2466  CB  PRO A 424       8.328   3.925  75.180  1.00231.54           C  
ANISOU 2466  CB  PRO A 424    26530  34996  26450  -2093   3224    880       C  
ATOM   2467  CG  PRO A 424       7.167   4.639  74.560  1.00222.21           C  
ANISOU 2467  CG  PRO A 424    25168  33708  25554  -2441   3242   1261       C  
ATOM   2468  CD  PRO A 424       6.220   3.603  73.992  1.00226.06           C  
ANISOU 2468  CD  PRO A 424    25951  33906  26037  -2653   2917   1595       C  
ATOM   2469  N   PRO A 425       7.882   1.854  77.860  1.00276.55           N  
ANISOU 2469  N   PRO A 425    32537  40498  32042  -1755   3038   1022       N  
ATOM   2470  CA  PRO A 425       7.368   1.796  79.236  1.00287.72           C  
ANISOU 2470  CA  PRO A 425    33870  41884  33566  -1717   3124   1169       C  
ATOM   2471  C   PRO A 425       7.563   3.075  80.034  1.00278.87           C  
ANISOU 2471  C   PRO A 425    32439  40950  32567  -1723   3487   1094       C  
ATOM   2472  O   PRO A 425       6.735   3.400  80.892  1.00285.65           O  
ANISOU 2472  O   PRO A 425    33190  41722  33621  -1821   3634   1325       O  
ATOM   2473  CB  PRO A 425       8.159   0.633  79.854  1.00287.03           C  
ANISOU 2473  CB  PRO A 425    33996  41823  33238  -1460   2963    955       C  
ATOM   2474  CG  PRO A 425       8.713  -0.132  78.682  1.00287.66           C  
ANISOU 2474  CG  PRO A 425    34327  41840  33131  -1404   2757    809       C  
ATOM   2475  CD  PRO A 425       8.973   0.893  77.636  1.00285.52           C  
ANISOU 2475  CD  PRO A 425    33919  41668  32899  -1522   2892    719       C  
ATOM   2476  N   GLY A 426       8.653   3.802  79.777  1.00308.74           N  
ANISOU 2476  N   GLY A 426    36095  44977  36236  -1624   3648    777       N  
ATOM   2477  CA  GLY A 426       8.871   5.060  80.477  1.00284.82           C  
ANISOU 2477  CA  GLY A 426    32793  42131  33296  -1652   4003    698       C  
ATOM   2478  C   GLY A 426       7.781   6.079  80.201  1.00259.19           C  
ANISOU 2478  C   GLY A 426    29316  38789  30374  -1907   4215    994       C  
ATOM   2479  O   GLY A 426       7.340   6.793  81.104  1.00248.65           O  
ANISOU 2479  O   GLY A 426    27824  37449  29204  -1987   4506   1105       O  
ATOM   2480  N   LEU A 427       7.339   6.163  78.945  1.00283.32           N  
ANISOU 2480  N   LEU A 427    32353  41756  33538  -2058   4087   1142       N  
ATOM   2481  CA  LEU A 427       6.223   7.033  78.583  1.00275.37           C  
ANISOU 2481  CA  LEU A 427    31110  40631  32889  -2330   4250   1502       C  
ATOM   2482  C   LEU A 427       4.954   6.684  79.358  1.00277.53           C  
ANISOU 2482  C   LEU A 427    31407  40640  33403  -2448   4265   1914       C  
ATOM   2483  O   LEU A 427       4.154   7.574  79.672  1.00281.55           O  
ANISOU 2483  O   LEU A 427    31672  41066  34239  -2613   4557   2186       O  
ATOM   2484  CB  LEU A 427       5.961   6.952  77.081  1.00270.02           C  
ANISOU 2484  CB  LEU A 427    30459  39883  32252  -2509   4027   1626       C  
ATOM   2485  CG  LEU A 427       6.790   7.894  76.195  1.00265.88           C  
ANISOU 2485  CG  LEU A 427    29750  39595  31678  -2513   4145   1358       C  
ATOM   2486  CD1 LEU A 427       6.102   8.143  74.848  1.00265.72           C  
ANISOU 2486  CD1 LEU A 427    29658  39468  31837  -2817   4006   1632       C  
ATOM   2487  CD2 LEU A 427       7.097   9.214  76.910  1.00264.24           C  
ANISOU 2487  CD2 LEU A 427    29214  39589  31596  -2472   4565   1235       C  
ATOM   2488  N   LEU A 428       4.753   5.401  79.678  1.00290.36           N  
ANISOU 2488  N   LEU A 428    33318  42119  34888  -2359   3970   1977       N  
ATOM   2489  CA  LEU A 428       3.547   4.970  80.382  1.00270.71           C  
ANISOU 2489  CA  LEU A 428    30871  39370  32616  -2454   3943   2376       C  
ATOM   2490  C   LEU A 428       3.594   5.332  81.863  1.00277.38           C  
ANISOU 2490  C   LEU A 428    31641  40250  33501  -2365   4250   2304       C  
ATOM   2491  O   LEU A 428       2.595   5.803  82.415  1.00274.73           O  
ANISOU 2491  O   LEU A 428    31172  39736  33479  -2506   4480   2636       O  
ATOM   2492  CB  LEU A 428       3.341   3.469  80.184  1.00246.81           C  
ANISOU 2492  CB  LEU A 428    28180  36186  29409  -2389   3511   2455       C  
ATOM   2493  CG  LEU A 428       1.873   3.034  80.150  1.00230.24           C  
ANISOU 2493  CG  LEU A 428    26125  33777  27578  -2585   3359   2996       C  
ATOM   2494  CD1 LEU A 428       1.156   3.708  78.990  1.00222.44           C  
ANISOU 2494  CD1 LEU A 428    24972  32695  26850  -2883   3361   3337       C  
ATOM   2495  CD2 LEU A 428       1.758   1.522  80.041  1.00228.04           C  
ANISOU 2495  CD2 LEU A 428    26200  33365  27078  -2502   2937   3034       C  
ATOM   2496  N   GLY A 429       4.731   5.125  82.528  1.00269.92           N  
ANISOU 2496  N   GLY A 429    30787  39516  32255  -2157   4272   1901       N  
ATOM   2497  CA  GLY A 429       4.847   5.581  83.902  1.00267.07           C  
ANISOU 2497  CA  GLY A 429    30368  39206  31900  -2132   4581   1820       C  
ATOM   2498  C   GLY A 429       5.829   4.861  84.807  1.00266.29           C  
ANISOU 2498  C   GLY A 429    30445  39259  31473  -1936   4465   1508       C  
ATOM   2499  O   GLY A 429       6.193   5.396  85.860  1.00265.97           O  
ANISOU 2499  O   GLY A 429    30358  39324  31373  -1947   4735   1374       O  
ATOM   2500  N   ASN A 430       6.270   3.664  84.434  1.00277.66           N  
ANISOU 2500  N   ASN A 430    32089  40704  32703  -1782   4081   1405       N  
ATOM   2501  CA  ASN A 430       7.241   2.958  85.257  1.00245.28           C  
ANISOU 2501  CA  ASN A 430    28119  36750  28326  -1602   3965   1143       C  
ATOM   2502  C   ASN A 430       8.625   3.577  85.103  1.00248.40           C  
ANISOU 2502  C   ASN A 430    28422  37443  28516  -1500   4090    785       C  
ATOM   2503  O   ASN A 430       8.951   4.182  84.077  1.00252.98           O  
ANISOU 2503  O   ASN A 430    28900  38110  29110  -1505   4142    692       O  
ATOM   2504  CB  ASN A 430       7.291   1.469  84.904  1.00225.97           C  
ANISOU 2504  CB  ASN A 430    25909  34201  25750  -1462   3548   1160       C  
ATOM   2505  CG  ASN A 430       6.121   0.691  85.475  1.00211.65           C  
ANISOU 2505  CG  ASN A 430    24212  32135  24072  -1520   3398   1476       C  
ATOM   2506  OD1 ASN A 430       5.872   0.712  86.679  1.00208.20           O  
ANISOU 2506  OD1 ASN A 430    23897  31503  23706  -1555   3152   1697       O  
ATOM   2507  ND2 ASN A 430       5.380   0.016  84.602  1.00206.94           N  
ANISOU 2507  ND2 ASN A 430    23594  31537  23496  -1544   3539   1502       N  
ATOM   2508  N   SER A 431       9.440   3.429  86.143  1.00234.30           N  
ANISOU 2508  N   SER A 431    26667  35815  26542  -1423   4128    603       N  
ATOM   2509  CA  SER A 431      10.829   3.859  86.062  1.00238.02           C  
ANISOU 2509  CA  SER A 431    27067  36567  26802  -1313   4194    298       C  
ATOM   2510  C   SER A 431      11.610   2.874  85.201  1.00243.83           C  
ANISOU 2510  C   SER A 431    27921  37329  27394  -1100   3882    162       C  
ATOM   2511  O   SER A 431      11.390   1.663  85.264  1.00244.07           O  
ANISOU 2511  O   SER A 431    28120  37217  27398  -1016   3615    244       O  
ATOM   2512  CB  SER A 431      11.447   3.949  87.458  1.00233.18           C  
ANISOU 2512  CB  SER A 431    26465  36104  26030  -1341   4303    200       C  
ATOM   2513  OG  SER A 431      10.621   4.687  88.340  1.00227.42           O  
ANISOU 2513  OG  SER A 431    25694  35288  25428  -1555   4601    340       O  
ATOM   2514  N   TRP A 432      12.494   3.400  84.359  1.00231.21           N  
ANISOU 2514  N   TRP A 432    26239  35894  25717  -1013   3935    -40       N  
ATOM   2515  CA  TRP A 432      13.233   2.593  83.404  1.00226.09           C  
ANISOU 2515  CA  TRP A 432    25710  35238  24957   -822   3708   -174       C  
ATOM   2516  C   TRP A 432      14.714   2.581  83.767  1.00217.28           C  
ANISOU 2516  C   TRP A 432    24547  34356  23654   -647   3724   -401       C  
ATOM   2517  O   TRP A 432      15.148   3.204  84.739  1.00218.94           O  
ANISOU 2517  O   TRP A 432    24642  34747  23798   -700   3884   -447       O  
ATOM   2518  CB  TRP A 432      12.999   3.118  81.984  1.00230.73           C  
ANISOU 2518  CB  TRP A 432    26261  35781  25625   -875   3733   -192       C  
ATOM   2519  CG  TRP A 432      13.343   2.159  80.878  1.00234.59           C  
ANISOU 2519  CG  TRP A 432    26954  36150  26031   -750   3499   -263       C  
ATOM   2520  CD1 TRP A 432      14.240   2.362  79.870  1.00235.00           C  
ANISOU 2520  CD1 TRP A 432    27008  36287  25995   -642   3512   -473       C  
ATOM   2521  CD2 TRP A 432      12.812   0.842  80.682  1.00235.89           C  
ANISOU 2521  CD2 TRP A 432    27373  36072  26183   -729   3239   -129       C  
ATOM   2522  NE1 TRP A 432      14.286   1.262  79.048  1.00236.08           N  
ANISOU 2522  NE1 TRP A 432    27405  36229  26065   -571   3303   -481       N  
ATOM   2523  CE2 TRP A 432      13.420   0.314  79.526  1.00236.85           C  
ANISOU 2523  CE2 TRP A 432    27663  36128  26200   -626   3130   -272       C  
ATOM   2524  CE3 TRP A 432      11.876   0.062  81.368  1.00236.94           C  
ANISOU 2524  CE3 TRP A 432    27618  36030  26379   -791   3095    100       C  
ATOM   2525  CZ2 TRP A 432      13.125  -0.959  79.043  1.00239.04           C  
ANISOU 2525  CZ2 TRP A 432    28235  36168  26424   -598   2900   -198       C  
ATOM   2526  CZ3 TRP A 432      11.585  -1.201  80.887  1.00238.16           C  
ANISOU 2526  CZ3 TRP A 432    28039  35969  26483   -747   2836    179       C  
ATOM   2527  CH2 TRP A 432      12.208  -1.700  79.737  1.00239.90           C  
ANISOU 2527  CH2 TRP A 432    28440  36124  26586   -659   2749     29       C  
ATOM   2528  N   GLY A 433      15.493   1.887  82.962  1.00226.56           N  
ANISOU 2528  N   GLY A 433    25821  35514  24748   -456   3572   -523       N  
ATOM   2529  CA  GLY A 433      16.884   1.743  83.363  1.00216.52           C  
ANISOU 2529  CA  GLY A 433    24497  34434  23339   -281   3572   -674       C  
ATOM   2530  C   GLY A 433      17.107   0.315  83.826  1.00206.47           C  
ANISOU 2530  C   GLY A 433    23373  33044  22033   -153   3348   -605       C  
ATOM   2531  O   GLY A 433      16.265  -0.278  84.515  1.00207.03           O  
ANISOU 2531  O   GLY A 433    23524  32988  22151   -241   3244   -445       O  
ATOM   2532  N   GLU A 434      18.244  -0.252  83.422  1.00211.25           N  
ANISOU 2532  N   GLU A 434    24009  33679  22577     62   3285   -713       N  
ATOM   2533  CA  GLU A 434      18.607  -1.605  83.811  1.00196.95           C  
ANISOU 2533  CA  GLU A 434    22308  31762  20762    203   3103   -646       C  
ATOM   2534  C   GLU A 434      18.561  -1.759  85.324  1.00195.73           C  
ANISOU 2534  C   GLU A 434    22064  31716  20588    105   3057   -521       C  
ATOM   2535  O   GLU A 434      19.275  -1.061  86.050  1.00204.57           O  
ANISOU 2535  O   GLU A 434    23021  33067  21639     53   3160   -545       O  
ATOM   2536  CB  GLU A 434      20.011  -1.924  83.286  1.00189.71           C  
ANISOU 2536  CB  GLU A 434    21371  30895  19817    442   3124   -763       C  
ATOM   2537  CG  GLU A 434      21.015  -0.776  83.460  1.00187.68           C  
ANISOU 2537  CG  GLU A 434    20893  30918  19498    459   3290   -861       C  
ATOM   2538  CD  GLU A 434      22.470  -1.221  83.367  1.00190.11           C  
ANISOU 2538  CD  GLU A 434    21139  31286  19807    691   3289   -886       C  
ATOM   2539  OE1 GLU A 434      22.724  -2.443  83.318  1.00192.20           O  
ANISOU 2539  OE1 GLU A 434    21511  31379  20136    834   3179   -818       O  
ATOM   2540  OE2 GLU A 434      23.363  -0.345  83.345  1.00190.64           O  
ANISOU 2540  OE2 GLU A 434    21042  31566  19827    731   3407   -955       O  
ATOM   2541  N   GLY A 435      17.715  -2.669  85.806  1.00197.96           N  
ANISOU 2541  N   GLY A 435    22465  31832  20918     58   2894   -380       N  
ATOM   2542  CA  GLY A 435      17.471  -2.836  87.228  1.00184.16           C  
ANISOU 2542  CA  GLY A 435    20658  30158  19156    -73   2840   -254       C  
ATOM   2543  C   GLY A 435      16.048  -2.556  87.671  1.00173.59           C  
ANISOU 2543  C   GLY A 435    19373  28705  17877   -278   2862   -131       C  
ATOM   2544  O   GLY A 435      15.639  -3.031  88.742  1.00178.48           O  
ANISOU 2544  O   GLY A 435    20010  29302  18504   -368   2769    -10       O  
ATOM   2545  N   ALA A 436      15.279  -1.802  86.889  1.00177.89           N  
ANISOU 2545  N   ALA A 436    19936  29169  18486   -363   2985   -137       N  
ATOM   2546  CA  ALA A 436      13.898  -1.509  87.240  1.00180.38           C  
ANISOU 2546  CA  ALA A 436    20284  29343  18909   -553   3032     28       C  
ATOM   2547  C   ALA A 436      13.057  -2.786  87.285  1.00193.80           C  
ANISOU 2547  C   ALA A 436    22156  30806  20671   -513   2772    193       C  
ATOM   2548  O   ALA A 436      13.361  -3.765  86.596  1.00196.15           O  
ANISOU 2548  O   ALA A 436    22581  31006  20941   -350   2585    162       O  
ATOM   2549  CB  ALA A 436      13.302  -0.527  86.235  1.00169.30           C  
ANISOU 2549  CB  ALA A 436    18840  27887  17599   -646   3198     28       C  
ATOM   2550  N   PRO A 437      12.002  -2.806  88.112  1.00191.15           N  
ANISOU 2550  N   PRO A 437    21841  30365  20421   -661   2770    373       N  
ATOM   2551  CA  PRO A 437      11.203  -4.037  88.256  1.00190.12           C  
ANISOU 2551  CA  PRO A 437    21868  30025  20345   -618   2503    543       C  
ATOM   2552  C   PRO A 437      10.623  -4.559  86.954  1.00185.84           C  
ANISOU 2552  C   PRO A 437    21488  29273  19851   -566   2351    619       C  
ATOM   2553  O   PRO A 437      10.683  -5.768  86.699  1.00180.60           O  
ANISOU 2553  O   PRO A 437    20981  28497  19144   -436   2110    640       O  
ATOM   2554  CB  PRO A 437      10.093  -3.613  89.229  1.00192.97           C  
ANISOU 2554  CB  PRO A 437    22200  30300  20819   -812   2606    732       C  
ATOM   2555  CG  PRO A 437      10.679  -2.480  89.997  1.00191.70           C  
ANISOU 2555  CG  PRO A 437    21889  30348  20598   -938   2897    614       C  
ATOM   2556  CD  PRO A 437      11.553  -1.744  89.029  1.00189.61           C  
ANISOU 2556  CD  PRO A 437    21539  30234  20273   -871   3028    427       C  
ATOM   2557  N   ALA A 438      10.058  -3.680  86.122  1.00200.15           N  
ANISOU 2557  N   ALA A 438    23271  31025  21751   -688   2488    674       N  
ATOM   2558  CA  ALA A 438       9.491  -4.123  84.852  1.00180.49           C  
ANISOU 2558  CA  ALA A 438    20952  28335  19289   -702   2334    773       C  
ATOM   2559  C   ALA A 438      10.573  -4.675  83.935  1.00161.57           C  
ANISOU 2559  C   ALA A 438    18672  25973  16746   -530   2258    552       C  
ATOM   2560  O   ALA A 438      10.363  -5.682  83.250  1.00154.92           O  
ANISOU 2560  O   ALA A 438    18060  24948  15854   -482   2053    601       O  
ATOM   2561  CB  ALA A 438       8.744  -2.975  84.176  1.00174.44           C  
ANISOU 2561  CB  ALA A 438    20089  27522  18668   -901   2508    897       C  
ATOM   2562  N   TRP A 439      11.736  -4.021  83.907  1.00162.31           N  
ANISOU 2562  N   TRP A 439    18620  26283  16767   -443   2437    319       N  
ATOM   2563  CA  TRP A 439      12.851  -4.490  83.093  1.00185.63           C  
ANISOU 2563  CA  TRP A 439    21666  29259  19608   -262   2410    115       C  
ATOM   2564  C   TRP A 439      13.230  -5.915  83.482  1.00208.58           C  
ANISOU 2564  C   TRP A 439    24713  32078  22460    -90   2216    120       C  
ATOM   2565  O   TRP A 439      13.237  -6.827  82.646  1.00196.48           O  
ANISOU 2565  O   TRP A 439    23414  30358  20880    -17   2092    110       O  
ATOM   2566  CB  TRP A 439      14.047  -3.554  83.277  1.00191.76           C  
ANISOU 2566  CB  TRP A 439    22226  30300  20334   -187   2627    -93       C  
ATOM   2567  CG  TRP A 439      15.219  -3.828  82.376  1.00187.14           C  
ANISOU 2567  CG  TRP A 439    21704  29734  19666      0   2653   -291       C  
ATOM   2568  CD1 TRP A 439      15.952  -4.979  82.285  1.00187.92           C  
ANISOU 2568  CD1 TRP A 439    21932  29749  19722    197   2550   -342       C  
ATOM   2569  CD2 TRP A 439      15.848  -2.885  81.501  1.00180.88           C  
ANISOU 2569  CD2 TRP A 439    20829  29052  18846     16   2824   -461       C  
ATOM   2570  NE1 TRP A 439      16.962  -4.824  81.365  1.00190.56           N  
ANISOU 2570  NE1 TRP A 439    22289  30104  20010    333   2662   -523       N  
ATOM   2571  CE2 TRP A 439      16.925  -3.544  80.877  1.00188.64           C  
ANISOU 2571  CE2 TRP A 439    21919  29990  19767    227   2817   -606       C  
ATOM   2572  CE3 TRP A 439      15.594  -1.550  81.175  1.00171.98           C  
ANISOU 2572  CE3 TRP A 439    19541  28048  17756   -126   2993   -496       C  
ATOM   2573  CZ2 TRP A 439      17.745  -2.912  79.943  1.00193.30           C  
ANISOU 2573  CZ2 TRP A 439    22472  30653  20320    303   2961   -790       C  
ATOM   2574  CZ3 TRP A 439      16.407  -0.925  80.248  1.00178.88           C  
ANISOU 2574  CZ3 TRP A 439    20364  29016  18586    -54   3116   -685       C  
ATOM   2575  CH2 TRP A 439      17.469  -1.606  79.642  1.00190.95           C  
ANISOU 2575  CH2 TRP A 439    22014  30497  20042    160   3093   -833       C  
ATOM   2576  N   VAL A 440      13.567  -6.113  84.762  1.00189.72           N  
ANISOU 2576  N   VAL A 440    22186  29822  20077    -44   2199    140       N  
ATOM   2577  CA  VAL A 440      13.996  -7.422  85.250  1.00195.67           C  
ANISOU 2577  CA  VAL A 440    23012  30524  20810    114   2023    161       C  
ATOM   2578  C   VAL A 440      12.876  -8.443  85.101  1.00186.90           C  
ANISOU 2578  C   VAL A 440    22124  29164  19726     82   1794    335       C  
ATOM   2579  O   VAL A 440      13.123  -9.619  84.809  1.00187.39           O  
ANISOU 2579  O   VAL A 440    22350  29091  19758    220   1654    330       O  
ATOM   2580  CB  VAL A 440      14.470  -7.311  86.710  1.00208.61           C  
ANISOU 2580  CB  VAL A 440    24439  32370  22454    100   2037    184       C  
ATOM   2581  CG1 VAL A 440      14.973  -8.658  87.209  1.00214.29           C  
ANISOU 2581  CG1 VAL A 440    25187  33050  23183    255   1853    226       C  
ATOM   2582  CG2 VAL A 440      15.546  -6.251  86.826  1.00213.90           C  
ANISOU 2582  CG2 VAL A 440    24909  33286  23076    100   2252     40       C  
ATOM   2583  N   LEU A 441      11.631  -8.017  85.321  1.00200.78           N  
ANISOU 2583  N   LEU A 441    23890  30848  21551   -102   1763    512       N  
ATOM   2584  CA  LEU A 441      10.491  -8.899  85.092  1.00176.13           C  
ANISOU 2584  CA  LEU A 441    20984  27482  18456   -152   1533    718       C  
ATOM   2585  C   LEU A 441      10.476  -9.414  83.657  1.00182.13           C  
ANISOU 2585  C   LEU A 441    22012  28049  19138   -136   1460    687       C  
ATOM   2586  O   LEU A 441      10.375 -10.624  83.420  1.00194.05           O  
ANISOU 2586  O   LEU A 441    23744  29395  20593    -52   1275    728       O  
ATOM   2587  CB  LEU A 441       9.192  -8.167  85.414  1.00145.76           C  
ANISOU 2587  CB  LEU A 441    17078  23573  14731   -364   1559    945       C  
ATOM   2588  CG  LEU A 441       8.048  -9.055  85.890  1.00134.44           C  
ANISOU 2588  CG  LEU A 441    15771  21951  13358   -401   1314   1203       C  
ATOM   2589  CD1 LEU A 441       8.460  -9.869  87.110  1.00124.49           C  
ANISOU 2589  CD1 LEU A 441    14448  20779  12074   -270   1201   1164       C  
ATOM   2590  CD2 LEU A 441       6.841  -8.192  86.197  1.00128.87           C  
ANISOU 2590  CD2 LEU A 441    14975  21173  12817   -606   1402   1449       C  
ATOM   2591  N   LEU A 442      10.563  -8.507  82.679  1.00173.59           N  
ANISOU 2591  N   LEU A 442    20929  26981  18046   -236   1611    616       N  
ATOM   2592  CA  LEU A 442      10.559  -8.933  81.282  1.00151.31           C  
ANISOU 2592  CA  LEU A 442    18391  23971  15130   -271   1556    580       C  
ATOM   2593  C   LEU A 442      11.747  -9.835  80.976  1.00147.21           C  
ANISOU 2593  C   LEU A 442    18004  23422  14508    -43   1579    368       C  
ATOM   2594  O   LEU A 442      11.598 -10.855  80.292  1.00157.80           O  
ANISOU 2594  O   LEU A 442    19657  24538  15762    -30   1459    390       O  
ATOM   2595  CB  LEU A 442      10.561  -7.718  80.356  1.00144.91           C  
ANISOU 2595  CB  LEU A 442    17511  23214  14334   -424   1725    524       C  
ATOM   2596  CG  LEU A 442       9.322  -6.823  80.392  1.00149.28           C  
ANISOU 2596  CG  LEU A 442    17948  23744  15029   -679   1729    778       C  
ATOM   2597  CD1 LEU A 442       9.505  -5.656  79.441  1.00138.78           C  
ANISOU 2597  CD1 LEU A 442    16520  22490  13722   -813   1907    696       C  
ATOM   2598  CD2 LEU A 442       8.062  -7.610  80.052  1.00157.59           C  
ANISOU 2598  CD2 LEU A 442    19251  24533  16095   -842   1470   1085       C  
ATOM   2599  N   ASP A 443      12.936  -9.470  81.460  1.00131.55           N  
ANISOU 2599  N   ASP A 443    15795  21647  12540    126   1748    182       N  
ATOM   2600  CA  ASP A 443      14.116 -10.290  81.213  1.00135.81           C  
ANISOU 2600  CA  ASP A 443    16418  22146  13037    353   1805     21       C  
ATOM   2601  C   ASP A 443      13.954 -11.684  81.807  1.00137.99           C  
ANISOU 2601  C   ASP A 443    16808  22296  13327    463   1621    125       C  
ATOM   2602  O   ASP A 443      14.450 -12.670  81.248  1.00136.06           O  
ANISOU 2602  O   ASP A 443    16779  21875  13042    593   1629     59       O  
ATOM   2603  CB  ASP A 443      15.360  -9.602  81.773  1.00146.60           C  
ANISOU 2603  CB  ASP A 443    17479  23775  14447    492   1994   -125       C  
ATOM   2604  CG  ASP A 443      16.639 -10.133  81.164  1.00156.18           C  
ANISOU 2604  CG  ASP A 443    18766  24927  15649    709   2126   -284       C  
ATOM   2605  OD1 ASP A 443      16.555 -10.872  80.160  1.00151.67           O  
ANISOU 2605  OD1 ASP A 443    18509  24099  15018    729   2120   -323       O  
ATOM   2606  OD2 ASP A 443      17.727  -9.805  81.687  1.00171.81           O  
ANISOU 2606  OD2 ASP A 443    20501  27098  17681    844   2247   -352       O  
ATOM   2607  N   GLU A 444      13.290 -11.781  82.961  1.00145.93           N  
ANISOU 2607  N   GLU A 444    17669  23383  14395    413   1475    283       N  
ATOM   2608  CA  GLU A 444      13.019 -13.089  83.544  1.00158.38           C  
ANISOU 2608  CA  GLU A 444    19339  24848  15989    504   1271    396       C  
ATOM   2609  C   GLU A 444      12.019 -13.878  82.711  1.00164.07           C  
ANISOU 2609  C   GLU A 444    20426  25284  16631    411   1097    515       C  
ATOM   2610  O   GLU A 444      12.123 -15.106  82.606  1.00155.29           O  
ANISOU 2610  O   GLU A 444    19505  24012  15488    523    995    530       O  
ATOM   2611  CB  GLU A 444      12.517 -12.925  84.977  1.00150.59           C  
ANISOU 2611  CB  GLU A 444    18117  24019  15083    449   1158    534       C  
ATOM   2612  CG  GLU A 444      13.628 -12.614  85.944  1.00142.08           C  
ANISOU 2612  CG  GLU A 444    16733  23194  14058    541   1270    447       C  
ATOM   2613  CD  GLU A 444      14.655 -13.722  85.981  1.00148.35           C  
ANISOU 2613  CD  GLU A 444    17529  23952  14887    756   1253    397       C  
ATOM   2614  OE1 GLU A 444      14.253 -14.906  85.994  1.00152.97           O  
ANISOU 2614  OE1 GLU A 444    18274  24368  15482    824   1080    482       O  
ATOM   2615  OE2 GLU A 444      15.864 -13.409  85.975  1.00154.06           O  
ANISOU 2615  OE2 GLU A 444    18088  24806  15641    858   1421    290       O  
ATOM   2616  N   CYS A 445      11.038 -13.193  82.119  1.00168.35           N  
ANISOU 2616  N   CYS A 445    21067  25755  17145    190   1063    625       N  
ATOM   2617  CA  CYS A 445      10.122 -13.873  81.212  1.00169.20           C  
ANISOU 2617  CA  CYS A 445    21544  25588  17155     51    890    769       C  
ATOM   2618  C   CYS A 445      10.831 -14.329  79.942  1.00158.50           C  
ANISOU 2618  C   CYS A 445    20495  24062  15667     85   1005    593       C  
ATOM   2619  O   CYS A 445      10.425 -15.324  79.332  1.00156.74           O  
ANISOU 2619  O   CYS A 445    20631  23592  15330     34    876    663       O  
ATOM   2620  CB  CYS A 445       8.928 -12.974  80.876  1.00174.20           C  
ANISOU 2620  CB  CYS A 445    22176  26188  17826   -224    828    981       C  
ATOM   2621  SG  CYS A 445       7.947 -12.414  82.299  1.00182.91           S  
ANISOU 2621  SG  CYS A 445    22967  27420  19109   -291    746   1221       S  
ATOM   2622  N   GLY A 446      11.894 -13.633  79.542  1.00170.29           N  
ANISOU 2622  N   GLY A 446    21869  25669  17166    166   1256    368       N  
ATOM   2623  CA  GLY A 446      12.695 -14.054  78.410  1.00163.48           C  
ANISOU 2623  CA  GLY A 446    21285  24634  16196    224   1415    182       C  
ATOM   2624  C   GLY A 446      12.788 -13.076  77.255  1.00160.45           C  
ANISOU 2624  C   GLY A 446    20985  24238  15742     54   1559     79       C  
ATOM   2625  O   GLY A 446      13.238 -13.452  76.167  1.00137.36           O  
ANISOU 2625  O   GLY A 446    18374  21115  12699     35   1673    -53       O  
ATOM   2626  N   LEU A 447      12.395 -11.821  77.466  1.00152.72           N  
ANISOU 2626  N   LEU A 447    19733  23457  14837    -78   1576    134       N  
ATOM   2627  CA  LEU A 447      12.436 -10.834  76.395  1.00168.58           C  
ANISOU 2627  CA  LEU A 447    21777  25475  16800   -255   1698     52       C  
ATOM   2628  C   LEU A 447      13.718 -10.021  76.496  1.00196.29           C  
ANISOU 2628  C   LEU A 447    25009  29208  20365    -60   1957   -198       C  
ATOM   2629  O   LEU A 447      14.142  -9.625  77.588  1.00173.88           O  
ANISOU 2629  O   LEU A 447    21829  26604  17634     91   2010   -217       O  
ATOM   2630  CB  LEU A 447      11.221  -9.899  76.429  1.00147.82           C  
ANISOU 2630  CB  LEU A 447    19010  22908  14245   -535   1587    286       C  
ATOM   2631  CG  LEU A 447       9.793 -10.455  76.333  1.00131.13           C  
ANISOU 2631  CG  LEU A 447    17115  20593  12114   -776   1314    615       C  
ATOM   2632  CD1 LEU A 447       8.765  -9.329  76.215  1.00129.60           C  
ANISOU 2632  CD1 LEU A 447    16734  20460  12048  -1055   1278    856       C  
ATOM   2633  CD2 LEU A 447       9.663 -11.406  75.157  1.00133.14           C  
ANISOU 2633  CD2 LEU A 447    17866  20552  12169   -914   1218    620       C  
ATOM   2634  N   GLU A 448      14.329  -9.775  75.343  1.00199.34           N  
ANISOU 2634  N   GLU A 448    25561  29514  20667    -85   2112   -378       N  
ATOM   2635  CA  GLU A 448      15.571  -9.025  75.284  1.00218.84           C  
ANISOU 2635  CA  GLU A 448    27797  32171  23181    103   2353   -608       C  
ATOM   2636  C   GLU A 448      15.247  -7.535  75.306  1.00228.23           C  
ANISOU 2636  C   GLU A 448    28684  33602  24433    -49   2398   -594       C  
ATOM   2637  O   GLU A 448      14.453  -7.054  74.491  1.00235.16           O  
ANISOU 2637  O   GLU A 448    29669  34407  25275   -320   2340   -514       O  
ATOM   2638  CB  GLU A 448      16.335  -9.393  74.011  1.00229.82           C  
ANISOU 2638  CB  GLU A 448    29509  33350  24463    140   2518   -805       C  
ATOM   2639  CG  GLU A 448      17.834  -9.264  74.131  1.00240.05           C  
ANISOU 2639  CG  GLU A 448    30634  34747  25828    449   2763  -1011       C  
ATOM   2640  CD  GLU A 448      18.370 -10.112  75.268  1.00246.32           C  
ANISOU 2640  CD  GLU A 448    31285  35577  26730    710   2751   -949       C  
ATOM   2641  OE1 GLU A 448      17.996 -11.303  75.343  1.00250.66           O  
ANISOU 2641  OE1 GLU A 448    32086  35902  27250    717   2653   -858       O  
ATOM   2642  OE2 GLU A 448      19.158  -9.593  76.085  1.00249.64           O  
ANISOU 2642  OE2 GLU A 448    31342  36250  27261    887   2831   -975       O  
ATOM   2643  N   LEU A 449      15.842  -6.809  76.245  1.00237.85           N  
ANISOU 2643  N   LEU A 449    29526  35101  25747    102   2502   -651       N  
ATOM   2644  CA  LEU A 449      15.634  -5.373  76.359  1.00212.88           C  
ANISOU 2644  CA  LEU A 449    26061  32176  22649    -21   2589   -654       C  
ATOM   2645  C   LEU A 449      16.905  -4.621  75.993  1.00213.58           C  
ANISOU 2645  C   LEU A 449    25988  32437  22726    141   2805   -896       C  
ATOM   2646  O   LEU A 449      18.012  -5.165  76.030  1.00219.37           O  
ANISOU 2646  O   LEU A 449    26755  33153  23441    385   2892  -1024       O  
ATOM   2647  CB  LEU A 449      15.177  -4.981  77.766  1.00200.56           C  
ANISOU 2647  CB  LEU A 449    24213  30802  21190    -35   2553   -508       C  
ATOM   2648  CG  LEU A 449      14.023  -5.807  78.324  1.00196.14           C  
ANISOU 2648  CG  LEU A 449    23784  30080  20660   -141   2338   -262       C  
ATOM   2649  CD1 LEU A 449      13.589  -5.242  79.656  1.00196.16           C  
ANISOU 2649  CD1 LEU A 449    23505  30261  20766   -180   2353   -138       C  
ATOM   2650  CD2 LEU A 449      12.864  -5.805  77.341  1.00191.74           C  
ANISOU 2650  CD2 LEU A 449    23445  29316  20092   -414   2217    -96       C  
ATOM   2651  N   GLY A 450      16.726  -3.351  75.639  1.00219.89           N  
ANISOU 2651  N   GLY A 450    26594  33398  23555      3   2895   -934       N  
ATOM   2652  CA  GLY A 450      17.841  -2.484  75.317  1.00229.33           C  
ANISOU 2652  CA  GLY A 450    27603  34789  24742    141   3086  -1150       C  
ATOM   2653  C   GLY A 450      17.652  -1.096  75.889  1.00233.31           C  
ANISOU 2653  C   GLY A 450    27745  35583  25321     51   3182  -1132       C  
ATOM   2654  O   GLY A 450      16.729  -0.873  76.679  1.00219.13           O  
ANISOU 2654  O   GLY A 450    25838  33824  23597    -94   3128   -950       O  
ATOM   2655  N   GLU A 451      18.498  -0.145  75.494  1.00232.38           N  
ANISOU 2655  N   GLU A 451    27448  35656  25191    131   3342  -1313       N  
ATOM   2656  CA  GLU A 451      18.401   1.198  76.050  1.00242.61           C  
ANISOU 2656  CA  GLU A 451    28404  37230  26545     52   3464  -1311       C  
ATOM   2657  C   GLU A 451      17.739   2.191  75.107  1.00247.75           C  
ANISOU 2657  C   GLU A 451    28977  37904  27253   -178   3513  -1310       C  
ATOM   2658  O   GLU A 451      17.065   3.117  75.573  1.00242.99           O  
ANISOU 2658  O   GLU A 451    28144  37430  26750   -341   3589  -1203       O  
ATOM   2659  CB  GLU A 451      19.805   1.718  76.383  1.00248.79           C  
ANISOU 2659  CB  GLU A 451    28988  38257  27282    287   3605  -1486       C  
ATOM   2660  CG  GLU A 451      20.627   0.804  77.289  1.00253.84           C  
ANISOU 2660  CG  GLU A 451    29657  38898  27893    506   3563  -1458       C  
ATOM   2661  CD  GLU A 451      20.009   0.554  78.649  1.00256.35           C  
ANISOU 2661  CD  GLU A 451    29905  39257  28238    414   3487  -1275       C  
ATOM   2662  OE1 GLU A 451      20.311  -0.506  79.236  1.00258.81           O  
ANISOU 2662  OE1 GLU A 451    30308  39480  28546    534   3388  -1202       O  
ATOM   2663  OE2 GLU A 451      19.214   1.394  79.124  1.00254.42           O  
ANISOU 2663  OE2 GLU A 451    29517  39118  28032    218   3539  -1197       O  
ATOM   2664  N   ASP A 452      17.895   2.001  73.802  1.00255.06           N  
ANISOU 2664  N   ASP A 452    30093  38690  28127   -214   3485  -1413       N  
ATOM   2665  CA  ASP A 452      17.294   2.825  72.762  1.00261.92           C  
ANISOU 2665  CA  ASP A 452    30912  39559  29048   -465   3498  -1398       C  
ATOM   2666  C   ASP A 452      16.522   1.924  71.792  1.00278.46           C  
ANISOU 2666  C   ASP A 452    33372  41333  31095   -677   3323  -1281       C  
ATOM   2667  O   ASP A 452      16.380   0.719  72.011  1.00282.08           O  
ANISOU 2667  O   ASP A 452    34109  41580  31487   -623   3204  -1210       O  
ATOM   2668  CB  ASP A 452      18.353   3.717  72.108  1.00254.52           C  
ANISOU 2668  CB  ASP A 452    29816  38817  28073   -339   3649  -1655       C  
ATOM   2669  CG  ASP A 452      18.935   4.734  73.088  1.00246.76           C  
ANISOU 2669  CG  ASP A 452    28466  38161  27128   -199   3810  -1721       C  
ATOM   2670  OD1 ASP A 452      18.165   5.218  73.949  1.00243.06           O  
ANISOU 2670  OD1 ASP A 452    27817  37778  26757   -335   3845  -1555       O  
ATOM   2671  OD2 ASP A 452      20.138   5.055  73.007  1.00244.37           O  
ANISOU 2671  OD2 ASP A 452    28072  38018  26761     31   3910  -1922       O  
ATOM   2672  N   THR A 453      16.046   2.515  70.688  1.00275.55           N  
ANISOU 2672  N   THR A 453    33012  40931  30755   -940   3302  -1254       N  
ATOM   2673  CA  THR A 453      15.026   1.847  69.889  1.00285.61           C  
ANISOU 2673  CA  THR A 453    34597  41921  32001  -1253   3112  -1049       C  
ATOM   2674  C   THR A 453      15.626   0.962  68.798  1.00289.36           C  
ANISOU 2674  C   THR A 453    35498  42164  32280  -1236   3075  -1227       C  
ATOM   2675  O   THR A 453      16.690   1.268  68.252  1.00290.61           O  
ANISOU 2675  O   THR A 453    35650  42398  32370  -1072   3215  -1502       O  
ATOM   2676  CB  THR A 453      14.114   2.892  69.243  1.00287.51           C  
ANISOU 2676  CB  THR A 453    34634  42220  32387  -1613   3090   -866       C  
ATOM   2677  OG1 THR A 453      13.211   2.258  68.328  1.00290.69           O  
ANISOU 2677  OG1 THR A 453    35363  42346  32741  -1960   2884   -650       O  
ATOM   2678  CG2 THR A 453      14.941   3.935  68.492  1.00286.90           C  
ANISOU 2678  CG2 THR A 453    34359  42346  32303  -1573   3240  -1122       C  
ATOM   2679  N   PRO A 454      14.950  -0.160  68.467  1.00298.19           N  
ANISOU 2679  N   PRO A 454    37014  42980  33304  -1410   2901  -1066       N  
ATOM   2680  CA  PRO A 454      13.786  -0.690  69.197  1.00288.66           C  
ANISOU 2680  CA  PRO A 454    35841  41666  32170  -1547   2724   -739       C  
ATOM   2681  C   PRO A 454      14.130  -1.272  70.568  1.00274.35           C  
ANISOU 2681  C   PRO A 454    33942  39915  30384  -1218   2752   -756       C  
ATOM   2682  O   PRO A 454      14.983  -2.157  70.680  1.00276.07           O  
ANISOU 2682  O   PRO A 454    34362  40042  30490   -964   2794   -929       O  
ATOM   2683  CB  PRO A 454      13.243  -1.771  68.259  1.00292.31           C  
ANISOU 2683  CB  PRO A 454    36814  41784  32466  -1806   2542   -625       C  
ATOM   2684  CG  PRO A 454      14.417  -2.201  67.470  1.00294.53           C  
ANISOU 2684  CG  PRO A 454    37375  41964  32569  -1647   2679   -957       C  
ATOM   2685  CD  PRO A 454      15.252  -0.966  67.271  1.00295.44           C  
ANISOU 2685  CD  PRO A 454    37140  42355  32760  -1517   2872  -1187       C  
ATOM   2686  N   HIS A 455      13.455  -0.774  71.596  1.00291.79           N  
ANISOU 2686  N   HIS A 455    35849  42262  32755  -1243   2740   -559       N  
ATOM   2687  CA  HIS A 455      13.731  -1.130  72.975  1.00272.49           C  
ANISOU 2687  CA  HIS A 455    33273  39914  30347   -982   2770   -562       C  
ATOM   2688  C   HIS A 455      13.293  -2.549  73.306  1.00272.49           C  
ANISOU 2688  C   HIS A 455    33586  39672  30276   -956   2582   -423       C  
ATOM   2689  O   HIS A 455      13.303  -2.918  74.489  1.00281.04           O  
ANISOU 2689  O   HIS A 455    34565  40814  31403   -793   2564   -370       O  
ATOM   2690  CB  HIS A 455      13.014  -0.168  73.926  1.00257.30           C  
ANISOU 2690  CB  HIS A 455    30982  38167  28614  -1072   2835   -377       C  
ATOM   2691  CG  HIS A 455      13.529   1.237  73.871  1.00243.88           C  
ANISOU 2691  CG  HIS A 455    28937  36739  26989  -1053   3053   -525       C  
ATOM   2692  ND1 HIS A 455      13.374   2.034  72.757  1.00240.19           N  
ANISOU 2692  ND1 HIS A 455    28405  36296  26560  -1254   3091   -542       N  
ATOM   2693  CD2 HIS A 455      14.202   1.987  74.776  1.00239.31           C  
ANISOU 2693  CD2 HIS A 455    28064  36421  26442   -877   3239   -657       C  
ATOM   2694  CE1 HIS A 455      13.910   3.220  72.985  1.00237.27           C  
ANISOU 2694  CE1 HIS A 455    27701  36194  26257  -1179   3296   -684       C  
ATOM   2695  NE2 HIS A 455      14.426   3.216  74.201  1.00237.23           N  
ANISOU 2695  NE2 HIS A 455    27566  36333  26237   -954   3391   -756       N  
ATOM   2696  N   VAL A 456      12.888  -3.359  72.334  1.00259.33           N  
ANISOU 2696  N   VAL A 456    32308  37734  28491  -1130   2438   -355       N  
ATOM   2697  CA  VAL A 456      12.293  -4.656  72.632  1.00246.69           C  
ANISOU 2697  CA  VAL A 456    31005  35900  26827  -1146   2242   -183       C  
ATOM   2698  C   VAL A 456      12.458  -5.580  71.433  1.00235.61           C  
ANISOU 2698  C   VAL A 456    30086  34213  25223  -1252   2181   -259       C  
ATOM   2699  O   VAL A 456      12.407  -5.144  70.277  1.00228.79           O  
ANISOU 2699  O   VAL A 456    29353  33287  24292  -1486   2200   -297       O  
ATOM   2700  CB  VAL A 456      10.800  -4.496  73.000  1.00244.00           C  
ANISOU 2700  CB  VAL A 456    30590  35503  26618  -1415   2060    203       C  
ATOM   2701  CG1 VAL A 456       9.986  -4.221  71.757  1.00241.37           C  
ANISOU 2701  CG1 VAL A 456    30430  35017  26263  -1813   1945    394       C  
ATOM   2702  CG2 VAL A 456      10.278  -5.720  73.748  1.00243.73           C  
ANISOU 2702  CG2 VAL A 456    30744  35308  26554  -1341   1872    371       C  
ATOM   2703  N   CYS A 457      12.765  -6.843  71.715  1.00230.16           N  
ANISOU 2703  N   CYS A 457    29661  33353  24434  -1075   2137   -304       N  
ATOM   2704  CA  CYS A 457      12.608  -7.917  70.746  1.00226.31           C  
ANISOU 2704  CA  CYS A 457    29698  32537  23751  -1226   2054   -297       C  
ATOM   2705  C   CYS A 457      11.584  -8.889  71.317  1.00223.54           C  
ANISOU 2705  C   CYS A 457    29515  32032  23387  -1307   1805    -14       C  
ATOM   2706  O   CYS A 457      11.628  -9.202  72.513  1.00230.53           O  
ANISOU 2706  O   CYS A 457    30190  33024  24377  -1068   1775     27       O  
ATOM   2707  CB  CYS A 457      13.945  -8.617  70.475  1.00227.46           C  
ANISOU 2707  CB  CYS A 457    30043  32579  23803   -934   2269   -607       C  
ATOM   2708  SG  CYS A 457      15.345  -7.487  70.278  1.00225.00           S  
ANISOU 2708  SG  CYS A 457    29405  32517  23567   -695   2571   -929       S  
ATOM   2709  N   TRP A 458      10.664  -9.364  70.480  1.00213.79           N  
ANISOU 2709  N   TRP A 458    28661  30550  22019  -1658   1613    195       N  
ATOM   2710  CA  TRP A 458       9.632 -10.296  70.918  1.00184.16           C  
ANISOU 2710  CA  TRP A 458    25098  26636  18238  -1761   1350    493       C  
ATOM   2711  C   TRP A 458       9.946 -11.680  70.372  1.00171.48           C  
ANISOU 2711  C   TRP A 458    24025  24729  16401  -1742   1340    393       C  
ATOM   2712  O   TRP A 458      10.179 -11.843  69.168  1.00182.82           O  
ANISOU 2712  O   TRP A 458    25845  25970  17647  -1953   1409    288       O  
ATOM   2713  CB  TRP A 458       8.230  -9.856  70.488  1.00180.52           C  
ANISOU 2713  CB  TRP A 458    24667  26109  17815  -2197   1109    891       C  
ATOM   2714  CG  TRP A 458       7.264 -11.008  70.415  1.00178.70           C  
ANISOU 2714  CG  TRP A 458    24825  25615  17456  -2386    826   1184       C  
ATOM   2715  CD1 TRP A 458       6.958 -11.734  69.299  1.00187.77           C  
ANISOU 2715  CD1 TRP A 458    26514  26478  18351  -2704    706   1261       C  
ATOM   2716  CD2 TRP A 458       6.532 -11.609  71.495  1.00169.77           C  
ANISOU 2716  CD2 TRP A 458    23605  24479  16423  -2270    633   1426       C  
ATOM   2717  NE1 TRP A 458       6.062 -12.726  69.608  1.00185.11           N  
ANISOU 2717  NE1 TRP A 458    26422  25965  17945  -2796    439   1552       N  
ATOM   2718  CE2 TRP A 458       5.785 -12.674  70.949  1.00172.20           C  
ANISOU 2718  CE2 TRP A 458    24396  24499  16531  -2519    385   1656       C  
ATOM   2719  CE3 TRP A 458       6.425 -11.342  72.862  1.00166.10           C  
ANISOU 2719  CE3 TRP A 458    22715  24215  16181  -2003    646   1475       C  
ATOM   2720  CZ2 TRP A 458       4.945 -13.472  71.722  1.00165.16           C  
ANISOU 2720  CZ2 TRP A 458    23550  23530  15673  -2478    139   1932       C  
ATOM   2721  CZ3 TRP A 458       5.586 -12.139  73.631  1.00160.65           C  
ANISOU 2721  CZ3 TRP A 458    22077  23437  15526  -1972    411   1741       C  
ATOM   2722  CH2 TRP A 458       4.859 -13.190  73.057  1.00159.45           C  
ANISOU 2722  CH2 TRP A 458    22386  23010  15187  -2194    155   1966       C  
ATOM   2723  N   GLU A 459       9.957 -12.667  71.259  1.00170.88           N  
ANISOU 2723  N   GLU A 459    23975  24608  16342  -1502   1271    424       N  
ATOM   2724  CA  GLU A 459      10.208 -14.048  70.901  1.00168.98           C  
ANISOU 2724  CA  GLU A 459    24210  24081  15913  -1456   1275    350       C  
ATOM   2725  C   GLU A 459       9.023 -14.948  71.235  1.00163.97           C  
ANISOU 2725  C   GLU A 459    23791  23294  15216  -1608    955    677       C  
ATOM   2726  O   GLU A 459       8.300 -14.707  72.208  1.00139.67           O  
ANISOU 2726  O   GLU A 459    20393  20371  12303  -1565    773    904       O  
ATOM   2727  CB  GLU A 459      11.482 -14.563  71.580  1.00141.70           C  
ANISOU 2727  CB  GLU A 459    20610  20685  12544  -1001   1514     73       C  
ATOM   2728  CG  GLU A 459      12.664 -13.644  71.318  1.00152.44           C  
ANISOU 2728  CG  GLU A 459    21727  22209  13984   -832   1814   -214       C  
ATOM   2729  CD  GLU A 459      13.965 -14.178  71.865  1.00169.25           C  
ANISOU 2729  CD  GLU A 459    23733  24362  16211   -414   2057   -438       C  
ATOM   2730  OE1 GLU A 459      13.926 -15.095  72.711  1.00184.35           O  
ANISOU 2730  OE1 GLU A 459    25616  26245  18182   -230   1976   -359       O  
ATOM   2731  OE2 GLU A 459      15.030 -13.678  71.445  1.00169.22           O  
ANISOU 2731  OE2 GLU A 459    23647  24407  16242   -275   2324   -672       O  
ATOM   2732  N   PRO A 460       8.797 -15.987  70.428  1.00154.59           N  
ANISOU 2732  N   PRO A 460    23166  21788  13782  -1800    891    713       N  
ATOM   2733  CA  PRO A 460       7.656 -16.879  70.676  1.00157.80           C  
ANISOU 2733  CA  PRO A 460    23815  22040  14103  -1962    566   1041       C  
ATOM   2734  C   PRO A 460       7.819 -17.752  71.904  1.00169.94           C  
ANISOU 2734  C   PRO A 460    25185  23634  15752  -1585    519   1027       C  
ATOM   2735  O   PRO A 460       6.812 -18.171  72.488  1.00160.51           O  
ANISOU 2735  O   PRO A 460    23977  22426  14583  -1647    226   1325       O  
ATOM   2736  CB  PRO A 460       7.612 -17.734  69.403  1.00155.51           C  
ANISOU 2736  CB  PRO A 460    24213  21388  13485  -2266    579   1014       C  
ATOM   2737  CG  PRO A 460       9.010 -17.759  68.918  1.00156.15           C  
ANISOU 2737  CG  PRO A 460    24389  21414  13528  -2056    976    597       C  
ATOM   2738  CD  PRO A 460       9.602 -16.423  69.273  1.00156.08           C  
ANISOU 2738  CD  PRO A 460    23819  21729  13755  -1875   1133    450       C  
ATOM   2739  N   GLN A 461       9.056 -18.039  72.317  1.00172.38           N  
ANISOU 2739  N   GLN A 461    25350  24004  16141  -1205    793    713       N  
ATOM   2740  CA  GLN A 461       9.277 -18.977  73.412  1.00174.69           C  
ANISOU 2740  CA  GLN A 461    25506  24331  16536   -874    751    706       C  
ATOM   2741  C   GLN A 461       8.750 -18.450  74.742  1.00162.66           C  
ANISOU 2741  C   GLN A 461    23464  23096  15242   -746    566    881       C  
ATOM   2742  O   GLN A 461       8.415 -19.245  75.629  1.00162.21           O  
ANISOU 2742  O   GLN A 461    23344  23048  15242   -597    395    998       O  
ATOM   2743  CB  GLN A 461      10.768 -19.292  73.523  1.00184.04           C  
ANISOU 2743  CB  GLN A 461    26607  25521  17801   -523   1104    375       C  
ATOM   2744  CG  GLN A 461      11.091 -20.470  74.418  1.00188.27           C  
ANISOU 2744  CG  GLN A 461    27086  26021  18425   -221   1089    370       C  
ATOM   2745  CD  GLN A 461      10.668 -21.787  73.795  1.00197.68           C  
ANISOU 2745  CD  GLN A 461    28849  26863  19399   -351   1022    436       C  
ATOM   2746  OE1 GLN A 461       9.581 -22.295  74.069  1.00198.91           O  
ANISOU 2746  OE1 GLN A 461    29134  26966  19475   -490    701    687       O  
ATOM   2747  NE2 GLN A 461      11.526 -22.343  72.946  1.00203.55           N  
ANISOU 2747  NE2 GLN A 461    29952  27346  20041   -312   1338    220       N  
ATOM   2748  N   ALA A 462       8.664 -17.132  74.903  1.00167.97           N  
ANISOU 2748  N   ALA A 462    23778  23996  16047   -811    609    900       N  
ATOM   2749  CA  ALA A 462       8.145 -16.533  76.125  1.00152.73           C  
ANISOU 2749  CA  ALA A 462    21389  22313  14329   -729    485   1063       C  
ATOM   2750  C   ALA A 462       6.623 -16.463  76.141  1.00155.20           C  
ANISOU 2750  C   ALA A 462    21780  22544  14646  -1016    175   1457       C  
ATOM   2751  O   ALA A 462       6.060 -15.694  76.923  1.00150.02           O  
ANISOU 2751  O   ALA A 462    20766  22057  14177  -1029    116   1623       O  
ATOM   2752  CB  ALA A 462       8.735 -15.134  76.321  1.00148.43           C  
ANISOU 2752  CB  ALA A 462    20431  22033  13931   -675    704    915       C  
ATOM   2753  N   GLN A 463       5.955 -17.258  75.308  1.00164.47           N  
ANISOU 2753  N   GLN A 463    23423  23447  15621  -1255    -11   1628       N  
ATOM   2754  CA  GLN A 463       4.501 -17.255  75.204  1.00164.46           C  
ANISOU 2754  CA  GLN A 463    23531  23338  15617  -1560   -327   2058       C  
ATOM   2755  C   GLN A 463       3.801 -17.599  76.516  1.00166.74           C  
ANISOU 2755  C   GLN A 463    23570  23710  16072  -1396   -535   2278       C  
ATOM   2756  O   GLN A 463       3.083 -16.761  77.071  1.00157.78           O  
ANISOU 2756  O   GLN A 463    22116  22691  15141  -1469   -595   2510       O  
ATOM   2757  CB  GLN A 463       4.075 -18.237  74.110  1.00157.41           C  
ANISOU 2757  CB  GLN A 463    23244  22129  14434  -1835   -489   2178       C  
ATOM   2758  CG  GLN A 463       2.607 -18.600  74.105  1.00140.33           C  
ANISOU 2758  CG  GLN A 463    21253  19823  12242  -2114   -869   2660       C  
ATOM   2759  CD  GLN A 463       2.287 -19.629  73.044  1.00142.10           C  
ANISOU 2759  CD  GLN A 463    22118  19735  12137  -2400  -1020   2759       C  
ATOM   2760  OE1 GLN A 463       1.153 -20.102  72.945  1.00143.99           O  
ANISOU 2760  OE1 GLN A 463    22689  19848  12172  -2407   -807   2454       O  
ATOM   2761  NE2 GLN A 463       3.280 -19.974  72.235  1.00145.05           N  
ANISOU 2761  NE2 GLN A 463    22689  19969  12455  -2646  -1378   3199       N  
ATOM   2762  N   GLY A 464       3.989 -18.822  77.012  1.00167.14           N  
ANISOU 2762  N   GLY A 464    23765  23691  16051  -1182   -630   2215       N  
ATOM   2763  CA  GLY A 464       3.309 -19.287  78.210  1.00172.90           C  
ANISOU 2763  CA  GLY A 464    24301  24479  16913  -1037   -855   2421       C  
ATOM   2764  C   GLY A 464       3.491 -18.445  79.459  1.00175.64           C  
ANISOU 2764  C   GLY A 464    24112  25101  17524   -841   -746   2373       C  
ATOM   2765  O   GLY A 464       2.515 -17.993  80.066  1.00179.31           O  
ANISOU 2765  O   GLY A 464    24382  25602  18148   -927   -885   2664       O  
ATOM   2766  N   ARG A 465       4.753 -18.259  79.855  1.00181.88           N  
ANISOU 2766  N   ARG A 465    24679  26067  18360   -589   -485   2020       N  
ATOM   2767  CA  ARG A 465       5.084 -17.502  81.061  1.00165.42           C  
ANISOU 2767  CA  ARG A 465    22119  24248  16484   -423   -362   1941       C  
ATOM   2768  C   ARG A 465       4.486 -16.098  81.030  1.00156.10           C  
ANISOU 2768  C   ARG A 465    20712  23154  15443   -626   -278   2095       C  
ATOM   2769  O   ARG A 465       3.905 -15.640  82.020  1.00167.00           O  
ANISOU 2769  O   ARG A 465    21822  24633  16997   -619   -312   2255       O  
ATOM   2770  CB  ARG A 465       6.599 -17.458  81.238  1.00167.09           C  
ANISOU 2770  CB  ARG A 465    22171  24616  16700   -181    -92   1571       C  
ATOM   2771  CG  ARG A 465       7.313 -18.424  80.318  1.00179.26           C  
ANISOU 2771  CG  ARG A 465    24067  25973  18069   -112    -26   1394       C  
ATOM   2772  CD  ARG A 465       8.538 -19.044  80.968  1.00186.47           C  
ANISOU 2772  CD  ARG A 465    24816  26988  19048    200    117   1162       C  
ATOM   2773  NE  ARG A 465       9.340 -19.760  79.977  1.00189.57           N  
ANISOU 2773  NE  ARG A 465    25533  27184  19313    263    283    977       N  
ATOM   2774  CZ  ARG A 465       9.181 -21.041  79.652  1.00189.16           C  
ANISOU 2774  CZ  ARG A 465    25825  26898  19149    292    187   1014       C  
ATOM   2775  NH1 ARG A 465       8.251 -21.774  80.248  1.00194.18           N  
ANISOU 2775  NH1 ARG A 465    26510  27490  19781    279   -110   1232       N  
ATOM   2776  NH2 ARG A 465       9.956 -21.591  78.726  1.00185.68           N  
ANISOU 2776  NH2 ARG A 465    25692  26255  18603    335    406    833       N  
ATOM   2777  N   MET A 466       4.618 -15.398  79.896  1.00152.19           N  
ANISOU 2777  N   MET A 466    20327  22613  14883   -817   -150   2052       N  
ATOM   2778  CA  MET A 466       4.139 -14.020  79.801  1.00158.81           C  
ANISOU 2778  CA  MET A 466    20922  23540  15878  -1008    -35   2188       C  
ATOM   2779  C   MET A 466       2.654 -13.926  80.118  1.00172.91           C  
ANISOU 2779  C   MET A 466    22683  25209  17806  -1201   -253   2638       C  
ATOM   2780  O   MET A 466       2.223 -13.034  80.857  1.00180.38           O  
ANISOU 2780  O   MET A 466    23307  26258  18970  -1224   -151   2768       O  
ATOM   2781  CB  MET A 466       4.430 -13.456  78.411  1.00168.58           C  
ANISOU 2781  CB  MET A 466    22326  24718  17009  -1215     83   2104       C  
ATOM   2782  CG  MET A 466       5.838 -12.907  78.241  1.00172.43           C  
ANISOU 2782  CG  MET A 466    22667  25384  17463  -1041    388   1694       C  
ATOM   2783  SD  MET A 466       6.013 -11.288  79.021  1.00171.23           S  
ANISOU 2783  SD  MET A 466    21992  25521  17544  -1015    642   1645       S  
ATOM   2784  CE  MET A 466       4.815 -10.329  78.093  1.00169.25           C  
ANISOU 2784  CE  MET A 466    21749  25160  17396  -1416    594   1991       C  
ATOM   2785  N   CYS A 467       1.852 -14.821  79.544  1.00173.76           N  
ANISOU 2785  N   CYS A 467    23140  25084  17797  -1354   -537   2899       N  
ATOM   2786  CA  CYS A 467       0.425 -14.818  79.840  1.00170.81           C  
ANISOU 2786  CA  CYS A 467    22749  24579  17571  -1530   -769   3377       C  
ATOM   2787  C   CYS A 467       0.185 -15.006  81.332  1.00174.62           C  
ANISOU 2787  C   CYS A 467    22969  25158  18221  -1300   -799   3419       C  
ATOM   2788  O   CYS A 467      -0.670 -14.336  81.923  1.00179.36           O  
ANISOU 2788  O   CYS A 467    23338  25752  19061  -1382   -782   3706       O  
ATOM   2789  CB  CYS A 467      -0.277 -15.913  79.038  1.00159.68           C  
ANISOU 2789  CB  CYS A 467    21795  22913  15965  -1714  -1097   3634       C  
ATOM   2790  SG  CYS A 467      -0.070 -15.767  77.249  1.00151.41           S  
ANISOU 2790  SG  CYS A 467    21133  21717  14681  -2062  -1080   3610       S  
ATOM   2791  N   ALA A 468       0.926 -15.927  81.956  1.00168.81           N  
ANISOU 2791  N   ALA A 468    22267  24497  17377  -1024   -832   3150       N  
ATOM   2792  CA  ALA A 468       0.813 -16.123  83.398  1.00168.36           C  
ANISOU 2792  CA  ALA A 468    21959  24551  17460   -822   -862   3156       C  
ATOM   2793  C   ALA A 468       1.219 -14.869  84.163  1.00167.65           C  
ANISOU 2793  C   ALA A 468    21477  24672  17551   -785   -551   3018       C  
ATOM   2794  O   ALA A 468       0.590 -14.520  85.168  1.00174.27           O  
ANISOU 2794  O   ALA A 468    22108  25533  18575   -782   -538   3191       O  
ATOM   2795  CB  ALA A 468       1.653 -17.323  83.835  1.00174.22           C  
ANISOU 2795  CB  ALA A 468    22787  25349  18061   -557   -943   2889       C  
ATOM   2796  N   LEU A 469       2.282 -14.190  83.719  1.00171.77           N  
ANISOU 2796  N   LEU A 469    21911  25340  18015   -760   -288   2705       N  
ATOM   2797  CA  LEU A 469       2.659 -12.921  84.336  1.00164.87           C  
ANISOU 2797  CA  LEU A 469    20694  24662  17288   -761     16   2584       C  
ATOM   2798  C   LEU A 469       1.514 -11.920  84.267  1.00165.38           C  
ANISOU 2798  C   LEU A 469    20637  24633  17569   -995     86   2928       C  
ATOM   2799  O   LEU A 469       1.187 -11.262  85.262  1.00164.18           O  
ANISOU 2799  O   LEU A 469    20240  24543  17598   -998    237   3006       O  
ATOM   2800  CB  LEU A 469       3.897 -12.343  83.654  1.00164.08           C  
ANISOU 2800  CB  LEU A 469    20551  24710  17083   -719    259   2237       C  
ATOM   2801  CG  LEU A 469       4.210 -10.924  84.128  1.00163.23           C  
ANISOU 2801  CG  LEU A 469    20114  24795  17111   -763    575   2139       C  
ATOM   2802  CD1 LEU A 469       4.545 -10.934  85.610  1.00168.83           C  
ANISOU 2802  CD1 LEU A 469    20605  25665  17877   -624    644   2043       C  
ATOM   2803  CD2 LEU A 469       5.333 -10.315  83.319  1.00157.09           C  
ANISOU 2803  CD2 LEU A 469    19305  24149  16234   -737    788   1836       C  
ATOM   2804  N   TYR A 470       0.916 -11.773  83.083  1.00170.03           N  
ANISOU 2804  N   TYR A 470    21395  25060  18149  -1214     -2   3149       N  
ATOM   2805  CA  TYR A 470      -0.264 -10.929  82.935  1.00177.22           C  
ANISOU 2805  CA  TYR A 470    22186  25844  19305  -1459     35   3561       C  
ATOM   2806  C   TYR A 470      -1.379 -11.380  83.868  1.00184.81           C  
ANISOU 2806  C   TYR A 470    23120  26665  20433  -1445   -135   3917       C  
ATOM   2807  O   TYR A 470      -2.009 -10.561  84.547  1.00189.24           O  
ANISOU 2807  O   TYR A 470    23441  27204  21259  -1510     44   4125       O  
ATOM   2808  CB  TYR A 470      -0.741 -10.952  81.482  1.00177.25           C  
ANISOU 2808  CB  TYR A 470    22421  25681  19245  -1729   -115   3788       C  
ATOM   2809  CG  TYR A 470      -2.072 -10.266  81.261  1.00177.57           C  
ANISOU 2809  CG  TYR A 470    22350  25553  19565  -2011   -140   4315       C  
ATOM   2810  CD1 TYR A 470      -2.146  -8.890  81.100  1.00182.72           C  
ANISOU 2810  CD1 TYR A 470    22710  26273  20444  -2154    159   4376       C  
ATOM   2811  CD2 TYR A 470      -3.256 -10.996  81.222  1.00181.69           C  
ANISOU 2811  CD2 TYR A 470    23045  25843  20146  -2134   -458   4780       C  
ATOM   2812  CE1 TYR A 470      -3.361  -8.260  80.899  1.00190.70           C  
ANISOU 2812  CE1 TYR A 470    23585  27112  21760  -2416    162   4900       C  
ATOM   2813  CE2 TYR A 470      -4.475 -10.374  81.025  1.00188.97           C  
ANISOU 2813  CE2 TYR A 470    23842  26594  21364  -2397   -478   5320       C  
ATOM   2814  CZ  TYR A 470      -4.522  -9.007  80.863  1.00196.79           C  
ANISOU 2814  CZ  TYR A 470    24523  27644  22605  -2538   -157   5385       C  
ATOM   2815  OH  TYR A 470      -5.735  -8.389  80.665  1.00206.29           O  
ANISOU 2815  OH  TYR A 470    25571  28659  24150  -2805   -154   5962       O  
ATOM   2816  N   ALA A 471      -1.642 -12.689  83.902  1.00179.33           N  
ANISOU 2816  N   ALA A 471    22682  25861  19594  -1362   -466   3997       N  
ATOM   2817  CA  ALA A 471      -2.715 -13.217  84.737  1.00166.37           C  
ANISOU 2817  CA  ALA A 471    21037  24079  18098  -1336   -669   4346       C  
ATOM   2818  C   ALA A 471      -2.478 -12.901  86.208  1.00173.96           C  
ANISOU 2818  C   ALA A 471    21727  25179  19190  -1161   -474   4191       C  
ATOM   2819  O   ALA A 471      -3.381 -12.415  86.899  1.00161.36           O  
ANISOU 2819  O   ALA A 471    19975  23484  17849  -1227   -394   4490       O  
ATOM   2820  CB  ALA A 471      -2.851 -14.724  84.520  1.00149.17           C  
ANISOU 2820  CB  ALA A 471    19185  21793  15700  -1249  -1052   4387       C  
ATOM   2821  N   SER A 472      -1.274 -13.188  86.711  1.00184.58           N  
ANISOU 2821  N   SER A 472    23024  26739  20370   -956   -390   3749       N  
ATOM   2822  CA  SER A 472      -0.952 -12.868  88.100  1.00183.71           C  
ANISOU 2822  CA  SER A 472    22676  26777  20348   -842   -209   3591       C  
ATOM   2823  C   SER A 472      -1.206 -11.394  88.398  1.00193.76           C  
ANISOU 2823  C   SER A 472    23706  28073  21842   -991    165   3665       C  
ATOM   2824  O   SER A 472      -1.865 -11.054  89.386  1.00198.74           O  
ANISOU 2824  O   SER A 472    24209  28639  22664  -1022    275   3840       O  
ATOM   2825  CB  SER A 472       0.502 -13.239  88.408  1.00174.21           C  
ANISOU 2825  CB  SER A 472    21435  25814  18942   -653   -153   3133       C  
ATOM   2826  OG  SER A 472       0.732 -14.625  88.222  1.00169.11           O  
ANISOU 2826  OG  SER A 472    20994  25131  18128   -505   -459   3075       O  
ATOM   2827  N   LEU A 473      -0.696 -10.507  87.539  1.00198.14           N  
ANISOU 2827  N   LEU A 473    24202  28705  22378  -1089    381   3534       N  
ATOM   2828  CA  LEU A 473      -0.887  -9.070  87.726  1.00187.96           C  
ANISOU 2828  CA  LEU A 473    22676  27442  21299  -1234    762   3593       C  
ATOM   2829  C   LEU A 473      -2.365  -8.700  87.748  1.00191.45           C  
ANISOU 2829  C   LEU A 473    23073  27622  22049  -1409    775   4107       C  
ATOM   2830  O   LEU A 473      -2.814  -7.941  88.615  1.00196.44           O  
ANISOU 2830  O   LEU A 473    23527  28208  22906  -1465   1053   4225       O  
ATOM   2831  CB  LEU A 473      -0.147  -8.304  86.627  1.00179.11           C  
ANISOU 2831  CB  LEU A 473    21516  26438  20100  -1309    931   3393       C  
ATOM   2832  CG  LEU A 473       1.372  -8.261  86.791  1.00174.69           C  
ANISOU 2832  CG  LEU A 473    20910  26150  19313  -1147   1052   2901       C  
ATOM   2833  CD1 LEU A 473       2.018  -7.397  85.726  1.00177.88           C  
ANISOU 2833  CD1 LEU A 473    21258  26658  19671  -1223   1238   2729       C  
ATOM   2834  CD2 LEU A 473       1.699  -7.720  88.169  1.00175.27           C  
ANISOU 2834  CD2 LEU A 473    20788  26367  19441  -1106   1300   2760       C  
ATOM   2835  N   ALA A 474      -3.133  -9.213  86.787  1.00192.38           N  
ANISOU 2835  N   ALA A 474    23358  27549  22188  -1516    492   4439       N  
ATOM   2836  CA  ALA A 474      -4.544  -8.855  86.705  1.00195.93           C  
ANISOU 2836  CA  ALA A 474    23747  27735  22961  -1703    487   4997       C  
ATOM   2837  C   ALA A 474      -5.316  -9.324  87.930  1.00197.31           C  
ANISOU 2837  C   ALA A 474    23904  27778  23286  -1608    424   5213       C  
ATOM   2838  O   ALA A 474      -6.317  -8.703  88.308  1.00196.69           O  
ANISOU 2838  O   ALA A 474    23683  27507  23544  -1724    600   5606       O  
ATOM   2839  CB  ALA A 474      -5.159  -9.438  85.434  1.00199.02           C  
ANISOU 2839  CB  ALA A 474    24360  27959  23300  -1865    138   5328       C  
ATOM   2840  N   LEU A 475      -4.876 -10.417  88.554  1.00203.80           N  
ANISOU 2840  N   LEU A 475    24861  28689  23883  -1402    185   4979       N  
ATOM   2841  CA  LEU A 475      -5.546 -10.923  89.747  1.00206.08           C  
ANISOU 2841  CA  LEU A 475    25138  28871  24292  -1306    102   5149       C  
ATOM   2842  C   LEU A 475      -5.179 -10.126  90.994  1.00218.25           C  
ANISOU 2842  C   LEU A 475    26477  30517  25931  -1278    497   4929       C  
ATOM   2843  O   LEU A 475      -6.044  -9.849  91.832  1.00217.53           O  
ANISOU 2843  O   LEU A 475    26308  30251  26093  -1319    637   5200       O  
ATOM   2844  CB  LEU A 475      -5.199 -12.395  89.960  1.00187.46           C  
ANISOU 2844  CB  LEU A 475    22980  26580  21666  -1110   -304   4983       C  
ATOM   2845  CG  LEU A 475      -5.803 -13.429  89.014  1.00169.43           C  
ANISOU 2845  CG  LEU A 475    20958  24138  19282  -1137   -738   5266       C  
ATOM   2846  CD1 LEU A 475      -5.401 -14.828  89.453  1.00162.18           C  
ANISOU 2846  CD1 LEU A 475    20200  23299  18124   -918  -1068   5062       C  
ATOM   2847  CD2 LEU A 475      -7.313 -13.289  88.967  1.00165.11           C  
ANISOU 2847  CD2 LEU A 475    20405  23297  19033  -1284   -834   5881       C  
ATOM   2848  N   LEU A 476      -3.904  -9.744  91.129  1.00206.63           N  
ANISOU 2848  N   LEU A 476    24937  29313  24259  -1225    690   4454       N  
ATOM   2849  CA  LEU A 476      -3.473  -9.033  92.328  1.00205.00           C  
ANISOU 2849  CA  LEU A 476    24581  29221  24089  -1236   1046   4231       C  
ATOM   2850  C   LEU A 476      -4.071  -7.634  92.371  1.00209.33           C  
ANISOU 2850  C   LEU A 476    24965  29634  24938  -1426   1496   4444       C  
ATOM   2851  O   LEU A 476      -4.532  -7.179  93.425  1.00211.57           O  
ANISOU 2851  O   LEU A 476    25179  29811  25395  -1485   1765   4538       O  
ATOM   2852  CB  LEU A 476      -1.947  -8.949  92.377  1.00201.49           C  
ANISOU 2852  CB  LEU A 476    24102  29095  23358  -1157   1122   3720       C  
ATOM   2853  CG  LEU A 476      -1.093 -10.216  92.242  1.00198.60           C  
ANISOU 2853  CG  LEU A 476    23861  28888  22709   -967    756   3464       C  
ATOM   2854  CD1 LEU A 476       0.395  -9.881  92.332  1.00201.04           C  
ANISOU 2854  CD1 LEU A 476    24086  29492  22809   -917    917   3023       C  
ATOM   2855  CD2 LEU A 476      -1.481 -11.300  93.236  1.00196.84           C  
ANISOU 2855  CD2 LEU A 476    23705  28614  22472   -860    485   3543       C  
ATOM   2856  N   SER A 477      -4.065  -6.933  91.232  1.00216.21           N  
ANISOU 2856  N   SER A 477    25772  30496  25881  -1536   1604   4523       N  
ATOM   2857  CA  SER A 477      -4.663  -5.603  91.163  1.00201.96           C  
ANISOU 2857  CA  SER A 477    23782  28553  24401  -1722   2037   4762       C  
ATOM   2858  C   SER A 477      -6.131  -5.643  91.554  1.00195.14           C  
ANISOU 2858  C   SER A 477    22898  27345  23901  -1798   2060   5307       C  
ATOM   2859  O   SER A 477      -6.649  -4.677  92.132  1.00185.06           O  
ANISOU 2859  O   SER A 477    21478  25918  22919  -1912   2495   5479       O  
ATOM   2860  CB  SER A 477      -4.483  -5.029  89.761  1.00193.85           C  
ANISOU 2860  CB  SER A 477    22691  27569  23393  -1833   2056   4802       C  
ATOM   2861  OG  SER A 477      -5.103  -5.845  88.784  1.00191.97           O  
ANISOU 2861  OG  SER A 477    22596  27190  23154  -1862   1643   5114       O  
ATOM   2862  N   GLY A 478      -6.816  -6.746  91.236  1.00208.63           N  
ANISOU 2862  N   GLY A 478    24757  28911  25604  -1739   1612   5599       N  
ATOM   2863  CA  GLY A 478      -8.216  -6.869  91.597  1.00206.75           C  
ANISOU 2863  CA  GLY A 478    24502  28338  25714  -1795   1592   6154       C  
ATOM   2864  C   GLY A 478      -8.461  -6.840  93.092  1.00200.30           C  
ANISOU 2864  C   GLY A 478    23668  27438  24998  -1731   1817   6114       C  
ATOM   2865  O   GLY A 478      -9.462  -6.280  93.544  1.00199.81           O  
ANISOU 2865  O   GLY A 478    23508  27093  25316  -1824   2099   6511       O  
ATOM   2866  N   LEU A 479      -7.567  -7.428  93.884  1.00210.00           N  
ANISOU 2866  N   LEU A 479    24988  28893  25908  -1591   1712   5659       N  
ATOM   2867  CA  LEU A 479      -7.784  -7.368  95.325  1.00201.45           C  
ANISOU 2867  CA  LEU A 479    23906  27733  24903  -1578   1931   5614       C  
ATOM   2868  C   LEU A 479      -7.192  -6.119  95.958  1.00200.78           C  
ANISOU 2868  C   LEU A 479    23713  27735  24838  -1709   2501   5335       C  
ATOM   2869  O   LEU A 479      -7.463  -5.851  97.133  1.00197.79           O  
ANISOU 2869  O   LEU A 479    23350  27242  24557  -1764   2784   5333       O  
ATOM   2870  CB  LEU A 479      -7.202  -8.593  96.036  1.00195.11           C  
ANISOU 2870  CB  LEU A 479    23238  27112  23781  -1406   1553   5312       C  
ATOM   2871  CG  LEU A 479      -7.593 -10.001  95.632  1.00191.99           C  
ANISOU 2871  CG  LEU A 479    22983  26679  23286  -1249    972   5484       C  
ATOM   2872  CD1 LEU A 479      -7.307 -10.906  96.789  1.00193.53           C  
ANISOU 2872  CD1 LEU A 479    23248  26976  23311  -1123    772   5269       C  
ATOM   2873  CD2 LEU A 479      -9.029 -10.048  95.251  1.00190.90           C  
ANISOU 2873  CD2 LEU A 479    22852  26196  23486  -1300    886   6090       C  
ATOM   2874  N   SER A 480      -6.349  -5.386  95.240  1.00202.04           N  
ANISOU 2874  N   SER A 480    23787  28099  24879  -1767   2669   5079       N  
ATOM   2875  CA  SER A 480      -5.820  -4.126  95.783  1.00200.97           C  
ANISOU 2875  CA  SER A 480    23554  28040  24763  -1910   3226   4839       C  
ATOM   2876  C   SER A 480      -6.656  -2.947  95.283  1.00207.93           C  
ANISOU 2876  C   SER A 480    24272  28673  26057  -2072   3652   5212       C  
ATOM   2877  O   SER A 480      -7.528  -2.440  95.991  1.00214.49           O  
ANISOU 2877  O   SER A 480    25071  29218  27209  -2169   4016   5497       O  
ATOM   2878  CB  SER A 480      -4.345  -3.923  95.419  1.00193.84           C  
ANISOU 2878  CB  SER A 480    22634  27518  23498  -1879   3204   4332       C  
ATOM   2879  OG  SER A 480      -3.778  -2.859  96.174  1.00189.64           O  
ANISOU 2879  OG  SER A 480    22052  27079  22922  -2020   3695   4077       O  
TER    2880      SER A 480                                                      
ATOM   2881  N   SER B   3      18.969 -35.639  42.898  1.00208.21           N  
ANISOU 2881  N   SER B   3    28212  26321  24577   5555  -3745    -92       N  
ATOM   2882  CA  SER B   3      18.170 -34.987  43.931  1.00206.96           C  
ANISOU 2882  CA  SER B   3    27541  26367  24726   4913  -3426     23       C  
ATOM   2883  C   SER B   3      18.960 -34.889  45.229  1.00218.69           C  
ANISOU 2883  C   SER B   3    28681  28217  26194   4568  -3083    -26       C  
ATOM   2884  O   SER B   3      18.419 -34.512  46.269  1.00209.77           O  
ANISOU 2884  O   SER B   3    27142  27269  25292   4003  -2861     71       O  
ATOM   2885  CB  SER B   3      16.858 -35.749  44.154  1.00199.97           C  
ANISOU 2885  CB  SER B   3    26752  25205  24024   4543  -4050    242       C  
ATOM   2886  OG  SER B   3      15.925 -34.965  44.880  1.00193.31           O  
ANISOU 2886  OG  SER B   3    25437  24517  23494   4001  -3712    371       O  
ATOM   2887  N   ALA B   4      20.249 -35.232  45.155  1.00219.57           N  
ANISOU 2887  N   ALA B   4    28964  28435  26030   4917  -3040   -170       N  
ATOM   2888  CA  ALA B   4      21.087 -35.235  46.350  1.00222.36           C  
ANISOU 2888  CA  ALA B   4    29023  29130  26334   4621  -2757   -216       C  
ATOM   2889  C   ALA B   4      21.170 -33.854  46.994  1.00222.57           C  
ANISOU 2889  C   ALA B   4    28499  29535  26533   4298  -1946   -266       C  
ATOM   2890  O   ALA B   4      21.033 -33.726  48.216  1.00223.36           O  
ANISOU 2890  O   ALA B   4    28236  29858  26773   3758  -1769   -205       O  
ATOM   2891  CB  ALA B   4      22.485 -35.751  46.008  1.00223.94           C  
ANISOU 2891  CB  ALA B   4    29512  29382  26194   5117  -2811   -357       C  
ATOM   2892  N   PHE B   5      21.417 -32.807  46.194  1.00247.21           N  
ANISOU 2892  N   PHE B   5    31555  32734  29641   4625  -1438   -379       N  
ATOM   2893  CA  PHE B   5      21.464 -31.459  46.763  1.00206.95           C  
ANISOU 2893  CA  PHE B   5    25950  27980  24703   4323   -655   -426       C  
ATOM   2894  C   PHE B   5      20.155 -31.110  47.456  1.00199.43           C  
ANISOU 2894  C   PHE B   5    24683  27017  24073   3733   -612   -257       C  
ATOM   2895  O   PHE B   5      20.148 -30.361  48.438  1.00200.06           O  
ANISOU 2895  O   PHE B   5    24326  27393  24294   3287   -106   -250       O  
ATOM   2896  CB  PHE B   5      21.787 -30.421  45.693  1.00181.13           C  
ANISOU 2896  CB  PHE B   5    22690  24747  21383   4780   -163   -559       C  
ATOM   2897  CG  PHE B   5      21.862 -29.018  46.227  1.00154.82           C  
ANISOU 2897  CG  PHE B   5    18863  21761  18201   4492    655   -615       C  
ATOM   2898  CD1 PHE B   5      22.904 -28.644  47.062  1.00151.00           C  
ANISOU 2898  CD1 PHE B   5    18109  21641  17623   4337   1109   -716       C  
ATOM   2899  CD2 PHE B   5      20.900 -28.082  45.908  1.00138.59           C  
ANISOU 2899  CD2 PHE B   5    16616  19669  16373   4369    970   -560       C  
ATOM   2900  CE1 PHE B   5      22.987 -27.357  47.563  1.00142.35           C  
ANISOU 2900  CE1 PHE B   5    16576  20857  16655   4062   1860   -769       C  
ATOM   2901  CE2 PHE B   5      20.981 -26.796  46.401  1.00125.91           C  
ANISOU 2901  CE2 PHE B   5    14575  18373  14894   4109   1731   -611       C  
ATOM   2902  CZ  PHE B   5      22.023 -26.432  47.232  1.00125.00           C  
ANISOU 2902  CZ  PHE B   5    14207  18610  14680   3950   2174   -719       C  
ATOM   2903  N   GLU B   6      19.039 -31.616  46.934  1.00196.25           N  
ANISOU 2903  N   GLU B   6    24502  26277  23788   3731  -1128   -114       N  
ATOM   2904  CA  GLU B   6      17.767 -31.491  47.633  1.00193.45           C  
ANISOU 2904  CA  GLU B   6    23884  25888  23731   3165  -1196     81       C  
ATOM   2905  C   GLU B   6      17.784 -32.322  48.909  1.00204.43           C  
ANISOU 2905  C   GLU B   6    25166  27356  25153   2695  -1497    172       C  
ATOM   2906  O   GLU B   6      17.494 -31.817  49.999  1.00204.82           O  
ANISOU 2906  O   GLU B   6    24801  27637  25386   2173  -1150    238       O  
ATOM   2907  CB  GLU B   6      16.612 -31.911  46.725  1.00184.20           C  
ANISOU 2907  CB  GLU B   6    23000  24331  22658   3298  -1721    222       C  
ATOM   2908  CG  GLU B   6      16.099 -30.798  45.837  1.00173.54           C  
ANISOU 2908  CG  GLU B   6    21557  22958  21421   3495  -1300    208       C  
ATOM   2909  CD  GLU B   6      15.435 -29.692  46.632  1.00160.51           C  
ANISOU 2909  CD  GLU B   6    19391  21549  20047   2990   -710    296       C  
ATOM   2910  OE1 GLU B   6      16.125 -28.703  46.970  1.00154.79           O  
ANISOU 2910  OE1 GLU B   6    18370  21139  19306   2960    -14    165       O  
ATOM   2911  OE2 GLU B   6      14.230 -29.822  46.933  1.00154.09           O  
ANISOU 2911  OE2 GLU B   6    18474  20610  19462   2618   -944    504       O  
ATOM   2912  N   ARG B   7      18.110 -33.611  48.774  1.00194.15           N  
ANISOU 2912  N   ARG B   7    24247  25852  23668   2883  -2150    180       N  
ATOM   2913  CA  ARG B   7      18.087 -34.555  49.888  1.00208.16           C  
ANISOU 2913  CA  ARG B   7    25978  27653  25459   2480  -2530    274       C  
ATOM   2914  C   ARG B   7      18.772 -33.984  51.127  1.00230.04           C  
ANISOU 2914  C   ARG B   7    28309  30838  28256   2104  -1969    211       C  
ATOM   2915  O   ARG B   7      18.226 -34.034  52.236  1.00227.60           O  
ANISOU 2915  O   ARG B   7    27708  30633  28138   1550  -1963    334       O  
ATOM   2916  CB  ARG B   7      18.788 -35.843  49.459  1.00196.25           C  
ANISOU 2916  CB  ARG B   7    24955  25943  23668   2872  -3139    222       C  
ATOM   2917  CG  ARG B   7      19.011 -36.854  50.574  1.00185.54           C  
ANISOU 2917  CG  ARG B   7    23581  24640  22275   2531  -3504    287       C  
ATOM   2918  CD  ARG B   7      17.691 -37.491  51.003  1.00180.99           C  
ANISOU 2918  CD  ARG B   7    23005  23834  21928   2099  -4027    507       C  
ATOM   2919  NE  ARG B   7      17.260 -38.430  49.970  1.00177.45           N  
ANISOU 2919  NE  ARG B   7    23076  22969  21378   2452  -4721    561       N  
ATOM   2920  CZ  ARG B   7      16.265 -39.299  50.096  1.00170.86           C  
ANISOU 2920  CZ  ARG B   7    22401  21858  20660   2214  -5350    742       C  
ATOM   2921  NH1 ARG B   7      15.572 -39.363  51.223  1.00168.30           N  
ANISOU 2921  NH1 ARG B   7    21748  21630  20570   1622  -5378    893       N  
ATOM   2922  NH2 ARG B   7      15.971 -40.108  49.087  1.00171.46           N  
ANISOU 2922  NH2 ARG B   7    22975  21558  20615   2571  -5953    773       N  
ATOM   2923  N   VAL B   8      19.983 -33.446  50.956  1.00207.14           N  
ANISOU 2923  N   VAL B   8    25362  28179  25162   2400  -1499     24       N  
ATOM   2924  CA  VAL B   8      20.729 -32.926  52.098  1.00204.19           C  
ANISOU 2924  CA  VAL B   8    24592  28205  24784   2064   -974    -44       C  
ATOM   2925  C   VAL B   8      19.993 -31.745  52.722  1.00203.84           C  
ANISOU 2925  C   VAL B   8    24081  28350  25020   1591   -401     19       C  
ATOM   2926  O   VAL B   8      19.713 -31.735  53.925  1.00208.63           O  
ANISOU 2926  O   VAL B   8    24381  29118  25770   1050   -308    106       O  
ATOM   2927  CB  VAL B   8      22.170 -32.567  51.684  1.00203.25           C  
ANISOU 2927  CB  VAL B   8    24534  28298  24394   2509   -592   -248       C  
ATOM   2928  CG1 VAL B   8      22.966 -33.838  51.436  1.00205.18           C  
ANISOU 2928  CG1 VAL B   8    25183  28413  24362   2860  -1148   -283       C  
ATOM   2929  CG2 VAL B   8      22.193 -31.696  50.438  1.00204.14           C  
ANISOU 2929  CG2 VAL B   8    24743  28340  24479   2971   -265   -345       C  
ATOM   2930  N   VAL B   9      19.658 -30.740  51.908  1.00215.71           N  
ANISOU 2930  N   VAL B   9    25531  29829  26600   1794     -8    -20       N  
ATOM   2931  CA  VAL B   9      18.948 -29.569  52.417  1.00178.53           C  
ANISOU 2931  CA  VAL B   9    20399  25288  22146   1382    564     43       C  
ATOM   2932  C   VAL B   9      17.597 -29.967  53.000  1.00167.56           C  
ANISOU 2932  C   VAL B   9    18912  23733  21019    906    204    275       C  
ATOM   2933  O   VAL B   9      17.147 -29.398  54.002  1.00164.03           O  
ANISOU 2933  O   VAL B   9    18083  23474  20768    392    556    361       O  
ATOM   2934  CB  VAL B   9      18.808 -28.505  51.314  1.00166.60           C  
ANISOU 2934  CB  VAL B   9    18897  23747  20658   1742    996    -35       C  
ATOM   2935  CG1 VAL B   9      18.107 -27.272  51.857  1.00100.08           C  
ANISOU 2935  CG1 VAL B   9    10038  15503  12483   1321   1621     32       C  
ATOM   2936  CG2 VAL B   9      20.179 -28.132  50.770  1.00154.64           C  
ANISOU 2936  CG2 VAL B   9    17471  22403  18882   2211   1349   -258       C  
ATOM   2937  N   ARG B  10      16.926 -30.939  52.377  1.00181.12           N  
ANISOU 2937  N   ARG B  10    20977  25096  22742   1069   -498    387       N  
ATOM   2938  CA  ARG B  10      15.666 -31.443  52.914  1.00175.81           C  
ANISOU 2938  CA  ARG B  10    20240  24254  22308    630   -912    622       C  
ATOM   2939  C   ARG B  10      15.841 -31.935  54.343  1.00176.20           C  
ANISOU 2939  C   ARG B  10    20068  24480  22402    131   -986    681       C  
ATOM   2940  O   ARG B  10      15.157 -31.474  55.263  1.00174.40           O  
ANISOU 2940  O   ARG B  10    19483  24377  22404   -380   -737    811       O  
ATOM   2941  CB  ARG B  10      15.127 -32.568  52.028  1.00173.51           C  
ANISOU 2941  CB  ARG B  10    20409  23556  21960    916  -1714    712       C  
ATOM   2942  CG  ARG B  10      14.461 -32.100  50.750  1.00172.57           C  
ANISOU 2942  CG  ARG B  10    20457  23217  21895   1256  -1718    739       C  
ATOM   2943  CD  ARG B  10      14.072 -33.283  49.878  1.00176.50           C  
ANISOU 2943  CD  ARG B  10    21450  23316  22297   1558  -2533    809       C  
ATOM   2944  NE  ARG B  10      13.618 -32.858  48.558  1.00184.21           N  
ANISOU 2944  NE  ARG B  10    22626  24087  23277   1957  -2533    803       N  
ATOM   2945  CZ  ARG B  10      12.376 -32.476  48.283  1.00184.54           C  
ANISOU 2945  CZ  ARG B  10    22567  23997  23552   1781  -2566    981       C  
ATOM   2946  NH1 ARG B  10      11.454 -32.479  49.237  1.00185.31           N  
ANISOU 2946  NH1 ARG B  10    22371  24138  23899   1217  -2608   1185       N  
ATOM   2947  NH2 ARG B  10      12.050 -32.101  47.054  1.00180.11           N  
ANISOU 2947  NH2 ARG B  10    22200  23261  22975   2173  -2560    963       N  
ATOM   2948  N   ARG B  11      16.761 -32.880  54.545  1.00177.95           N  
ANISOU 2948  N   ARG B  11    20501  24712  22399    282  -1325    592       N  
ATOM   2949  CA  ARG B  11      16.993 -33.410  55.883  1.00169.48           C  
ANISOU 2949  CA  ARG B  11    19236  23808  21351   -165  -1418    641       C  
ATOM   2950  C   ARG B  11      17.505 -32.335  56.833  1.00167.84           C  
ANISOU 2950  C   ARG B  11    18573  24003  21196   -494   -653    562       C  
ATOM   2951  O   ARG B  11      17.310 -32.447  58.046  1.00173.93           O  
ANISOU 2951  O   ARG B  11    19072  24924  22088   -997   -605    649       O  
ATOM   2952  CB  ARG B  11      17.953 -34.601  55.830  1.00168.84           C  
ANISOU 2952  CB  ARG B  11    19487  23669  20996    112  -1900    554       C  
ATOM   2953  CG  ARG B  11      19.419 -34.266  56.026  1.00172.06           C  
ANISOU 2953  CG  ARG B  11    19820  24389  21166    308  -1459    350       C  
ATOM   2954  CD  ARG B  11      20.208 -35.486  56.488  1.00183.21           C  
ANISOU 2954  CD  ARG B  11    21433  25807  22371    359  -1914    325       C  
ATOM   2955  NE  ARG B  11      20.312 -36.517  55.458  1.00194.11           N  
ANISOU 2955  NE  ARG B  11    23335  26855  23565    853  -2547    316       N  
ATOM   2956  CZ  ARG B  11      19.833 -37.751  55.580  1.00197.23           C  
ANISOU 2956  CZ  ARG B  11    23991  26988  23958    782  -3255    437       C  
ATOM   2957  NH1 ARG B  11      19.977 -38.619  54.587  1.00200.90           N  
ANISOU 2957  NH1 ARG B  11    24950  27150  24234   1256  -3791    418       N  
ATOM   2958  NH2 ARG B  11      19.221 -38.125  56.695  1.00197.75           N  
ANISOU 2958  NH2 ARG B  11    23835  27093  24207    240  -3428    579       N  
ATOM   2959  N   VAL B  12      18.163 -31.295  56.312  1.00164.24           N  
ANISOU 2959  N   VAL B  12    18031  23724  20647   -224    -52    400       N  
ATOM   2960  CA  VAL B  12      18.616 -30.199  57.170  1.00152.17           C  
ANISOU 2960  CA  VAL B  12    16078  22571  19168   -542    699    326       C  
ATOM   2961  C   VAL B  12      17.433 -29.516  57.843  1.00146.55           C  
ANISOU 2961  C   VAL B  12    15026  21889  18767  -1061    964    496       C  
ATOM   2962  O   VAL B  12      17.384 -29.392  59.071  1.00156.76           O  
ANISOU 2962  O   VAL B  12    16017  23384  20162  -1556   1161    553       O  
ATOM   2963  CB  VAL B  12      19.459 -29.189  56.374  1.00101.66           C  
ANISOU 2963  CB  VAL B  12     9675  16329  12623   -132   1278    129       C  
ATOM   2964  CG1 VAL B  12      19.638 -27.918  57.184  1.00 99.70           C  
ANISOU 2964  CG1 VAL B  12     8981  16425  12474   -503   2074     82       C  
ATOM   2965  CG2 VAL B  12      20.814 -29.780  56.051  1.00102.23           C  
ANISOU 2965  CG2 VAL B  12     9990  16470  12381    285   1131    -35       C  
ATOM   2966  N   VAL B  13      16.459 -29.064  57.052  1.00148.24           N  
ANISOU 2966  N   VAL B  13    15286  21904  19134   -952    977    589       N  
ATOM   2967  CA  VAL B  13      15.335 -28.365  57.664  1.00159.78           C  
ANISOU 2967  CA  VAL B  13    16420  23401  20887  -1426   1264    765       C  
ATOM   2968  C   VAL B  13      14.343 -29.352  58.269  1.00171.62           C  
ANISOU 2968  C   VAL B  13    17946  24705  22558  -1786    647    996       C  
ATOM   2969  O   VAL B  13      13.641 -29.018  59.231  1.00174.81           O  
ANISOU 2969  O   VAL B  13    18037  25203  23178  -2291    840   1148       O  
ATOM   2970  CB  VAL B  13      14.656 -27.432  56.648  1.00160.86           C  
ANISOU 2970  CB  VAL B  13    16559  23429  21131  -1198   1565    792       C  
ATOM   2971  CG1 VAL B  13      14.021 -26.249  57.366  1.00162.10           C  
ANISOU 2971  CG1 VAL B  13    16297  23779  21516  -1640   2214    885       C  
ATOM   2972  CG2 VAL B  13      15.660 -26.960  55.611  1.00153.59           C  
ANISOU 2972  CG2 VAL B  13    15811  22564  19983   -639   1852    560       C  
ATOM   2973  N   GLN B  14      14.247 -30.563  57.714  1.00158.38           N  
ANISOU 2973  N   GLN B  14    16643  22747  20789  -1534    -95   1035       N  
ATOM   2974  CA  GLN B  14      13.482 -31.622  58.363  1.00177.89           C  
ANISOU 2974  CA  GLN B  14    19155  25048  23388  -1872   -715   1235       C  
ATOM   2975  C   GLN B  14      13.979 -31.856  59.782  1.00187.18           C  
ANISOU 2975  C   GLN B  14    20078  26477  24564  -2305   -600   1227       C  
ATOM   2976  O   GLN B  14      13.213 -31.799  60.750  1.00182.70           O  
ANISOU 2976  O   GLN B  14    19242  25957  24218  -2808   -570   1401       O  
ATOM   2977  CB  GLN B  14      13.575 -32.921  57.568  1.00187.84           C  
ANISOU 2977  CB  GLN B  14    20890  25995  24488  -1497  -1504   1233       C  
ATOM   2978  CG  GLN B  14      12.526 -33.937  57.978  1.00190.72           C  
ANISOU 2978  CG  GLN B  14    21331  26118  25017  -1807  -2176   1470       C  
ATOM   2979  CD  GLN B  14      12.882 -35.338  57.543  1.00191.09           C  
ANISOU 2979  CD  GLN B  14    21822  25917  24865  -1516  -2932   1442       C  
ATOM   2980  OE1 GLN B  14      13.730 -35.530  56.671  1.00190.95           O  
ANISOU 2980  OE1 GLN B  14    22109  25844  24599  -1013  -3000   1268       O  
ATOM   2981  NE2 GLN B  14      12.239 -36.332  58.149  1.00189.55           N  
ANISOU 2981  NE2 GLN B  14    21675  25571  24776  -1827  -3502   1618       N  
ATOM   2982  N   GLU B  15      15.278 -32.139  59.913  1.00180.69           N  
ANISOU 2982  N   GLU B  15    19344  25820  23489  -2105   -540   1031       N  
ATOM   2983  CA  GLU B  15      15.876 -32.409  61.213  1.00187.31           C  
ANISOU 2983  CA  GLU B  15    19964  26910  24294  -2477   -443   1007       C  
ATOM   2984  C   GLU B  15      15.942 -31.140  62.057  1.00186.04           C  
ANISOU 2984  C   GLU B  15    19357  27077  24254  -2857    346    983       C  
ATOM   2985  O   GLU B  15      16.124 -31.226  63.275  1.00195.46           O  
ANISOU 2985  O   GLU B  15    20303  28470  25493  -3283    466   1013       O  
ATOM   2986  CB  GLU B  15      17.270 -33.017  60.990  1.00199.31           C  
ANISOU 2986  CB  GLU B  15    21716  28517  25494  -2107   -580    810       C  
ATOM   2987  CG  GLU B  15      17.726 -34.106  61.953  1.00205.92           C  
ANISOU 2987  CG  GLU B  15    22574  29417  26249  -2327   -975    832       C  
ATOM   2988  CD  GLU B  15      18.060 -33.593  63.328  1.00211.71           C  
ANISOU 2988  CD  GLU B  15    22889  30500  27050  -2825   -497    823       C  
ATOM   2989  OE1 GLU B  15      17.762 -34.304  64.307  1.00213.97           O  
ANISOU 2989  OE1 GLU B  15    23084  30790  27426  -3205   -805    939       O  
ATOM   2990  OE2 GLU B  15      18.615 -32.482  63.438  1.00210.78           O  
ANISOU 2990  OE2 GLU B  15    22539  30651  26897  -2844    184    700       O  
ATOM   2991  N   LEU B  16      15.782 -29.965  61.435  1.00191.48           N  
ANISOU 2991  N   LEU B  16    19946  27816  24992  -2713    886    932       N  
ATOM   2992  CA  LEU B  16      15.698 -28.696  62.148  1.00160.23           C  
ANISOU 2992  CA  LEU B  16    15586  24133  21162  -3070   1644    927       C  
ATOM   2993  C   LEU B  16      14.282 -28.381  62.615  1.00175.08           C  
ANISOU 2993  C   LEU B  16    17252  25915  23355  -3495   1673   1172       C  
ATOM   2994  O   LEU B  16      14.096 -27.437  63.391  1.00181.22           O  
ANISOU 2994  O   LEU B  16    17690  26906  24259  -3866   2256   1204       O  
ATOM   2995  CB  LEU B  16      16.214 -27.555  61.255  1.00130.86           C  
ANISOU 2995  CB  LEU B  16    11861  20518  17342  -2706   2236    756       C  
ATOM   2996  CG  LEU B  16      16.461 -26.156  61.823  1.00122.71           C  
ANISOU 2996  CG  LEU B  16    10463  19798  16363  -2966   3098    684       C  
ATOM   2997  CD1 LEU B  16      17.214 -26.243  63.136  1.00139.20           C  
ANISOU 2997  CD1 LEU B  16    12431  22054  18406  -3271   3240    627       C  
ATOM   2998  CD2 LEU B  16      17.234 -25.323  60.819  1.00113.71           C  
ANISOU 2998  CD2 LEU B  16     9405  18744  15056  -2502   3545    481       C  
ATOM   2999  N   ASP B  17      13.294 -29.164  62.178  1.00180.77           N  
ANISOU 2999  N   ASP B  17    18169  26321  24197  -3453   1055   1353       N  
ATOM   3000  CA  ASP B  17      11.891 -28.988  62.559  1.00194.37           C  
ANISOU 3000  CA  ASP B  17    19710  27925  26217  -3834   1000   1618       C  
ATOM   3001  C   ASP B  17      11.438 -27.540  62.361  1.00229.76           C  
ANISOU 3001  C   ASP B  17    23945  32520  30833  -3897   1720   1640       C  
ATOM   3002  O   ASP B  17      10.792 -26.934  63.221  1.00223.34           O  
ANISOU 3002  O   ASP B  17    22902  31736  30220  -4267   2057   1742       O  
ATOM   3003  CB  ASP B  17      11.659 -29.459  63.993  1.00172.54           C  
ANISOU 3003  CB  ASP B  17    16718  25264  23573  -4378    877   1748       C  
ATOM   3004  CG  ASP B  17      12.147 -30.879  64.221  1.00160.69           C  
ANISOU 3004  CG  ASP B  17    15457  23666  21934  -4316    190   1720       C  
ATOM   3005  OD1 ASP B  17      13.147 -31.272  63.583  1.00155.99           O  
ANISOU 3005  OD1 ASP B  17    15120  23065  21082  -3896     44   1525       O  
ATOM   3006  OD2 ASP B  17      11.521 -31.607  65.019  1.00158.72           O  
ANISOU 3006  OD2 ASP B  17    15140  23339  21828  -4676   -203   1900       O  
ATOM   3007  N   HIS B  18      11.772 -27.000  61.189  1.00217.76           N  
ANISOU 3007  N   HIS B  18    22585  30958  29196  -3431   1929   1501       N  
ATOM   3008  CA  HIS B  18      11.474 -25.615  60.814  1.00222.67           C  
ANISOU 3008  CA  HIS B  18    23017  31681  29906  -3398   2623   1488       C  
ATOM   3009  C   HIS B  18      11.949 -24.634  61.882  1.00227.07           C  
ANISOU 3009  C   HIS B  18    23530  32216  30531  -3506   3236   1325       C  
ATOM   3010  O   HIS B  18      11.206 -23.759  62.331  1.00227.49           O  
ANISOU 3010  O   HIS B  18    23731  31843  30862  -3438   3497   1350       O  
ATOM   3011  CB  HIS B  18       9.984 -25.424  60.530  1.00223.37           C  
ANISOU 3011  CB  HIS B  18    23050  31563  30258  -3536   2502   1757       C  
ATOM   3012  CG  HIS B  18       9.672 -24.195  59.730  1.00224.11           C  
ANISOU 3012  CG  HIS B  18    23065  31680  30404  -3333   3067   1736       C  
ATOM   3013  ND1 HIS B  18       8.426 -23.605  59.724  1.00223.85           N  
ANISOU 3013  ND1 HIS B  18    23012  31443  30598  -3459   3200   1866       N  
ATOM   3014  CD2 HIS B  18      10.442 -23.454  58.898  1.00222.92           C  
ANISOU 3014  CD2 HIS B  18    22989  31620  30092  -2927   3493   1515       C  
ATOM   3015  CE1 HIS B  18       8.443 -22.551  58.928  1.00223.13           C  
ANISOU 3015  CE1 HIS B  18    23022  31298  30461  -3156   3659   1685       C  
ATOM   3016  NE2 HIS B  18       9.654 -22.436  58.414  1.00222.51           N  
ANISOU 3016  NE2 HIS B  18    22926  31437  30181  -2856   3875   1533       N  
ATOM   3017  N   GLY B  19      13.200 -24.792  62.302  1.00213.60           N  
ANISOU 3017  N   GLY B  19    21872  30657  28630  -3421   3316   1150       N  
ATOM   3018  CA  GLY B  19      13.749 -23.876  63.278  1.00188.96           C  
ANISOU 3018  CA  GLY B  19    18973  27207  25617  -3221   3651   1105       C  
ATOM   3019  C   GLY B  19      13.983 -22.540  62.607  1.00171.87           C  
ANISOU 3019  C   GLY B  19    16946  24902  23453  -2780   4063   1155       C  
ATOM   3020  O   GLY B  19      14.898 -22.416  61.789  1.00165.35           O  
ANISOU 3020  O   GLY B  19    16151  24289  22386  -2532   4212    994       O  
ATOM   3021  N   GLY B  20      13.187 -21.528  62.953  1.00191.86           N  
ANISOU 3021  N   GLY B  20    19601  27133  26164  -2629   4143   1402       N  
ATOM   3022  CA  GLY B  20      13.263 -20.243  62.278  1.00198.71           C  
ANISOU 3022  CA  GLY B  20    20626  28038  26837  -2219   4276   1541       C  
ATOM   3023  C   GLY B  20      12.750 -20.321  60.855  1.00211.38           C  
ANISOU 3023  C   GLY B  20    22144  29763  28408  -2144   4348   1487       C  
ATOM   3024  O   GLY B  20      12.809 -21.389  60.238  1.00213.67           O  
ANISOU 3024  O   GLY B  20    22239  30179  28768  -2347   4361   1261       O  
ATOM   3025  N   GLU B  21      12.174 -19.219  60.358  1.00217.25           N  
ANISOU 3025  N   GLU B  21    22969  30646  28929  -1923   4300   1676       N  
ATOM   3026  CA  GLU B  21      11.655 -19.152  58.994  1.00219.95           C  
ANISOU 3026  CA  GLU B  21    23228  31257  29084  -1876   4321   1576       C  
ATOM   3027  C   GLU B  21      12.510 -19.937  58.006  1.00214.73           C  
ANISOU 3027  C   GLU B  21    22478  30650  28457  -1738   4539   1285       C  
ATOM   3028  O   GLU B  21      12.058 -20.933  57.430  1.00221.19           O  
ANISOU 3028  O   GLU B  21    23093  31395  29555  -1913   4573   1161       O  
ATOM   3029  CB  GLU B  21      11.561 -17.685  58.563  1.00226.98           C  
ANISOU 3029  CB  GLU B  21    24276  32427  29539  -1689   4289   1497       C  
ATOM   3030  CG  GLU B  21      10.475 -17.386  57.555  1.00237.21           C  
ANISOU 3030  CG  GLU B  21    25549  33837  30743  -1827   4320   1273       C  
ATOM   3031  CD  GLU B  21      10.059 -15.932  57.588  1.00244.69           C  
ANISOU 3031  CD  GLU B  21    26622  34828  31520  -1759   4348   1264       C  
ATOM   3032  OE1 GLU B  21      10.520 -15.198  58.488  1.00249.06           O  
ANISOU 3032  OE1 GLU B  21    27205  35296  32132  -1744   4512   1339       O  
ATOM   3033  OE2 GLU B  21       9.312 -15.507  56.685  1.00247.79           O  
ANISOU 3033  OE2 GLU B  21    27042  35204  31903  -1755   4428   1110       O  
ATOM   3034  N   PHE B  22      13.763 -19.511  57.839  1.00210.62           N  
ANISOU 3034  N   PHE B  22    22107  30217  27702  -1425   4672   1144       N  
ATOM   3035  CA  PHE B  22      14.764 -20.192  57.023  1.00188.06           C  
ANISOU 3035  CA  PHE B  22    19216  27441  24798  -1209   4864    843       C  
ATOM   3036  C   PHE B  22      14.254 -20.731  55.690  1.00179.57           C  
ANISOU 3036  C   PHE B  22    17971  26480  23778  -1098   4952    637       C  
ATOM   3037  O   PHE B  22      14.172 -21.951  55.516  1.00186.51           O  
ANISOU 3037  O   PHE B  22    18952  27244  24671  -1089   4442    600       O  
ATOM   3038  CB  PHE B  22      15.408 -21.331  57.821  1.00178.48           C  
ANISOU 3038  CB  PHE B  22    17887  26277  23652  -1506   4781    669       C  
ATOM   3039  CG  PHE B  22      16.596 -20.899  58.639  1.00171.82           C  
ANISOU 3039  CG  PHE B  22    17228  25372  22684  -1384   4840    698       C  
ATOM   3040  CD1 PHE B  22      17.053 -19.591  58.584  1.00166.91           C  
ANISOU 3040  CD1 PHE B  22    16847  24677  21893  -1043   4890    853       C  
ATOM   3041  CD2 PHE B  22      17.275 -21.808  59.436  1.00167.63           C  
ANISOU 3041  CD2 PHE B  22    16634  24970  22087  -1637   4685    542       C  
ATOM   3042  CE1 PHE B  22      18.150 -19.189  59.324  1.00159.29           C  
ANISOU 3042  CE1 PHE B  22    16029  23671  20824   -956   4887    876       C  
ATOM   3043  CE2 PHE B  22      18.376 -21.413  60.177  1.00162.32           C  
ANISOU 3043  CE2 PHE B  22    16123  24226  21325  -1530   4747    561       C  
ATOM   3044  CZ  PHE B  22      18.814 -20.101  60.121  1.00159.05           C  
ANISOU 3044  CZ  PHE B  22    15909  23671  20851  -1183   4896    755       C  
ATOM   3045  N   ILE B  23      13.892 -19.855  54.756  1.00176.01           N  
ANISOU 3045  N   ILE B  23    17640  26066  23170   -875   5027    518       N  
ATOM   3046  CA  ILE B  23      13.463 -20.352  53.441  1.00167.08           C  
ANISOU 3046  CA  ILE B  23    16567  24631  22286   -455   5032    561       C  
ATOM   3047  C   ILE B  23      14.613 -21.120  52.801  1.00151.14           C  
ANISOU 3047  C   ILE B  23    14873  22562  19992     22   4670    360       C  
ATOM   3048  O   ILE B  23      15.730 -20.578  52.679  1.00155.52           O  
ANISOU 3048  O   ILE B  23    15396  23324  20370    235   5108    145       O  
ATOM   3049  CB  ILE B  23      12.995 -19.203  52.537  1.00174.92           C  
ANISOU 3049  CB  ILE B  23    17670  25575  23216   -257   5243    465       C  
ATOM   3050  CG1 ILE B  23      11.784 -18.514  53.163  1.00184.59           C  
ANISOU 3050  CG1 ILE B  23    18848  26826  24461   -717   5127    590       C  
ATOM   3051  CG2 ILE B  23      12.682 -19.713  51.133  1.00176.06           C  
ANISOU 3051  CG2 ILE B  23    17994  25447  23454    303   5044    565       C  
ATOM   3052  CD1 ILE B  23      11.315 -17.323  52.402  1.00187.97           C  
ANISOU 3052  CD1 ILE B  23    19432  27248  24739   -567   5167    497       C  
ATOM   3053  N   PRO B  24      14.405 -22.361  52.378  1.00152.34           N  
ANISOU 3053  N   PRO B  24    15346  22444  20092    207   3890    426       N  
ATOM   3054  CA  PRO B  24      15.516 -23.173  51.863  1.00160.94           C  
ANISOU 3054  CA  PRO B  24    16758  23484  20909    643   3525    251       C  
ATOM   3055  C   PRO B  24      16.028 -22.741  50.496  1.00184.51           C  
ANISOU 3055  C   PRO B  24    19963  26401  23743   1264   3688     86       C  
ATOM   3056  O   PRO B  24      15.618 -21.711  49.949  1.00187.53           O  
ANISOU 3056  O   PRO B  24    20228  26805  24222   1367   4154     83       O  
ATOM   3057  CB  PRO B  24      14.910 -24.582  51.789  1.00147.99           C  
ANISOU 3057  CB  PRO B  24    15400  21539  19290    624   2640    405       C  
ATOM   3058  CG  PRO B  24      13.706 -24.541  52.692  1.00130.67           C  
ANISOU 3058  CG  PRO B  24    12946  19328  17373     48   2596    649       C  
ATOM   3059  CD  PRO B  24      13.176 -23.153  52.546  1.00 96.45           C  
ANISOU 3059  CD  PRO B  24     8332  15114  13199    -43   3294    680       C  
ATOM   3060  N   VAL B  25      16.929 -23.563  49.944  1.00172.50           N  
ANISOU 3060  N   VAL B  25    18773  24791  21979   1690   3292    -44       N  
ATOM   3061  CA  VAL B  25      17.526 -23.325  48.634  1.00167.92           C  
ANISOU 3061  CA  VAL B  25    18450  24128  21224   2325   3367   -205       C  
ATOM   3062  C   VAL B  25      16.502 -23.638  47.543  1.00169.57           C  
ANISOU 3062  C   VAL B  25    18925  23985  21520   2590   2928    -86       C  
ATOM   3063  O   VAL B  25      15.485 -24.302  47.777  1.00177.05           O  
ANISOU 3063  O   VAL B  25    19924  24730  22616   2327   2433    112       O  
ATOM   3064  CB  VAL B  25      18.808 -24.165  48.476  1.00167.18           C  
ANISOU 3064  CB  VAL B  25    18628  24054  20840   2674   3067   -359       C  
ATOM   3065  CG1 VAL B  25      18.472 -25.650  48.360  1.00173.93           C  
ANISOU 3065  CG1 VAL B  25    19835  24608  21643   2732   2185   -249       C  
ATOM   3066  CG2 VAL B  25      19.694 -23.664  47.320  1.00167.17           C  
ANISOU 3066  CG2 VAL B  25    18803  24073  20642   3299   3348   -555       C  
ATOM   3067  N   THR B  26      16.766 -23.143  46.332  1.00185.56           N  
ANISOU 3067  N   THR B  26    21117  25936  23451   3116   3112   -204       N  
ATOM   3068  CA  THR B  26      15.773 -23.224  45.263  1.00168.11           C  
ANISOU 3068  CA  THR B  26    19117  23421  21335   3363   2805    -97       C  
ATOM   3069  C   THR B  26      15.932 -24.454  44.367  1.00163.45           C  
ANISOU 3069  C   THR B  26    19029  22508  20567   3808   2036   -110       C  
ATOM   3070  O   THR B  26      15.030 -25.296  44.303  1.00164.15           O  
ANISOU 3070  O   THR B  26    19292  22333  20743   3680   1417     64       O  
ATOM   3071  CB  THR B  26      15.856 -21.952  44.412  1.00151.17           C  
ANISOU 3071  CB  THR B  26    16869  21362  19206   3680   3446   -205       C  
ATOM   3072  OG1 THR B  26      17.145 -21.886  43.783  1.00159.74           O  
ANISOU 3072  OG1 THR B  26    18137  22522  20035   4192   3600   -435       O  
ATOM   3073  CG2 THR B  26      15.663 -20.714  45.282  1.00124.56           C  
ANISOU 3073  CG2 THR B  26    13021  18298  16007   3238   4219   -187       C  
ATOM   3074  N   SER B  27      17.068 -24.584  43.691  1.00159.85           N  
ANISOU 3074  N   SER B  27    18814  22066  19857   4325   2060   -307       N  
ATOM   3075  CA  SER B  27      17.258 -25.641  42.706  1.00169.26           C  
ANISOU 3075  CA  SER B  27    20510  22941  20861   4815   1391   -332       C  
ATOM   3076  C   SER B  27      18.345 -26.624  43.127  1.00161.14           C  
ANISOU 3076  C   SER B  27    19679  21953  19594   4914   1062   -420       C  
ATOM   3077  O   SER B  27      19.104 -26.396  44.073  1.00146.26           O  
ANISOU 3077  O   SER B  27    17541  20366  17666   4671   1409   -491       O  
ATOM   3078  CB  SER B  27      17.565 -25.059  41.320  1.00176.60           C  
ANISOU 3078  CB  SER B  27    21636  23782  21683   5434   1612   -465       C  
ATOM   3079  OG  SER B  27      16.529 -25.389  40.406  1.00166.88           O  
ANISOU 3079  OG  SER B  27    20659  22214  20533   5602   1164   -342       O  
ATOM   3080  N   LEU B  28      18.402 -27.722  42.372  1.00174.16           N  
ANISOU 3080  N   LEU B  28    21801  23290  21081   5288    383   -411       N  
ATOM   3081  CA  LEU B  28      19.346 -28.810  42.594  1.00169.30           C  
ANISOU 3081  CA  LEU B  28    21460  22646  20221   5454    -34   -474       C  
ATOM   3082  C   LEU B  28      20.717 -28.444  42.047  1.00188.70           C  
ANISOU 3082  C   LEU B  28    24011  25258  22427   5971    333   -686       C  
ATOM   3083  O   LEU B  28      20.844 -28.020  40.894  1.00196.02           O  
ANISOU 3083  O   LEU B  28    25121  26076  23282   6467    461   -771       O  
ATOM   3084  CB  LEU B  28      18.843 -30.073  41.889  1.00151.46           C  
ANISOU 3084  CB  LEU B  28    19703  19969  17877   5691   -884   -381       C  
ATOM   3085  CG  LEU B  28      19.505 -31.454  42.012  1.00145.00           C  
ANISOU 3085  CG  LEU B  28    19265  19008  16819   5855  -1505   -394       C  
ATOM   3086  CD1 LEU B  28      18.489 -32.526  41.699  1.00150.20           C  
ANISOU 3086  CD1 LEU B  28    20267  19277  17527   5794  -2298   -229       C  
ATOM   3087  CD2 LEU B  28      20.698 -31.619  41.088  1.00137.90           C  
ANISOU 3087  CD2 LEU B  28    18707  18074  15613   6528  -1486   -569       C  
ATOM   3088  N   GLN B  29      21.746 -28.621  42.880  1.00191.65           N  
ANISOU 3088  N   GLN B  29    24259  25892  22668   5857    496   -762       N  
ATOM   3089  CA  GLN B  29      23.133 -28.411  42.471  1.00188.03           C  
ANISOU 3089  CA  GLN B  29    23893  25598  21953   6327    794   -942       C  
ATOM   3090  C   GLN B  29      23.291 -27.012  41.865  1.00184.09           C  
ANISOU 3090  C   GLN B  29    23178  25259  21510   6542   1507  -1056       C  
ATOM   3091  O   GLN B  29      24.081 -26.783  40.946  1.00189.25           O  
ANISOU 3091  O   GLN B  29    24023  25905  21979   7101   1665  -1188       O  
ATOM   3092  CB  GLN B  29      23.562 -29.535  41.513  1.00190.17           C  
ANISOU 3092  CB  GLN B  29    24729  25560  21968   6900    167   -968       C  
ATOM   3093  CG  GLN B  29      24.987 -29.521  40.976  1.00193.06           C  
ANISOU 3093  CG  GLN B  29    25272  26041  22041   7458    361  -1129       C  
ATOM   3094  CD  GLN B  29      25.401 -30.875  40.424  1.00188.27           C  
ANISOU 3094  CD  GLN B  29    25208  25148  21179   7879   -336  -1116       C  
ATOM   3095  OE1 GLN B  29      24.564 -31.753  40.213  1.00186.83           O  
ANISOU 3095  OE1 GLN B  29    25313  24638  21036   7825   -966  -1002       O  
ATOM   3096  NE2 GLN B  29      26.698 -31.053  40.195  1.00181.83           N  
ANISOU 3096  NE2 GLN B  29    24537  24456  20096   8297   -225  -1225       N  
ATOM   3097  N   SER B  30      22.502 -26.058  42.368  1.00191.47           N  
ANISOU 3097  N   SER B  30    23714  26332  22703   6099   1949   -998       N  
ATOM   3098  CA  SER B  30      22.540 -24.691  41.869  1.00188.40           C  
ANISOU 3098  CA  SER B  30    23096  26096  22391   6247   2646  -1092       C  
ATOM   3099  C   SER B  30      23.216 -23.715  42.822  1.00191.27           C  
ANISOU 3099  C   SER B  30    23009  26882  22784   5920   3377  -1178       C  
ATOM   3100  O   SER B  30      24.231 -23.120  42.456  1.00192.90           O  
ANISOU 3100  O   SER B  30    23253  27071  22971   5819   3572  -1263       O  
ATOM   3101  CB  SER B  30      21.108 -24.222  41.587  1.00180.95           C  
ANISOU 3101  CB  SER B  30    22054  24986  21715   6039   2653   -960       C  
ATOM   3102  OG  SER B  30      20.388 -24.064  42.804  1.00160.17           O  
ANISOU 3102  OG  SER B  30    19068  22484  19303   5361   2758   -825       O  
ATOM   3103  N   SER B  31      22.717 -23.590  44.060  1.00186.33           N  
ANISOU 3103  N   SER B  31    22049  26411  22335   5276   3495  -1076       N  
ATOM   3104  CA  SER B  31      23.259 -22.650  45.044  1.00194.19           C  
ANISOU 3104  CA  SER B  31    22631  27760  23394   4841   4142  -1138       C  
ATOM   3105  C   SER B  31      23.739 -21.373  44.354  1.00210.21           C  
ANISOU 3105  C   SER B  31    24710  29533  25627   4502   4355  -1254       C  
ATOM   3106  O   SER B  31      24.852 -20.901  44.623  1.00219.66           O  
ANISOU 3106  O   SER B  31    25877  30733  26851   4186   4481  -1377       O  
ATOM   3107  CB  SER B  31      24.384 -23.303  45.848  1.00183.79           C  
ANISOU 3107  CB  SER B  31    21292  26680  21859   4816   4072  -1199       C  
ATOM   3108  OG  SER B  31      25.551 -23.475  45.066  1.00178.75           O  
ANISOU 3108  OG  SER B  31    20971  25884  21061   5123   3897  -1300       O  
ATOM   3109  N   THR B  32      22.908 -20.815  43.473  1.00207.88           N  
ANISOU 3109  N   THR B  32    24471  29035  25479   4571   4367  -1232       N  
ATOM   3110  CA  THR B  32      23.291 -19.659  42.662  1.00208.37           C  
ANISOU 3110  CA  THR B  32    24570  28900  25701   4327   4479  -1373       C  
ATOM   3111  C   THR B  32      23.371 -18.396  43.505  1.00211.77           C  
ANISOU 3111  C   THR B  32    24685  29411  26365   3556   4784  -1544       C  
ATOM   3112  O   THR B  32      22.383 -17.991  44.120  1.00211.21           O  
ANISOU 3112  O   THR B  32    24396  29430  26424   3224   4916  -1517       O  
ATOM   3113  CB  THR B  32      22.295 -19.455  41.517  1.00204.35           C  
ANISOU 3113  CB  THR B  32    24194  28191  25260   4615   4375  -1304       C  
ATOM   3114  OG1 THR B  32      22.489 -20.460  40.516  1.00202.25           O  
ANISOU 3114  OG1 THR B  32    24305  27781  24761   5303   3999  -1244       O  
ATOM   3115  CG2 THR B  32      22.459 -18.069  40.884  1.00204.53           C  
ANISOU 3115  CG2 THR B  32    24137  28099  25476   4234   4522  -1467       C  
ATOM   3116  N   GLY B  33      24.528 -17.745  43.476  1.00225.92           N  
ANISOU 3116  N   GLY B  33    26467  31185  28188   3287   4836  -1745       N  
ATOM   3117  CA  GLY B  33      24.667 -16.497  44.202  1.00210.84           C  
ANISOU 3117  CA  GLY B  33    24299  29418  26395   2653   5008  -1968       C  
ATOM   3118  C   GLY B  33      24.410 -16.786  45.665  1.00197.02           C  
ANISOU 3118  C   GLY B  33    22367  27837  24654   2250   5064  -1953       C  
ATOM   3119  O   GLY B  33      25.122 -17.578  46.294  1.00180.16           O  
ANISOU 3119  O   GLY B  33    20263  25736  22454   2311   5126  -1902       O  
ATOM   3120  N   PHE B  34      23.359 -16.170  46.207  1.00188.85           N  
ANISOU 3120  N   PHE B  34    21159  26962  23633   1925   5030  -1912       N  
ATOM   3121  CA  PHE B  34      23.009 -16.281  47.622  1.00221.80           C  
ANISOU 3121  CA  PHE B  34    25158  31358  27757   1510   4989  -1848       C  
ATOM   3122  C   PHE B  34      24.241 -16.080  48.508  1.00268.66           C  
ANISOU 3122  C   PHE B  34    31080  37401  33596   1288   5026  -1895       C  
ATOM   3123  O   PHE B  34      24.750 -17.002  49.142  1.00267.02           O  
ANISOU 3123  O   PHE B  34    30950  37010  33495   1180   5075  -1908       O  
ATOM   3124  CB  PHE B  34      22.320 -17.613  47.938  1.00212.76           C  
ANISOU 3124  CB  PHE B  34    23969  30179  26691   1788   5185  -1604       C  
ATOM   3125  CG  PHE B  34      20.985 -17.786  47.272  1.00202.26           C  
ANISOU 3125  CG  PHE B  34    22607  28806  25436   2080   5213  -1416       C  
ATOM   3126  CD1 PHE B  34      19.923 -16.957  47.601  1.00192.04           C  
ANISOU 3126  CD1 PHE B  34    21134  27665  24168   1724   5193  -1373       C  
ATOM   3127  CD2 PHE B  34      20.771 -18.815  46.376  1.00200.00           C  
ANISOU 3127  CD2 PHE B  34    22529  28368  25093   2772   5105  -1185       C  
ATOM   3128  CE1 PHE B  34      18.687 -17.124  46.996  1.00188.34           C  
ANISOU 3128  CE1 PHE B  34    20670  27055  23838   1961   5240  -1147       C  
ATOM   3129  CE2 PHE B  34      19.540 -18.988  45.771  1.00197.36           C  
ANISOU 3129  CE2 PHE B  34    22203  27949  24835   3057   5067   -975       C  
ATOM   3130  CZ  PHE B  34      18.496 -18.144  46.084  1.00192.61           C  
ANISOU 3130  CZ  PHE B  34    21402  27371  24412   2613   5193   -940       C  
ATOM   3131  N   GLN B  35      24.709 -14.854  48.520  1.00237.04           N  
ANISOU 3131  N   GLN B  35    27005  33650  29410   1279   5042  -1855       N  
ATOM   3132  CA  GLN B  35      25.802 -14.466  49.390  1.00247.82           C  
ANISOU 3132  CA  GLN B  35    28299  35261  30600   1127   5023  -1840       C  
ATOM   3133  C   GLN B  35      25.221 -13.831  50.641  1.00228.44           C  
ANISOU 3133  C   GLN B  35    25651  33323  27821   1171   4900  -1266       C  
ATOM   3134  O   GLN B  35      24.029 -13.519  50.686  1.00231.52           O  
ANISOU 3134  O   GLN B  35    26012  33661  28294   1149   4957  -1057       O  
ATOM   3135  CB  GLN B  35      26.736 -13.496  48.656  1.00257.31           C  
ANISOU 3135  CB  GLN B  35    29579  36410  31779   1290   5147  -1897       C  
ATOM   3136  CG  GLN B  35      27.159 -13.950  47.249  1.00266.92           C  
ANISOU 3136  CG  GLN B  35    31027  37200  33192   1614   5271  -2020       C  
ATOM   3137  CD  GLN B  35      28.102 -15.146  47.218  1.00270.77           C  
ANISOU 3137  CD  GLN B  35    31681  37451  33750   1760   5314  -2049       C  
ATOM   3138  OE1 GLN B  35      27.870 -16.164  47.869  1.00272.46           O  
ANISOU 3138  OE1 GLN B  35    31915  37584  34025   1669   5283  -2013       O  
ATOM   3139  NE2 GLN B  35      29.164 -15.031  46.426  1.00272.57           N  
ANISOU 3139  NE2 GLN B  35    32030  37611  33923   2049   5372  -2066       N  
ATOM   3140  N   PRO B  36      26.019 -13.663  51.707  1.00246.33           N  
ANISOU 3140  N   PRO B  36    27918  35726  29950   1299   4936   -814       N  
ATOM   3141  CA  PRO B  36      25.460 -13.059  52.933  1.00230.47           C  
ANISOU 3141  CA  PRO B  36    25909  33519  28139   1151   5184   -365       C  
ATOM   3142  C   PRO B  36      24.661 -11.786  52.684  1.00219.95           C  
ANISOU 3142  C   PRO B  36    24537  32123  26911    980   5338   -451       C  
ATOM   3143  O   PRO B  36      23.522 -11.673  53.154  1.00220.51           O  
ANISOU 3143  O   PRO B  36    24547  32113  27124    782   5395   -335       O  
ATOM   3144  CB  PRO B  36      26.710 -12.809  53.784  1.00224.80           C  
ANISOU 3144  CB  PRO B  36    25254  32706  27453   1145   5344   -218       C  
ATOM   3145  CG  PRO B  36      27.638 -13.901  53.382  1.00222.99           C  
ANISOU 3145  CG  PRO B  36    25160  32444  27121   1476   5233   -159       C  
ATOM   3146  CD  PRO B  36      27.407 -14.122  51.909  1.00230.76           C  
ANISOU 3146  CD  PRO B  36    25982  33873  27823   1439   4854   -824       C  
ATOM   3147  N   TYR B  37      25.226 -10.825  51.963  1.00224.43           N  
ANISOU 3147  N   TYR B  37    25561  35124  24589  -3208    973  -2456       N  
ATOM   3148  CA  TYR B  37      24.521  -9.605  51.560  1.00227.07           C  
ANISOU 3148  CA  TYR B  37    26062  35189  25025  -3574    665  -2001       C  
ATOM   3149  C   TYR B  37      23.959  -9.681  50.142  1.00232.38           C  
ANISOU 3149  C   TYR B  37    26839  35918  25538  -4225    564  -1720       C  
ATOM   3150  O   TYR B  37      24.152  -8.764  49.340  1.00236.54           O  
ANISOU 3150  O   TYR B  37    27460  36496  25920  -4843    361  -1563       O  
ATOM   3151  CB  TYR B  37      25.411  -8.382  51.733  1.00232.09           C  
ANISOU 3151  CB  TYR B  37    26687  35909  25588  -3797    540  -2095       C  
ATOM   3152  CG  TYR B  37      25.664  -7.999  53.176  1.00232.77           C  
ANISOU 3152  CG  TYR B  37    26706  35820  25917  -3166    564  -2221       C  
ATOM   3153  CD1 TYR B  37      26.390  -8.817  54.029  1.00231.88           C  
ANISOU 3153  CD1 TYR B  37    26450  35860  25796  -2656    823  -2648       C  
ATOM   3154  CD2 TYR B  37      25.140  -6.818  53.692  1.00234.52           C  
ANISOU 3154  CD2 TYR B  37    27005  35704  26398  -3090    310  -1908       C  
ATOM   3155  CE1 TYR B  37      26.608  -8.457  55.348  1.00232.74           C  
ANISOU 3155  CE1 TYR B  37    26509  35797  26126  -2106    842  -2749       C  
ATOM   3156  CE2 TYR B  37      25.349  -6.452  55.007  1.00233.95           C  
ANISOU 3156  CE2 TYR B  37    26852  35478  26559  -2543    344  -2014       C  
ATOM   3157  CZ  TYR B  37      26.084  -7.275  55.831  1.00233.98           C  
ANISOU 3157  CZ  TYR B  37    26729  35643  26531  -2059    618  -2427       C  
ATOM   3158  OH  TYR B  37      26.297  -6.916  57.142  1.00234.13           O  
ANISOU 3158  OH  TYR B  37    26676  35504  26778  -1537    654  -2526       O  
ATOM   3159  N   CYS B  38      23.249 -10.757  49.802  1.00229.76           N  
ANISOU 3159  N   CYS B  38    26506  35573  25219  -4118    697  -1645       N  
ATOM   3160  CA  CYS B  38      22.602 -10.870  48.495  1.00225.64           C  
ANISOU 3160  CA  CYS B  38    26087  35071  24575  -4700    611  -1345       C  
ATOM   3161  C   CYS B  38      21.104 -10.690  48.689  1.00222.06           C  
ANISOU 3161  C   CYS B  38    25804  34133  24434  -4462    419   -898       C  
ATOM   3162  O   CYS B  38      20.387 -11.633  49.030  1.00227.59           O  
ANISOU 3162  O   CYS B  38    26495  34720  25258  -4022    575   -883       O  
ATOM   3163  CB  CYS B  38      22.898 -12.204  47.818  1.00222.39           C  
ANISOU 3163  CB  CYS B  38    25530  35032  23937  -4828    910  -1588       C  
ATOM   3164  SG  CYS B  38      24.285 -12.168  46.675  1.00225.18           S  
ANISOU 3164  SG  CYS B  38    25745  35947  23866  -5635   1012  -1945       S  
ATOM   3165  N   LEU B  39      20.640  -9.474  48.429  1.00230.24           N  
ANISOU 3165  N   LEU B  39    27001  34887  25591  -4784     68   -555       N  
ATOM   3166  CA  LEU B  39      19.226  -9.155  48.536  1.00201.06           C  
ANISOU 3166  CA  LEU B  39    23467  30707  22221  -4629   -172   -154       C  
ATOM   3167  C   LEU B  39      18.441  -9.918  47.478  1.00180.80           C  
ANISOU 3167  C   LEU B  39    20978  28154  19563  -4916   -118     53       C  
ATOM   3168  O   LEU B  39      18.891 -10.077  46.339  1.00176.13           O  
ANISOU 3168  O   LEU B  39    20387  27865  18669  -5531    -79     55       O  
ATOM   3169  CB  LEU B  39      19.001  -7.647  48.404  1.00196.79           C  
ANISOU 3169  CB  LEU B  39    23067  29875  21828  -4971   -602    141       C  
ATOM   3170  CG  LEU B  39      19.228  -6.926  47.076  1.00198.11           C  
ANISOU 3170  CG  LEU B  39    23377  30143  21751  -5832   -856    354       C  
ATOM   3171  CD1 LEU B  39      18.679  -5.515  47.165  1.00199.69           C  
ANISOU 3171  CD1 LEU B  39    23738  29925  22212  -6003  -1331    688       C  
ATOM   3172  CD2 LEU B  39      20.700  -6.890  46.706  1.00200.55           C  
ANISOU 3172  CD2 LEU B  39    23586  30953  21660  -6225   -685     16       C  
ATOM   3173  N   VAL B  40      17.267 -10.403  47.858  1.00191.40           N  
ANISOU 3173  N   VAL B  40    22384  29176  21164  -4483   -102    208       N  
ATOM   3174  CA  VAL B  40      16.420 -11.148  46.943  1.00172.02           C  
ANISOU 3174  CA  VAL B  40    20005  26703  18653  -4678    -33    411       C  
ATOM   3175  C   VAL B  40      15.137 -10.366  46.700  1.00157.87           C  
ANISOU 3175  C   VAL B  40    18422  24403  17161  -4793   -409    823       C  
ATOM   3176  O   VAL B  40      14.724  -9.522  47.502  1.00156.83           O  
ANISOU 3176  O   VAL B  40    18341  23901  17347  -4524   -660    899       O  
ATOM   3177  CB  VAL B  40      16.104 -12.562  47.473  1.00171.41           C  
ANISOU 3177  CB  VAL B  40    19832  26715  18582  -4089    342    207       C  
ATOM   3178  CG1 VAL B  40      17.289 -13.489  47.257  1.00165.82           C  
ANISOU 3178  CG1 VAL B  40    18918  26543  17543  -4154    685   -164       C  
ATOM   3179  CG2 VAL B  40      15.719 -12.505  48.946  1.00169.32           C  
ANISOU 3179  CG2 VAL B  40    19569  26144  18623  -3361    345     89       C  
ATOM   3180  N   VAL B  41      14.506 -10.652  45.565  1.00140.05           N  
ANISOU 3180  N   VAL B  41    16273  22125  14815  -5211   -454   1076       N  
ATOM   3181  CA  VAL B  41      13.260 -10.009  45.171  1.00139.43           C  
ANISOU 3181  CA  VAL B  41    16403  21563  15012  -5369   -822   1458       C  
ATOM   3182  C   VAL B  41      12.174 -11.074  45.094  1.00126.38           C  
ANISOU 3182  C   VAL B  41    14780  19785  13453  -5025   -608   1515       C  
ATOM   3183  O   VAL B  41      12.435 -12.218  44.703  1.00116.62           O  
ANISOU 3183  O   VAL B  41    13442  18910  11960  -5011   -233   1384       O  
ATOM   3184  CB  VAL B  41      13.413  -9.249  43.833  1.00157.17           C  
ANISOU 3184  CB  VAL B  41    18803  23835  17080  -6237  -1136   1746       C  
ATOM   3185  CG1 VAL B  41      13.852 -10.183  42.709  1.00165.49           C  
ANISOU 3185  CG1 VAL B  41    19798  25341  17740  -6697   -838   1709       C  
ATOM   3186  CG2 VAL B  41      12.127  -8.516  43.470  1.00151.84           C  
ANISOU 3186  CG2 VAL B  41    18356  22607  16729  -6386  -1580   2132       C  
ATOM   3187  N   ARG B  42      10.964 -10.704  45.508  1.00136.07           N  
ANISOU 3187  N   ARG B  42    16135  20506  15061  -4733   -841   1677       N  
ATOM   3188  CA  ARG B  42       9.807 -11.586  45.472  1.00133.82           C  
ANISOU 3188  CA  ARG B  42    15911  20038  14897  -4400   -674   1727       C  
ATOM   3189  C   ARG B  42       8.627 -10.834  44.881  1.00138.57           C  
ANISOU 3189  C   ARG B  42    16722  20144  15786  -4666  -1099   2068       C  
ATOM   3190  O   ARG B  42       8.297  -9.739  45.348  1.00149.12           O  
ANISOU 3190  O   ARG B  42    18122  21086  17449  -4639  -1497   2144       O  
ATOM   3191  CB  ARG B  42       9.421 -12.069  46.871  1.00147.52           C  
ANISOU 3191  CB  ARG B  42    17581  21619  16850  -3615   -476   1457       C  
ATOM   3192  CG  ARG B  42       8.371 -13.150  46.837  1.00151.78           C  
ANISOU 3192  CG  ARG B  42    18181  22062  17427  -3266   -221   1443       C  
ATOM   3193  CD  ARG B  42       7.401 -13.067  48.000  1.00147.27           C  
ANISOU 3193  CD  ARG B  42    17666  21059  17229  -2677   -277   1311       C  
ATOM   3194  NE  ARG B  42       8.026 -13.062  49.314  1.00143.23           N  
ANISOU 3194  NE  ARG B  42    17040  20612  16769  -2228   -158   1008       N  
ATOM   3195  CZ  ARG B  42       7.338 -13.181  50.442  1.00160.46           C  
ANISOU 3195  CZ  ARG B  42    19249  22502  19216  -1701   -121    819       C  
ATOM   3196  NH1 ARG B  42       7.953 -13.167  51.616  1.00177.20           N  
ANISOU 3196  NH1 ARG B  42    21271  24688  21369  -1336    -16    555       N  
ATOM   3197  NH2 ARG B  42       6.024 -13.324  50.389  1.00157.92           N  
ANISOU 3197  NH2 ARG B  42    19060  21819  19126  -1557   -186    876       N  
ATOM   3198  N   LYS B  43       8.001 -11.402  43.848  1.00146.04           N  
ANISOU 3198  N   LYS B  43    17763  21100  16625  -4933  -1030   2267       N  
ATOM   3199  CA  LYS B  43       6.788 -10.795  43.334  1.00146.06           C  
ANISOU 3199  CA  LYS B  43    17974  20594  16930  -5120  -1428   2562       C  
ATOM   3200  C   LYS B  43       5.725 -10.820  44.432  1.00154.61           C  
ANISOU 3200  C   LYS B  43    19075  21238  18431  -4448  -1464   2414       C  
ATOM   3201  O   LYS B  43       5.783 -11.652  45.341  1.00141.82           O  
ANISOU 3201  O   LYS B  43    17341  19766  16780  -3876  -1084   2126       O  
ATOM   3202  CB  LYS B  43       6.295 -11.523  42.082  1.00134.07           C  
ANISOU 3202  CB  LYS B  43    16543  19182  15214  -5475  -1288   2779       C  
ATOM   3203  CG  LYS B  43       5.439 -12.752  42.341  1.00126.76           C  
ANISOU 3203  CG  LYS B  43    15590  18253  14319  -4933   -889   2659       C  
ATOM   3204  CD  LYS B  43       4.884 -13.298  41.031  1.00132.87           C  
ANISOU 3204  CD  LYS B  43    16461  19085  14937  -5336   -806   2922       C  
ATOM   3205  CE  LYS B  43       3.777 -14.312  41.264  1.00135.53           C  
ANISOU 3205  CE  LYS B  43    16824  19294  15378  -4799   -499   2843       C  
ATOM   3206  NZ  LYS B  43       3.287 -14.895  39.985  1.00142.86           N  
ANISOU 3206  NZ  LYS B  43    17823  20320  16138  -5180   -373   3099       N  
ATOM   3207  N   PRO B  44       4.761  -9.902  44.386  1.00161.31           N  
ANISOU 3207  N   PRO B  44    20071  21539  19682  -4526  -1937   2582       N  
ATOM   3208  CA  PRO B  44       3.723  -9.878  45.424  1.00166.77           C  
ANISOU 3208  CA  PRO B  44    20766  21802  20798  -3932  -1988   2392       C  
ATOM   3209  C   PRO B  44       2.984 -11.201  45.552  1.00166.86           C  
ANISOU 3209  C   PRO B  44    20788  21878  20733  -3490  -1541   2240       C  
ATOM   3210  O   PRO B  44       2.630 -11.843  44.562  1.00173.22           O  
ANISOU 3210  O   PRO B  44    21676  22789  21349  -3709  -1397   2408       O  
ATOM   3211  CB  PRO B  44       2.786  -8.761  44.955  1.00171.90           C  
ANISOU 3211  CB  PRO B  44    21582  21876  21855  -4240  -2597   2634       C  
ATOM   3212  CG  PRO B  44       3.666  -7.858  44.174  1.00173.02           C  
ANISOU 3212  CG  PRO B  44    21773  22144  21823  -4905  -2927   2892       C  
ATOM   3213  CD  PRO B  44       4.659  -8.744  43.480  1.00169.70           C  
ANISOU 3213  CD  PRO B  44    21294  22336  20848  -5173  -2490   2913       C  
ATOM   3214  N   SER B  45       2.756 -11.595  46.800  1.00166.14           N  
ANISOU 3214  N   SER B  45    20617  21723  20785  -2877  -1321   1914       N  
ATOM   3215  CA  SER B  45       2.113 -12.865  47.104  1.00155.92           C  
ANISOU 3215  CA  SER B  45    19345  20503  19396  -2408   -879   1716       C  
ATOM   3216  C   SER B  45       0.694 -12.920  46.551  1.00142.26           C  
ANISOU 3216  C   SER B  45    17784  18358  17909  -2418  -1026   1825       C  
ATOM   3217  O   SER B  45      -0.131 -12.046  46.837  1.00146.12           O  
ANISOU 3217  O   SER B  45    18342  18334  18842  -2391  -1433   1812       O  
ATOM   3218  CB  SER B  45       2.111 -13.090  48.612  1.00170.63           C  
ANISOU 3218  CB  SER B  45    21125  22308  21397  -1810   -699   1340       C  
ATOM   3219  OG  SER B  45       3.435 -13.063  49.118  1.00180.56           O  
ANISOU 3219  OG  SER B  45    22231  23940  22434  -1787   -563   1232       O  
ATOM   3220  N   SER B  46       0.409 -13.947  45.750  1.00129.46           N  
ANISOU 3220  N   SER B  46    16217  16959  16012  -2458   -697   1916       N  
ATOM   3221  CA  SER B  46      -0.926 -14.120  45.185  1.00142.12           C  
ANISOU 3221  CA  SER B  46    17985  18203  17810  -2443   -778   2007       C  
ATOM   3222  C   SER B  46      -1.921 -14.580  46.246  1.00151.06           C  
ANISOU 3222  C   SER B  46    19161  19059  19178  -1819   -608   1647       C  
ATOM   3223  O   SER B  46      -2.829 -13.832  46.620  1.00160.78           O  
ANISOU 3223  O   SER B  46    20466  19767  20858  -1729   -966   1554       O  
ATOM   3224  CB  SER B  46      -0.911 -15.128  44.034  1.00148.48           C  
ANISOU 3224  CB  SER B  46    18817  19363  18235  -2662   -432   2206       C  
ATOM   3225  OG  SER B  46      -0.053 -14.706  42.991  1.00159.68           O  
ANISOU 3225  OG  SER B  46    20209  21030  19434  -3308   -592   2519       O  
ATOM   3226  N   SER B  47      -1.746 -15.804  46.733  1.00141.66           N  
ANISOU 3226  N   SER B  47    17925  18214  17687  -1409    -76   1420       N  
ATOM   3227  CA  SER B  47      -2.514 -16.360  47.835  1.00139.02           C  
ANISOU 3227  CA  SER B  47    17641  17698  17481   -828    149   1036       C  
ATOM   3228  C   SER B  47      -1.893 -15.953  49.163  1.00148.96           C  
ANISOU 3228  C   SER B  47    18793  18953  18854   -572    100    768       C  
ATOM   3229  O   SER B  47      -0.741 -15.512  49.229  1.00157.34           O  
ANISOU 3229  O   SER B  47    19724  20258  19798   -773     13    863       O  
ATOM   3230  CB  SER B  47      -2.569 -17.878  47.761  1.00140.01           C  
ANISOU 3230  CB  SER B  47    17787  18206  17204   -523    728    921       C  
ATOM   3231  OG  SER B  47      -1.398 -18.444  48.314  1.00152.33           O  
ANISOU 3231  OG  SER B  47    19213  20222  18444   -374   1017    797       O  
ATOM   3232  N   TRP B  48      -2.672 -16.111  50.235  1.00151.36           N  
ANISOU 3232  N   TRP B  48    19155  18976  19380   -137    168    409       N  
ATOM   3233  CA  TRP B  48      -2.194 -15.698  51.547  1.00141.71           C  
ANISOU 3233  CA  TRP B  48    17836  17706  18303     97    113    143       C  
ATOM   3234  C   TRP B  48      -1.180 -16.677  52.128  1.00127.27           C  
ANISOU 3234  C   TRP B  48    15943  16364  16049    356    548     -4       C  
ATOM   3235  O   TRP B  48      -0.431 -16.297  53.034  1.00133.93           O  
ANISOU 3235  O   TRP B  48    16682  17268  16938    457    498   -141       O  
ATOM   3236  CB  TRP B  48      -3.374 -15.556  52.520  1.00140.85           C  
ANISOU 3236  CB  TRP B  48    17808  17136  18573    430     46   -231       C  
ATOM   3237  CG  TRP B  48      -4.089 -14.226  52.476  1.00147.05           C  
ANISOU 3237  CG  TRP B  48    18571  17384  19917    217   -503   -204       C  
ATOM   3238  CD1 TRP B  48      -4.343 -13.394  53.529  1.00143.96           C  
ANISOU 3238  CD1 TRP B  48    18091  16656  19950    327   -764   -468       C  
ATOM   3239  CD2 TRP B  48      -4.724 -13.629  51.335  1.00162.59           C  
ANISOU 3239  CD2 TRP B  48    20608  19068  22103   -136   -865     73       C  
ATOM   3240  NE1 TRP B  48      -5.048 -12.293  53.103  1.00157.84           N  
ANISOU 3240  NE1 TRP B  48    19837  17947  22187     66  -1283   -374       N  
ATOM   3241  CE2 TRP B  48      -5.300 -12.417  51.762  1.00169.61           C  
ANISOU 3241  CE2 TRP B  48    21442  19446  23558   -218  -1367    -40       C  
ATOM   3242  CE3 TRP B  48      -4.844 -13.994  49.988  1.00161.36           C  
ANISOU 3242  CE3 TRP B  48    20550  19035  21723   -412   -826    408       C  
ATOM   3243  CZ2 TRP B  48      -5.983 -11.567  50.889  1.00174.72           C  
ANISOU 3243  CZ2 TRP B  48    22147  19685  24556   -552  -1859    168       C  
ATOM   3244  CZ3 TRP B  48      -5.520 -13.150  49.126  1.00158.27           C  
ANISOU 3244  CZ3 TRP B  48    20231  18243  21662   -758  -1296    628       C  
ATOM   3245  CH2 TRP B  48      -6.081 -11.952  49.579  1.00166.05           C  
ANISOU 3245  CH2 TRP B  48    21178  18703  23213   -818  -1822    506       C  
ATOM   3246  N   PHE B  49      -1.139 -17.920  51.637  1.00 92.87           N  
ANISOU 3246  N   PHE B  49    11641  12349  11297    467    960     16       N  
ATOM   3247  CA  PHE B  49      -0.246 -18.964  52.148  1.00 85.32           C  
ANISOU 3247  CA  PHE B  49    10633  11840   9944    731   1360   -147       C  
ATOM   3248  C   PHE B  49       0.585 -19.594  51.025  1.00193.77           C  
ANISOU 3248  C   PHE B  49    24272  26065  23285    462   1564    107       C  
ATOM   3249  O   PHE B  49       0.648 -20.817  50.894  1.00 83.63           O  
ANISOU 3249  O   PHE B  49    10342  12426   9009    664   1956     27       O  
ATOM   3250  CB  PHE B  49      -0.982 -20.055  52.926  1.00123.82           C  
ANISOU 3250  CB  PHE B  49    15663  16679  14704   1213   1712   -483       C  
ATOM   3251  CG  PHE B  49      -2.434 -20.165  52.598  1.00121.00           C  
ANISOU 3251  CG  PHE B  49    15471  15974  14527   1281   1708   -527       C  
ATOM   3252  CD1 PHE B  49      -2.851 -20.830  51.463  1.00127.06           C  
ANISOU 3252  CD1 PHE B  49    16291  16891  15094   1171   1899   -323       C  
ATOM   3253  CD2 PHE B  49      -3.385 -19.616  53.443  1.00125.60           C  
ANISOU 3253  CD2 PHE B  49    16147  16085  15491   1451   1524   -804       C  
ATOM   3254  CE1 PHE B  49      -4.192 -20.928  51.158  1.00138.69           C  
ANISOU 3254  CE1 PHE B  49    17921  18036  16738   1248   1899   -380       C  
ATOM   3255  CE2 PHE B  49      -4.727 -19.715  53.149  1.00126.05           C  
ANISOU 3255  CE2 PHE B  49    16354  15811  15730   1517   1515   -897       C  
ATOM   3256  CZ  PHE B  49      -5.134 -20.374  52.006  1.00136.16           C  
ANISOU 3256  CZ  PHE B  49    17701  17233  16799   1428   1705   -683       C  
ATOM   3257  N   TRP B  50       1.242 -18.773  50.200  1.00130.41           N  
ANISOU 3257  N   TRP B  50    16139  18126  15285    -19   1298    399       N  
ATOM   3258  CA  TRP B  50       2.201 -19.278  49.214  1.00128.62           C  
ANISOU 3258  CA  TRP B  50    15786  18394  14691   -336   1477    588       C  
ATOM   3259  C   TRP B  50       3.301 -18.243  49.080  1.00134.88           C  
ANISOU 3259  C   TRP B  50    16446  19284  15519   -721   1183    712       C  
ATOM   3260  O   TRP B  50       3.022 -17.086  48.752  1.00135.21           O  
ANISOU 3260  O   TRP B  50    16528  19015  15832  -1040    778    907       O  
ATOM   3261  CB  TRP B  50       1.578 -19.505  47.825  1.00137.46           C  
ANISOU 3261  CB  TRP B  50    16961  19534  15736   -680   1502    888       C  
ATOM   3262  CG  TRP B  50       0.718 -20.716  47.641  1.00146.36           C  
ANISOU 3262  CG  TRP B  50    18180  20722  16708   -378   1882    813       C  
ATOM   3263  CD1 TRP B  50       0.796 -21.901  48.311  1.00149.36           C  
ANISOU 3263  CD1 TRP B  50    18561  21336  16853     81   2286    541       C  
ATOM   3264  CD2 TRP B  50      -0.361 -20.853  46.709  1.00145.49           C  
ANISOU 3264  CD2 TRP B  50    18190  20429  16663   -520   1884   1014       C  
ATOM   3265  NE1 TRP B  50      -0.178 -22.763  47.863  1.00140.17           N  
ANISOU 3265  NE1 TRP B  50    17506  20160  15594    241   2554    557       N  
ATOM   3266  CE2 TRP B  50      -0.899 -22.141  46.878  1.00133.36           C  
ANISOU 3266  CE2 TRP B  50    16710  19045  14915   -115   2327    843       C  
ATOM   3267  CE3 TRP B  50      -0.923 -20.008  45.748  1.00159.38           C  
ANISOU 3267  CE3 TRP B  50    20024  21898  18635   -955   1541   1320       C  
ATOM   3268  CZ2 TRP B  50      -1.972 -22.601  46.128  1.00142.95           C  
ANISOU 3268  CZ2 TRP B  50    18041  20147  16127   -114   2465    962       C  
ATOM   3269  CZ3 TRP B  50      -1.990 -20.466  45.006  1.00166.04           C  
ANISOU 3269  CZ3 TRP B  50    20988  22608  19491   -959   1657   1439       C  
ATOM   3270  CH2 TRP B  50      -2.505 -21.750  45.201  1.00162.91           C  
ANISOU 3270  CH2 TRP B  50    20632  22384  18881   -533   2131   1257       C  
ATOM   3271  N   LYS B  51       4.547 -18.665  49.303  1.00139.75           N  
ANISOU 3271  N   LYS B  51    16910  20328  15860   -700   1376    585       N  
ATOM   3272  CA  LYS B  51       5.678 -17.769  49.139  1.00145.39           C  
ANISOU 3272  CA  LYS B  51    17496  21192  16555  -1070   1147    664       C  
ATOM   3273  C   LYS B  51       6.304 -17.998  47.771  1.00136.04           C  
ANISOU 3273  C   LYS B  51    16218  20394  15076  -1609   1220    878       C  
ATOM   3274  O   LYS B  51       6.917 -19.057  47.553  1.00136.61           O  
ANISOU 3274  O   LYS B  51    16170  20900  14836  -1551   1569    753       O  
ATOM   3275  CB  LYS B  51       6.708 -17.994  50.247  1.00156.64           C  
ANISOU 3275  CB  LYS B  51    18805  22827  17883   -742   1286    355       C  
ATOM   3276  CG  LYS B  51       6.887 -16.805  51.186  1.00157.76           C  
ANISOU 3276  CG  LYS B  51    18940  22672  18330   -669    970    291       C  
ATOM   3277  CD  LYS B  51       7.771 -17.175  52.361  1.00154.45           C  
ANISOU 3277  CD  LYS B  51    18432  22433  17820   -279   1147    -33       C  
ATOM   3278  CE  LYS B  51       7.974 -16.006  53.311  1.00154.37           C  
ANISOU 3278  CE  LYS B  51    18390  22151  18112   -207    864    -95       C  
ATOM   3279  NZ  LYS B  51       6.696 -15.453  53.845  1.00156.10           N  
ANISOU 3279  NZ  LYS B  51    18729  21857  18725    -41    658    -84       N  
ATOM   3280  N   PRO B  52       6.175 -17.068  46.828  1.00129.27           N  
ANISOU 3280  N   PRO B  52    15410  19400  14307  -2157    895   1183       N  
ATOM   3281  CA  PRO B  52       6.874 -17.216  45.549  1.00133.55           C  
ANISOU 3281  CA  PRO B  52    15863  20327  14552  -2747    953   1364       C  
ATOM   3282  C   PRO B  52       8.382 -17.200  45.750  1.00146.81           C  
ANISOU 3282  C   PRO B  52    17351  22433  15999  -2879   1044   1166       C  
ATOM   3283  O   PRO B  52       8.899 -16.581  46.683  1.00136.11           O  
ANISOU 3283  O   PRO B  52    15963  20986  14764  -2681    906   1005       O  
ATOM   3284  CB  PRO B  52       6.384 -16.018  44.728  1.00135.15           C  
ANISOU 3284  CB  PRO B  52    16209  20193  14947  -3285    495   1711       C  
ATOM   3285  CG  PRO B  52       5.741 -15.096  45.707  1.00125.94           C  
ANISOU 3285  CG  PRO B  52    15147  18511  14192  -2974    165   1666       C  
ATOM   3286  CD  PRO B  52       5.225 -15.946  46.813  1.00122.15           C  
ANISOU 3286  CD  PRO B  52    14665  17959  13788  -2273    462   1373       C  
ATOM   3287  N   ARG B  53       9.079 -17.928  44.874  1.00156.71           N  
ANISOU 3287  N   ARG B  53    18460  24160  16921  -3209   1297   1151       N  
ATOM   3288  CA  ARG B  53      10.527 -18.091  44.962  1.00167.08           C  
ANISOU 3288  CA  ARG B  53    19566  25924  17992  -3348   1429    900       C  
ATOM   3289  C   ARG B  53      11.237 -16.751  45.112  1.00176.10           C  
ANISOU 3289  C   ARG B  53    20725  26973  19213  -3670   1076    930       C  
ATOM   3290  O   ARG B  53      10.837 -15.744  44.519  1.00183.57           O  
ANISOU 3290  O   ARG B  53    21813  27659  20279  -4104    728   1225       O  
ATOM   3291  CB  ARG B  53      11.042 -18.782  43.699  1.00167.20           C  
ANISOU 3291  CB  ARG B  53    19431  26408  17689  -3867   1654    940       C  
ATOM   3292  CG  ARG B  53      10.514 -20.180  43.450  1.00161.39           C  
ANISOU 3292  CG  ARG B  53    18627  25860  16833  -3596   2043    896       C  
ATOM   3293  CD  ARG B  53      10.695 -20.550  41.981  1.00158.75           C  
ANISOU 3293  CD  ARG B  53    18183  25871  16263  -4252   2169   1066       C  
ATOM   3294  NE  ARG B  53      12.092 -20.471  41.562  1.00169.25           N  
ANISOU 3294  NE  ARG B  53    19295  27652  17361  -4722   2210    862       N  
ATOM   3295  CZ  ARG B  53      12.780 -21.480  41.035  1.00179.87           C  
ANISOU 3295  CZ  ARG B  53    20377  29502  18463  -4890   2539    655       C  
ATOM   3296  NH1 ARG B  53      12.203 -22.658  40.839  1.00183.73           N  
ANISOU 3296  NH1 ARG B  53    20789  30122  18897  -4621   2861    659       N  
ATOM   3297  NH2 ARG B  53      14.050 -21.306  40.695  1.00181.34           N  
ANISOU 3297  NH2 ARG B  53    20367  30068  18464  -5339   2545    420       N  
ATOM   3298  N   TYR B  54      12.307 -16.745  45.904  1.00175.09           N  
ANISOU 3298  N   TYR B  54    20458  27055  19014  -3458   1157    616       N  
ATOM   3299  CA  TYR B  54      13.120 -15.549  46.088  1.00165.99           C  
ANISOU 3299  CA  TYR B  54    19295  25879  17893  -3736    877    597       C  
ATOM   3300  C   TYR B  54      14.218 -15.545  45.035  1.00171.11           C  
ANISOU 3300  C   TYR B  54    19814  26988  18211  -4399    936    541       C  
ATOM   3301  O   TYR B  54      15.141 -16.365  45.091  1.00174.81           O  
ANISOU 3301  O   TYR B  54    20081  27879  18459  -4332   1229    218       O  
ATOM   3302  CB  TYR B  54      13.723 -15.505  47.487  1.00154.37           C  
ANISOU 3302  CB  TYR B  54    17743  24393  16519  -3179    938    276       C  
ATOM   3303  CG  TYR B  54      12.741 -15.146  48.564  1.00141.17           C  
ANISOU 3303  CG  TYR B  54    16204  22232  15201  -2654    796    325       C  
ATOM   3304  CD1 TYR B  54      11.381 -15.067  48.297  1.00146.60           C  
ANISOU 3304  CD1 TYR B  54    17058  22544  16098  -2623    669    585       C  
ATOM   3305  CD2 TYR B  54      13.175 -14.854  49.841  1.00128.46           C  
ANISOU 3305  CD2 TYR B  54    14548  20532  13729  -2218    782     93       C  
ATOM   3306  CE1 TYR B  54      10.488 -14.737  49.283  1.00144.37           C  
ANISOU 3306  CE1 TYR B  54    16878  21822  16153  -2176    541    573       C  
ATOM   3307  CE2 TYR B  54      12.293 -14.513  50.825  1.00137.14           C  
ANISOU 3307  CE2 TYR B  54    15749  21199  15158  -1790    658    110       C  
ATOM   3308  CZ  TYR B  54      10.951 -14.456  50.548  1.00149.71           C  
ANISOU 3308  CZ  TYR B  54    17493  22432  16957  -1776    538    334       C  
ATOM   3309  OH  TYR B  54      10.078 -14.119  51.554  1.00167.76           O  
ANISOU 3309  OH  TYR B  54    19862  24292  19587  -1371    418    291       O  
ATOM   3310  N   LYS B  55      14.125 -14.632  44.077  1.00168.50           N  
ANISOU 3310  N   LYS B  55    19602  26573  17849  -5059    643    830       N  
ATOM   3311  CA  LYS B  55      15.165 -14.473  43.072  1.00178.68           C  
ANISOU 3311  CA  LYS B  55    20799  28276  18816  -5778    661    766       C  
ATOM   3312  C   LYS B  55      16.129 -13.368  43.478  1.00185.09           C  
ANISOU 3312  C   LYS B  55    21608  29111  19605  -5955    438    635       C  
ATOM   3313  O   LYS B  55      15.745 -12.390  44.120  1.00185.53           O  
ANISOU 3313  O   LYS B  55    21798  28776  19917  -5765    135    778       O  
ATOM   3314  CB  LYS B  55      14.575 -14.182  41.688  1.00185.24           C  
ANISOU 3314  CB  LYS B  55    21780  29039  19563  -6488    483   1147       C  
ATOM   3315  CG  LYS B  55      14.034 -15.421  41.003  1.00178.24           C  
ANISOU 3315  CG  LYS B  55    20817  28338  18569  -6491    803   1202       C  
ATOM   3316  CD  LYS B  55      13.293 -15.109  39.722  1.00171.34           C  
ANISOU 3316  CD  LYS B  55    20119  27322  17660  -7135    609   1614       C  
ATOM   3317  CE  LYS B  55      12.983 -16.403  38.990  1.00165.63           C  
ANISOU 3317  CE  LYS B  55    19262  26892  16779  -7190    992   1621       C  
ATOM   3318  NZ  LYS B  55      14.222 -17.208  38.793  1.00160.63           N  
ANISOU 3318  NZ  LYS B  55    18322  26862  15848  -7358   1347   1233       N  
ATOM   3319  N   CYS B  56      17.385 -13.534  43.081  1.00189.77           N  
ANISOU 3319  N   CYS B  56    22036  30174  19894  -6334    595    342       N  
ATOM   3320  CA  CYS B  56      18.455 -12.600  43.395  1.00195.75           C  
ANISOU 3320  CA  CYS B  56    22770  31040  20565  -6532    448    149       C  
ATOM   3321  C   CYS B  56      18.636 -11.585  42.262  1.00203.59           C  
ANISOU 3321  C   CYS B  56    23926  32046  21383  -7424    142    390       C  
ATOM   3322  O   CYS B  56      18.219 -11.812  41.124  1.00210.57           O  
ANISOU 3322  O   CYS B  56    24884  32987  22136  -7966    120    615       O  
ATOM   3323  CB  CYS B  56      19.758 -13.362  43.666  1.00190.06           C  
ANISOU 3323  CB  CYS B  56    21777  30817  19619  -6422    789   -377       C  
ATOM   3324  SG  CYS B  56      19.764 -15.104  43.131  1.00181.93           S  
ANISOU 3324  SG  CYS B  56    20518  30181  18427  -6350   1230   -589       S  
ATOM   3325  N   VAL B  57      19.234 -10.436  42.598  1.00204.43           N  
ANISOU 3325  N   VAL B  57    24104  32082  21488  -7578   -107    352       N  
ATOM   3326  CA  VAL B  57      19.510  -9.363  41.639  1.00205.93           C  
ANISOU 3326  CA  VAL B  57    24480  32275  21490  -8424   -434    549       C  
ATOM   3327  C   VAL B  57      20.992  -9.272  41.287  1.00212.47           C  
ANISOU 3327  C   VAL B  57    25179  33612  21939  -8911   -282    141       C  
ATOM   3328  O   VAL B  57      21.385  -8.372  40.526  1.00208.83           O  
ANISOU 3328  O   VAL B  57    24878  33204  21262  -9655   -531    236       O  
ATOM   3329  CB  VAL B  57      18.998  -8.000  42.163  1.00197.97           C  
ANISOU 3329  CB  VAL B  57    23683  30778  20760  -8325   -889    846       C  
ATOM   3330  CG1 VAL B  57      18.664  -7.041  41.016  1.00197.58           C  
ANISOU 3330  CG1 VAL B  57    23912  30551  20608  -9167  -1316   1229       C  
ATOM   3331  CG2 VAL B  57      17.784  -8.178  43.067  1.00192.09           C  
ANISOU 3331  CG2 VAL B  57    22962  29567  20456  -7565   -948   1035       C  
ATOM   3332  N   ASN B  58      21.819 -10.181  41.808  1.00218.62           N  
ANISOU 3332  N   ASN B  58    25682  34755  22627  -8533    106   -333       N  
ATOM   3333  CA  ASN B  58      23.263 -10.250  41.559  1.00217.88           C  
ANISOU 3333  CA  ASN B  58    25418  35164  22201  -8919    296   -825       C  
ATOM   3334  C   ASN B  58      23.934  -8.901  41.834  1.00222.31           C  
ANISOU 3334  C   ASN B  58    26108  35668  22690  -9153     35   -868       C  
ATOM   3335  O   ASN B  58      24.529  -8.267  40.956  1.00223.40           O  
ANISOU 3335  O   ASN B  58    26350  36006  22524  -9957    -93   -908       O  
ATOM   3336  CB  ASN B  58      23.559 -10.756  40.138  1.00216.41           C  
ANISOU 3336  CB  ASN B  58    25184  35361  21682  -9765    420   -893       C  
ATOM   3337  CG  ASN B  58      23.203 -12.240  39.945  1.00211.54           C  
ANISOU 3337  CG  ASN B  58    24346  34929  21101  -9494    770   -990       C  
ATOM   3338  OD1 ASN B  58      23.204 -13.030  40.894  1.00208.18           O  
ANISOU 3338  OD1 ASN B  58    23745  34503  20851  -8716    995  -1207       O  
ATOM   3339  ND2 ASN B  58      22.888 -12.613  38.708  1.00213.71           N  
ANISOU 3339  ND2 ASN B  58    24640  35358  21203 -10155    809   -822       N  
ATOM   3340  N   LEU B  59      23.816  -8.467  43.086  1.00218.63           N  
ANISOU 3340  N   LEU B  59    25639  34926  22505  -8445    -39   -861       N  
ATOM   3341  CA  LEU B  59      24.407  -7.217  43.557  1.00225.93           C  
ANISOU 3341  CA  LEU B  59    26653  35776  23416  -8512   -258   -903       C  
ATOM   3342  C   LEU B  59      24.317  -7.177  45.082  1.00250.81           C  
ANISOU 3342  C   LEU B  59    29698  38696  26902  -7582   -198   -993       C  
ATOM   3343  O   LEU B  59      23.690  -8.033  45.712  1.00251.20           O  
ANISOU 3343  O   LEU B  59    29657  38599  27190  -6948    -37   -978       O  
ATOM   3344  CB  LEU B  59      23.750  -6.004  42.888  1.00209.47           C  
ANISOU 3344  CB  LEU B  59    24876  33364  21349  -9084   -723   -410       C  
ATOM   3345  CG  LEU B  59      22.236  -5.800  42.922  1.00194.60           C  
ANISOU 3345  CG  LEU B  59    23168  30942  19828  -8867  -1016    128       C  
ATOM   3346  CD1 LEU B  59      21.852  -4.822  44.013  1.00188.55           C  
ANISOU 3346  CD1 LEU B  59    22457  29763  19421  -8355  -1282    295       C  
ATOM   3347  CD2 LEU B  59      21.734  -5.285  41.574  1.00192.55           C  
ANISOU 3347  CD2 LEU B  59    23177  30569  19413  -9734  -1346    512       C  
ATOM   3348  N   SER B  60      24.999  -6.204  45.669  1.00236.04           N  
ANISOU 3348  N   SER B  60    27838  36820  25025  -7528   -308  -1116       N  
ATOM   3349  CA  SER B  60      25.079  -5.989  47.105  1.00233.05           C  
ANISOU 3349  CA  SER B  60    27358  36256  24936  -6740   -261  -1223       C  
ATOM   3350  C   SER B  60      24.102  -4.893  47.496  1.00234.76           C  
ANISOU 3350  C   SER B  60    27745  35968  25485  -6615   -649   -753       C  
ATOM   3351  O   SER B  60      23.245  -4.499  46.707  1.00238.04           O  
ANISOU 3351  O   SER B  60    28353  36144  25946  -7038   -942   -348       O  
ATOM   3352  CB  SER B  60      26.517  -5.653  47.507  1.00234.88           C  
ANISOU 3352  CB  SER B  60    27461  36833  24949  -6751   -102  -1698       C  
ATOM   3353  OG  SER B  60      26.583  -5.171  48.838  1.00233.63           O  
ANISOU 3353  OG  SER B  60    27237  36463  25069  -6087   -117  -1733       O  
ATOM   3354  N   ILE B  61      24.226  -4.404  48.726  1.00254.64           N  
ANISOU 3354  N   ILE B  61    30180  38315  28255  -6038   -660   -820       N  
ATOM   3355  CA  ILE B  61      23.323  -3.382  49.243  1.00229.88           C  
ANISOU 3355  CA  ILE B  61    27149  34703  25494  -5856  -1016   -431       C  
ATOM   3356  C   ILE B  61      24.010  -2.027  49.383  1.00239.11           C  
ANISOU 3356  C   ILE B  61    28359  35896  26595  -6117  -1232   -425       C  
ATOM   3357  O   ILE B  61      23.319  -1.007  49.545  1.00239.57           O  
ANISOU 3357  O   ILE B  61    28521  35580  26925  -6155  -1603    -76       O  
ATOM   3358  CB  ILE B  61      22.697  -3.823  50.587  1.00199.08           C  
ANISOU 3358  CB  ILE B  61    23120  30521  22001  -4995   -895   -456       C  
ATOM   3359  CG1 ILE B  61      22.055  -5.202  50.433  1.00173.51           C  
ANISOU 3359  CG1 ILE B  61    19859  27283  18785  -4747   -667   -484       C  
ATOM   3360  CG2 ILE B  61      21.619  -2.866  51.076  1.00198.97           C  
ANISOU 3360  CG2 ILE B  61    23184  29994  22423  -4827  -1265    -76       C  
ATOM   3361  CD1 ILE B  61      22.688  -6.275  51.275  1.00149.38           C  
ANISOU 3361  CD1 ILE B  61    16616  24460  15681  -4177   -267   -908       C  
ATOM   3362  N   LYS B  62      25.339  -1.977  49.289  1.00237.76           N  
ANISOU 3362  N   LYS B  62    28111  36153  26073  -6319  -1023   -815       N  
ATOM   3363  CA  LYS B  62      26.049  -0.706  49.322  1.00248.54           C  
ANISOU 3363  CA  LYS B  62    29535  37585  27313  -6623  -1206   -832       C  
ATOM   3364  C   LYS B  62      25.859   0.094  48.037  1.00276.57           C  
ANISOU 3364  C   LYS B  62    33350  41102  30633  -7503  -1571   -533       C  
ATOM   3365  O   LYS B  62      26.020   1.318  48.064  1.00274.17           O  
ANISOU 3365  O   LYS B  62    33155  40691  30329  -7748  -1860   -380       O  
ATOM   3366  CB  LYS B  62      27.544  -0.923  49.592  1.00231.32           C  
ANISOU 3366  CB  LYS B  62    27201  35879  24811  -6582   -856  -1389       C  
ATOM   3367  CG  LYS B  62      28.412  -1.080  48.351  1.00219.41           C  
ANISOU 3367  CG  LYS B  62    25773  34805  22790  -7376   -773  -1647       C  
ATOM   3368  CD  LYS B  62      28.240  -2.452  47.734  1.00212.59           C  
ANISOU 3368  CD  LYS B  62    24840  34121  21815  -7458   -539  -1788       C  
ATOM   3369  CE  LYS B  62      28.462  -2.409  46.236  1.00208.17           C  
ANISOU 3369  CE  LYS B  62    24440  33806  20851  -8416   -628  -1774       C  
ATOM   3370  NZ  LYS B  62      28.376  -3.765  45.634  1.00199.82           N  
ANISOU 3370  NZ  LYS B  62    23269  32969  19685  -8508   -366  -1946       N  
ATOM   3371  N   ASP B  63      25.544  -0.572  46.920  1.00251.59           N  
ANISOU 3371  N   ASP B  63    30296  38032  27266  -7996  -1567   -452       N  
ATOM   3372  CA  ASP B  63      25.312   0.074  45.628  1.00256.67           C  
ANISOU 3372  CA  ASP B  63    31218  38630  27675  -8883  -1919   -158       C  
ATOM   3373  C   ASP B  63      24.464   1.338  45.744  1.00263.89           C  
ANISOU 3373  C   ASP B  63    32321  39056  28891  -8958  -2443    321       C  
ATOM   3374  O   ASP B  63      24.693   2.313  45.021  1.00272.89           O  
ANISOU 3374  O   ASP B  63    33688  40189  29810  -9640  -2772    476       O  
ATOM   3375  CB  ASP B  63      24.645  -0.907  44.662  1.00252.64           C  
ANISOU 3375  CB  ASP B  63    30773  38129  27089  -9188  -1866    -18       C  
ATOM   3376  CG  ASP B  63      25.211  -0.816  43.260  1.00252.75           C  
ANISOU 3376  CG  ASP B  63    30961  38460  26613 -10180  -1919    -77       C  
ATOM   3377  OD1 ASP B  63      26.226  -1.491  42.991  1.00252.44           O  
ANISOU 3377  OD1 ASP B  63    30777  38904  26235 -10369  -1553   -540       O  
ATOM   3378  OD2 ASP B  63      24.654  -0.061  42.435  1.00253.25           O  
ANISOU 3378  OD2 ASP B  63    31306  38283  26634 -10792  -2341    318       O  
ATOM   3379  N   ILE B  64      23.481   1.336  46.644  1.00300.62           N  
ANISOU 3379  N   ILE B  64    36882  43290  34049  -8289  -2542    537       N  
ATOM   3380  CA  ILE B  64      22.644   2.507  46.867  1.00263.06           C  
ANISOU 3380  CA  ILE B  64    32248  38047  29656  -8291  -3046    945       C  
ATOM   3381  C   ILE B  64      23.039   3.237  48.143  1.00272.90           C  
ANISOU 3381  C   ILE B  64    33309  39235  31144  -7744  -3020    822       C  
ATOM   3382  O   ILE B  64      22.288   4.092  48.622  1.00268.92           O  
ANISOU 3382  O   ILE B  64    32814  38311  31051  -7558  -3382   1107       O  
ATOM   3383  CB  ILE B  64      21.145   2.160  46.871  1.00214.34           C  
ANISOU 3383  CB  ILE B  64    26122  31397  23919  -8034  -3256   1288       C  
ATOM   3384  CG1 ILE B  64      20.729   1.485  48.184  1.00193.04           C  
ANISOU 3384  CG1 ILE B  64    23164  28568  21613  -7111  -2966   1136       C  
ATOM   3385  CG2 ILE B  64      20.799   1.323  45.649  1.00198.35           C  
ANISOU 3385  CG2 ILE B  64    24251  29469  21644  -8526  -3210   1387       C  
ATOM   3386  CD1 ILE B  64      20.780  -0.018  48.153  1.00132.79           C  
ANISOU 3386  CD1 ILE B  64    15424  21187  13843  -6833  -2502    895       C  
ATOM   3387  N   LEU B  65      24.162   2.867  48.746  1.00268.69           N  
ANISOU 3387  N   LEU B  65    32586  39101  30403  -7449  -2594    389       N  
ATOM   3388  CA  LEU B  65      24.690   3.580  49.892  1.00263.82           C  
ANISOU 3388  CA  LEU B  65    31798  38486  29957  -6990  -2536    249       C  
ATOM   3389  C   LEU B  65      25.953   4.355  49.510  1.00268.34           C  
ANISOU 3389  C   LEU B  65    32444  39425  30087  -7485  -2524     37       C  
ATOM   3390  O   LEU B  65      26.447   4.298  48.380  1.00273.79           O  
ANISOU 3390  O   LEU B  65    33318  40381  30329  -8194  -2545    -36       O  
ATOM   3391  CB  LEU B  65      24.998   2.588  51.012  1.00255.14           C  
ANISOU 3391  CB  LEU B  65    30427  37524  28992  -6207  -2064   -102       C  
ATOM   3392  CG  LEU B  65      23.842   1.788  51.601  1.00247.03           C  
ANISOU 3392  CG  LEU B  65    29313  36160  28387  -5637  -2017     33       C  
ATOM   3393  CD1 LEU B  65      24.309   1.069  52.854  1.00242.34           C  
ANISOU 3393  CD1 LEU B  65    28475  35695  27909  -4889  -1599   -324       C  
ATOM   3394  CD2 LEU B  65      22.645   2.677  51.879  1.00244.36           C  
ANISOU 3394  CD2 LEU B  65    29024  35294  28529  -5558  -2463    451       C  
ATOM   3395  N   GLU B  66      26.462   5.098  50.484  1.00264.61           N  
ANISOU 3395  N   GLU B  66    31827  38967  29747  -7115  -2482    -72       N  
ATOM   3396  CA  GLU B  66      27.684   5.896  50.439  1.00261.16           C  
ANISOU 3396  CA  GLU B  66    31414  38866  28951  -7406  -2420   -315       C  
ATOM   3397  C   GLU B  66      28.971   5.066  50.551  1.00258.29           C  
ANISOU 3397  C   GLU B  66    30915  39021  28203  -7302  -1897   -897       C  
ATOM   3398  O   GLU B  66      29.912   5.293  49.779  1.00258.90           O  
ANISOU 3398  O   GLU B  66    31116  39459  27793  -7900  -1838  -1144       O  
ATOM   3399  CB  GLU B  66      27.649   6.966  51.531  1.00259.23           C  
ANISOU 3399  CB  GLU B  66    31026  38414  29054  -6970  -2556   -199       C  
ATOM   3400  CG  GLU B  66      28.600   8.121  51.271  1.00262.23           C  
ANISOU 3400  CG  GLU B  66    31514  39024  29097  -7418  -2667   -282       C  
ATOM   3401  CD  GLU B  66      28.225   8.925  50.033  1.00264.30           C  
ANISOU 3401  CD  GLU B  66    32118  39148  29155  -8276  -3173     65       C  
ATOM   3402  OE1 GLU B  66      27.040   8.909  49.635  1.00263.97           O  
ANISOU 3402  OE1 GLU B  66    32192  38703  29401  -8399  -3537    467       O  
ATOM   3403  OE2 GLU B  66      29.121   9.580  49.458  1.00263.71           O  
ANISOU 3403  OE2 GLU B  66    32212  39361  28625  -8841  -3214    -80       O  
ATOM   3404  N   PRO B  67      29.068   4.115  51.521  1.00251.44           N  
ANISOU 3404  N   PRO B  67    29797  38196  27543  -6565  -1523  -1157       N  
ATOM   3405  CA  PRO B  67      30.314   3.357  51.730  1.00256.26           C  
ANISOU 3405  CA  PRO B  67    30260  39264  27843  -6408  -1060  -1743       C  
ATOM   3406  C   PRO B  67      31.058   2.828  50.522  1.00271.99           C  
ANISOU 3406  C   PRO B  67    32361  41669  29314  -7092   -923  -2058       C  
ATOM   3407  O   PRO B  67      30.466   2.377  49.537  1.00275.94           O  
ANISOU 3407  O   PRO B  67    33002  42123  29719  -7547  -1052  -1866       O  
ATOM   3408  CB  PRO B  67      29.845   2.166  52.577  1.00251.79           C  
ANISOU 3408  CB  PRO B  67    29500  38569  27601  -5667   -805  -1832       C  
ATOM   3409  CG  PRO B  67      28.361   2.105  52.350  1.00252.34           C  
ANISOU 3409  CG  PRO B  67    29672  38196  28009  -5665  -1112  -1322       C  
ATOM   3410  CD  PRO B  67      27.995   3.538  52.335  1.00251.36           C  
ANISOU 3410  CD  PRO B  67    29656  37816  28032  -5908  -1517   -954       C  
ATOM   3411  N   ASP B  68      32.383   2.876  50.632  1.00274.15           N  
ANISOU 3411  N   ASP B  68    32551  42353  29259  -7159   -645  -2576       N  
ATOM   3412  CA  ASP B  68      33.295   2.336  49.638  1.00281.10           C  
ANISOU 3412  CA  ASP B  68    33473  43685  29648  -7763   -447  -3023       C  
ATOM   3413  C   ASP B  68      33.963   1.089  50.200  1.00279.59           C  
ANISOU 3413  C   ASP B  68    33018  43741  29471  -7241    -14  -3565       C  
ATOM   3414  O   ASP B  68      35.093   1.152  50.691  1.00281.00           O  
ANISOU 3414  O   ASP B  68    33067  44202  29498  -7053    239  -4065       O  
ATOM   3415  CB  ASP B  68      34.342   3.372  49.234  1.00288.89           C  
ANISOU 3415  CB  ASP B  68    34585  44966  30215  -8326   -480  -3270       C  
ATOM   3416  CG  ASP B  68      35.107   2.967  47.989  1.00299.04           C  
ANISOU 3416  CG  ASP B  68    35968  46679  30975  -9153   -361  -3670       C  
ATOM   3417  OD1 ASP B  68      34.990   1.796  47.566  1.00301.84           O  
ANISOU 3417  OD1 ASP B  68    36226  47151  31306  -9196   -188  -3838       O  
ATOM   3418  OD2 ASP B  68      35.810   3.828  47.421  1.00305.09           O  
ANISOU 3418  OD2 ASP B  68    36907  47668  31347  -9788   -444  -3823       O  
ATOM   3419  N   TYR B  83      30.953  -4.680  56.044  1.00236.70           N  
ANISOU 3419  N   TYR B  83    26766  37063  26104  -2675    859  -3614       N  
ATOM   3420  CA  TYR B  83      31.050  -5.181  57.411  1.00237.78           C  
ANISOU 3420  CA  TYR B  83    26797  37054  26497  -1920   1014  -3794       C  
ATOM   3421  C   TYR B  83      31.531  -6.623  57.455  1.00237.84           C  
ANISOU 3421  C   TYR B  83    26717  37256  26398  -1678   1246  -4228       C  
ATOM   3422  O   TYR B  83      32.330  -7.049  56.622  1.00246.12           O  
ANISOU 3422  O   TYR B  83    27710  38663  27143  -2053   1354  -4582       O  
ATOM   3423  CB  TYR B  83      29.703  -5.076  58.119  1.00239.40           C  
ANISOU 3423  CB  TYR B  83    27064  36798  27099  -1547    865  -3340       C  
ATOM   3424  CG  TYR B  83      29.451  -3.736  58.755  1.00244.24           C  
ANISOU 3424  CG  TYR B  83    27672  37179  27951  -1467    692  -3058       C  
ATOM   3425  CD1 TYR B  83      30.450  -2.777  58.826  1.00250.16           C  
ANISOU 3425  CD1 TYR B  83    28362  38133  28556  -1623    710  -3223       C  
ATOM   3426  CD2 TYR B  83      28.217  -3.436  59.297  1.00245.78           C  
ANISOU 3426  CD2 TYR B  83    27905  36956  28524  -1235    517  -2657       C  
ATOM   3427  CE1 TYR B  83      30.217  -1.550  59.413  1.00254.07           C  
ANISOU 3427  CE1 TYR B  83    28828  38425  29281  -1544    553  -2960       C  
ATOM   3428  CE2 TYR B  83      27.974  -2.218  59.886  1.00250.27           C  
ANISOU 3428  CE2 TYR B  83    28431  37314  29347  -1170    348  -2419       C  
ATOM   3429  CZ  TYR B  83      28.973  -1.277  59.942  1.00256.64           C  
ANISOU 3429  CZ  TYR B  83    29170  38333  30009  -1319    365  -2555       C  
ATOM   3430  OH  TYR B  83      28.721  -0.061  60.532  1.00262.15           O  
ANISOU 3430  OH  TYR B  83    29803  38828  30972  -1249    197  -2311       O  
ATOM   3431  N   ASP B  84      31.033  -7.370  58.437  1.00238.15           N  
ANISOU 3431  N   ASP B  84    26742  37051  26694  -1068   1310  -4215       N  
ATOM   3432  CA  ASP B  84      31.391  -8.770  58.599  1.00227.81           C  
ANISOU 3432  CA  ASP B  84    25364  35869  25324   -776   1491  -4600       C  
ATOM   3433  C   ASP B  84      30.243  -9.488  59.292  1.00244.89           C  
ANISOU 3433  C   ASP B  84    27612  37677  27758   -309   1467  -4342       C  
ATOM   3434  O   ASP B  84      29.368  -8.862  59.899  1.00234.20           O  
ANISOU 3434  O   ASP B  84    26333  35985  26666   -123   1343  -3968       O  
ATOM   3435  CB  ASP B  84      32.696  -8.931  59.390  1.00204.60           C  
ANISOU 3435  CB  ASP B  84    22294  33104  22340   -429   1653  -5143       C  
ATOM   3436  CG  ASP B  84      33.616  -9.985  58.795  1.00192.76           C  
ANISOU 3436  CG  ASP B  84    20679  31962  20598   -565   1802  -5685       C  
ATOM   3437  OD1 ASP B  84      33.324 -10.474  57.682  1.00192.70           O  
ANISOU 3437  OD1 ASP B  84    20677  32115  20427  -1004   1795  -5634       O  
ATOM   3438  OD2 ASP B  84      34.633 -10.323  59.438  1.00185.09           O  
ANISOU 3438  OD2 ASP B  84    19601  31107  19618   -240   1918  -6175       O  
ATOM   3439  N   ALA B  85      30.249 -10.813  59.183  1.00245.62           N  
ANISOU 3439  N   ALA B  85    27685  37855  27784   -141   1583  -4571       N  
ATOM   3440  CA  ALA B  85      29.210 -11.655  59.760  1.00240.26           C  
ANISOU 3440  CA  ALA B  85    27107  36880  27302    273   1582  -4385       C  
ATOM   3441  C   ALA B  85      29.725 -12.271  61.055  1.00241.58           C  
ANISOU 3441  C   ALA B  85    27249  36955  27586    892   1679  -4722       C  
ATOM   3442  O   ALA B  85      30.725 -12.999  61.047  1.00244.13           O  
ANISOU 3442  O   ALA B  85    27471  37519  27766    985   1787  -5191       O  
ATOM   3443  CB  ALA B  85      28.780 -12.742  58.775  1.00239.49           C  
ANISOU 3443  CB  ALA B  85    27022  36921  27050     49   1636  -4378       C  
ATOM   3444  N   MET B  86      29.052 -11.969  62.161  1.00254.03           N  
ANISOU 3444  N   MET B  86    28915  38173  29431   1288   1625  -4503       N  
ATOM   3445  CA  MET B  86      29.391 -12.554  63.448  1.00235.11           C  
ANISOU 3445  CA  MET B  86    26540  35633  27160   1858   1693  -4769       C  
ATOM   3446  C   MET B  86      28.553 -13.824  63.641  1.00220.90           C  
ANISOU 3446  C   MET B  86    24873  33667  25392   2118   1714  -4732       C  
ATOM   3447  O   MET B  86      27.962 -14.357  62.697  1.00221.40           O  
ANISOU 3447  O   MET B  86    24969  33809  25344   1864   1716  -4592       O  
ATOM   3448  CB  MET B  86      29.180 -11.531  64.566  1.00238.74           C  
ANISOU 3448  CB  MET B  86    27012  35817  27881   2106   1638  -4586       C  
ATOM   3449  CG  MET B  86      29.944 -11.835  65.860  1.00241.75           C  
ANISOU 3449  CG  MET B  86    27379  36123  28352   2609   1714  -4926       C  
ATOM   3450  SD  MET B  86      29.267 -11.041  67.331  1.00239.25           S  
ANISOU 3450  SD  MET B  86    27113  35395  28396   2961   1665  -4663       S  
ATOM   3451  CE  MET B  86      30.392 -11.646  68.587  1.00234.21           C  
ANISOU 3451  CE  MET B  86    26471  34746  27771   3476   1763  -5140       C  
ATOM   3452  N   ASP B  87      28.512 -14.332  64.874  1.00252.96           N  
ANISOU 3452  N   ASP B  87    29021  37500  29593   2617   1732  -4867       N  
ATOM   3453  CA  ASP B  87      27.758 -15.523  65.251  1.00238.47           C  
ANISOU 3453  CA  ASP B  87    27348  35480  27781   2906   1747  -4863       C  
ATOM   3454  C   ASP B  87      28.238 -16.752  64.472  1.00236.53           C  
ANISOU 3454  C   ASP B  87    27054  35514  27304   2839   1812  -5162       C  
ATOM   3455  O   ASP B  87      27.525 -17.342  63.657  1.00227.37           O  
ANISOU 3455  O   ASP B  87    25933  34406  26050   2654   1833  -5002       O  
ATOM   3456  CB  ASP B  87      26.248 -15.301  65.072  1.00220.96           C  
ANISOU 3456  CB  ASP B  87    25262  33001  25692   2798   1690  -4405       C  
ATOM   3457  CG  ASP B  87      25.713 -14.135  65.900  1.00206.99           C  
ANISOU 3457  CG  ASP B  87    23513  30935  24200   2870   1608  -4143       C  
ATOM   3458  OD1 ASP B  87      25.841 -14.167  67.143  1.00201.68           O  
ANISOU 3458  OD1 ASP B  87    22895  30063  23672   3239   1619  -4266       O  
ATOM   3459  OD2 ASP B  87      25.157 -13.183  65.311  1.00202.39           O  
ANISOU 3459  OD2 ASP B  87    22888  30309  23701   2544   1519  -3820       O  
ATOM   3460  N   GLY B  88      29.487 -17.122  64.752  1.00244.82           N  
ANISOU 3460  N   GLY B  88    28000  36742  28278   2997   1840  -5624       N  
ATOM   3461  CA  GLY B  88      30.052 -18.322  64.166  1.00242.05           C  
ANISOU 3461  CA  GLY B  88    27633  36506  27831   2895   1807  -5836       C  
ATOM   3462  C   GLY B  88      29.410 -19.504  64.858  1.00228.94           C  
ANISOU 3462  C   GLY B  88    26220  34481  26285   3200   1718  -5699       C  
ATOM   3463  O   GLY B  88      30.070 -20.280  65.557  1.00228.95           O  
ANISOU 3463  O   GLY B  88    26339  34244  26409   3375   1576  -5801       O  
ATOM   3464  N   GLN B  89      28.104 -19.647  64.645  1.00254.00           N  
ANISOU 3464  N   GLN B  89    33297  39031  24182   -806  -5484   1844       N  
ATOM   3465  CA  GLN B  89      27.296 -20.712  65.217  1.00240.21           C  
ANISOU 3465  CA  GLN B  89    31793  36566  22910   -267  -4843   1480       C  
ATOM   3466  C   GLN B  89      27.578 -22.064  64.584  1.00250.56           C  
ANISOU 3466  C   GLN B  89    32487  38378  24336    751  -4855   1798       C  
ATOM   3467  O   GLN B  89      26.767 -22.564  63.794  1.00237.90           O  
ANISOU 3467  O   GLN B  89    30638  36140  23614   1500  -4645   1403       O  
ATOM   3468  CB  GLN B  89      25.809 -20.365  65.088  1.00216.15           C  
ANISOU 3468  CB  GLN B  89    29125  32068  20934   -195  -4365    588       C  
ATOM   3469  CG  GLN B  89      25.407 -19.128  65.859  1.00202.79           C  
ANISOU 3469  CG  GLN B  89    28123  29770  19160  -1181  -4262    217       C  
ATOM   3470  CD  GLN B  89      23.941 -18.791  65.696  1.00190.55           C  
ANISOU 3470  CD  GLN B  89    26935  26789  18678  -1102  -3797   -661       C  
ATOM   3471  OE1 GLN B  89      23.176 -19.550  65.096  1.00180.61           O  
ANISOU 3471  OE1 GLN B  89    25451  24926  18247   -290  -3499  -1014       O  
ATOM   3472  NE2 GLN B  89      23.547 -17.632  66.201  1.00192.84           N  
ANISOU 3472  NE2 GLN B  89    27782  26528  18960  -1943  -3752  -1014       N  
ATOM   3473  N   ILE B  90      28.739 -22.640  64.891  1.00247.42           N  
ANISOU 3473  N   ILE B  90    31827  39125  23054    786  -5125   2521       N  
ATOM   3474  CA  ILE B  90      29.102 -23.958  64.386  1.00247.19           C  
ANISOU 3474  CA  ILE B  90    31227  39670  23024   1716  -5155   2882       C  
ATOM   3475  C   ILE B  90      27.983 -24.880  64.846  1.00238.62           C  
ANISOU 3475  C   ILE B  90    30424  37586  22657   2269  -4465   2323       C  
ATOM   3476  O   ILE B  90      27.806 -25.113  66.048  1.00248.43           O  
ANISOU 3476  O   ILE B  90    32188  38550  23654   1956  -4068   2207       O  
ATOM   3477  CB  ILE B  90      30.466 -24.434  64.926  1.00250.91           C  
ANISOU 3477  CB  ILE B  90    31516  41439  22381   1552  -5465   3697       C  
ATOM   3478  CG1 ILE B  90      31.567 -23.395  64.670  1.00251.83           C  
ANISOU 3478  CG1 ILE B  90    31463  42483  21739    860  -6124   4240       C  
ATOM   3479  CG2 ILE B  90      30.846 -25.791  64.336  1.00248.08           C  
ANISOU 3479  CG2 ILE B  90    30538  41701  22021   2531  -5524   4076       C  
ATOM   3480  CD1 ILE B  90      32.242 -23.511  63.317  1.00248.97           C  
ANISOU 3480  CD1 ILE B  90    30405  42556  21635   1339  -6513   4551       C  
ATOM   3481  N   GLN B  91      27.211 -25.405  63.896  1.00262.56           N  
ANISOU 3481  N   GLN B  91    33121  40047  26593   3103  -4318   1971       N  
ATOM   3482  CA  GLN B  91      26.048 -26.210  64.233  1.00216.92           C  
ANISOU 3482  CA  GLN B  91    27597  33213  21611   3652  -3669   1391       C  
ATOM   3483  C   GLN B  91      26.326 -27.693  64.093  1.00191.09           C  
ANISOU 3483  C   GLN B  91    23888  30436  18281   4560  -3582   1719       C  
ATOM   3484  O   GLN B  91      25.390 -28.481  63.912  1.00171.34           O  
ANISOU 3484  O   GLN B  91    21364  27151  16587   5283  -3161   1291       O  
ATOM   3485  CB  GLN B  91      24.877 -25.814  63.338  1.00202.56           C  
ANISOU 3485  CB  GLN B  91    25762  30280  20922   3979  -3511    711       C  
ATOM   3486  CG  GLN B  91      24.248 -24.479  63.664  1.00195.49           C  
ANISOU 3486  CG  GLN B  91    25437  28564  20279   3133  -3403    189       C  
ATOM   3487  CD  GLN B  91      23.429 -24.504  64.922  1.00187.28           C  
ANISOU 3487  CD  GLN B  91    25130  26599  19430   2780  -2776   -297       C  
ATOM   3488  OE1 GLN B  91      22.974 -25.560  65.355  1.00181.44           O  
ANISOU 3488  OE1 GLN B  91    24462  25502  18976   3334  -2325   -439       O  
ATOM   3489  NE2 GLN B  91      23.231 -23.337  65.521  1.00188.58           N  
ANISOU 3489  NE2 GLN B  91    25848  26365  19440   1860  -2746   -552       N  
ATOM   3490  N   GLY B  92      27.595 -28.075  64.192  1.00200.59           N  
ANISOU 3490  N   GLY B  92    24755  32920  18539   4524  -3978   2472       N  
ATOM   3491  CA  GLY B  92      28.016 -29.454  64.205  1.00196.67           C  
ANISOU 3491  CA  GLY B  92    23876  33041  17807   5271  -3931   2857       C  
ATOM   3492  C   GLY B  92      27.437 -30.367  63.150  1.00191.31           C  
ANISOU 3492  C   GLY B  92    22691  32049  17947   6373  -3857   2689       C  
ATOM   3493  O   GLY B  92      26.843 -29.926  62.155  1.00188.81           O  
ANISOU 3493  O   GLY B  92    22192  31173  18375   6640  -3951   2354       O  
ATOM   3494  N   SER B  93      27.560 -31.661  63.425  1.00194.32           N  
ANISOU 3494  N   SER B  93    22884  32734  18214   7015  -3659   2888       N  
ATOM   3495  CA  SER B  93      27.035 -32.707  62.569  1.00192.76           C  
ANISOU 3495  CA  SER B  93    22225  32277  18739   8118  -3556   2766       C  
ATOM   3496  C   SER B  93      25.527 -32.590  62.351  1.00181.86           C  
ANISOU 3496  C   SER B  93    21127  29402  18568   8430  -3073   1928       C  
ATOM   3497  O   SER B  93      24.793 -32.081  63.186  1.00185.72           O  
ANISOU 3497  O   SER B  93    22241  29006  19316   7901  -2643   1415       O  
ATOM   3498  CB  SER B  93      27.346 -34.086  63.176  1.00208.30           C  
ANISOU 3498  CB  SER B  93    24074  34735  20335   8629  -3343   3058       C  
ATOM   3499  OG  SER B  93      28.737 -34.357  63.086  1.00216.56           O  
ANISOU 3499  OG  SER B  93    24797  36880  20606   8267  -3659   3707       O  
ATOM   3500  N   SER B 117      25.442 -36.998  58.748  1.00207.07           N  
ANISOU 3500  N   SER B 117    23172  31781  23725   9470  -2473   1896       N  
ATOM   3501  CA  SER B 117      26.807 -37.063  59.255  1.00222.47           C  
ANISOU 3501  CA  SER B 117    24969  34873  24686   9280  -2681   2444       C  
ATOM   3502  C   SER B 117      27.710 -36.075  58.523  1.00239.97           C  
ANISOU 3502  C   SER B 117    27000  37512  26665   8783  -3096   2729       C  
ATOM   3503  O   SER B 117      28.757 -36.444  57.991  1.00233.32           O  
ANISOU 3503  O   SER B 117    26007  37037  25608   8407  -3164   3007       O  
ATOM   3504  CB  SER B 117      27.361 -38.482  59.123  1.00216.73           C  
ANISOU 3504  CB  SER B 117    24180  34324  23843   9183  -2442   2576       C  
ATOM   3505  OG  SER B 117      27.556 -38.827  57.763  1.00208.20           O  
ANISOU 3505  OG  SER B 117    23007  32848  23252   8851  -2476   2511       O  
ATOM   3506  N   MET B 118      27.284 -34.814  58.502  1.00222.97           N  
ANISOU 3506  N   MET B 118    24895  35227  24596   8779  -3358   2614       N  
ATOM   3507  CA  MET B 118      28.015 -33.739  57.838  1.00231.65           C  
ANISOU 3507  CA  MET B 118    25863  36644  25510   8260  -3770   2841       C  
ATOM   3508  C   MET B 118      27.802 -32.468  58.643  1.00234.50           C  
ANISOU 3508  C   MET B 118    26376  37336  25389   8186  -4106   2878       C  
ATOM   3509  O   MET B 118      26.658 -32.056  58.863  1.00237.67           O  
ANISOU 3509  O   MET B 118    26940  37157  26207   8651  -4056   2446       O  
ATOM   3510  CB  MET B 118      27.577 -33.560  56.382  1.00237.26           C  
ANISOU 3510  CB  MET B 118    26490  36575  27085   8182  -3760   2552       C  
ATOM   3511  CG  MET B 118      26.092 -33.361  56.177  1.00240.75           C  
ANISOU 3511  CG  MET B 118    27070  36028  28375   8560  -3554   1992       C  
ATOM   3512  SD  MET B 118      25.099 -34.690  56.870  1.00241.76           S  
ANISOU 3512  SD  MET B 118    27407  35541  28910   9011  -3012   1657       S  
ATOM   3513  CE  MET B 118      23.491 -34.176  56.290  1.00237.17           C  
ANISOU 3513  CE  MET B 118    27000  33587  29525   9059  -2765   1003       C  
ATOM   3514  N   ASN B 119      28.891 -31.853  59.094  1.00268.41           N  
ANISOU 3514  N   ASN B 119    30693  42446  28845   7531  -4429   3336       N  
ATOM   3515  CA  ASN B 119      28.754 -30.671  59.927  1.00228.35           C  
ANISOU 3515  CA  ASN B 119    25893  37742  23126   7205  -4767   3398       C  
ATOM   3516  C   ASN B 119      28.352 -29.468  59.082  1.00182.86           C  
ANISOU 3516  C   ASN B 119    20083  31633  17763   7055  -5083   3148       C  
ATOM   3517  O   ASN B 119      28.713 -29.350  57.908  1.00154.00           O  
ANISOU 3517  O   ASN B 119    16182  27724  14608   6883  -5131   3154       O  
ATOM   3518  CB  ASN B 119      30.057 -30.374  60.675  1.00215.99           C  
ANISOU 3518  CB  ASN B 119    24464  36995  20607   6332  -4947   3917       C  
ATOM   3519  CG  ASN B 119      31.276 -30.381  59.769  1.00200.70           C  
ANISOU 3519  CG  ASN B 119    22269  35166  18820   5874  -5047   4170       C  
ATOM   3520  OD1 ASN B 119      31.162 -30.332  58.545  1.00197.51           O  
ANISOU 3520  OD1 ASN B 119    21645  34318  19084   6043  -5064   4000       O  
ATOM   3521  ND2 ASN B 119      32.455 -30.426  60.375  1.00193.03           N  
ANISOU 3521  ND2 ASN B 119    21389  34710  17243   5303  -5100   4539       N  
ATOM   3522  N   VAL B 120      27.568 -28.581  59.691  1.00192.99           N  
ANISOU 3522  N   VAL B 120    21817  32414  19095   6757  -5027   2721       N  
ATOM   3523  CA  VAL B 120      27.054 -27.405  59.008  1.00179.64           C  
ANISOU 3523  CA  VAL B 120    20213  30097  17945   6425  -5170   2304       C  
ATOM   3524  C   VAL B 120      27.491 -26.161  59.768  1.00191.55           C  
ANISOU 3524  C   VAL B 120    22174  31804  18801   5256  -5319   2367       C  
ATOM   3525  O   VAL B 120      27.798 -26.199  60.962  1.00203.38           O  
ANISOU 3525  O   VAL B 120    24083  33511  19682   4713  -5134   2504       O  
ATOM   3526  CB  VAL B 120      25.518 -27.445  58.863  1.00169.98           C  
ANISOU 3526  CB  VAL B 120    19299  27365  17920   6778  -4636   1429       C  
ATOM   3527  CG1 VAL B 120      25.083 -28.746  58.212  1.00166.25           C  
ANISOU 3527  CG1 VAL B 120    18407  26684  18077   7951  -4471   1383       C  
ATOM   3528  CG2 VAL B 120      24.849 -27.284  60.211  1.00174.48           C  
ANISOU 3528  CG2 VAL B 120    20609  27155  18530   6207  -4071    977       C  
ATOM   3529  N   TYR B 121      27.503 -25.044  59.050  1.00182.84           N  
ANISOU 3529  N   TYR B 121    20997  30619  17855   4880  -5664   2256       N  
ATOM   3530  CA  TYR B 121      27.938 -23.763  59.578  1.00191.95           C  
ANISOU 3530  CA  TYR B 121    22512  31993  18429   3797  -5894   2330       C  
ATOM   3531  C   TYR B 121      26.965 -22.663  59.191  1.00184.54           C  
ANISOU 3531  C   TYR B 121    21871  29998  18247   3442  -5798   1628       C  
ATOM   3532  O   TYR B 121      26.115 -22.832  58.317  1.00181.21           O  
ANISOU 3532  O   TYR B 121    21275  28823  18753   4055  -5664   1169       O  
ATOM   3533  CB  TYR B 121      29.346 -23.414  59.079  1.00208.31           C  
ANISOU 3533  CB  TYR B 121    24095  35427  19625   3573  -6592   3130       C  
ATOM   3534  CG  TYR B 121      29.917 -22.168  59.704  1.00224.04           C  
ANISOU 3534  CG  TYR B 121    26443  37762  20920   2460  -6861   3296       C  
ATOM   3535  CD1 TYR B 121      30.056 -22.049  61.079  1.00232.39           C  
ANISOU 3535  CD1 TYR B 121    28067  38811  21417   1784  -6615   3327       C  
ATOM   3536  CD2 TYR B 121      30.313 -21.103  58.910  1.00227.89           C  
ANISOU 3536  CD2 TYR B 121    26699  38571  21316   2095  -7370   3422       C  
ATOM   3537  CE1 TYR B 121      30.574 -20.900  61.644  1.00238.33           C  
ANISOU 3537  CE1 TYR B 121    29151  39863  21540    779  -6881   3487       C  
ATOM   3538  CE2 TYR B 121      30.837 -19.961  59.461  1.00234.53           C  
ANISOU 3538  CE2 TYR B 121    27888  39611  21610   1086  -7581   3543       C  
ATOM   3539  CZ  TYR B 121      30.965 -19.861  60.829  1.00239.68           C  
ANISOU 3539  CZ  TYR B 121    29070  40366  21632    437  -7399   3620       C  
ATOM   3540  OH  TYR B 121      31.487 -18.715  61.380  1.00243.82           O  
ANISOU 3540  OH  TYR B 121    29927  41136  21579   -544  -7652   3769       O  
ATOM   3541  N   SER B 122      27.105 -21.525  59.862  1.00196.33           N  
ANISOU 3541  N   SER B 122    23826  31443  19326   2437  -5878   1551       N  
ATOM   3542  CA  SER B 122      26.260 -20.381  59.581  1.00185.45           C  
ANISOU 3542  CA  SER B 122    22767  29135  18559   1979  -5819    910       C  
ATOM   3543  C   SER B 122      27.034 -19.098  59.840  1.00197.98           C  
ANISOU 3543  C   SER B 122    24508  31321  19393    968  -6274   1201       C  
ATOM   3544  O   SER B 122      28.007 -19.073  60.600  1.00206.54           O  
ANISOU 3544  O   SER B 122    25669  33279  19529    494  -6473   1768       O  
ATOM   3545  CB  SER B 122      24.985 -20.418  60.429  1.00169.78           C  
ANISOU 3545  CB  SER B 122    21454  25840  17215   1840  -5134    157       C  
ATOM   3546  OG  SER B 122      25.291 -20.162  61.786  1.00179.31           O  
ANISOU 3546  OG  SER B 122    23203  27207  17720   1078  -4976    293       O  
ATOM   3547  N   LEU B 123      26.580 -18.033  59.184  1.00195.50           N  
ANISOU 3547  N   LEU B 123    24238  30512  19529    651  -6442    796       N  
ATOM   3548  CA  LEU B 123      27.067 -16.680  59.396  1.00203.99           C  
ANISOU 3548  CA  LEU B 123    25526  31917  20062   -338  -6828    912       C  
ATOM   3549  C   LEU B 123      25.851 -15.787  59.562  1.00202.17           C  
ANISOU 3549  C   LEU B 123    25851  30416  20549   -791  -6498     67       C  
ATOM   3550  O   LEU B 123      24.886 -15.879  58.789  1.00202.78           O  
ANISOU 3550  O   LEU B 123    25844  29617  21585   -287  -6286   -507       O  
ATOM   3551  CB  LEU B 123      27.942 -16.184  58.241  1.00208.02           C  
ANISOU 3551  CB  LEU B 123    25417  33320  20303   -282  -7506   1374       C  
ATOM   3552  CG  LEU B 123      29.248 -16.922  57.967  1.00220.48           C  
ANISOU 3552  CG  LEU B 123    26405  36244  21123    109  -7922   2264       C  
ATOM   3553  CD1 LEU B 123      29.824 -16.464  56.643  1.00221.04           C  
ANISOU 3553  CD1 LEU B 123    25906  36798  21282    325  -8442   2521       C  
ATOM   3554  CD2 LEU B 123      30.225 -16.634  59.090  1.00229.60           C  
ANISOU 3554  CD2 LEU B 123    27829  38213  21197   -673  -8100   2815       C  
ATOM   3555  N   SER B 124      25.915 -14.908  60.560  1.00209.20           N  
ANISOU 3555  N   SER B 124    27309  31214  20965  -1747  -6472      1       N  
ATOM   3556  CA  SER B 124      24.763 -14.120  60.958  1.00211.65           C  
ANISOU 3556  CA  SER B 124    28240  30312  21866  -2241  -6100   -783       C  
ATOM   3557  C   SER B 124      25.163 -12.663  61.165  1.00223.85           C  
ANISOU 3557  C   SER B 124    30036  32120  22896  -3274  -6507   -725       C  
ATOM   3558  O   SER B 124      26.340 -12.288  61.075  1.00241.57           O  
ANISOU 3558  O   SER B 124    31995  35479  24312  -3616  -7059    -64       O  
ATOM   3559  CB  SER B 124      24.143 -14.711  62.234  1.00218.01           C  
ANISOU 3559  CB  SER B 124    29646  30447  22739  -2296  -5461  -1056       C  
ATOM   3560  OG  SER B 124      23.582 -15.987  61.972  1.00217.33           O  
ANISOU 3560  OG  SER B 124    29351  29940  23283  -1327  -5052  -1231       O  
ATOM   3561  N   VAL B 125      24.164 -11.822  61.429  1.00225.36           N  
ANISOU 3561  N   VAL B 125    30764  31266  23598  -3771  -6240  -1425       N  
ATOM   3562  CA  VAL B 125      24.422 -10.432  61.787  1.00222.97           C  
ANISOU 3562  CA  VAL B 125    30800  31095  22823  -4801  -6563  -1435       C  
ATOM   3563  C   VAL B 125      23.276  -9.933  62.663  1.00211.59           C  
ANISOU 3563  C   VAL B 125    30144  28438  21812  -5307  -6042  -2156       C  
ATOM   3564  O   VAL B 125      22.108  -9.946  62.256  1.00212.56           O  
ANISOU 3564  O   VAL B 125    30407  27466  22892  -5007  -5669  -2870       O  
ATOM   3565  CB  VAL B 125      24.641  -9.549  60.539  1.00222.22           C  
ANISOU 3565  CB  VAL B 125    30264  31274  22897  -4891  -7104  -1457       C  
ATOM   3566  CG1 VAL B 125      23.583  -9.789  59.491  1.00212.31           C  
ANISOU 3566  CG1 VAL B 125    28810  29089  22768  -4209  -6861  -2108       C  
ATOM   3567  CG2 VAL B 125      24.669  -8.086  60.921  1.00225.07           C  
ANISOU 3567  CG2 VAL B 125    31041  31555  22921  -5948  -7363  -1615       C  
ATOM   3568  N   ASP B 126      23.606  -9.494  63.875  1.00213.59           N  
ANISOU 3568  N   ASP B 126    30925  28866  21365  -6070  -6015  -1966       N  
ATOM   3569  CA  ASP B 126      22.599  -9.097  64.848  1.00214.28           C  
ANISOU 3569  CA  ASP B 126    31793  27862  21762  -6553  -5505  -2574       C  
ATOM   3570  C   ASP B 126      21.935  -7.780  64.446  1.00203.51           C  
ANISOU 3570  C   ASP B 126    30675  25840  20811  -7145  -5633  -3145       C  
ATOM   3571  O   ASP B 126      22.516  -6.983  63.705  1.00201.36           O  
ANISOU 3571  O   ASP B 126    30056  26170  20281  -7434  -6205  -2931       O  
ATOM   3572  CB  ASP B 126      23.205  -8.988  66.246  1.00226.79           C  
ANISOU 3572  CB  ASP B 126    33868  29865  22437  -7197  -5478  -2168       C  
ATOM   3573  CG  ASP B 126      24.470  -8.169  66.272  1.00226.35           C  
ANISOU 3573  CG  ASP B 126    33636  30967  21401  -7854  -6172  -1504       C  
ATOM   3574  OD1 ASP B 126      24.823  -7.588  65.226  1.00224.93           O  
ANISOU 3574  OD1 ASP B 126    32987  31217  21258  -7873  -6665  -1400       O  
ATOM   3575  OD2 ASP B 126      25.112  -8.107  67.341  1.00224.92           O  
ANISOU 3575  OD2 ASP B 126    33789  31253  20417  -8345  -6226  -1083       O  
ATOM   3576  N   PRO B 127      20.688  -7.542  64.905  1.00196.10           N  
ANISOU 3576  N   PRO B 127    30329  23637  20543  -7316  -5099  -3893       N  
ATOM   3577  CA  PRO B 127      20.022  -6.258  64.630  1.00200.72           C  
ANISOU 3577  CA  PRO B 127    31214  23556  21493  -7945  -5197  -4464       C  
ATOM   3578  C   PRO B 127      20.845  -5.058  65.067  1.00215.82           C  
ANISOU 3578  C   PRO B 127    33314  26185  22501  -8937  -5730  -4092       C  
ATOM   3579  O   PRO B 127      20.637  -3.941  64.576  1.00214.37           O  
ANISOU 3579  O   PRO B 127    33046  25850  22554  -9249  -5908  -4307       O  
ATOM   3580  CB  PRO B 127      18.716  -6.359  65.432  1.00202.65           C  
ANISOU 3580  CB  PRO B 127    32165  22451  22382  -8023  -4485  -5178       C  
ATOM   3581  CG  PRO B 127      18.931  -7.471  66.406  1.00209.20           C  
ANISOU 3581  CG  PRO B 127    33162  23427  22896  -7690  -4099  -4856       C  
ATOM   3582  CD  PRO B 127      19.835  -8.433  65.710  1.00200.94           C  
ANISOU 3582  CD  PRO B 127    31370  23376  21604  -6950  -4381  -4247       C  
ATOM   3583  N   ASN B 128      21.775  -5.275  65.999  1.00209.76           N  
ANISOU 3583  N   ASN B 128    32674  26215  20810  -9228  -5860  -3451       N  
ATOM   3584  CA  ASN B 128      22.638  -4.191  66.447  1.00225.29           C  
ANISOU 3584  CA  ASN B 128    34805  28920  21876 -10141  -6393  -3028       C  
ATOM   3585  C   ASN B 128      23.485  -3.644  65.307  1.00238.34           C  
ANISOU 3585  C   ASN B 128    35742  31481  23334 -10074  -7028  -2618       C  
ATOM   3586  O   ASN B 128      23.818  -2.453  65.296  1.00242.68           O  
ANISOU 3586  O   ASN B 128    36143  32228  23835 -10312  -7085  -2388       O  
ATOM   3587  CB  ASN B 128      23.546  -4.690  67.573  1.00233.05           C  
ANISOU 3587  CB  ASN B 128    35973  30634  21940 -10318  -6409  -2362       C  
ATOM   3588  CG  ASN B 128      24.549  -3.647  68.019  1.00241.02           C  
ANISOU 3588  CG  ASN B 128    37076  32480  22020 -11155  -6963  -1824       C  
ATOM   3589  OD1 ASN B 128      24.207  -2.484  68.223  1.00243.65           O  
ANISOU 3589  OD1 ASN B 128    37557  32356  22662 -11444  -6775  -1979       O  
ATOM   3590  ND2 ASN B 128      25.808  -4.057  68.140  1.00244.20           N  
ANISOU 3590  ND2 ASN B 128    37127  34047  21610 -11093  -7349  -1022       N  
ATOM   3591  N   THR B 129      23.829  -4.487  64.332  1.00254.76           N  
ANISOU 3591  N   THR B 129    37182  34034  25579  -9340  -7211  -2400       N  
ATOM   3592  CA  THR B 129      24.582  -4.041  63.169  1.00236.70           C  
ANISOU 3592  CA  THR B 129    34193  32547  23195  -9177  -7769  -2036       C  
ATOM   3593  C   THR B 129      23.698  -3.455  62.074  1.00214.88           C  
ANISOU 3593  C   THR B 129    31189  29006  21450  -8835  -7600  -2660       C  
ATOM   3594  O   THR B 129      24.219  -2.800  61.165  1.00210.46           O  
ANISOU 3594  O   THR B 129    30058  28914  20995  -8600  -7827  -2409       O  
ATOM   3595  CB  THR B 129      25.410  -5.201  62.608  1.00241.17           C  
ANISOU 3595  CB  THR B 129    34121  34021  23493  -8440  -8000  -1441       C  
ATOM   3596  OG1 THR B 129      25.718  -6.125  63.658  1.00249.43           O  
ANISOU 3596  OG1 THR B 129    35394  35281  24098  -8293  -7689  -1093       O  
ATOM   3597  CG2 THR B 129      26.710  -4.693  62.023  1.00242.25           C  
ANISOU 3597  CG2 THR B 129    33616  35266  23162  -8370  -8455   -704       C  
ATOM   3598  N   TRP B 130      22.382  -3.669  62.137  1.00224.30           N  
ANISOU 3598  N   TRP B 130    32786  28986  23453  -8710  -7119  -3457       N  
ATOM   3599  CA  TRP B 130      21.489  -3.070  61.151  1.00209.96           C  
ANISOU 3599  CA  TRP B 130    30688  26420  22670  -8276  -6840  -4030       C  
ATOM   3600  C   TRP B 130      21.283  -1.589  61.433  1.00218.74           C  
ANISOU 3600  C   TRP B 130    31844  27337  23929  -8553  -6586  -4085       C  
ATOM   3601  O   TRP B 130      21.381  -0.755  60.527  1.00221.24           O  
ANISOU 3601  O   TRP B 130    31688  27822  24551  -8324  -6678  -4094       O  
ATOM   3602  CB  TRP B 130      20.142  -3.800  61.125  1.00196.53           C  
ANISOU 3602  CB  TRP B 130    29286  23474  21910  -7845  -6274  -4795       C  
ATOM   3603  CG  TRP B 130      20.233  -5.173  60.549  1.00193.94           C  
ANISOU 3603  CG  TRP B 130    28702  23230  21756  -7160  -6378  -4734       C  
ATOM   3604  CD1 TRP B 130      20.059  -6.352  61.210  1.00196.32           C  
ANISOU 3604  CD1 TRP B 130    29126  23342  22124  -6642  -5898  -4635       C  
ATOM   3605  CD2 TRP B 130      20.590  -5.516  59.206  1.00199.44           C  
ANISOU 3605  CD2 TRP B 130    28662  24382  22733  -6470  -6712  -4552       C  
ATOM   3606  NE1 TRP B 130      20.252  -7.409  60.354  1.00199.66           N  
ANISOU 3606  NE1 TRP B 130    28936  24055  22871  -5670  -5911  -4421       N  
ATOM   3607  CE2 TRP B 130      20.584  -6.922  59.118  1.00201.49           C  
ANISOU 3607  CE2 TRP B 130    28638  24683  23237  -5541  -6408  -4358       C  
ATOM   3608  CE3 TRP B 130      20.902  -4.769  58.065  1.00196.44           C  
ANISOU 3608  CE3 TRP B 130    27842  24365  22432  -6537  -7237  -4540       C  
ATOM   3609  CZ2 TRP B 130      20.878  -7.597  57.934  1.00194.96           C  
ANISOU 3609  CZ2 TRP B 130    27112  24244  22722  -4680  -6619  -4143       C  
ATOM   3610  CZ3 TRP B 130      21.194  -5.440  56.891  1.00188.89           C  
ANISOU 3610  CZ3 TRP B 130    26197  23781  21793  -5678  -7435  -4332       C  
ATOM   3611  CH2 TRP B 130      21.180  -6.840  56.834  1.00187.99           C  
ANISOU 3611  CH2 TRP B 130    25821  23695  21911  -4760  -7130  -4131       C  
ATOM   3612  N   GLN B 131      20.992  -1.247  62.690  1.00220.30           N  
ANISOU 3612  N   GLN B 131    32613  27187  23903  -9006  -6265  -4115       N  
ATOM   3613  CA  GLN B 131      20.730   0.144  63.038  1.00224.14           C  
ANISOU 3613  CA  GLN B 131    33163  27479  24522  -9219  -6045  -4146       C  
ATOM   3614  C   GLN B 131      21.976   1.010  62.862  1.00233.09           C  
ANISOU 3614  C   GLN B 131    34025  29589  24949  -9543  -6525  -3491       C  
ATOM   3615  O   GLN B 131      21.884   2.143  62.377  1.00234.16           O  
ANISOU 3615  O   GLN B 131    33897  29696  25376  -9439  -6485  -3550       O  
ATOM   3616  CB  GLN B 131      20.205   0.229  64.470  1.00223.14           C  
ANISOU 3616  CB  GLN B 131    33703  26828  24254  -9599  -5632  -4250       C  
ATOM   3617  CG  GLN B 131      19.761   1.619  64.876  1.00219.93           C  
ANISOU 3617  CG  GLN B 131    33358  26153  24051  -9724  -5384  -4318       C  
ATOM   3618  CD  GLN B 131      18.558   2.085  64.073  1.00210.82           C  
ANISOU 3618  CD  GLN B 131    31775  24305  24023  -9044  -5005  -4910       C  
ATOM   3619  OE1 GLN B 131      18.484   3.242  63.658  1.00210.50           O  
ANISOU 3619  OE1 GLN B 131    31429  24361  24189  -8951  -5034  -4917       O  
ATOM   3620  NE2 GLN B 131      17.608   1.183  63.852  1.00207.10           N  
ANISOU 3620  NE2 GLN B 131    31231  23147  24310  -8517  -4641  -5392       N  
ATOM   3621  N   THR B 132      23.149   0.505  63.264  1.00224.08           N  
ANISOU 3621  N   THR B 132    32904  29325  22913  -9864  -6940  -2846       N  
ATOM   3622  CA  THR B 132      24.377   1.283  63.102  1.00230.65           C  
ANISOU 3622  CA  THR B 132    33408  31057  23171 -10057  -7315  -2178       C  
ATOM   3623  C   THR B 132      24.743   1.460  61.630  1.00249.71           C  
ANISOU 3623  C   THR B 132    35114  33836  25928  -9515  -7555  -2128       C  
ATOM   3624  O   THR B 132      25.241   2.522  61.238  1.00244.37           O  
ANISOU 3624  O   THR B 132    34181  33443  25224  -9534  -7646  -1907       O  
ATOM   3625  CB  THR B 132      25.534   0.653  63.884  1.00222.88           C  
ANISOU 3625  CB  THR B 132    32507  30928  21250 -10376  -7613  -1471       C  
ATOM   3626  OG1 THR B 132      26.714   1.452  63.720  1.00223.94           O  
ANISOU 3626  OG1 THR B 132    32289  31824  20974 -10482  -7877   -842       O  
ATOM   3627  CG2 THR B 132      25.827  -0.759  63.412  1.00217.21           C  
ANISOU 3627  CG2 THR B 132    31487  30641  20400  -9947  -7834  -1336       C  
ATOM   3628  N   LEU B 133      24.513   0.440  60.798  1.00252.21           N  
ANISOU 3628  N   LEU B 133    35120  34132  26575  -9010  -7651  -2332       N  
ATOM   3629  CA  LEU B 133      24.814   0.589  59.377  1.00249.96           C  
ANISOU 3629  CA  LEU B 133    34175  34148  26649  -8452  -7849  -2312       C  
ATOM   3630  C   LEU B 133      23.842   1.550  58.708  1.00242.29           C  
ANISOU 3630  C   LEU B 133    33120  32431  26508  -8230  -7529  -2943       C  
ATOM   3631  O   LEU B 133      24.242   2.357  57.861  1.00242.52           O  
ANISOU 3631  O   LEU B 133    32743  32735  26667  -8013  -7627  -2846       O  
ATOM   3632  CB  LEU B 133      24.766  -0.769  58.673  1.00251.54           C  
ANISOU 3632  CB  LEU B 133    34062  34502  27010  -7925  -8035  -2359       C  
ATOM   3633  CG  LEU B 133      25.457  -0.861  57.308  1.00257.22           C  
ANISOU 3633  CG  LEU B 133    34051  35824  27856  -7307  -8320  -2090       C  
ATOM   3634  CD1 LEU B 133      26.056  -2.225  57.054  1.00260.40           C  
ANISOU 3634  CD1 LEU B 133    34123  36874  27943  -6863  -8609  -1661       C  
ATOM   3635  CD2 LEU B 133      24.471  -0.529  56.202  1.00256.60           C  
ANISOU 3635  CD2 LEU B 133    33754  35041  28701  -6891  -8111  -2789       C  
ATOM   3636  N   LEU B 134      22.561   1.472  59.065  1.00266.36           N  
ANISOU 3636  N   LEU B 134    36511  34531  30163  -8203  -7085  -3594       N  
ATOM   3637  CA  LEU B 134      21.581   2.362  58.455  1.00245.23           C  
ANISOU 3637  CA  LEU B 134    33647  31194  28335  -7867  -6699  -4180       C  
ATOM   3638  C   LEU B 134      21.804   3.817  58.858  1.00241.77           C  
ANISOU 3638  C   LEU B 134    33300  30872  27688  -8180  -6650  -3995       C  
ATOM   3639  O   LEU B 134      21.561   4.726  58.058  1.00237.40           O  
ANISOU 3639  O   LEU B 134    32392  30222  27587  -7873  -6547  -4222       O  
ATOM   3640  CB  LEU B 134      20.158   1.903  58.782  1.00237.54           C  
ANISOU 3640  CB  LEU B 134    32905  29207  28142  -7626  -6149  -4863       C  
ATOM   3641  CG  LEU B 134      19.538   1.952  60.179  1.00237.47           C  
ANISOU 3641  CG  LEU B 134    33493  28654  28080  -7967  -5790  -4976       C  
ATOM   3642  CD1 LEU B 134      18.943   3.318  60.485  1.00235.84           C  
ANISOU 3642  CD1 LEU B 134    33278  28127  28202  -7977  -5494  -5149       C  
ATOM   3643  CD2 LEU B 134      18.476   0.866  60.309  1.00235.05           C  
ANISOU 3643  CD2 LEU B 134    33316  27541  28453  -7584  -5363  -5495       C  
ATOM   3644  N   HIS B 135      22.210   4.074  60.104  1.00254.27           N  
ANISOU 3644  N   HIS B 135    35365  32633  28615  -8774  -6689  -3615       N  
ATOM   3645  CA  HIS B 135      22.410   5.470  60.481  1.00241.66           C  
ANISOU 3645  CA  HIS B 135    33861  31128  26832  -9057  -6646  -3434       C  
ATOM   3646  C   HIS B 135      23.770   6.009  60.043  1.00252.36           C  
ANISOU 3646  C   HIS B 135    34918  33344  27622  -9187  -7059  -2813       C  
ATOM   3647  O   HIS B 135      23.886   7.206  59.757  1.00254.55           O  
ANISOU 3647  O   HIS B 135    35058  33665  27995  -9169  -7030  -2786       O  
ATOM   3648  CB  HIS B 135      22.231   5.646  61.988  1.00220.84           C  
ANISOU 3648  CB  HIS B 135    31854  28278  23776  -9617  -6471  -3303       C  
ATOM   3649  CG  HIS B 135      22.432   7.055  62.451  1.00206.90           C  
ANISOU 3649  CG  HIS B 135    30217  26609  21787  -9921  -6440  -3091       C  
ATOM   3650  ND1 HIS B 135      23.199   7.383  63.547  1.00209.18           N  
ANISOU 3650  ND1 HIS B 135    30904  27283  21290 -10550  -6585  -2554       N  
ATOM   3651  CD2 HIS B 135      21.961   8.224  61.957  1.00202.47           C  
ANISOU 3651  CD2 HIS B 135    29439  25813  21677  -9682  -6285  -3333       C  
ATOM   3652  CE1 HIS B 135      23.189   8.694  63.712  1.00206.09           C  
ANISOU 3652  CE1 HIS B 135    30541  26867  20895 -10674  -6520  -2484       C  
ATOM   3653  NE2 HIS B 135      22.446   9.228  62.759  1.00204.16           N  
ANISOU 3653  NE2 HIS B 135    30001  26267  21305 -10248  -6359  -2899       N  
ATOM   3654  N   GLU B 136      24.799   5.158  59.955  1.00247.84           N  
ANISOU 3654  N   GLU B 136    34195  33463  26511  -9242  -7417  -2309       N  
ATOM   3655  CA  GLU B 136      26.117   5.650  59.557  1.00252.62           C  
ANISOU 3655  CA  GLU B 136    34461  34862  26661  -9274  -7736  -1698       C  
ATOM   3656  C   GLU B 136      26.187   5.874  58.051  1.00260.96           C  
ANISOU 3656  C   GLU B 136    34941  36000  28212  -8664  -7806  -1887       C  
ATOM   3657  O   GLU B 136      27.033   6.641  57.577  1.00265.89           O  
ANISOU 3657  O   GLU B 136    35298  37054  28674  -8615  -7947  -1556       O  
ATOM   3658  CB  GLU B 136      27.234   4.699  60.014  1.00245.48           C  
ANISOU 3658  CB  GLU B 136    33510  34709  25051  -9435  -8033  -1052       C  
ATOM   3659  CG  GLU B 136      28.635   5.249  59.717  1.00236.57           C  
ANISOU 3659  CG  GLU B 136    32029  34343  23515  -9440  -8273   -407       C  
ATOM   3660  CD  GLU B 136      29.574   4.240  59.109  1.00229.19           C  
ANISOU 3660  CD  GLU B 136    30623  34085  22374  -9011  -8516      8       C  
ATOM   3661  OE1 GLU B 136      29.266   3.031  59.152  1.00227.57           O  
ANISOU 3661  OE1 GLU B 136    30413  33885  22166  -8803  -8550    -78       O  
ATOM   3662  OE2 GLU B 136      30.623   4.660  58.572  1.00228.16           O  
ANISOU 3662  OE2 GLU B 136    30126  34457  22108  -8839  -8647    412       O  
ATOM   3663  N   ARG B 137      25.288   5.247  57.297  1.00260.29           N  
ANISOU 3663  N   ARG B 137    34675  35461  28761  -8193  -7673  -2443       N  
ATOM   3664  CA  ARG B 137      25.299   5.269  55.844  1.00255.89           C  
ANISOU 3664  CA  ARG B 137    33570  34970  28685  -7580  -7724  -2662       C  
ATOM   3665  C   ARG B 137      23.897   5.619  55.375  1.00259.45           C  
ANISOU 3665  C   ARG B 137    33981  34595  30003  -7267  -7318  -3466       C  
ATOM   3666  O   ARG B 137      22.927   5.013  55.833  1.00263.58           O  
ANISOU 3666  O   ARG B 137    34746  34538  30864  -7272  -7061  -3877       O  
ATOM   3667  CB  ARG B 137      25.682   3.888  55.306  1.00252.03           C  
ANISOU 3667  CB  ARG B 137    32789  34860  28112  -7213  -7966  -2490       C  
ATOM   3668  CG  ARG B 137      27.111   3.443  55.537  1.00253.11           C  
ANISOU 3668  CG  ARG B 137    32777  35891  27503  -7290  -8309  -1689       C  
ATOM   3669  CD  ARG B 137      27.152   1.925  55.716  1.00251.88           C  
ANISOU 3669  CD  ARG B 137    32582  35954  27167  -7102  -8453  -1545       C  
ATOM   3670  NE  ARG B 137      28.418   1.307  55.323  1.00253.04           N  
ANISOU 3670  NE  ARG B 137    32311  36940  26891  -6747  -8717   -895       N  
ATOM   3671  CZ  ARG B 137      29.576   1.436  55.962  1.00258.54           C  
ANISOU 3671  CZ  ARG B 137    33026  38256  26952  -7004  -8822   -238       C  
ATOM   3672  NH1 ARG B 137      30.655   0.821  55.500  1.00261.41           N  
ANISOU 3672  NH1 ARG B 137    32984  39267  27073  -6559  -8968    271       N  
ATOM   3673  NH2 ARG B 137      29.669   2.179  57.050  1.00260.89           N  
ANISOU 3673  NH2 ARG B 137    33742  38488  26899  -7668  -8745   -103       N  
ATOM   3674  N   HIS B 138      23.787   6.562  54.445  1.00261.24           N  
ANISOU 3674  N   HIS B 138    34010  34752  30498  -7151  -7281  -3563       N  
ATOM   3675  CA  HIS B 138      22.489   7.040  53.989  1.00265.85           C  
ANISOU 3675  CA  HIS B 138    34648  34601  31761  -7036  -6921  -4148       C  
ATOM   3676  C   HIS B 138      22.277   6.760  52.510  1.00273.45           C  
ANISOU 3676  C   HIS B 138    35128  35568  33203  -6515  -6885  -4442       C  
ATOM   3677  O   HIS B 138      23.230   6.641  51.734  1.00271.13           O  
ANISOU 3677  O   HIS B 138    34498  35860  32658  -6317  -7187  -4105       O  
ATOM   3678  CB  HIS B 138      22.277   8.528  54.300  1.00262.22           C  
ANISOU 3678  CB  HIS B 138    34523  33954  31155  -7490  -6843  -4019       C  
ATOM   3679  CG  HIS B 138      21.944   8.794  55.736  1.00262.32           C  
ANISOU 3679  CG  HIS B 138    35054  33708  30907  -7955  -6686  -3955       C  
ATOM   3680  ND1 HIS B 138      20.655   8.711  56.219  1.00261.08           N  
ANISOU 3680  ND1 HIS B 138    35150  32816  31232  -7907  -6296  -4437       N  
ATOM   3681  CD2 HIS B 138      22.721   9.120  56.796  1.00264.64           C  
ANISOU 3681  CD2 HIS B 138    35654  34379  30516  -8460  -6839  -3458       C  
ATOM   3682  CE1 HIS B 138      20.652   8.983  57.511  1.00263.41           C  
ANISOU 3682  CE1 HIS B 138    35904  33049  31133  -8359  -6225  -4244       C  
ATOM   3683  NE2 HIS B 138      21.892   9.235  57.886  1.00265.33           N  
ANISOU 3683  NE2 HIS B 138    36190  33961  30663  -8714  -6550  -3664       N  
ATOM   3684  N   LEU B 139      20.998   6.645  52.151  1.00272.98           N  
ANISOU 3684  N   LEU B 139    35044  34856  33820  -6307  -6449  -5053       N  
ATOM   3685  CA  LEU B 139      20.593   6.235  50.816  1.00262.85           C  
ANISOU 3685  CA  LEU B 139    33345  33566  32959  -5909  -6213  -5390       C  
ATOM   3686  C   LEU B 139      21.217   7.110  49.738  1.00266.66           C  
ANISOU 3686  C   LEU B 139    33590  34430  33298  -5849  -6448  -5140       C  
ATOM   3687  O   LEU B 139      21.191   8.341  49.812  1.00275.81           O  
ANISOU 3687  O   LEU B 139    34942  35460  34394  -6096  -6510  -5031       O  
ATOM   3688  CB  LEU B 139      19.063   6.276  50.697  1.00255.40           C  
ANISOU 3688  CB  LEU B 139    32549  31882  32610  -5897  -5528  -5944       C  
ATOM   3689  CG  LEU B 139      18.317   7.618  50.627  1.00255.36           C  
ANISOU 3689  CG  LEU B 139    32720  31444  32860  -6028  -5343  -6097       C  
ATOM   3690  CD1 LEU B 139      16.854   7.379  50.319  1.00252.89           C  
ANISOU 3690  CD1 LEU B 139    32589  30560  32940  -5926  -4520  -6361       C  
ATOM   3691  CD2 LEU B 139      18.457   8.450  51.899  1.00261.33           C  
ANISOU 3691  CD2 LEU B 139    33894  32032  33367  -6389  -5628  -5877       C  
ATOM   3692  N   ARG B 140      21.827   6.447  48.758  1.00291.21           N  
ANISOU 3692  N   ARG B 140    36294  38049  36302  -5528  -6581  -4992       N  
ATOM   3693  CA  ARG B 140      22.255   7.071  47.510  1.00267.83           C  
ANISOU 3693  CA  ARG B 140    33063  35388  33312  -5383  -6689  -4834       C  
ATOM   3694  C   ARG B 140      20.991   7.146  46.657  1.00250.28           C  
ANISOU 3694  C   ARG B 140    30932  32687  31475  -5424  -6093  -5189       C  
ATOM   3695  O   ARG B 140      20.792   6.378  45.718  1.00239.17           O  
ANISOU 3695  O   ARG B 140    29518  31255  30102  -5256  -5969  -4986       O  
ATOM   3696  CB  ARG B 140      23.373   6.233  46.900  1.00255.27           C  
ANISOU 3696  CB  ARG B 140    31076  34507  31409  -5020  -7041  -4432       C  
ATOM   3697  CG  ARG B 140      24.283   6.770  45.827  1.00245.96           C  
ANISOU 3697  CG  ARG B 140    29611  33774  30067  -4820  -7318  -4087       C  
ATOM   3698  CD  ARG B 140      24.919   5.515  45.253  1.00236.65           C  
ANISOU 3698  CD  ARG B 140    28040  33155  28722  -4356  -7457  -3833       C  
ATOM   3699  NE  ARG B 140      26.129   5.721  44.475  1.00232.66           N  
ANISOU 3699  NE  ARG B 140    27257  33168  27975  -4059  -7819  -3377       N  
ATOM   3700  CZ  ARG B 140      26.934   4.729  44.111  1.00228.59           C  
ANISOU 3700  CZ  ARG B 140    26430  33167  27255  -3587  -8027  -3041       C  
ATOM   3701  NH1 ARG B 140      28.023   4.982  43.408  1.00227.25           N  
ANISOU 3701  NH1 ARG B 140    26085  33355  26905  -3349  -8309  -2612       N  
ATOM   3702  NH2 ARG B 140      26.667   3.482  44.480  1.00228.24           N  
ANISOU 3702  NH2 ARG B 140    26283  33260  27178  -3366  -7934  -3092       N  
ATOM   3703  N   GLN B 141      20.120   8.081  47.048  1.00243.31           N  
ANISOU 3703  N   GLN B 141    30338  31264  30845  -5639  -5803  -5468       N  
ATOM   3704  CA  GLN B 141      18.761   8.166  46.508  1.00247.52           C  
ANISOU 3704  CA  GLN B 141    31246  31158  31642  -5715  -5212  -5584       C  
ATOM   3705  C   GLN B 141      18.647   8.047  44.987  1.00259.92           C  
ANISOU 3705  C   GLN B 141    32866  32590  33301  -5477  -5304  -5279       C  
ATOM   3706  O   GLN B 141      17.690   7.401  44.526  1.00262.35           O  
ANISOU 3706  O   GLN B 141    33489  32138  34054  -5057  -5177  -5199       O  
ATOM   3707  CB  GLN B 141      18.062   9.438  47.029  1.00243.73           C  
ANISOU 3707  CB  GLN B 141    30912  30317  31376  -5874  -4989  -5873       C  
ATOM   3708  CG  GLN B 141      18.603  10.794  46.597  1.00243.44           C  
ANISOU 3708  CG  GLN B 141    30681  30517  31298  -5894  -5322  -5831       C  
ATOM   3709  CD  GLN B 141      19.787  11.261  47.417  1.00247.35           C  
ANISOU 3709  CD  GLN B 141    31176  31336  31470  -6046  -6003  -5537       C  
ATOM   3710  OE1 GLN B 141      20.900  10.760  47.266  1.00251.09           O  
ANISOU 3710  OE1 GLN B 141    31475  32323  31603  -5965  -6375  -5165       O  
ATOM   3711  NE2 GLN B 141      19.552  12.232  48.293  1.00246.83           N  
ANISOU 3711  NE2 GLN B 141    31466  31005  31312  -6352  -6076  -5446       N  
ATOM   3712  N   PRO B 142      19.541   8.612  44.154  1.00246.89           N  
ANISOU 3712  N   PRO B 142    30859  31456  31491  -5380  -5604  -5089       N  
ATOM   3713  CA  PRO B 142      19.429   8.329  42.719  1.00243.16           C  
ANISOU 3713  CA  PRO B 142    30382  30671  31337  -4854  -5746  -4780       C  
ATOM   3714  C   PRO B 142      19.828   6.893  42.404  1.00241.30           C  
ANISOU 3714  C   PRO B 142    29969  30475  31237  -4364  -5968  -4546       C  
ATOM   3715  O   PRO B 142      21.010   6.537  42.461  1.00249.01           O  
ANISOU 3715  O   PRO B 142    30568  32271  31773  -4437  -6246  -4317       O  
ATOM   3716  CB  PRO B 142      20.394   9.338  42.079  1.00244.78           C  
ANISOU 3716  CB  PRO B 142    30244  31512  31249  -4975  -5963  -4661       C  
ATOM   3717  CG  PRO B 142      20.738  10.311  43.165  1.00251.29           C  
ANISOU 3717  CG  PRO B 142    30947  32710  31823  -5382  -5965  -4976       C  
ATOM   3718  CD  PRO B 142      20.677   9.511  44.410  1.00252.55           C  
ANISOU 3718  CD  PRO B 142    31172  32841  31944  -5461  -5951  -5122       C  
ATOM   3719  N   GLU B 143      18.836   6.060  42.092  1.00244.54           N  
ANISOU 3719  N   GLU B 143    30544  30061  32311  -3734  -5834  -4656       N  
ATOM   3720  CA  GLU B 143      19.051   4.668  41.700  1.00227.65           C  
ANISOU 3720  CA  GLU B 143    28184  27836  30479  -3090  -5998  -4539       C  
ATOM   3721  C   GLU B 143      17.894   4.217  40.824  1.00228.33           C  
ANISOU 3721  C   GLU B 143    28210  27029  31517  -2129  -5822  -4768       C  
ATOM   3722  O   GLU B 143      16.734   4.349  41.219  1.00228.59           O  
ANISOU 3722  O   GLU B 143    28431  26524  31900  -2047  -5511  -5023       O  
ATOM   3723  CB  GLU B 143      19.196   3.734  42.903  1.00214.40           C  
ANISOU 3723  CB  GLU B 143    26606  26363  28492  -3387  -5972  -4550       C  
ATOM   3724  CG  GLU B 143      19.335   2.256  42.508  1.00201.57           C  
ANISOU 3724  CG  GLU B 143    24747  24628  27212  -2674  -6123  -4447       C  
ATOM   3725  CD  GLU B 143      20.639   1.928  41.794  1.00200.74           C  
ANISOU 3725  CD  GLU B 143    24188  25338  26745  -2519  -6506  -4021       C  
ATOM   3726  OE1 GLU B 143      21.490   1.237  42.396  1.00206.84           O  
ANISOU 3726  OE1 GLU B 143    24738  26891  26963  -2728  -6701  -3736       O  
ATOM   3727  OE2 GLU B 143      20.822   2.362  40.638  1.00197.00           O  
ANISOU 3727  OE2 GLU B 143    23550  24786  26513  -2158  -6586  -3940       O  
ATOM   3728  N   HIS B 144      18.209   3.715  39.631  1.00227.44           N  
ANISOU 3728  N   HIS B 144    27757  26850  31811  -1385  -6002  -4673       N  
ATOM   3729  CA  HIS B 144      17.201   3.235  38.692  1.00233.53           C  
ANISOU 3729  CA  HIS B 144    28267  26940  33525   -357  -5866  -4888       C  
ATOM   3730  C   HIS B 144      17.423   1.781  38.304  1.00238.27           C  
ANISOU 3730  C   HIS B 144    28609  27430  34492    372  -5986  -4853       C  
ATOM   3731  O   HIS B 144      16.856   1.310  37.312  1.00238.91           O  
ANISOU 3731  O   HIS B 144    28325  27114  35335   1305  -5968  -4958       O  
ATOM   3732  CB  HIS B 144      17.135   4.119  37.448  1.00232.92           C  
ANISOU 3732  CB  HIS B 144    27996  26742  33760     13  -5906  -4893       C  
ATOM   3733  CG  HIS B 144      16.171   5.255  37.574  1.00233.81           C  
ANISOU 3733  CG  HIS B 144    28198  26650  33987   -211  -5675  -5064       C  
ATOM   3734  ND1 HIS B 144      15.949   5.916  38.763  1.00238.06           N  
ANISOU 3734  ND1 HIS B 144    29148  27299  34004  -1071  -5506  -5117       N  
ATOM   3735  CD2 HIS B 144      15.362   5.839  36.661  1.00232.70           C  
ANISOU 3735  CD2 HIS B 144    27764  26247  34403    306  -5585  -5187       C  
ATOM   3736  CE1 HIS B 144      15.047   6.862  38.574  1.00239.17           C  
ANISOU 3736  CE1 HIS B 144    29300  27213  34359  -1077  -5305  -5269       C  
ATOM   3737  NE2 HIS B 144      14.676   6.838  37.307  1.00235.70           N  
ANISOU 3737  NE2 HIS B 144    28404  26588  34564   -263  -5358  -5307       N  
ATOM   3738  N   LYS B 145      18.266   1.071  39.049  1.00229.78           N  
ANISOU 3738  N   LYS B 145    27637  26809  32858    -37  -6137  -4672       N  
ATOM   3739  CA  LYS B 145      18.490  -0.347  38.818  1.00223.82           C  
ANISOU 3739  CA  LYS B 145    26691  25991  32361    583  -6231  -4638       C  
ATOM   3740  C   LYS B 145      17.612  -1.201  39.723  1.00246.41           C  
ANISOU 3740  C   LYS B 145    29617  28495  35513    727  -6033  -4843       C  
ATOM   3741  O   LYS B 145      16.954  -2.132  39.251  1.00232.57           O  
ANISOU 3741  O   LYS B 145    27567  26329  34470   1584  -5975  -4972       O  
ATOM   3742  CB  LYS B 145      19.964  -0.716  39.016  1.00203.98           C  
ANISOU 3742  CB  LYS B 145    24064  24431  29010    126  -6541  -4193       C  
ATOM   3743  CG  LYS B 145      20.313  -2.079  38.424  1.00180.98           C  
ANISOU 3743  CG  LYS B 145    20927  21516  26323    842  -6620  -4096       C  
ATOM   3744  CD  LYS B 145      21.796  -2.400  38.535  1.00164.71           C  
ANISOU 3744  CD  LYS B 145    18544  20679  23361    483  -6897  -3432       C  
ATOM   3745  CE  LYS B 145      22.650  -1.388  37.782  1.00153.74           C  
ANISOU 3745  CE  LYS B 145    17008  19823  21584    195  -7024  -3126       C  
ATOM   3746  NZ  LYS B 145      24.085  -1.793  37.735  1.00141.98           N  
ANISOU 3746  NZ  LYS B 145    15084  19558  19305     45  -7231  -2390       N  
ATOM   3747  N   VAL B 146      17.579  -0.899  41.018  1.00226.38           N  
ANISOU 3747  N   VAL B 146    27422  26158  32435   -106  -5926  -4858       N  
ATOM   3748  CA  VAL B 146      16.673  -1.575  41.932  1.00243.95           C  
ANISOU 3748  CA  VAL B 146    29810  27976  34903    -61  -5643  -5075       C  
ATOM   3749  C   VAL B 146      15.438  -0.733  42.237  1.00254.50           C  
ANISOU 3749  C   VAL B 146    31315  28876  36508   -228  -5270  -5297       C  
ATOM   3750  O   VAL B 146      14.331  -1.265  42.292  1.00268.47           O  
ANISOU 3750  O   VAL B 146    32911  30267  38828    207  -5020  -5453       O  
ATOM   3751  CB  VAL B 146      17.418  -1.973  43.226  1.00247.56           C  
ANISOU 3751  CB  VAL B 146    30560  28918  34585   -828  -5726  -4956       C  
ATOM   3752  CG1 VAL B 146      18.082  -0.767  43.872  1.00250.33           C  
ANISOU 3752  CG1 VAL B 146    31135  29864  34113  -1859  -5807  -4808       C  
ATOM   3753  CG2 VAL B 146      16.472  -2.651  44.198  1.00251.09           C  
ANISOU 3753  CG2 VAL B 146    31287  28833  35282   -794  -5357  -5206       C  
ATOM   3754  N   LEU B 147      15.586   0.589  42.379  1.00279.22           N  
ANISOU 3754  N   LEU B 147    37421  36336  32336  -4594  -2685   4126       N  
ATOM   3755  CA  LEU B 147      14.433   1.422  42.723  1.00231.97           C  
ANISOU 3755  CA  LEU B 147    31986  29777  26375  -4725  -2658   4059       C  
ATOM   3756  C   LEU B 147      13.411   1.435  41.594  1.00229.93           C  
ANISOU 3756  C   LEU B 147    31895  29108  26360  -4534  -2546   3877       C  
ATOM   3757  O   LEU B 147      12.204   1.317  41.832  1.00224.29           O  
ANISOU 3757  O   LEU B 147    31483  27849  25888  -4316  -2466   3806       O  
ATOM   3758  CB  LEU B 147      14.881   2.847  43.044  1.00199.03           C  
ANISOU 3758  CB  LEU B 147    28106  25727  21789  -5313  -2769   4118       C  
ATOM   3759  CG  LEU B 147      15.136   3.296  44.484  1.00172.86           C  
ANISOU 3759  CG  LEU B 147    24982  22439  18257  -5550  -2874   4261       C  
ATOM   3760  CD1 LEU B 147      13.820   3.435  45.224  1.00156.80           C  
ANISOU 3760  CD1 LEU B 147    23414  19772  16390  -5398  -2816   4240       C  
ATOM   3761  CD2 LEU B 147      16.073   2.346  45.215  1.00172.58           C  
ANISOU 3761  CD2 LEU B 147    24509  22842  18222  -5369  -2922   4391       C  
ATOM   3762  N   GLN B 148      13.890   1.589  40.360  1.00231.88           N  
ANISOU 3762  N   GLN B 148    31948  29613  26543  -4606  -2540   3803       N  
ATOM   3763  CA  GLN B 148      13.024   1.580  39.187  1.00235.80           C  
ANISOU 3763  CA  GLN B 148    32564  29771  27259  -4409  -2438   3619       C  
ATOM   3764  C   GLN B 148      12.343   0.229  39.004  1.00239.39           C  
ANISOU 3764  C   GLN B 148    32822  29978  28155  -3826  -2345   3548       C  
ATOM   3765  O   GLN B 148      11.190   0.160  38.563  1.00231.00           O  
ANISOU 3765  O   GLN B 148    31995  28425  27351  -3606  -2254   3403       O  
ATOM   3766  CB  GLN B 148      13.842   1.943  37.950  1.00243.00           C  
ANISOU 3766  CB  GLN B 148    33253  31076  28001  -4578  -2457   3578       C  
ATOM   3767  CG  GLN B 148      13.050   2.038  36.672  1.00253.02           C  
ANISOU 3767  CG  GLN B 148    34642  32037  29454  -4398  -2357   3382       C  
ATOM   3768  CD  GLN B 148      12.662   3.464  36.364  1.00261.14           C  
ANISOU 3768  CD  GLN B 148    36118  32858  30243  -4809  -2341   3303       C  
ATOM   3769  OE1 GLN B 148      12.253   4.212  37.251  1.00263.26           O  
ANISOU 3769  OE1 GLN B 148    36771  32893  30364  -5078  -2364   3347       O  
ATOM   3770  NE2 GLN B 148      12.802   3.857  35.103  1.00263.58           N  
ANISOU 3770  NE2 GLN B 148    36387  33258  30503  -4852  -2298   3191       N  
ATOM   3771  N   GLN B 149      13.052  -0.860  39.321  1.00239.95           N  
ANISOU 3771  N   GLN B 149    32461  30393  28315  -3567  -2363   3646       N  
ATOM   3772  CA  GLN B 149      12.499  -2.198  39.128  1.00241.62           C  
ANISOU 3772  CA  GLN B 149    32455  30411  28941  -3009  -2274   3584       C  
ATOM   3773  C   GLN B 149      11.185  -2.387  39.878  1.00231.64           C  
ANISOU 3773  C   GLN B 149    31525  28532  27958  -2791  -2199   3540       C  
ATOM   3774  O   GLN B 149      10.254  -3.010  39.357  1.00228.70           O  
ANISOU 3774  O   GLN B 149    31175  27777  27943  -2418  -2109   3410       O  
ATOM   3775  CB  GLN B 149      13.517  -3.241  39.585  1.00248.75           C  
ANISOU 3775  CB  GLN B 149    32883  31798  29834  -2813  -2303   3724       C  
ATOM   3776  CG  GLN B 149      13.415  -4.567  38.860  1.00251.53           C  
ANISOU 3776  CG  GLN B 149    32880  32174  30517  -2295  -2230   3659       C  
ATOM   3777  CD  GLN B 149      14.008  -4.501  37.470  1.00256.61           C  
ANISOU 3777  CD  GLN B 149    33295  33129  31077  -2315  -2252   3601       C  
ATOM   3778  OE1 GLN B 149      15.199  -4.748  37.281  1.00262.16           O  
ANISOU 3778  OE1 GLN B 149    33639  34394  31576  -2378  -2309   3717       O  
ATOM   3779  NE2 GLN B 149      13.184  -4.156  36.488  1.00254.87           N  
ANISOU 3779  NE2 GLN B 149    33284  32547  31007  -2252  -2205   3427       N  
ATOM   3780  N   LEU B 150      11.084  -1.862  41.100  1.00230.21           N  
ANISOU 3780  N   LEU B 150    31606  28238  27625  -3009  -2238   3651       N  
ATOM   3781  CA  LEU B 150       9.842  -2.017  41.852  1.00206.75           C  
ANISOU 3781  CA  LEU B 150    28963  24679  24914  -2796  -2166   3633       C  
ATOM   3782  C   LEU B 150       8.740  -1.103  41.330  1.00202.68           C  
ANISOU 3782  C   LEU B 150    28917  23668  24425  -2934  -2122   3500       C  
ATOM   3783  O   LEU B 150       7.604  -1.544  41.136  1.00204.85           O  
ANISOU 3783  O   LEU B 150    29330  23457  25046  -2608  -2028   3399       O  
ATOM   3784  CB  LEU B 150      10.075  -1.783  43.342  1.00202.42           C  
ANISOU 3784  CB  LEU B 150    28552  24159  24199  -2944  -2221   3804       C  
ATOM   3785  CG  LEU B 150      10.888  -2.824  44.118  1.00206.36           C  
ANISOU 3785  CG  LEU B 150    28643  25027  24740  -2710  -2231   3933       C  
ATOM   3786  CD1 LEU B 150      10.750  -4.212  43.501  1.00207.81           C  
ANISOU 3786  CD1 LEU B 150    28441  25220  25296  -2196  -2134   3860       C  
ATOM   3787  CD2 LEU B 150      12.340  -2.425  44.256  1.00211.35           C  
ANISOU 3787  CD2 LEU B 150    29032  26304  24966  -3070  -2352   4046       C  
ATOM   3788  N   ARG B 151       9.044   0.176  41.105  1.00208.79           N  
ANISOU 3788  N   ARG B 151    29944  24554  24834  -3414  -2185   3500       N  
ATOM   3789  CA  ARG B 151       7.989   1.094  40.684  1.00218.72           C  
ANISOU 3789  CA  ARG B 151    31678  25344  26082  -3555  -2132   3381       C  
ATOM   3790  C   ARG B 151       7.381   0.693  39.347  1.00226.02           C  
ANISOU 3790  C   ARG B 151    32520  26075  27281  -3269  -2040   3182       C  
ATOM   3791  O   ARG B 151       6.211   0.995  39.085  1.00226.72           O  
ANISOU 3791  O   ARG B 151    32956  25663  27522  -3185  -1962   3067       O  
ATOM   3792  CB  ARG B 151       8.530   2.520  40.601  1.00223.40           C  
ANISOU 3792  CB  ARG B 151    32526  26140  26216  -4124  -2208   3411       C  
ATOM   3793  CG  ARG B 151       7.461   3.578  40.780  1.00221.45           C  
ANISOU 3793  CG  ARG B 151    32869  25397  25875  -4329  -2166   3364       C  
ATOM   3794  CD  ARG B 151       7.132   3.744  42.248  1.00215.33           C  
ANISOU 3794  CD  ARG B 151    32372  24397  25047  -4382  -2207   3522       C  
ATOM   3795  NE  ARG B 151       8.309   4.171  42.995  1.00211.93           N  
ANISOU 3795  NE  ARG B 151    31837  24422  24265  -4734  -2339   3679       N  
ATOM   3796  CZ  ARG B 151       8.304   4.496  44.281  1.00211.68           C  
ANISOU 3796  CZ  ARG B 151    32035  24306  24089  -4868  -2408   3831       C  
ATOM   3797  NH1 ARG B 151       7.178   4.439  44.980  1.00208.98           N  
ANISOU 3797  NH1 ARG B 151    32043  23436  23923  -4671  -2352   3861       N  
ATOM   3798  NH2 ARG B 151       9.430   4.874  44.870  1.00217.26           N  
ANISOU 3798  NH2 ARG B 151    32617  25455  24476  -5190  -2536   3958       N  
ATOM   3799  N   SER B 152       8.146   0.023  38.488  1.00228.10           N  
ANISOU 3799  N   SER B 152    32338  26726  27605  -3109  -2051   3141       N  
ATOM   3800  CA  SER B 152       7.560  -0.500  37.260  1.00225.33           C  
ANISOU 3800  CA  SER B 152    31884  26181  27550  -2772  -1972   2953       C  
ATOM   3801  C   SER B 152       6.727  -1.755  37.510  1.00222.78           C  
ANISOU 3801  C   SER B 152    31445  25507  27696  -2245  -1900   2914       C  
ATOM   3802  O   SER B 152       5.568  -1.830  37.090  1.00223.45           O  
ANISOU 3802  O   SER B 152    31747  25103  28050  -2030  -1820   2770       O  
ATOM   3803  CB  SER B 152       8.666  -0.782  36.241  1.00228.22           C  
ANISOU 3803  CB  SER B 152    31824  27076  27814  -2763  -2012   2935       C  
ATOM   3804  OG  SER B 152       9.540  -1.794  36.711  1.00229.50           O  
ANISOU 3804  OG  SER B 152    31550  27627  28022  -2577  -2057   3070       O  
ATOM   3805  N   ARG B 153       7.303  -2.749  38.187  1.00217.43           N  
ANISOU 3805  N   ARG B 153    30422  25071  27119  -2029  -1921   3038       N  
ATOM   3806  CA  ARG B 153       6.613  -4.012  38.431  1.00210.63           C  
ANISOU 3806  CA  ARG B 153    29409  23915  26705  -1517  -1847   3010       C  
ATOM   3807  C   ARG B 153       5.832  -4.085  39.744  1.00218.21           C  
ANISOU 3807  C   ARG B 153    30636  24472  27803  -1440  -1807   3104       C  
ATOM   3808  O   ARG B 153       4.789  -4.747  39.788  1.00216.92           O  
ANISOU 3808  O   ARG B 153    30537  23849  28033  -1072  -1723   3033       O  
ATOM   3809  CB  ARG B 153       7.622  -5.159  38.383  1.00203.75           C  
ANISOU 3809  CB  ARG B 153    28004  23518  25894  -1266  -1868   3086       C  
ATOM   3810  CG  ARG B 153       8.147  -5.512  37.006  1.00196.32           C  
ANISOU 3810  CG  ARG B 153    26751  22870  24972  -1140  -1882   2983       C  
ATOM   3811  CD  ARG B 153       8.825  -6.872  37.054  1.00191.74           C  
ANISOU 3811  CD  ARG B 153    25683  22622  24549   -771  -1876   3054       C  
ATOM   3812  NE  ARG B 153       9.764  -7.070  35.956  1.00183.77           N  
ANISOU 3812  NE  ARG B 153    24338  22078  23407   -754  -1923   3037       N  
ATOM   3813  CZ  ARG B 153       9.666  -8.044  35.058  1.00172.60           C  
ANISOU 3813  CZ  ARG B 153    22655  20663  22261   -343  -1893   2944       C  
ATOM   3814  NH1 ARG B 153       8.673  -8.920  35.133  1.00165.14           N  
ANISOU 3814  NH1 ARG B 153    21727  19278  21742     74  -1817   2850       N  
ATOM   3815  NH2 ARG B 153      10.569  -8.148  34.093  1.00172.23           N  
ANISOU 3815  NH2 ARG B 153    22324  21056  22061   -342  -1943   2951       N  
ATOM   3816  N   GLY B 154       6.291  -3.428  40.808  1.00211.84           N  
ANISOU 3816  N   GLY B 154    29989  23811  26691  -1764  -1868   3264       N  
ATOM   3817  CA  GLY B 154       5.585  -3.458  42.079  1.00208.20           C  
ANISOU 3817  CA  GLY B 154    29793  22972  26341  -1682  -1836   3370       C  
ATOM   3818  C   GLY B 154       5.883  -4.626  42.998  1.00199.45           C  
ANISOU 3818  C   GLY B 154    28377  21972  25432  -1339  -1807   3489       C  
ATOM   3819  O   GLY B 154       5.027  -4.987  43.814  1.00191.67           O  
ANISOU 3819  O   GLY B 154    27561  20563  24701  -1095  -1738   3536       O  
ATOM   3820  N   ASP B 155       7.071  -5.225  42.901  1.00209.04           N  
ANISOU 3820  N   ASP B 155    29148  23744  26534  -1304  -1848   3547       N  
ATOM   3821  CA  ASP B 155       7.449  -6.375  43.716  1.00185.29           C  
ANISOU 3821  CA  ASP B 155    25816  20895  23690   -967  -1807   3654       C  
ATOM   3822  C   ASP B 155       7.842  -5.963  45.135  1.00182.90           C  
ANISOU 3822  C   ASP B 155    25653  20694  23146  -1163  -1855   3834       C  
ATOM   3823  O   ASP B 155       7.785  -4.792  45.525  1.00186.92           O  
ANISOU 3823  O   ASP B 155    26524  21128  23370  -1559  -1928   3882       O  
ATOM   3824  CB  ASP B 155       8.614  -7.141  43.088  1.00174.87           C  
ANISOU 3824  CB  ASP B 155    23980  20162  22301   -863  -1832   3660       C  
ATOM   3825  CG  ASP B 155       8.432  -7.391  41.610  1.00167.41           C  
ANISOU 3825  CG  ASP B 155    22896  19201  21509   -729  -1814   3492       C  
ATOM   3826  OD1 ASP B 155       8.556  -6.425  40.842  1.00165.87           O  
ANISOU 3826  OD1 ASP B 155    22860  19074  21091  -1059  -1873   3424       O  
ATOM   3827  OD2 ASP B 155       8.199  -8.552  41.212  1.00165.18           O  
ANISOU 3827  OD2 ASP B 155    22344  18853  21564   -288  -1741   3430       O  
ATOM   3828  N   ASN B 156       8.228  -6.966  45.919  1.00182.71           N  
ANISOU 3828  N   ASN B 156    25341  20836  23244   -861  -1809   3932       N  
ATOM   3829  CA  ASN B 156       8.826  -6.793  47.232  1.00170.27           C  
ANISOU 3829  CA  ASN B 156    23786  19469  21439   -982  -1855   4103       C  
ATOM   3830  C   ASN B 156      10.303  -7.147  47.137  1.00164.48           C  
ANISOU 3830  C   ASN B 156    22607  19450  20439  -1076  -1918   4171       C  
ATOM   3831  O   ASN B 156      10.688  -8.045  46.385  1.00160.85           O  
ANISOU 3831  O   ASN B 156    21764  19240  20114   -829  -1873   4117       O  
ATOM   3832  CB  ASN B 156       8.157  -7.705  48.267  1.00164.82           C  
ANISOU 3832  CB  ASN B 156    23099  18434  21089   -531  -1736   4169       C  
ATOM   3833  CG  ASN B 156       6.932  -7.082  48.898  1.00164.75           C  
ANISOU 3833  CG  ASN B 156    23596  17795  21204   -544  -1708   4192       C  
ATOM   3834  OD1 ASN B 156       6.764  -5.864  48.890  1.00170.17           O  
ANISOU 3834  OD1 ASN B 156    24656  18373  21629   -946  -1796   4199       O  
ATOM   3835  ND2 ASN B 156       6.051  -7.925  49.430  1.00159.58           N  
ANISOU 3835  ND2 ASN B 156    22961  16715  20956    -94  -1580   4207       N  
ATOM   3836  N   VAL B 157      11.131  -6.448  47.907  1.00172.40           N  
ANISOU 3836  N   VAL B 157    23662  20782  21058  -1428  -2024   4295       N  
ATOM   3837  CA  VAL B 157      12.570  -6.686  47.912  1.00164.39           C  
ANISOU 3837  CA  VAL B 157    22244  20463  19755  -1556  -2094   4376       C  
ATOM   3838  C   VAL B 157      13.020  -6.867  49.351  1.00169.90           C  
ANISOU 3838  C   VAL B 157    22913  21314  20329  -1513  -2107   4525       C  
ATOM   3839  O   VAL B 157      12.673  -6.062  50.222  1.00167.74           O  
ANISOU 3839  O   VAL B 157    23009  20793  19931  -1716  -2161   4587       O  
ATOM   3840  CB  VAL B 157      13.360  -5.554  47.231  1.00152.90           C  
ANISOU 3840  CB  VAL B 157    20828  19368  17898  -2095  -2235   4371       C  
ATOM   3841  CG1 VAL B 157      13.523  -5.843  45.753  1.00166.03           C  
ANISOU 3841  CG1 VAL B 157    22253  21188  19644  -2032  -2214   4256       C  
ATOM   3842  CG2 VAL B 157      12.655  -4.251  47.420  1.00128.87           C  
ANISOU 3842  CG2 VAL B 157    18312  15927  14725  -2453  -2295   4349       C  
ATOM   3843  N   TYR B 158      13.795  -7.917  49.592  1.00174.45           N  
ANISOU 3843  N   TYR B 158    23056  22299  20928  -1240  -2056   4583       N  
ATOM   3844  CA  TYR B 158      14.223  -8.307  50.924  1.00172.30           C  
ANISOU 3844  CA  TYR B 158    22698  22189  20580  -1102  -2037   4710       C  
ATOM   3845  C   TYR B 158      15.742  -8.373  50.946  1.00179.11           C  
ANISOU 3845  C   TYR B 158    23179  23799  21074  -1304  -2124   4795       C  
ATOM   3846  O   TYR B 158      16.388  -8.443  49.899  1.00185.11           O  
ANISOU 3846  O   TYR B 158    23677  24930  21726  -1421  -2161   4760       O  
ATOM   3847  CB  TYR B 158      13.644  -9.673  51.319  1.00165.24           C  
ANISOU 3847  CB  TYR B 158    21632  21055  20098   -496  -1854   4701       C  
ATOM   3848  CG  TYR B 158      12.141  -9.794  51.198  1.00157.29           C  
ANISOU 3848  CG  TYR B 158    20936  19319  19508   -237  -1752   4616       C  
ATOM   3849  CD1 TYR B 158      11.322  -8.677  51.248  1.00157.12           C  
ANISOU 3849  CD1 TYR B 158    21397  18849  19452   -515  -1818   4593       C  
ATOM   3850  CD2 TYR B 158      11.544 -11.031  51.034  1.00157.59           C  
ANISOU 3850  CD2 TYR B 158    20784  19121  19970    288  -1589   4562       C  
ATOM   3851  CE1 TYR B 158       9.957  -8.784  51.138  1.00155.23           C  
ANISOU 3851  CE1 TYR B 158    21438  17957  19584   -279  -1724   4524       C  
ATOM   3852  CE2 TYR B 158      10.181 -11.148  50.922  1.00160.76           C  
ANISOU 3852  CE2 TYR B 158    21455  18862  20762    522  -1500   4487       C  
ATOM   3853  CZ  TYR B 158       9.390 -10.023  50.977  1.00160.12           C  
ANISOU 3853  CZ  TYR B 158    21848  18353  20635    238  -1567   4471       C  
ATOM   3854  OH  TYR B 158       8.025 -10.141  50.867  1.00164.34           O  
ANISOU 3854  OH  TYR B 158    22652  18236  21555    474  -1476   4405       O  
ATOM   3855  N   VAL B 159      16.309  -8.355  52.150  1.00187.07           N  
ANISOU 3855  N   VAL B 159    24158  25029  21891  -1332  -2157   4912       N  
ATOM   3856  CA  VAL B 159      17.752  -8.439  52.350  1.00160.17           C  
ANISOU 3856  CA  VAL B 159    20393  22335  18129  -1508  -2238   5005       C  
ATOM   3857  C   VAL B 159      18.056  -9.691  53.161  1.00145.78           C  
ANISOU 3857  C   VAL B 159    18262  20701  16427  -1036  -2104   5068       C  
ATOM   3858  O   VAL B 159      17.404  -9.945  54.180  1.00147.63           O  
ANISOU 3858  O   VAL B 159    18681  20572  16839   -771  -2023   5095       O  
ATOM   3859  CB  VAL B 159      18.300  -7.193  53.071  1.00144.11           C  
ANISOU 3859  CB  VAL B 159    18593  20464  15698  -2014  -2417   5086       C  
ATOM   3860  CG1 VAL B 159      19.812  -7.247  53.146  1.00139.21           C  
ANISOU 3860  CG1 VAL B 159    17585  20598  14712  -2224  -2509   5176       C  
ATOM   3861  CG2 VAL B 159      17.836  -5.921  52.388  1.00162.39           C  
ANISOU 3861  CG2 VAL B 159    21282  22506  17914  -2457  -2527   5022       C  
ATOM   3862  N   VAL B 160      19.057 -10.458  52.723  1.00148.35           N  
ANISOU 3862  N   VAL B 160    18124  21599  16643   -927  -2075   5099       N  
ATOM   3863  CA  VAL B 160      19.486 -11.634  53.474  1.00161.84           C  
ANISOU 3863  CA  VAL B 160    19514  23568  18408   -500  -1942   5162       C  
ATOM   3864  C   VAL B 160      20.198 -11.177  54.744  1.00185.46           C  
ANISOU 3864  C   VAL B 160    22544  26839  21083   -686  -2027   5271       C  
ATOM   3865  O   VAL B 160      21.170 -10.413  54.689  1.00196.71           O  
ANISOU 3865  O   VAL B 160    23904  28714  22124  -1127  -2190   5327       O  
ATOM   3866  CB  VAL B 160      20.379 -12.543  52.617  1.00150.37           C  
ANISOU 3866  CB  VAL B 160    17572  22669  16893   -343  -1890   5175       C  
ATOM   3867  CG1 VAL B 160      21.053 -13.605  53.477  1.00150.67           C  
ANISOU 3867  CG1 VAL B 160    17278  23092  16878     17  -1770   5259       C  
ATOM   3868  CG2 VAL B 160      19.557 -13.220  51.530  1.00141.43           C  
ANISOU 3868  CG2 VAL B 160    16401  21199  16139    -32  -1780   5063       C  
ATOM   3869  N   THR B 161      19.712 -11.652  55.897  1.00172.47           N  
ANISOU 3869  N   THR B 161    21002  24921  19606   -336  -1916   5300       N  
ATOM   3870  CA  THR B 161      20.235 -11.285  57.207  1.00172.17           C  
ANISOU 3870  CA  THR B 161    21037  25065  19316   -433  -1982   5395       C  
ATOM   3871  C   THR B 161      20.979 -12.422  57.896  1.00167.82           C  
ANISOU 3871  C   THR B 161    20094  24948  18722    -41  -1848   5455       C  
ATOM   3872  O   THR B 161      21.645 -12.182  58.908  1.00185.21           O  
ANISOU 3872  O   THR B 161    22277  27432  20662   -126  -1909   5532       O  
ATOM   3873  CB  THR B 161      19.092 -10.799  58.118  1.00171.73           C  
ANISOU 3873  CB  THR B 161    21460  24337  19452   -347  -1970   5397       C  
ATOM   3874  OG1 THR B 161      19.554 -10.674  59.470  1.00183.00           O  
ANISOU 3874  OG1 THR B 161    22928  25920  20682   -315  -2003   5488       O  
ATOM   3875  CG2 THR B 161      17.920 -11.771  58.079  1.00171.80           C  
ANISOU 3875  CG2 THR B 161    21514  23806  19957    200  -1754   5340       C  
ATOM   3876  N   GLU B 162      20.896 -13.643  57.374  1.00156.58           N  
ANISOU 3876  N   GLU B 162    18363  23592  17536    386  -1667   5421       N  
ATOM   3877  CA  GLU B 162      21.594 -14.783  57.950  1.00163.43           C  
ANISOU 3877  CA  GLU B 162    18852  24884  18360    780  -1516   5474       C  
ATOM   3878  C   GLU B 162      21.810 -15.807  56.850  1.00159.30           C  
ANISOU 3878  C   GLU B 162    17963  24598  17965   1030  -1399   5438       C  
ATOM   3879  O   GLU B 162      20.938 -15.999  56.002  1.00163.49           O  
ANISOU 3879  O   GLU B 162    18591  24715  18813   1149  -1348   5352       O  
ATOM   3880  CB  GLU B 162      20.794 -15.395  59.107  1.00179.62           C  
ANISOU 3880  CB  GLU B 162    21048  26498  20702   1267  -1338   5479       C  
ATOM   3881  CG  GLU B 162      21.496 -16.530  59.827  1.00198.97           C  
ANISOU 3881  CG  GLU B 162    23135  29372  23092   1688  -1165   5532       C  
ATOM   3882  CD  GLU B 162      20.868 -16.845  61.174  1.00218.52           C  
ANISOU 3882  CD  GLU B 162    25798  31465  25765   2081  -1027   5556       C  
ATOM   3883  OE1 GLU B 162      20.288 -15.928  61.794  1.00226.00           O  
ANISOU 3883  OE1 GLU B 162    27144  31999  26724   1901  -1133   5572       O  
ATOM   3884  OE2 GLU B 162      20.966 -18.008  61.619  1.00226.17           O  
ANISOU 3884  OE2 GLU B 162    26517  32548  26868   2580   -808   5566       O  
ATOM   3885  N   VAL B 163      22.968 -16.458  56.867  1.00166.30           N  
ANISOU 3885  N   VAL B 163    18436  26152  18597   1114  -1359   5506       N  
ATOM   3886  CA  VAL B 163      23.300 -17.441  55.848  1.00177.14           C  
ANISOU 3886  CA  VAL B 163    19450  27816  20038   1351  -1256   5493       C  
ATOM   3887  C   VAL B 163      23.751 -18.714  56.545  1.00188.97           C  
ANISOU 3887  C   VAL B 163    20630  29630  21541   1845  -1047   5542       C  
ATOM   3888  O   VAL B 163      24.303 -18.680  57.649  1.00200.23           O  
ANISOU 3888  O   VAL B 163    22012  31313  22752   1865  -1034   5607       O  
ATOM   3889  CB  VAL B 163      24.381 -16.918  54.866  1.00188.02           C  
ANISOU 3889  CB  VAL B 163    20615  29773  21052    914  -1430   5544       C  
ATOM   3890  CG1 VAL B 163      25.737 -16.813  55.544  1.00191.39           C  
ANISOU 3890  CG1 VAL B 163    20789  30901  21030    736  -1495   5662       C  
ATOM   3891  CG2 VAL B 163      24.463 -17.794  53.623  1.00189.42           C  
ANISOU 3891  CG2 VAL B 163    20511  30100  21358   1148  -1345   5520       C  
ATOM   3892  N   LEU B 164      23.486 -19.846  55.901  1.00191.55           N  
ANISOU 3892  N   LEU B 164    20744  29919  22118   2259   -876   5505       N  
ATOM   3893  CA  LEU B 164      23.888 -21.154  56.401  1.00182.28           C  
ANISOU 3893  CA  LEU B 164    19252  29046  20960   2758   -652   5544       C  
ATOM   3894  C   LEU B 164      24.692 -21.824  55.295  1.00202.32           C  
ANISOU 3894  C   LEU B 164    21412  32114  23346   2807   -636   5581       C  
ATOM   3895  O   LEU B 164      24.135 -22.215  54.263  1.00207.44           O  
ANISOU 3895  O   LEU B 164    22047  32513  24256   2945   -604   5515       O  
ATOM   3896  CB  LEU B 164      22.664 -21.979  56.803  1.00157.42           C  
ANISOU 3896  CB  LEU B 164    16236  25267  18307   3283   -432   5467       C  
ATOM   3897  CG  LEU B 164      22.774 -23.088  57.853  1.00152.17           C  
ANISOU 3897  CG  LEU B 164    15396  24707  17716   3811   -181   5499       C  
ATOM   3898  CD1 LEU B 164      21.388 -23.539  58.292  1.00135.29           C  
ANISOU 3898  CD1 LEU B 164    13495  21812  16097   4223     -9   5423       C  
ATOM   3899  CD2 LEU B 164      23.555 -24.276  57.317  1.00169.53           C  
ANISOU 3899  CD2 LEU B 164    17162  27446  19803   4108    -37   5534       C  
ATOM   3900  N   GLN B 165      25.996 -21.958  55.514  1.00202.60           N  
ANISOU 3900  N   GLN B 165    21144  32877  22957   2705   -661   5691       N  
ATOM   3901  CA  GLN B 165      26.918 -22.499  54.531  1.00217.01           C  
ANISOU 3901  CA  GLN B 165    22607  35285  24561   2712   -665   5761       C  
ATOM   3902  C   GLN B 165      27.715 -23.629  55.170  1.00246.08           C  
ANISOU 3902  C   GLN B 165    25945  39492  28061   3103   -468   5842       C  
ATOM   3903  O   GLN B 165      27.477 -24.017  56.317  1.00241.55           O  
ANISOU 3903  O   GLN B 165    25420  38789  27570   3389   -319   5828       O  
ATOM   3904  CB  GLN B 165      27.830 -21.392  53.987  1.00209.17           C  
ANISOU 3904  CB  GLN B 165    21577  34722  23174   2118   -920   5835       C  
ATOM   3905  CG  GLN B 165      28.848 -20.877  54.989  1.00202.92           C  
ANISOU 3905  CG  GLN B 165    20703  34430  21965   1855  -1004   5932       C  
ATOM   3906  CD  GLN B 165      29.626 -19.688  54.464  1.00194.77           C  
ANISOU 3906  CD  GLN B 165    19674  33737  20591   1242  -1265   5996       C  
ATOM   3907  OE1 GLN B 165      29.186 -19.009  53.536  1.00183.99           O  
ANISOU 3907  OE1 GLN B 165    18481  32089  19337    971  -1392   5947       O  
ATOM   3908  NE2 GLN B 165      30.785 -19.427  55.056  1.00200.37           N  
ANISOU 3908  NE2 GLN B 165    20191  35054  20885   1023  -1341   6104       N  
ATOM   3909  N   THR B 166      28.659 -24.175  54.413  1.00242.95           N  
ANISOU 3909  N   THR B 166    25205  39691  27413   3135   -459   5932       N  
ATOM   3910  CA  THR B 166      29.517 -25.246  54.892  1.00252.42           C  
ANISOU 3910  CA  THR B 166    26060  41463  28386   3486   -273   6022       C  
ATOM   3911  C   THR B 166      30.975 -24.820  54.801  1.00263.68           C  
ANISOU 3911  C   THR B 166    27228  43685  29272   3125   -416   6167       C  
ATOM   3912  O   THR B 166      31.378 -24.151  53.845  1.00269.89           O  
ANISOU 3912  O   THR B 166    27986  44655  29904   2738   -610   6214       O  
ATOM   3913  CB  THR B 166      29.302 -26.533  54.084  1.00251.35           C  
ANISOU 3913  CB  THR B 166    25722  41329  28450   3958    -89   6013       C  
ATOM   3914  OG1 THR B 166      30.355 -27.462  54.368  1.00251.87           O  
ANISOU 3914  OG1 THR B 166    25428  42079  28194   4218     62   6128       O  
ATOM   3915  CG2 THR B 166      29.284 -26.231  52.591  1.00253.11           C  
ANISOU 3915  CG2 THR B 166    25929  41538  28701   3738   -247   6016       C  
ATOM   3916  N   GLN B 167      31.762 -25.204  55.802  1.00272.66           N  
ANISOU 3916  N   GLN B 167    28178  45295  30128   3260   -313   6238       N  
ATOM   3917  CA  GLN B 167      33.217 -25.114  55.727  1.00264.24           C  
ANISOU 3917  CA  GLN B 167    26794  45061  28545   3031   -395   6390       C  
ATOM   3918  C   GLN B 167      33.796 -26.495  55.466  1.00266.17           C  
ANISOU 3918  C   GLN B 167    26682  45783  28667   3493   -173   6472       C  
ATOM   3919  O   GLN B 167      34.797 -26.909  56.060  1.00273.35           O  
ANISOU 3919  O   GLN B 167    27333  47313  29216   3584    -91   6572       O  
ATOM   3920  CB  GLN B 167      33.791 -24.503  57.003  1.00260.91           C  
ANISOU 3920  CB  GLN B 167    26401  44891  27843   2821   -458   6417       C  
ATOM   3921  CG  GLN B 167      35.209 -23.948  56.856  1.00256.75           C  
ANISOU 3921  CG  GLN B 167    25626  45131  26798   2396   -636   6562       C  
ATOM   3922  CD  GLN B 167      35.704 -23.257  58.115  1.00248.60           C  
ANISOU 3922  CD  GLN B 167    24652  44291  25512   2165   -725   6570       C  
ATOM   3923  OE1 GLN B 167      34.960 -22.527  58.772  1.00246.50           O  
ANISOU 3923  OE1 GLN B 167    24719  43502  25437   2033   -802   6473       O  
ATOM   3924  NE2 GLN B 167      36.969 -23.480  58.454  1.00243.01           N  
ANISOU 3924  NE2 GLN B 167    23625  44340  24367   2119   -721   6691       N  
ATOM   3925  N   LYS B 168      33.150 -27.221  54.558  1.00262.47           N  
ANISOU 3925  N   LYS B 168    26208  45018  28499   3794    -73   6429       N  
ATOM   3926  CA  LYS B 168      33.561 -28.556  54.161  1.00264.10           C  
ANISOU 3926  CA  LYS B 168    26114  45598  28633   4251    135   6501       C  
ATOM   3927  C   LYS B 168      33.052 -28.848  52.759  1.00272.85           C  
ANISOU 3927  C   LYS B 168    27237  46446  29987   4333     98   6478       C  
ATOM   3928  O   LYS B 168      32.024 -28.322  52.325  1.00270.22           O  
ANISOU 3928  O   LYS B 168    27182  45467  30020   4219      4   6356       O  
ATOM   3929  CB  LYS B 168      33.044 -29.612  55.146  1.00254.39           C  
ANISOU 3929  CB  LYS B 168    24882  44158  27615   4813    436   6428       C  
ATOM   3930  CG  LYS B 168      33.674 -30.980  54.976  1.00248.37           C  
ANISOU 3930  CG  LYS B 168    23789  43902  26677   5276    671   6520       C  
ATOM   3931  CD  LYS B 168      35.141 -30.978  55.332  1.00246.81           C  
ANISOU 3931  CD  LYS B 168    23335  44534  25906   5106    668   6661       C  
ATOM   3932  CE  LYS B 168      35.785 -32.297  54.941  1.00244.02           C  
ANISOU 3932  CE  LYS B 168    23001  44365  25349   5332    966   6621       C  
ATOM   3933  NZ  LYS B 168      37.264 -32.276  55.110  1.00243.95           N  
ANISOU 3933  NZ  LYS B 168    22769  45151  24771   5128    976   6759       N  
ATOM   3934  N   GLU B 169      33.778 -29.717  52.071  1.00269.20           N  
ANISOU 3934  N   GLU B 169    26477  46495  29313   4556    180   6599       N  
ATOM   3935  CA  GLU B 169      33.450 -30.160  50.721  1.00271.50           C  
ANISOU 3935  CA  GLU B 169    26735  46636  29786   4701    159   6599       C  
ATOM   3936  C   GLU B 169      32.777 -31.518  50.854  1.00267.74           C  
ANISOU 3936  C   GLU B 169    26398  45712  29619   5207    489   6433       C  
ATOM   3937  O   GLU B 169      33.445 -32.534  51.049  1.00271.95           O  
ANISOU 3937  O   GLU B 169    26922  46488  29918   5384    732   6414       O  
ATOM   3938  CB  GLU B 169      34.705 -30.228  49.857  1.00279.28           C  
ANISOU 3938  CB  GLU B 169    27529  48240  30344   4486    111   6732       C  
ATOM   3939  CG  GLU B 169      34.446 -30.437  48.376  1.00280.84           C  
ANISOU 3939  CG  GLU B 169    27801  48200  30705   4498     70   6692       C  
ATOM   3940  CD  GLU B 169      35.717 -30.353  47.553  1.00283.46           C  
ANISOU 3940  CD  GLU B 169    27982  49097  30624   4236     31   6821       C  
ATOM   3941  OE1 GLU B 169      36.506 -29.410  47.771  1.00286.05           O  
ANISOU 3941  OE1 GLU B 169    28179  49867  30638   3830   -153   6951       O  
ATOM   3942  OE2 GLU B 169      35.929 -31.228  46.687  1.00283.59           O  
ANISOU 3942  OE2 GLU B 169    28033  49085  30632   4424    189   6788       O  
ATOM   3943  N   VAL B 170      31.452 -31.537  50.759  1.00267.19           N  
ANISOU 3943  N   VAL B 170    26535  44927  30058   5389    499   6292       N  
ATOM   3944  CA  VAL B 170      30.670 -32.746  50.987  1.00252.78           C  
ANISOU 3944  CA  VAL B 170    24956  42521  28568   5781    796   6084       C  
ATOM   3945  C   VAL B 170      30.424 -33.414  49.645  1.00254.70           C  
ANISOU 3945  C   VAL B 170    25314  42501  28959   5856    819   5988       C  
ATOM   3946  O   VAL B 170      30.163 -32.746  48.636  1.00256.41           O  
ANISOU 3946  O   VAL B 170    25504  42632  29289   5687    602   6019       O  
ATOM   3947  CB  VAL B 170      29.346 -32.441  51.715  1.00240.79           C  
ANISOU 3947  CB  VAL B 170    23636  40319  27535   5930    818   5966       C  
ATOM   3948  CG1 VAL B 170      29.622 -31.864  53.092  1.00236.66           C  
ANISOU 3948  CG1 VAL B 170    23020  40050  26849   5892    809   6061       C  
ATOM   3949  CG2 VAL B 170      28.494 -31.478  50.905  1.00237.85           C  
ANISOU 3949  CG2 VAL B 170    23311  39588  27472   5776    556   5980       C  
ATOM   3950  N   GLU B 171      30.515 -34.743  49.628  1.00252.82           N  
ANISOU 3950  N   GLU B 171    25228  42128  28705   6099   1063   5872       N  
ATOM   3951  CA  GLU B 171      30.409 -35.527  48.399  1.00251.08           C  
ANISOU 3951  CA  GLU B 171    25126  41708  28567   6177   1090   5786       C  
ATOM   3952  C   GLU B 171      29.348 -36.614  48.565  1.00235.42           C  
ANISOU 3952  C   GLU B 171    23455  38989  27003   6442   1271   5539       C  
ATOM   3953  O   GLU B 171      29.638 -37.749  48.951  1.00238.04           O  
ANISOU 3953  O   GLU B 171    23907  39331  27208   6600   1466   5481       O  
ATOM   3954  CB  GLU B 171      31.785 -36.107  48.038  1.00260.37           C  
ANISOU 3954  CB  GLU B 171    26172  43547  29209   6138   1162   5926       C  
ATOM   3955  CG  GLU B 171      32.484 -36.850  49.184  1.00266.06           C  
ANISOU 3955  CG  GLU B 171    26902  44584  29606   6268   1374   5962       C  
ATOM   3956  CD  GLU B 171      33.624 -36.063  49.809  1.00272.09           C  
ANISOU 3956  CD  GLU B 171    27381  46098  29902   6055   1308   6171       C  
ATOM   3957  OE1 GLU B 171      33.752 -34.856  49.522  1.00275.60           O  
ANISOU 3957  OE1 GLU B 171    27631  46762  30322   5777   1081   6278       O  
ATOM   3958  OE2 GLU B 171      34.387 -36.650  50.606  1.00274.40           O  
ANISOU 3958  OE2 GLU B 171    27663  46749  29848   6144   1462   6224       O  
ATOM   3959  N   VAL B 172      28.108 -36.264  48.252  1.00249.04           N  
ANISOU 3959  N   VAL B 172    25329  40067  29228   6462   1188   5392       N  
ATOM   3960  CA  VAL B 172      27.001 -37.201  48.356  1.00226.48           C  
ANISOU 3960  CA  VAL B 172    22772  36466  26814   6646   1323   5136       C  
ATOM   3961  C   VAL B 172      26.053 -37.011  47.182  1.00215.13           C  
ANISOU 3961  C   VAL B 172    21450  34511  25778   6617   1180   4998       C  
ATOM   3962  O   VAL B 172      26.084 -37.777  46.220  1.00209.24           O  
ANISOU 3962  O   VAL B 172    20781  33666  25053   6659   1185   4912       O  
ATOM   3963  CB  VAL B 172      26.265 -37.041  49.686  1.00220.37           C  
ANISOU 3963  CB  VAL B 172    22124  35312  26297   6724   1424   5051       C  
ATOM   3964  CG1 VAL B 172      26.991 -37.800  50.788  1.00216.76           C  
ANISOU 3964  CG1 VAL B 172    21672  35158  25531   6828   1626   5086       C  
ATOM   3965  CG2 VAL B 172      26.158 -35.570  50.035  1.00220.42           C  
ANISOU 3965  CG2 VAL B 172    21975  35460  26314   6585   1255   5199       C  
ATOM   3966  N   THR B 205      27.975 -39.624  43.505  1.00241.03           N  
ANISOU 3966  N   THR B 205    24759  38416  28405   6703   1190   5018       N  
ATOM   3967  CA  THR B 205      29.028 -38.733  43.983  1.00237.49           C  
ANISOU 3967  CA  THR B 205    24051  38662  27524   6568   1151   5273       C  
ATOM   3968  C   THR B 205      28.891 -37.324  43.404  1.00235.12           C  
ANISOU 3968  C   THR B 205    23600  38438  27299   6371    910   5359       C  
ATOM   3969  O   THR B 205      28.610 -37.151  42.219  1.00232.13           O  
ANISOU 3969  O   THR B 205    23263  37870  27065   6332    775   5308       O  
ATOM   3970  CB  THR B 205      30.430 -39.284  43.643  1.00236.53           C  
ANISOU 3970  CB  THR B 205    23815  39214  26844   6558   1229   5457       C  
ATOM   3971  OG1 THR B 205      31.401 -38.238  43.776  1.00237.41           O  
ANISOU 3971  OG1 THR B 205    23651  39977  26576   6353   1129   5690       O  
ATOM   3972  CG2 THR B 205      30.471 -39.844  42.225  1.00238.60           C  
ANISOU 3972  CG2 THR B 205    24166  39363  27129   6594   1182   5406       C  
ATOM   3973  N   VAL B 206      29.093 -36.318  44.257  1.00246.05           N  
ANISOU 3973  N   VAL B 206    24819  40095  28574   6236    844   5491       N  
ATOM   3974  CA  VAL B 206      28.982 -34.917  43.875  1.00239.51           C  
ANISOU 3974  CA  VAL B 206    23851  39366  27785   6005    592   5596       C  
ATOM   3975  C   VAL B 206      30.219 -34.175  44.364  1.00245.93           C  
ANISOU 3975  C   VAL B 206    24386  40957  28097   5769    519   5848       C  
ATOM   3976  O   VAL B 206      31.060 -34.720  45.080  1.00238.29           O  
ANISOU 3976  O   VAL B 206    23340  40407  26793   5815    681   5926       O  
ATOM   3977  CB  VAL B 206      27.704 -34.249  44.423  1.00223.92           C  
ANISOU 3977  CB  VAL B 206    21993  36815  26272   6024    523   5485       C  
ATOM   3978  CG1 VAL B 206      26.469 -35.048  44.037  1.00212.93           C  
ANISOU 3978  CG1 VAL B 206    20889  34633  25382   6231    610   5211       C  
ATOM   3979  CG2 VAL B 206      27.796 -34.086  45.926  1.00221.15           C  
ANISOU 3979  CG2 VAL B 206    21590  36596  25842   6048    630   5543       C  
ATOM   3980  N   THR B 207      30.319 -32.909  43.962  1.00247.01           N  
ANISOU 3980  N   THR B 207    24393  41277  28183   5487    258   5969       N  
ATOM   3981  CA  THR B 207      31.457 -32.055  44.293  1.00249.67           C  
ANISOU 3981  CA  THR B 207    24481  42321  28059   5168    127   6197       C  
ATOM   3982  C   THR B 207      30.939 -30.754  44.913  1.00249.93           C  
ANISOU 3982  C   THR B 207    24478  42276  28209   4939   -103   6260       C  
ATOM   3983  O   THR B 207      31.181 -29.653  44.420  1.00253.88           O  
ANISOU 3983  O   THR B 207    24906  42983  28576   4597   -371   6378       O  
ATOM   3984  CB  THR B 207      32.330 -31.787  43.066  1.00256.64           C  
ANISOU 3984  CB  THR B 207    25267  43584  28661   4954      3   6309       C  
ATOM   3985  OG1 THR B 207      32.577 -33.020  42.379  1.00260.63           O  
ANISOU 3985  OG1 THR B 207    25864  44030  29134   5202    201   6234       O  
ATOM   3986  CG2 THR B 207      33.673 -31.198  43.485  1.00257.61           C  
ANISOU 3986  CG2 THR B 207    25155  44455  28272   4631    -62   6521       C  
ATOM   3987  N   ILE B 208      30.201 -30.886  46.012  1.00241.58           N  
ANISOU 3987  N   ILE B 208    23506  40888  27396   5119      4   6180       N  
ATOM   3988  CA  ILE B 208      29.594 -29.726  46.660  1.00241.66           C  
ANISOU 3988  CA  ILE B 208    23688  40584  27548   4829   -144   6140       C  
ATOM   3989  C   ILE B 208      30.660 -29.047  47.509  1.00259.68           C  
ANISOU 3989  C   ILE B 208    25870  43423  29373   4466   -211   6268       C  
ATOM   3990  O   ILE B 208      31.108 -29.611  48.517  1.00257.86           O  
ANISOU 3990  O   ILE B 208    25500  43497  28976   4662    -50   6323       O  
ATOM   3991  CB  ILE B 208      28.379 -30.125  47.512  1.00240.70           C  
ANISOU 3991  CB  ILE B 208    23778  39798  27879   5131     26   5974       C  
ATOM   3992  CG1 ILE B 208      27.249 -30.645  46.624  1.00266.56           C  
ANISOU 3992  CG1 ILE B 208    27178  42467  31637   5431     59   5833       C  
ATOM   3993  CG2 ILE B 208      27.903 -28.936  48.335  1.00222.32           C  
ANISOU 3993  CG2 ILE B 208    21741  37106  25624   4748    -78   5895       C  
ATOM   3994  CD1 ILE B 208      26.009 -31.072  47.384  1.00125.96           C  
ANISOU 3994  CD1 ILE B 208     9571  23979  14308   5744    228   5677       C  
ATOM   3995  N   PRO B 209      31.085 -27.844  47.140  1.00257.91           N  
ANISOU 3995  N   PRO B 209    25712  43341  28939   3943   -442   6313       N  
ATOM   3996  CA  PRO B 209      32.227 -27.208  47.803  1.00261.55           C  
ANISOU 3996  CA  PRO B 209    26041  44400  28935   3579   -529   6450       C  
ATOM   3997  C   PRO B 209      31.863 -26.608  49.155  1.00258.98           C  
ANISOU 3997  C   PRO B 209    25925  43814  28663   3418   -517   6368       C  
ATOM   3998  O   PRO B 209      30.696 -26.444  49.512  1.00259.99           O  
ANISOU 3998  O   PRO B 209    26340  43260  29183   3501   -478   6210       O  
ATOM   3999  CB  PRO B 209      32.628 -26.113  46.811  1.00266.92           C  
ANISOU 3999  CB  PRO B 209    26756  45212  29452   3090   -782   6506       C  
ATOM   4000  CG  PRO B 209      31.333 -25.726  46.172  1.00264.21           C  
ANISOU 4000  CG  PRO B 209    26724  44101  29561   3081   -839   6325       C  
ATOM   4001  CD  PRO B 209      30.505 -26.985  46.092  1.00260.16           C  
ANISOU 4001  CD  PRO B 209    26208  43225  29417   3663   -632   6230       C  
ATOM   4002  N   SER B 210      32.910 -26.285  49.910  1.00266.57           N  
ANISOU 4002  N   SER B 210    26732  45342  29210   3193   -555   6487       N  
ATOM   4003  CA  SER B 210      32.754 -25.504  51.126  1.00252.08           C  
ANISOU 4003  CA  SER B 210    25092  43340  27346   2951   -600   6432       C  
ATOM   4004  C   SER B 210      32.278 -24.095  50.785  1.00245.53           C  
ANISOU 4004  C   SER B 210    24568  42111  26612   2436   -838   6359       C  
ATOM   4005  O   SER B 210      32.560 -23.560  49.709  1.00241.49           O  
ANISOU 4005  O   SER B 210    24028  41717  26010   2151   -997   6403       O  
ATOM   4006  CB  SER B 210      34.071 -25.447  51.900  1.00254.26           C  
ANISOU 4006  CB  SER B 210    25114  44361  27131   2804   -610   6579       C  
ATOM   4007  OG  SER B 210      35.045 -24.688  51.207  1.00257.70           O  
ANISOU 4007  OG  SER B 210    25412  45285  27216   2350   -821   6709       O  
ATOM   4008  N   GLY B 211      31.549 -23.492  51.719  1.00225.82           N  
ANISOU 4008  N   GLY B 211    22371  39138  24292   2330   -854   6251       N  
ATOM   4009  CA  GLY B 211      30.976 -22.178  51.520  1.00244.81           C  
ANISOU 4009  CA  GLY B 211    25110  41104  26804   1874  -1056   6171       C  
ATOM   4010  C   GLY B 211      29.748 -22.149  50.640  1.00257.39           C  
ANISOU 4010  C   GLY B 211    26943  42020  28832   1978  -1055   6035       C  
ATOM   4011  O   GLY B 211      29.236 -21.058  50.357  1.00250.98           O  
ANISOU 4011  O   GLY B 211    26417  40836  28107   1606  -1215   5965       O  
ATOM   4012  N   SER B 212      29.265 -23.306  50.194  1.00247.71           N  
ANISOU 4012  N   SER B 212    25613  40628  27875   2472   -880   5993       N  
ATOM   4013  CA  SER B 212      28.035 -23.368  49.418  1.00247.25           C  
ANISOU 4013  CA  SER B 212    25781  39899  28263   2619   -867   5850       C  
ATOM   4014  C   SER B 212      26.857 -23.017  50.317  1.00243.72           C  
ANISOU 4014  C   SER B 212    25692  38759  28151   2663   -820   5720       C  
ATOM   4015  O   SER B 212      26.721 -23.563  51.416  1.00246.63           O  
ANISOU 4015  O   SER B 212    26050  39076  28581   2944   -665   5719       O  
ATOM   4016  CB  SER B 212      27.855 -24.760  48.814  1.00244.85           C  
ANISOU 4016  CB  SER B 212    25264  39611  28159   3158   -687   5842       C  
ATOM   4017  OG  SER B 212      26.700 -24.821  47.995  1.00243.79           O  
ANISOU 4017  OG  SER B 212    25331  38846  28451   3295   -690   5700       O  
ATOM   4018  N   THR B 213      26.005 -22.104  49.859  1.00267.28           N  
ANISOU 4018  N   THR B 213    28999  41213  31344   2398   -948   5616       N  
ATOM   4019  CA  THR B 213      24.901 -21.624  50.681  1.00221.26           C  
ANISOU 4019  CA  THR B 213    23540  34729  25799   2389   -928   5511       C  
ATOM   4020  C   THR B 213      23.751 -22.622  50.621  1.00213.85           C  
ANISOU 4020  C   THR B 213    22667  33233  25354   2913   -735   5402       C  
ATOM   4021  O   THR B 213      23.275 -22.969  49.534  1.00213.65           O  
ANISOU 4021  O   THR B 213    22625  32992  25559   3053   -730   5330       O  
ATOM   4022  CB  THR B 213      24.451 -20.244  50.210  1.00187.61           C  
ANISOU 4022  CB  THR B 213    19605  30134  21543   1898  -1132   5449       C  
ATOM   4023  OG1 THR B 213      25.455 -19.276  50.546  1.00192.36           O  
ANISOU 4023  OG1 THR B 213    20181  31200  21706   1412  -1300   5549       O  
ATOM   4024  CG2 THR B 213      23.135 -19.856  50.869  1.00156.75           C  
ANISOU 4024  CG2 THR B 213    16100  25472  17985   1951  -1097   5338       C  
ATOM   4025  N   LEU B 214      23.314 -23.094  51.789  1.00209.59           N  
ANISOU 4025  N   LEU B 214    22196  32460  24980   3212   -576   5389       N  
ATOM   4026  CA  LEU B 214      22.234 -24.070  51.864  1.00195.53           C  
ANISOU 4026  CA  LEU B 214    20468  30148  23678   3724   -377   5295       C  
ATOM   4027  C   LEU B 214      20.891 -23.470  52.252  1.00185.99           C  
ANISOU 4027  C   LEU B 214    19673  28154  22839   3690   -389   5190       C  
ATOM   4028  O   LEU B 214      19.856 -23.980  51.815  1.00193.74           O  
ANISOU 4028  O   LEU B 214    20748  28613  24251   3982   -299   5088       O  
ATOM   4029  CB  LEU B 214      22.582 -25.180  52.862  1.00193.06           C  
ANISOU 4029  CB  LEU B 214    19931  30075  23347   4172   -147   5353       C  
ATOM   4030  CG  LEU B 214      23.794 -26.057  52.546  1.00200.65           C  
ANISOU 4030  CG  LEU B 214    20470  31779  23989   4335    -74   5458       C  
ATOM   4031  CD1 LEU B 214      25.056 -25.514  53.208  1.00207.62           C  
ANISOU 4031  CD1 LEU B 214    21217  33317  24353   4019   -164   5585       C  
ATOM   4032  CD2 LEU B 214      23.524 -27.485  52.974  1.00204.38           C  
ANISOU 4032  CD2 LEU B 214    20769  32188  24697   4947    207   5444       C  
ATOM   4033  N   ALA B 215      20.876 -22.410  53.056  1.00181.78           N  
ANISOU 4033  N   ALA B 215    19394  27524  22151   3349   -501   5217       N  
ATOM   4034  CA  ALA B 215      19.629 -21.781  53.481  1.00152.71           C  
ANISOU 4034  CA  ALA B 215    16127  23113  18784   3306   -517   5140       C  
ATOM   4035  C   ALA B 215      19.931 -20.349  53.906  1.00148.85           C  
ANISOU 4035  C   ALA B 215    15891  22685  17980   2760   -725   5184       C  
ATOM   4036  O   ALA B 215      21.083 -19.907  53.882  1.00127.47           O  
ANISOU 4036  O   ALA B 215    13019  20571  14841   2436   -848   5266       O  
ATOM   4037  CB  ALA B 215      18.963 -22.583  54.601  1.00157.40           C  
ANISOU 4037  CB  ALA B 215    16769  23354  19684   3791   -296   5137       C  
ATOM   4038  N   PHE B 216      18.885 -19.622  54.300  1.00139.25           N  
ANISOU 4038  N   PHE B 216    15080  20849  16979   2659   -765   5133       N  
ATOM   4039  CA  PHE B 216      19.015 -18.202  54.622  1.00147.72           C  
ANISOU 4039  CA  PHE B 216    16450  21894  17783   2133   -969   5163       C  
ATOM   4040  C   PHE B 216      17.732 -17.706  55.288  1.00149.19           C  
ANISOU 4040  C   PHE B 216    17078  21341  18265   2185   -948   5125       C  
ATOM   4041  O   PHE B 216      16.755 -18.445  55.436  1.00146.88           O  
ANISOU 4041  O   PHE B 216    16849  20567  18394   2613   -782   5074       O  
ATOM   4042  CB  PHE B 216      19.329 -17.378  53.370  1.00160.51           C  
ANISOU 4042  CB  PHE B 216    18090  23679  19217   1679  -1156   5128       C  
ATOM   4043  CG  PHE B 216      18.290 -17.501  52.285  1.00172.96           C  
ANISOU 4043  CG  PHE B 216    19798  24757  21164   1791  -1131   5003       C  
ATOM   4044  CD1 PHE B 216      18.332 -18.550  51.380  1.00180.26           C  
ANISOU 4044  CD1 PHE B 216    20429  25795  22268   2119  -1031   4957       C  
ATOM   4045  CD2 PHE B 216      17.273 -16.566  52.168  1.00176.36           C  
ANISOU 4045  CD2 PHE B 216    20649  24608  21750   1574  -1210   4932       C  
ATOM   4046  CE1 PHE B 216      17.380 -18.666  50.380  1.00181.37           C  
ANISOU 4046  CE1 PHE B 216    20686  25476  22750   2232  -1016   4834       C  
ATOM   4047  CE2 PHE B 216      16.320 -16.679  51.171  1.00179.34           C  
ANISOU 4047  CE2 PHE B 216    21142  24535  22462   1684  -1185   4809       C  
ATOM   4048  CZ  PHE B 216      16.374 -17.730  50.277  1.00181.52           C  
ANISOU 4048  CZ  PHE B 216    21116  24926  22927   2014  -1092   4756       C  
ATOM   4049  N   ARG B 217      17.752 -16.427  55.670  1.00153.32           N  
ANISOU 4049  N   ARG B 217    17914  21783  18558   1737  -1123   5156       N  
ATOM   4050  CA  ARG B 217      16.637 -15.708  56.273  1.00147.20           C  
ANISOU 4050  CA  ARG B 217    17604  20353  17973   1686  -1146   5142       C  
ATOM   4051  C   ARG B 217      16.597 -14.325  55.646  1.00149.56           C  
ANISOU 4051  C   ARG B 217    18186  20584  18056   1113  -1363   5114       C  
ATOM   4052  O   ARG B 217      17.636 -13.777  55.272  1.00160.78           O  
ANISOU 4052  O   ARG B 217    19465  22530  19094    721  -1509   5147       O  
ATOM   4053  CB  ARG B 217      16.781 -15.556  57.801  1.00155.93           C  
ANISOU 4053  CB  ARG B 217    18836  21448  18962   1772  -1125   5241       C  
ATOM   4054  CG  ARG B 217      15.541 -14.978  58.493  1.00160.73           C  
ANISOU 4054  CG  ARG B 217    19925  21336  19809   1820  -1119   5247       C  
ATOM   4055  CD  ARG B 217      15.543 -15.148  60.013  1.00164.81           C  
ANISOU 4055  CD  ARG B 217    20532  21776  20312   2077  -1043   5345       C  
ATOM   4056  NE  ARG B 217      16.440 -16.191  60.501  1.00177.50           N  
ANISOU 4056  NE  ARG B 217    21722  23889  21829   2402   -909   5384       N  
ATOM   4057  CZ  ARG B 217      16.956 -16.198  61.727  1.00188.22           C  
ANISOU 4057  CZ  ARG B 217    23068  25452  22997   2502   -893   5470       C  
ATOM   4058  NH1 ARG B 217      16.670 -15.212  62.566  1.00195.69           N  
ANISOU 4058  NH1 ARG B 217    24396  26133  23825   2296  -1016   5529       N  
ATOM   4059  NH2 ARG B 217      17.763 -17.178  62.111  1.00189.76           N  
ANISOU 4059  NH2 ARG B 217    22877  26119  23106   2812   -754   5498       N  
ATOM   4060  N   VAL B 218      15.404 -13.752  55.531  1.00146.42           N  
ANISOU 4060  N   VAL B 218    18190  19544  17897   1064  -1377   5059       N  
ATOM   4061  CA  VAL B 218      15.273 -12.478  54.840  1.00140.40           C  
ANISOU 4061  CA  VAL B 218    17710  18684  16953    547  -1558   5018       C  
ATOM   4062  C   VAL B 218      14.710 -11.430  55.788  1.00136.53           C  
ANISOU 4062  C   VAL B 218    17693  17802  16381    328  -1643   5073       C  
ATOM   4063  O   VAL B 218      14.103 -11.737  56.817  1.00140.34           O  
ANISOU 4063  O   VAL B 218    18333  17934  17056    637  -1546   5125       O  
ATOM   4064  CB  VAL B 218      14.401 -12.589  53.577  1.00146.53           C  
ANISOU 4064  CB  VAL B 218    18555  19087  18032    612  -1521   4887       C  
ATOM   4065  CG1 VAL B 218      15.028 -13.569  52.604  1.00146.61           C  
ANISOU 4065  CG1 VAL B 218    18107  19511  18087    811  -1459   4841       C  
ATOM   4066  CG2 VAL B 218      12.988 -13.012  53.946  1.00150.94           C  
ANISOU 4066  CG2 VAL B 218    19363  18932  19055   1004  -1378   4848       C  
ATOM   4067  N   ALA B 219      14.916 -10.173  55.411  1.00125.58           N  
ANISOU 4067  N   ALA B 219    16541  16474  14701   -205  -1825   5067       N  
ATOM   4068  CA  ALA B 219      14.357  -9.030  56.123  1.00141.19           C  
ANISOU 4068  CA  ALA B 219    19010  18069  16566   -476  -1929   5113       C  
ATOM   4069  C   ALA B 219      13.929  -8.017  55.074  1.00150.64           C  
ANISOU 4069  C   ALA B 219    20477  19062  17699   -879  -2033   5028       C  
ATOM   4070  O   ALA B 219      14.772  -7.485  54.346  1.00158.66           O  
ANISOU 4070  O   ALA B 219    21356  20508  18419  -1267  -2153   5007       O  
ATOM   4071  CB  ALA B 219      15.365  -8.424  57.096  1.00142.35           C  
ANISOU 4071  CB  ALA B 219    19162  18630  16296   -764  -2068   5225       C  
ATOM   4072  N   GLN B 220      12.625  -7.770  54.986  1.00150.53           N  
ANISOU 4072  N   GLN B 220    20835  18398  17960   -774  -1977   4981       N  
ATOM   4073  CA  GLN B 220      12.097  -6.841  53.999  1.00155.36           C  
ANISOU 4073  CA  GLN B 220    21729  18768  18532  -1112  -2050   4890       C  
ATOM   4074  C   GLN B 220      12.599  -5.430  54.277  1.00157.69           C  
ANISOU 4074  C   GLN B 220    22309  19224  18381  -1686  -2240   4947       C  
ATOM   4075  O   GLN B 220      12.957  -5.084  55.403  1.00162.33           O  
ANISOU 4075  O   GLN B 220    23015  19899  18764  -1777  -2312   5061       O  
ATOM   4076  CB  GLN B 220      10.564  -6.880  53.996  1.00159.40           C  
ANISOU 4076  CB  GLN B 220    22601  18538  19427   -858  -1944   4843       C  
ATOM   4077  CG  GLN B 220       9.888  -5.762  53.195  1.00167.65           C  
ANISOU 4077  CG  GLN B 220    24037  19264  20400  -1217  -2016   4761       C  
ATOM   4078  CD  GLN B 220       8.395  -5.961  53.015  1.00172.99           C  
ANISOU 4078  CD  GLN B 220    24999  19246  21484   -924  -1896   4700       C  
ATOM   4079  OE1 GLN B 220       7.751  -6.661  53.795  1.00171.89           O  
ANISOU 4079  OE1 GLN B 220    24893  18771  21644   -512  -1781   4757       O  
ATOM   4080  NE2 GLN B 220       7.840  -5.352  51.972  1.00179.08           N  
ANISOU 4080  NE2 GLN B 220    25970  19801  22270  -1127  -1915   4582       N  
ATOM   4081  N   LEU B 221      12.673  -4.629  53.222  1.00156.66           N  
ANISOU 4081  N   LEU B 221    22273  19156  18094  -2067  -2322   4865       N  
ATOM   4082  CA  LEU B 221      12.896  -3.202  53.350  1.00159.38           C  
ANISOU 4082  CA  LEU B 221    22966  19531  18060  -2616  -2485   4899       C  
ATOM   4083  C   LEU B 221      11.791  -2.485  52.596  1.00162.95           C  
ANISOU 4083  C   LEU B 221    23821  19473  18620  -2746  -2464   4800       C  
ATOM   4084  O   LEU B 221      11.097  -3.077  51.771  1.00168.63           O  
ANISOU 4084  O   LEU B 221    24466  19941  19664  -2469  -2346   4691       O  
ATOM   4085  CB  LEU B 221      14.267  -2.762  52.803  1.00156.52           C  
ANISOU 4085  CB  LEU B 221    22319  19834  17319  -3034  -2617   4905       C  
ATOM   4086  CG  LEU B 221      14.794  -3.250  51.447  1.00149.78           C  
ANISOU 4086  CG  LEU B 221    21064  19333  16512  -3014  -2583   4812       C  
ATOM   4087  CD1 LEU B 221      14.074  -2.587  50.287  1.00161.84           C  
ANISOU 4087  CD1 LEU B 221    22840  20549  18103  -3192  -2572   4685       C  
ATOM   4088  CD2 LEU B 221      16.275  -2.954  51.347  1.00147.54           C  
ANISOU 4088  CD2 LEU B 221    20468  19747  15843  -3363  -2713   4879       C  
ATOM   4089  N   VAL B 222      11.589  -1.223  52.945  1.00164.46           N  
ANISOU 4089  N   VAL B 222    24457  19490  18542  -3149  -2574   4842       N  
ATOM   4090  CA  VAL B 222      10.630  -0.360  52.274  1.00169.72           C  
ANISOU 4090  CA  VAL B 222    25545  19715  19225  -3344  -2564   4757       C  
ATOM   4091  C   VAL B 222      11.401   0.887  51.879  1.00189.25           C  
ANISOU 4091  C   VAL B 222    28136  22516  21253  -3944  -2717   4754       C  
ATOM   4092  O   VAL B 222      12.277   1.341  52.625  1.00188.68           O  
ANISOU 4092  O   VAL B 222    28047  22779  20866  -4214  -2847   4859       O  
ATOM   4093  CB  VAL B 222       9.414  -0.016  53.160  1.00167.40           C  
ANISOU 4093  CB  VAL B 222    25761  18786  19057  -3209  -2527   4825       C  
ATOM   4094  CG1 VAL B 222       8.575  -1.261  53.414  1.00165.39           C  
ANISOU 4094  CG1 VAL B 222    25382  18174  19285  -2605  -2359   4818       C  
ATOM   4095  CG2 VAL B 222       9.855   0.607  54.466  1.00171.43           C  
ANISOU 4095  CG2 VAL B 222    26489  19383  19265  -3414  -2654   4982       C  
ATOM   4096  N   ILE B 223      11.100   1.438  50.708  1.00190.04           N  
ANISOU 4096  N   ILE B 223    28349  22530  21328  -4148  -2699   4631       N  
ATOM   4097  CA  ILE B 223      11.835   2.593  50.214  1.00205.59           C  
ANISOU 4097  CA  ILE B 223    30406  24814  22896  -4705  -2824   4618       C  
ATOM   4098  C   ILE B 223      10.809   3.638  49.813  1.00237.57           C  
ANISOU 4098  C   ILE B 223    34992  28381  26892  -4922  -2801   4548       C  
ATOM   4099  O   ILE B 223      10.058   3.455  48.847  1.00221.45           O  
ANISOU 4099  O   ILE B 223    32991  26073  25078  -4759  -2689   4416       O  
ATOM   4100  CB  ILE B 223      12.760   2.255  49.037  1.00185.20           C  
ANISOU 4100  CB  ILE B 223    27354  22738  20276  -4773  -2824   4538       C  
ATOM   4101  CG1 ILE B 223      13.570   0.988  49.319  1.00182.35           C  
ANISOU 4101  CG1 ILE B 223    26451  22791  20043  -4441  -2803   4595       C  
ATOM   4102  CG2 ILE B 223      13.713   3.411  48.788  1.00180.89           C  
ANISOU 4102  CG2 ILE B 223    26855  22584  19292  -5354  -2966   4565       C  
ATOM   4103  CD1 ILE B 223      14.610   1.151  50.399  1.00186.31           C  
ANISOU 4103  CD1 ILE B 223    26833  23703  20254  -4638  -2931   4741       C  
ATOM   4104  N   ASP B 224      10.782   4.728  50.565  1.00226.04           N  
ANISOU 4104  N   ASP B 224    28432  23549  33903  -2329  -3111  -2014       N  
ATOM   4105  CA  ASP B 224      10.106   5.981  50.271  1.00249.76           C  
ANISOU 4105  CA  ASP B 224    31065  26516  37319  -2039  -3595  -2322       C  
ATOM   4106  C   ASP B 224      11.038   7.087  50.738  1.00266.00           C  
ANISOU 4106  C   ASP B 224    32653  28590  39824  -1693  -4022  -2584       C  
ATOM   4107  O   ASP B 224      12.261   6.909  50.706  1.00263.59           O  
ANISOU 4107  O   ASP B 224    32401  28221  39532  -1698  -3957  -2359       O  
ATOM   4108  CB  ASP B 224       8.726   6.042  50.933  1.00259.76           C  
ANISOU 4108  CB  ASP B 224    32189  28003  38506  -2073  -3642  -2724       C  
ATOM   4109  CG  ASP B 224       8.784   5.847  52.433  1.00267.28           C  
ANISOU 4109  CG  ASP B 224    32891  29348  39315  -2103  -3635  -3125       C  
ATOM   4110  OD1 ASP B 224       9.764   5.249  52.922  1.00269.77           O  
ANISOU 4110  OD1 ASP B 224    33299  29751  39452  -2230  -3440  -2992       O  
ATOM   4111  OD2 ASP B 224       7.835   6.274  53.123  1.00273.30           O  
ANISOU 4111  OD2 ASP B 224    33350  30377  40116  -1994  -3823  -3580       O  
ATOM   4112  N   SER B 225      10.483   8.240  51.111  1.00267.11           N  
ANISOU 4112  N   SER B 225    32350  28794  40345  -1370  -4441  -3051       N  
ATOM   4113  CA  SER B 225      11.253   9.321  51.721  1.00264.21           C  
ANISOU 4113  CA  SER B 225    31518  28459  40410   -996  -4825  -3403       C  
ATOM   4114  C   SER B 225      12.322   8.803  52.684  1.00262.83           C  
ANISOU 4114  C   SER B 225    31307  28497  40058  -1076  -4678  -3451       C  
ATOM   4115  O   SER B 225      13.397   9.403  52.792  1.00271.61           O  
ANISOU 4115  O   SER B 225    32202  29527  41469   -857  -4889  -3492       O  
ATOM   4116  CB  SER B 225      10.316  10.288  52.452  1.00264.54           C  
ANISOU 4116  CB  SER B 225    31132  28668  40714   -681  -5137  -4020       C  
ATOM   4117  OG  SER B 225       9.645   9.647  53.525  1.00262.60           O  
ANISOU 4117  OG  SER B 225    30860  28826  40090   -838  -4943  -4323       O  
ATOM   4118  N   ASP B 226      12.056   7.697  53.380  1.00277.50           N  
ANISOU 4118  N   ASP B 226    33365  30638  41434  -1394  -4327  -3445       N  
ATOM   4119  CA  ASP B 226      13.044   7.074  54.253  1.00253.00           C  
ANISOU 4119  CA  ASP B 226    30250  27781  38097  -1524  -4162  -3446       C  
ATOM   4120  C   ASP B 226      13.162   5.594  53.898  1.00237.79           C  
ANISOU 4120  C   ASP B 226    28893  25768  35689  -1980  -3613  -2916       C  
ATOM   4121  O   ASP B 226      12.488   5.093  52.993  1.00240.28           O  
ANISOU 4121  O   ASP B 226    29599  25848  35848  -2157  -3366  -2584       O  
ATOM   4122  CB  ASP B 226      12.657   7.236  55.730  1.00241.84           C  
ANISOU 4122  CB  ASP B 226    28404  26955  36530  -1416  -4310  -4058       C  
ATOM   4123  CG  ASP B 226      12.710   8.678  56.202  1.00231.46           C  
ANISOU 4123  CG  ASP B 226    26557  25711  35677   -904  -4777  -4614       C  
ATOM   4124  OD1 ASP B 226      13.474   9.477  55.621  1.00226.62           O  
ANISOU 4124  OD1 ASP B 226    25870  24725  35508   -664  -4993  -4523       O  
ATOM   4125  OD2 ASP B 226      11.981   9.013  57.159  1.00227.49           O  
ANISOU 4125  OD2 ASP B 226    25711  25642  35084   -725  -4914  -5143       O  
ATOM   4126  N   LEU B 227      14.049   4.894  54.603  1.00232.05           N  
ANISOU 4126  N   LEU B 227    28214  25230  34723  -2148  -3404  -2837       N  
ATOM   4127  CA  LEU B 227      14.189   3.452  54.455  1.00223.76           C  
ANISOU 4127  CA  LEU B 227    27639  24004  33376  -2503  -2906  -2377       C  
ATOM   4128  C   LEU B 227      14.551   2.874  55.817  1.00228.30           C  
ANISOU 4128  C   LEU B 227    27659  24788  34298  -2480  -3172  -2739       C  
ATOM   4129  O   LEU B 227      15.198   3.536  56.632  1.00233.60           O  
ANISOU 4129  O   LEU B 227    27699  25769  35289  -2175  -3627  -3229       O  
ATOM   4130  CB  LEU B 227      15.210   3.072  53.371  1.00212.65           C  
ANISOU 4130  CB  LEU B 227    26734  22213  31849  -2551  -2522  -1729       C  
ATOM   4131  CG  LEU B 227      16.720   3.054  53.593  1.00205.39           C  
ANISOU 4131  CG  LEU B 227    25722  21202  31116  -2458  -2551  -1546       C  
ATOM   4132  CD1 LEU B 227      17.184   1.659  53.979  1.00198.19           C  
ANISOU 4132  CD1 LEU B 227    25061  20089  30154  -2656  -2163  -1103       C  
ATOM   4133  CD2 LEU B 227      17.425   3.518  52.330  1.00203.78           C  
ANISOU 4133  CD2 LEU B 227    25656  20700  31069  -2291  -2595  -1179       C  
ATOM   4134  N   ASP B 228      14.134   1.633  56.055  1.00213.22           N  
ANISOU 4134  N   ASP B 228    25952  22793  32269  -2788  -2834  -2515       N  
ATOM   4135  CA  ASP B 228      14.452   0.954  57.305  1.00217.15           C  
ANISOU 4135  CA  ASP B 228    25802  23629  33074  -2825  -2988  -2870       C  
ATOM   4136  C   ASP B 228      14.322  -0.547  57.096  1.00216.90           C  
ANISOU 4136  C   ASP B 228    26421  23455  32536  -3052  -2095  -1930       C  
ATOM   4137  O   ASP B 228      13.708  -1.009  56.131  1.00213.71           O  
ANISOU 4137  O   ASP B 228    26747  22366  32086  -3434  -1762  -1464       O  
ATOM   4138  CB  ASP B 228      13.558   1.418  58.463  1.00223.35           C  
ANISOU 4138  CB  ASP B 228    25732  25394  33737  -2558  -3444  -3861       C  
ATOM   4139  CG  ASP B 228      12.088   1.393  58.114  1.00224.71           C  
ANISOU 4139  CG  ASP B 228    26242  25533  33605  -2708  -3289  -3872       C  
ATOM   4140  OD1 ASP B 228      11.762   1.190  56.928  1.00221.57           O  
ANISOU 4140  OD1 ASP B 228    26677  24477  33034  -2966  -2897  -3206       O  
ATOM   4141  OD2 ASP B 228      11.258   1.572  59.031  1.00228.05           O  
ANISOU 4141  OD2 ASP B 228    26076  26748  33827  -2508  -3517  -4534       O  
ATOM   4142  N   VAL B 229      14.909  -1.295  58.013  1.00206.28           N  
ANISOU 4142  N   VAL B 229    24887  23029  30461  -2640  -1561  -1543       N  
ATOM   4143  CA  VAL B 229      14.903  -2.750  57.950  1.00202.96           C  
ANISOU 4143  CA  VAL B 229    25085  22700  29330  -2704   -592   -548       C  
ATOM   4144  C   VAL B 229      13.654  -3.267  58.647  1.00204.35           C  
ANISOU 4144  C   VAL B 229    25066  23631  28946  -2642   -333   -760       C  
ATOM   4145  O   VAL B 229      13.078  -2.613  59.524  1.00215.32           O  
ANISOU 4145  O   VAL B 229    25705  25813  30295  -2366   -807  -1623       O  
ATOM   4146  CB  VAL B 229      16.178  -3.341  58.590  1.00206.90           C  
ANISOU 4146  CB  VAL B 229    25499  23819  29295  -2279   -110     17       C  
ATOM   4147  CG1 VAL B 229      17.407  -2.977  57.772  1.00202.66           C  
ANISOU 4147  CG1 VAL B 229    25271  22438  29293  -2396   -264    372       C  
ATOM   4148  CG2 VAL B 229      16.323  -2.866  60.033  1.00215.39           C  
ANISOU 4148  CG2 VAL B 229    25602  26209  30028  -1680   -421   -705       C  
ATOM   4149  N   LEU B 230      13.231  -4.465  58.250  1.00199.47           N  
ANISOU 4149  N   LEU B 230    25134  22763  27893  -2900    434     44       N  
ATOM   4150  CA  LEU B 230      11.984  -5.051  58.723  1.00195.98           C  
ANISOU 4150  CA  LEU B 230    24631  22867  26966  -2936    744    -47       C  
ATOM   4151  C   LEU B 230      12.308  -6.412  59.318  1.00199.17           C  
ANISOU 4151  C   LEU B 230    25273  23929  26475  -2702   1686    797       C  
ATOM   4152  O   LEU B 230      11.775  -7.440  58.888  1.00199.46           O  
ANISOU 4152  O   LEU B 230    25938  23651  26196  -2997   2327   1463       O  
ATOM   4153  CB  LEU B 230      10.959  -5.180  57.593  1.00190.36           C  
ANISOU 4153  CB  LEU B 230    24546  21140  26642  -3539    740     67       C  
ATOM   4154  CG  LEU B 230       9.915  -4.076  57.392  1.00192.59           C  
ANISOU 4154  CG  LEU B 230    24458  21194  27523  -3733    -70   -914       C  
ATOM   4155  CD1 LEU B 230       8.907  -4.056  58.534  1.00198.30           C  
ANISOU 4155  CD1 LEU B 230    24513  23045  27789  -3453   -136  -1528       C  
ATOM   4156  CD2 LEU B 230      10.567  -2.708  57.213  1.00191.46           C  
ANISOU 4156  CD2 LEU B 230    23898  20732  28114  -3641   -932  -1594       C  
ATOM   4157  N   LEU B 231      13.209  -6.405  60.305  1.00216.17           N  
ANISOU 4157  N   LEU B 231    26919  26987  28227  -2164   1759    765       N  
ATOM   4158  CA  LEU B 231      13.568  -7.594  61.067  1.00206.46           C  
ANISOU 4158  CA  LEU B 231    25776  26563  26107  -1837   2600   1462       C  
ATOM   4159  C   LEU B 231      12.347  -8.359  61.553  1.00212.76           C  
ANISOU 4159  C   LEU B 231    26576  27915  26347  -1873   3051   1522       C  
ATOM   4160  O   LEU B 231      12.443  -9.561  61.830  1.00214.64           O  
ANISOU 4160  O   LEU B 231    27161  28493  25900  -1787   3879   2298       O  
ATOM   4161  CB  LEU B 231      14.431  -7.157  62.247  1.00191.42           C  
ANISOU 4161  CB  LEU B 231    23081  25730  23920  -1196   2380   1063       C  
ATOM   4162  CG  LEU B 231      15.686  -6.429  61.768  1.00177.11           C  
ANISOU 4162  CG  LEU B 231    21263  23366  22664  -1166   1956   1036       C  
ATOM   4163  CD1 LEU B 231      16.380  -5.751  62.923  1.00184.95           C  
ANISOU 4163  CD1 LEU B 231    21367  25391  23514   -558   1549    416       C  
ATOM   4164  CD2 LEU B 231      16.625  -7.388  61.055  1.00169.93           C  
ANISOU 4164  CD2 LEU B 231    21160  21834  21570  -1322   2657   2154       C  
ATOM   4165  N   PHE B 232      11.211  -7.684  61.667  1.00207.21           N  
ANISOU 4165  N   PHE B 232    25487  27316  25928  -1993   2524    722       N  
ATOM   4166  CA  PHE B 232       9.911  -8.281  61.919  1.00206.29           C  
ANISOU 4166  CA  PHE B 232    25413  27529  25440  -2136   2854    718       C  
ATOM   4167  C   PHE B 232       9.180  -8.320  60.584  1.00220.29           C  
ANISOU 4167  C   PHE B 232    27887  28056  27756  -2806   2791    895       C  
ATOM   4168  O   PHE B 232       8.532  -7.341  60.195  1.00222.36           O  
ANISOU 4168  O   PHE B 232    27935  27918  28634  -3023   2078    152       O  
ATOM   4169  CB  PHE B 232       9.122  -7.498  62.979  1.00192.85           C  
ANISOU 4169  CB  PHE B 232    22782  26829  23662  -1793   2306   -309       C  
ATOM   4170  CG  PHE B 232       8.884  -6.043  62.641  1.00177.08           C  
ANISOU 4170  CG  PHE B 232    20378  24421  22481  -1903   1290  -1288       C  
ATOM   4171  CD1 PHE B 232       9.933  -5.139  62.583  1.00162.39           C  
ANISOU 4171  CD1 PHE B 232    18241  22389  21070  -1716    736  -1619       C  
ATOM   4172  CD2 PHE B 232       7.597  -5.579  62.412  1.00170.42           C  
ANISOU 4172  CD2 PHE B 232    19411  23392  21948  -2183    890  -1888       C  
ATOM   4173  CE1 PHE B 232       9.707  -3.809  62.281  1.00148.45           C  
ANISOU 4173  CE1 PHE B 232    16106  20240  20059  -1816   -189  -2512       C  
ATOM   4174  CE2 PHE B 232       7.367  -4.251  62.111  1.00160.86           C  
ANISOU 4174  CE2 PHE B 232    17835  21810  21474  -2273    -36  -2785       C  
ATOM   4175  CZ  PHE B 232       8.424  -3.365  62.047  1.00150.63           C  
ANISOU 4175  CZ  PHE B 232    16280  20324  20627  -2089   -574  -3096       C  
ATOM   4176  N   PRO B 233       9.273  -9.410  59.841  1.00216.13           N  
ANISOU 4176  N   PRO B 233    28207  26880  27033  -3137   3504   1854       N  
ATOM   4177  CA  PRO B 233       8.717  -9.395  58.483  1.00215.44           C  
ANISOU 4177  CA  PRO B 233    28818  25525  27513  -3764   3405   2035       C  
ATOM   4178  C   PRO B 233       7.200  -9.389  58.498  1.00216.29           C  
ANISOU 4178  C   PRO B 233    28824  25711  27645  -4023   3296   1604       C  
ATOM   4179  O   PRO B 233       6.558 -10.445  58.496  1.00221.94           O  
ANISOU 4179  O   PRO B 233    29919  26500  27907  -4196   3952   2138       O  
ATOM   4180  CB  PRO B 233       9.275 -10.680  57.850  1.00216.91           C  
ANISOU 4180  CB  PRO B 233    29571  25438  27408  -3611   3800   3032       C  
ATOM   4181  CG  PRO B 233      10.332 -11.188  58.806  1.00218.83           C  
ANISOU 4181  CG  PRO B 233    29622  26500  27022  -3190   4271   3431       C  
ATOM   4182  CD  PRO B 233       9.957 -10.675  60.155  1.00219.39           C  
ANISOU 4182  CD  PRO B 233    29001  27632  26726  -2950   4410   2822       C  
ATOM   4183  N   ASP B 234       6.619  -8.191  58.511  1.00214.10           N  
ANISOU 4183  N   ASP B 234    28028  25414  27908  -4053   2459    629       N  
ATOM   4184  CA  ASP B 234       5.174  -8.063  58.422  1.00209.10           C  
ANISOU 4184  CA  ASP B 234    27299  24765  27386  -4326   2269    162       C  
ATOM   4185  C   ASP B 234       4.758  -8.290  56.977  1.00217.13           C  
ANISOU 4185  C   ASP B 234    29161  24452  28886  -4961   2330    549       C  
ATOM   4186  O   ASP B 234       5.329  -7.701  56.055  1.00221.93           O  
ANISOU 4186  O   ASP B 234    29954  24296  30074  -4933   1827    554       O  
ATOM   4187  CB  ASP B 234       4.730  -6.679  58.896  1.00202.40           C  
ANISOU 4187  CB  ASP B 234    25625  24318  26960  -4131   1334  -1015       C  
ATOM   4188  CG  ASP B 234       3.225  -6.575  59.089  1.00202.20           C  
ANISOU 4188  CG  ASP B 234    25351  24564  26910  -4298   1169  -1549       C  
ATOM   4189  OD1 ASP B 234       2.475  -7.364  58.476  1.00200.38           O  
ANISOU 4189  OD1 ASP B 234    25700  23840  26594  -4716   1618  -1076       O  
ATOM   4190  OD2 ASP B 234       2.790  -5.694  59.860  1.00205.29           O  
ANISOU 4190  OD2 ASP B 234    24958  25670  27372  -4004    580  -2455       O  
ATOM   4191  N   LYS B 235       3.759  -9.150  56.785  1.00216.49           N  
ANISOU 4191  N   LYS B 235    29409  24328  28518  -5183   2768    881       N  
ATOM   4192  CA  LYS B 235       3.318  -9.463  55.432  1.00213.81           C  
ANISOU 4192  CA  LYS B 235    29211  23537  28490  -4682   2238   1178       C  
ATOM   4193  C   LYS B 235       2.564  -8.293  54.810  1.00220.85           C  
ANISOU 4193  C   LYS B 235    29840  24020  30054  -4733   1433    503       C  
ATOM   4194  O   LYS B 235       2.656  -8.059  53.599  1.00206.47           O  
ANISOU 4194  O   LYS B 235    27854  21877  28719  -4255    895    692       O  
ATOM   4195  CB  LYS B 235       2.471 -10.730  55.430  1.00204.62           C  
ANISOU 4195  CB  LYS B 235    28172  22705  26871  -4532   2640   1599       C  
ATOM   4196  CG  LYS B 235       2.365 -11.325  54.048  1.00201.61           C  
ANISOU 4196  CG  LYS B 235    27752  22100  26750  -4047   2214   1940       C  
ATOM   4197  CD  LYS B 235       3.773 -11.517  53.491  1.00201.46           C  
ANISOU 4197  CD  LYS B 235    27932  21954  26658  -3809   2223   2185       C  
ATOM   4198  CE  LYS B 235       3.771 -11.603  51.983  1.00201.26           C  
ANISOU 4198  CE  LYS B 235    28233  21536  26702  -3718   2060   2060       C  
ATOM   4199  NZ  LYS B 235       3.338 -12.953  51.548  1.00200.60           N  
ANISOU 4199  NZ  LYS B 235    28504  21532  26182  -3661   2425   2216       N  
ATOM   4200  N   LYS B 236       1.800  -7.560  55.624  1.00223.68           N  
ANISOU 4200  N   LYS B 236    29919  24584  30484  -5212   1295   -342       N  
ATOM   4201  CA  LYS B 236       0.982  -6.459  55.123  1.00227.38           C  
ANISOU 4201  CA  LYS B 236    30029  24839  31528  -5016    384   -962       C  
ATOM   4202  C   LYS B 236       1.834  -5.409  54.416  1.00222.33           C  
ANISOU 4202  C   LYS B 236    29192  23794  31487  -4561   -432   -992       C  
ATOM   4203  O   LYS B 236       1.601  -5.087  53.246  1.00219.81           O  
ANISOU 4203  O   LYS B 236    28705  23319  31495  -3944   -813   -760       O  
ATOM   4204  CB  LYS B 236       0.204  -5.835  56.283  1.00236.18           C  
ANISOU 4204  CB  LYS B 236    30593  26582  32563  -5399    226  -2028       C  
ATOM   4205  CG  LYS B 236      -0.529  -4.553  55.938  1.00237.06           C  
ANISOU 4205  CG  LYS B 236    30423  26619  33028  -5018   -835  -2528       C  
ATOM   4206  CD  LYS B 236      -1.063  -3.882  57.193  1.00239.23           C  
ANISOU 4206  CD  LYS B 236    29873  27821  33204  -5021  -1063  -3614       C  
ATOM   4207  CE  LYS B 236      -1.641  -2.513  56.881  1.00237.72           C  
ANISOU 4207  CE  LYS B 236    29691  27629  33001  -4652  -1848  -3799       C  
ATOM   4208  NZ  LYS B 236      -1.897  -1.723  58.117  1.00240.29           N  
ANISOU 4208  NZ  LYS B 236    29100  28875  33325  -4302  -2160  -4705       N  
ATOM   4209  N   GLN B 237       2.817  -4.851  55.123  1.00228.90           N  
ANISOU 4209  N   GLN B 237    29903  24782  32287  -4716   -532  -1350       N  
ATOM   4210  CA  GLN B 237       3.621  -3.761  54.580  1.00216.17           C  
ANISOU 4210  CA  GLN B 237    28545  23127  30461  -4443  -1210  -1298       C  
ATOM   4211  C   GLN B 237       4.281  -4.165  53.265  1.00196.48           C  
ANISOU 4211  C   GLN B 237    25597  20262  28796  -3590  -1053   -647       C  
ATOM   4212  O   GLN B 237       4.905  -5.226  53.166  1.00195.21           O  
ANISOU 4212  O   GLN B 237    25676  20017  28477  -3686   -376    -98       O  
ATOM   4213  CB  GLN B 237       4.679  -3.332  55.595  1.00218.63           C  
ANISOU 4213  CB  GLN B 237    28410  23650  31010  -4660  -1071  -1930       C  
ATOM   4214  CG  GLN B 237       4.130  -2.494  56.739  1.00225.21           C  
ANISOU 4214  CG  GLN B 237    28243  25242  32083  -4480  -1490  -3061       C  
ATOM   4215  CD  GLN B 237       3.419  -1.243  56.256  1.00230.67           C  
ANISOU 4215  CD  GLN B 237    29038  26050  32556  -4240  -1961  -3254       C  
ATOM   4216  OE1 GLN B 237       3.827  -0.622  55.274  1.00231.79           O  
ANISOU 4216  OE1 GLN B 237    29653  25907  32510  -4184  -1891  -2928       O  
ATOM   4217  NE2 GLN B 237       2.347  -0.868  56.945  1.00234.75           N  
ANISOU 4217  NE2 GLN B 237    29037  27094  33061  -4098  -2238  -3827       N  
ATOM   4218  N   ARG B 238       4.128  -3.318  52.251  1.00203.30           N  
ANISOU 4218  N   ARG B 238    27445  21377  28424  -4126    311  -1432       N  
ATOM   4219  CA  ARG B 238       4.781  -3.496  50.962  1.00186.93           C  
ANISOU 4219  CA  ARG B 238    25099  18820  27106  -3674    477  -1070       C  
ATOM   4220  C   ARG B 238       5.963  -2.540  50.833  1.00174.62           C  
ANISOU 4220  C   ARG B 238    23975  17232  25141  -3827     90  -1068       C  
ATOM   4221  O   ARG B 238       6.042  -1.520  51.521  1.00170.04           O  
ANISOU 4221  O   ARG B 238    23238  16781  24588  -3960   -508  -1434       O  
ATOM   4222  CB  ARG B 238       3.780  -3.255  49.824  1.00190.52           C  
ANISOU 4222  CB  ARG B 238    25696  19120  27575  -3693    351  -1090       C  
ATOM   4223  CG  ARG B 238       4.181  -3.822  48.466  1.00198.38           C  
ANISOU 4223  CG  ARG B 238    26700  19793  28885  -3429    323   -524       C  
ATOM   4224  CD  ARG B 238       3.073  -3.634  47.428  1.00209.88           C  
ANISOU 4224  CD  ARG B 238    28290  21142  30311  -3490    231   -605       C  
ATOM   4225  NE  ARG B 238       1.751  -3.995  47.936  1.00216.87           N  
ANISOU 4225  NE  ARG B 238    28936  22112  31352  -3534    109   -726       N  
ATOM   4226  CZ  ARG B 238       0.819  -3.117  48.298  1.00218.69           C  
ANISOU 4226  CZ  ARG B 238    29250  22550  31293  -3776    152  -1325       C  
ATOM   4227  NH1 ARG B 238       1.057  -1.815  48.215  1.00217.54           N  
ANISOU 4227  NH1 ARG B 238    29445  22447  30764  -3991   -270  -1556       N  
ATOM   4228  NH2 ARG B 238      -0.353  -3.543  48.748  1.00219.34           N  
ANISOU 4228  NH2 ARG B 238    28968  22695  31675  -3729     31  -1428       N  
ATOM   4229  N   THR B 239       6.884  -2.881  49.925  1.00187.74           N  
ANISOU 4229  N   THR B 239    25690  18641  27003  -3582    323   -671       N  
ATOM   4230  CA  THR B 239       8.053  -2.035  49.695  1.00176.76           C  
ANISOU 4230  CA  THR B 239    24398  17120  25640  -3568    -36   -649       C  
ATOM   4231  C   THR B 239       7.704  -0.686  49.085  1.00202.84           C  
ANISOU 4231  C   THR B 239    27523  20349  29198  -3514   -684   -911       C  
ATOM   4232  O   THR B 239       8.384   0.307  49.369  1.00209.43           O  
ANISOU 4232  O   THR B 239    28043  21244  30285  -3349  -1168  -1069       O  
ATOM   4233  CB  THR B 239       9.061  -2.744  48.789  1.00132.15           C  
ANISOU 4233  CB  THR B 239    18868  11313  20032  -3328    328   -155       C  
ATOM   4234  OG1 THR B 239       8.957  -4.161  48.945  1.00117.52           O  
ANISOU 4234  OG1 THR B 239    16661   9500  18493  -3067    697    301       O  
ATOM   4235  CG2 THR B 239      10.464  -2.256  49.063  1.00127.64           C  
ANISOU 4235  CG2 THR B 239    18344  10694  19459  -3301    148    -89       C  
ATOM   4236  N   PHE B 240       6.670  -0.622  48.254  1.00191.36           N  
ANISOU 4236  N   PHE B 240    26130  18816  27763  -3527   -709   -936       N  
ATOM   4237  CA  PHE B 240       6.334   0.598  47.535  1.00192.66           C  
ANISOU 4237  CA  PHE B 240    26056  18939  28208  -3350  -1284  -1084       C  
ATOM   4238  C   PHE B 240       4.827   0.740  47.400  1.00196.95           C  
ANISOU 4238  C   PHE B 240    26567  19526  28738  -3437  -1369  -1307       C  
ATOM   4239  O   PHE B 240       4.078  -0.238  47.448  1.00195.58           O  
ANISOU 4239  O   PHE B 240    26630  19355  28326  -3638   -921  -1259       O  
ATOM   4240  CB  PHE B 240       6.995   0.645  46.150  1.00191.12           C  
ANISOU 4240  CB  PHE B 240    26011  18544  28063  -3219  -1278   -748       C  
ATOM   4241  CG  PHE B 240       8.491   0.770  46.197  1.00195.47           C  
ANISOU 4241  CG  PHE B 240    26527  19063  28681  -3102  -1315   -563       C  
ATOM   4242  CD1 PHE B 240       9.299  -0.346  46.290  1.00194.54           C  
ANISOU 4242  CD1 PHE B 240    26692  18907  28319  -3162   -778   -263       C  
ATOM   4243  CD2 PHE B 240       9.087   2.015  46.153  1.00201.93           C  
ANISOU 4243  CD2 PHE B 240    26983  19880  29863  -2890  -1871   -693       C  
ATOM   4244  CE1 PHE B 240      10.675  -0.216  46.338  1.00199.54           C  
ANISOU 4244  CE1 PHE B 240    27299  19518  29000  -3056   -816    -94       C  
ATOM   4245  CE2 PHE B 240      10.459   2.148  46.191  1.00203.41           C  
ANISOU 4245  CE2 PHE B 240    27115  20038  30133  -2790  -1912   -532       C  
ATOM   4246  CZ  PHE B 240      11.253   1.030  46.283  1.00202.77           C  
ANISOU 4246  CZ  PHE B 240    27364  19934  29744  -2892  -1391   -231       C  
ATOM   4247  N   GLN B 241       4.394   1.984  47.222  1.00196.83           N  
ANISOU 4247  N   GLN B 241    26208  19530  29047  -3241  -1928  -1558       N  
ATOM   4248  CA  GLN B 241       2.983   2.302  47.077  1.00202.52           C  
ANISOU 4248  CA  GLN B 241    26846  20291  29812  -3269  -2079  -1786       C  
ATOM   4249  C   GLN B 241       2.764   3.197  45.863  1.00202.18           C  
ANISOU 4249  C   GLN B 241    26699  20073  30048  -3055  -2438  -1724       C  
ATOM   4250  O   GLN B 241       3.138   4.370  45.871  1.00203.71           O  
ANISOU 4250  O   GLN B 241    26523  20248  30629  -2776  -2914  -1878       O  
ATOM   4251  CB  GLN B 241       2.470   2.999  48.338  1.00210.66           C  
ANISOU 4251  CB  GLN B 241    27456  21581  31002  -3191  -2415  -2265       C  
ATOM   4252  CG  GLN B 241       2.677   2.208  49.617  1.00214.22           C  
ANISOU 4252  CG  GLN B 241    27952  22281  31160  -3413  -2150  -2371       C  
ATOM   4253  CD  GLN B 241       3.259   3.056  50.731  1.00219.34           C  
ANISOU 4253  CD  GLN B 241    28103  23179  32056  -3186  -2549  -2747       C  
ATOM   4254  OE1 GLN B 241       3.923   4.063  50.479  1.00222.50           O  
ANISOU 4254  OE1 GLN B 241    28215  23481  32844  -2865  -2912  -2816       O  
ATOM   4255  NE2 GLN B 241       3.017   2.651  51.970  1.00219.32           N  
ANISOU 4255  NE2 GLN B 241    27973  23534  31825  -3335  -2497  -3005       N  
ATOM   4256  N   PHE B 283     -11.586 -15.858  54.798  1.00190.10           N  
ANISOU 4256  N   PHE B 283    26454  21717  24060  -5803   3593    856       N  
ATOM   4257  CA  PHE B 283     -10.133 -15.838  54.660  1.00187.77           C  
ANISOU 4257  CA  PHE B 283    26235  21326  23783  -5511   3544   1126       C  
ATOM   4258  C   PHE B 283      -9.429 -16.201  55.969  1.00176.37           C  
ANISOU 4258  C   PHE B 283    24635  20469  21910  -5512   4057   1379       C  
ATOM   4259  O   PHE B 283      -8.666 -15.405  56.517  1.00164.34           O  
ANISOU 4259  O   PHE B 283    23024  19106  20312  -5690   4138   1151       O  
ATOM   4260  CB  PHE B 283      -9.666 -14.463  54.171  1.00191.91           C  
ANISOU 4260  CB  PHE B 283    26679  21516  24722  -5551   3041    730       C  
ATOM   4261  CG  PHE B 283     -10.526 -13.330  54.644  1.00200.46           C  
ANISOU 4261  CG  PHE B 283    27556  22688  25920  -6050   2888      2       C  
ATOM   4262  CD1 PHE B 283     -10.367 -12.806  55.916  1.00208.99           C  
ANISOU 4262  CD1 PHE B 283    28356  24299  26753  -6552   3197   -455       C  
ATOM   4263  CD2 PHE B 283     -11.495 -12.789  53.817  1.00198.49           C  
ANISOU 4263  CD2 PHE B 283    27203  22136  26078  -5956   2363   -266       C  
ATOM   4264  CE1 PHE B 283     -11.159 -11.764  56.356  1.00210.79           C  
ANISOU 4264  CE1 PHE B 283    28117  24785  27189  -6939   2868  -1306       C  
ATOM   4265  CE2 PHE B 283     -12.290 -11.747  54.249  1.00203.46           C  
ANISOU 4265  CE2 PHE B 283    27500  22907  26898  -6258   2053   -969       C  
ATOM   4266  CZ  PHE B 283     -12.122 -11.234  55.521  1.00208.84           C  
ANISOU 4266  CZ  PHE B 283    27835  24145  27371  -6723   2249  -1549       C  
ATOM   4267  N   THR B 284      -9.694 -17.412  56.459  1.00166.24           N  
ANISOU 4267  N   THR B 284    23248  19573  20341  -5270   4380   1852       N  
ATOM   4268  CA  THR B 284      -9.047 -17.949  57.648  1.00164.52           C  
ANISOU 4268  CA  THR B 284    22775  20051  19684  -5031   4814   2235       C  
ATOM   4269  C   THR B 284      -7.796 -18.729  57.235  1.00162.59           C  
ANISOU 4269  C   THR B 284    22790  19593  19396  -4693   4793   2644       C  
ATOM   4270  O   THR B 284      -7.412 -18.741  56.063  1.00168.25           O  
ANISOU 4270  O   THR B 284    23955  19632  20341  -4727   4557   2502       O  
ATOM   4271  CB  THR B 284     -10.042 -18.793  58.449  1.00168.67           C  
ANISOU 4271  CB  THR B 284    23060  21143  19885  -4976   5173   2437       C  
ATOM   4272  OG1 THR B 284      -9.728 -20.185  58.299  1.00167.87           O  
ANISOU 4272  OG1 THR B 284    23182  20980  19619  -4725   5326   2913       O  
ATOM   4273  CG2 THR B 284     -11.479 -18.535  57.986  1.00173.11           C  
ANISOU 4273  CG2 THR B 284    23742  21408  20623  -5407   5078   2002       C  
ATOM   4274  N   GLU B 285      -7.140 -19.391  58.193  1.00164.02           N  
ANISOU 4274  N   GLU B 285    22741  20386  19192  -4397   5105   3060       N  
ATOM   4275  CA  GLU B 285      -5.878 -20.065  57.916  1.00161.95           C  
ANISOU 4275  CA  GLU B 285    22749  19939  18845  -4184   5133   3337       C  
ATOM   4276  C   GLU B 285      -5.966 -21.588  57.869  1.00151.89           C  
ANISOU 4276  C   GLU B 285    21719  18634  17357  -4095   5385   3640       C  
ATOM   4277  O   GLU B 285      -5.104 -22.214  57.245  1.00166.17           O  
ANISOU 4277  O   GLU B 285    23886  20046  19206  -3990   5375   3734       O  
ATOM   4278  CB  GLU B 285      -4.818 -19.649  58.954  1.00169.12           C  
ANISOU 4278  CB  GLU B 285    23232  21541  19484  -3911   5231   3554       C  
ATOM   4279  CG  GLU B 285      -3.362 -19.937  58.561  1.00174.88           C  
ANISOU 4279  CG  GLU B 285    24223  21996  20226  -3755   5151   3725       C  
ATOM   4280  CD  GLU B 285      -2.878 -21.313  58.979  1.00186.88           C  
ANISOU 4280  CD  GLU B 285    25825  23787  21394  -3573   5412   4103       C  
ATOM   4281  OE1 GLU B 285      -3.454 -21.884  59.928  1.00191.82           O  
ANISOU 4281  OE1 GLU B 285    26146  25084  21654  -3509   5658   4300       O  
ATOM   4282  OE2 GLU B 285      -1.921 -21.824  58.355  1.00191.77           O  
ANISOU 4282  OE2 GLU B 285    26804  23960  22099  -3490   5375   4170       O  
ATOM   4283  N   ASP B 286      -6.974 -22.200  58.487  1.00144.03           N  
ANISOU 4283  N   ASP B 286    20535  18039  16150  -4130   5619   3772       N  
ATOM   4284  CA  ASP B 286      -7.036 -23.655  58.521  1.00141.16           C  
ANISOU 4284  CA  ASP B 286    20374  17666  15594  -4064   5862   4068       C  
ATOM   4285  C   ASP B 286      -7.377 -24.207  57.135  1.00137.23           C  
ANISOU 4285  C   ASP B 286    20454  16303  15385  -4217   5768   3864       C  
ATOM   4286  O   ASP B 286      -7.496 -23.470  56.152  1.00125.28           O  
ANISOU 4286  O   ASP B 286    19174  14260  14167  -4350   5498   3505       O  
ATOM   4287  CB  ASP B 286      -8.060 -24.122  59.557  1.00150.43           C  
ANISOU 4287  CB  ASP B 286    21160  19538  16459  -4056   6131   4262       C  
ATOM   4288  CG  ASP B 286      -9.472 -23.613  59.271  1.00150.54           C  
ANISOU 4288  CG  ASP B 286    21136  19385  16679  -4307   6066   3957       C  
ATOM   4289  OD1 ASP B 286      -9.634 -22.728  58.402  1.00149.22           O  
ANISOU 4289  OD1 ASP B 286    21173  18662  16862  -4505   5777   3570       O  
ATOM   4290  OD2 ASP B 286     -10.424 -24.102  59.920  1.00144.20           O  
ANISOU 4290  OD2 ASP B 286    20090  19025  15675  -4315   6293   4089       O  
ATOM   4291  N   PHE B 287      -7.490 -25.540  57.057  1.00120.67           N  
ANISOU 4291  N   PHE B 287    12915  16842  16090   -694   1747   3366       N  
ATOM   4292  CA  PHE B 287      -7.850 -26.203  55.804  1.00135.87           C  
ANISOU 4292  CA  PHE B 287    15028  18575  18020   -880   1500   3368       C  
ATOM   4293  C   PHE B 287      -9.051 -25.526  55.155  1.00168.12           C  
ANISOU 4293  C   PHE B 287    19117  22709  22049   -851   1341   3522       C  
ATOM   4294  O   PHE B 287      -9.079 -25.320  53.936  1.00185.26           O  
ANISOU 4294  O   PHE B 287    21559  24712  24118   -925   1243   3423       O  
ATOM   4295  CB  PHE B 287      -8.126 -27.686  56.047  1.00136.95           C  
ANISOU 4295  CB  PHE B 287    14996  18693  18348  -1036   1314   3504       C  
ATOM   4296  CG  PHE B 287      -8.671 -28.406  54.846  1.00124.25           C  
ANISOU 4296  CG  PHE B 287    13534  16908  16767  -1220   1026   3542       C  
ATOM   4297  CD1 PHE B 287      -7.824 -28.798  53.823  1.00105.52           C  
ANISOU 4297  CD1 PHE B 287    11489  14287  14316  -1334    993   3301       C  
ATOM   4298  CD2 PHE B 287     -10.023 -28.691  54.740  1.00125.58           C  
ANISOU 4298  CD2 PHE B 287    13511  17169  17034  -1274    787   3814       C  
ATOM   4299  CE1 PHE B 287      -8.310 -29.464  52.718  1.00108.88           C  
ANISOU 4299  CE1 PHE B 287    12051  14553  14766  -1491    724   3325       C  
ATOM   4300  CE2 PHE B 287     -10.518 -29.354  53.635  1.00120.54           C  
ANISOU 4300  CE2 PHE B 287    13009  16367  16425  -1442    520   3841       C  
ATOM   4301  CZ  PHE B 287      -9.659 -29.742  52.622  1.00117.28           C  
ANISOU 4301  CZ  PHE B 287    12925  15699  15937  -1547    486   3592       C  
ATOM   4302  N   GLN B 288     -10.055 -25.177  55.966  1.00152.34           N  
ANISOU 4302  N   GLN B 288    16815  20955  20112   -736   1314   3769       N  
ATOM   4303  CA  GLN B 288     -11.206 -24.424  55.476  1.00152.06           C  
ANISOU 4303  CA  GLN B 288    16765  21005  20007   -675   1186   3919       C  
ATOM   4304  C   GLN B 288     -10.780 -23.133  54.786  1.00147.51           C  
ANISOU 4304  C   GLN B 288    16486  20334  19226   -574   1320   3723       C  
ATOM   4305  O   GLN B 288     -11.420 -22.705  53.816  1.00161.40           O  
ANISOU 4305  O   GLN B 288    18392  22034  20898   -594   1188   3751       O  
ATOM   4306  CB  GLN B 288     -12.169 -24.120  56.622  1.00154.21           C  
ANISOU 4306  CB  GLN B 288    16658  21587  20349   -525   1186   4186       C  
ATOM   4307  CG  GLN B 288     -13.367 -25.054  56.674  1.00160.66           C  
ANISOU 4307  CG  GLN B 288    17218  22510  21314   -640    920   4477       C  
ATOM   4308  CD  GLN B 288     -13.065 -26.360  57.391  1.00169.65           C  
ANISOU 4308  CD  GLN B 288    18158  23658  22642   -758    886   4551       C  
ATOM   4309  OE1 GLN B 288     -13.396 -27.441  56.898  1.00175.45           O  
ANISOU 4309  OE1 GLN B 288    18891  24284  23489   -954    667   4632       O  
ATOM   4310  NE2 GLN B 288     -12.448 -26.267  58.562  1.00169.26           N  
ANISOU 4310  NE2 GLN B 288    17941  23739  22631   -636   1096   4523       N  
ATOM   4311  N   GLY B 289      -9.719 -22.482  55.278  1.00143.99           N  
ANISOU 4311  N   GLY B 289    16130  19877  18702   -463   1581   3529       N  
ATOM   4312  CA  GLY B 289      -9.220 -21.300  54.590  1.00120.59           C  
ANISOU 4312  CA  GLY B 289    13468  16803  15549   -388   1707   3336       C  
ATOM   4313  C   GLY B 289      -8.777 -21.591  53.170  1.00120.81           C  
ANISOU 4313  C   GLY B 289    13837  16570  15494   -552   1613   3167       C  
ATOM   4314  O   GLY B 289      -9.065 -20.819  52.254  1.00144.67           O  
ANISOU 4314  O   GLY B 289    17066  19518  18385   -532   1570   3128       O  
ATOM   4315  N   LEU B 290      -8.069 -22.705  52.964  1.00109.92           N  
ANISOU 4315  N   LEU B 290    12523  15056  14184   -707   1578   3062       N  
ATOM   4316  CA  LEU B 290      -7.775 -23.145  51.603  1.00108.28           C  
ANISOU 4316  CA  LEU B 290    12610  14619  13912   -863   1446   2926       C  
ATOM   4317  C   LEU B 290      -9.060 -23.445  50.847  1.00126.35           C  
ANISOU 4317  C   LEU B 290    14860  16906  16242   -938   1165   3115       C  
ATOM   4318  O   LEU B 290      -9.253 -22.997  49.711  1.00144.24           O  
ANISOU 4318  O   LEU B 290    17358  19057  18389   -964   1085   3052       O  
ATOM   4319  CB  LEU B 290      -6.880 -24.380  51.612  1.00101.31           C  
ANISOU 4319  CB  LEU B 290    11774  13614  13107  -1004   1433   2800       C  
ATOM   4320  CG  LEU B 290      -5.377 -24.203  51.440  1.00102.81           C  
ANISOU 4320  CG  LEU B 290    12209  13679  13176  -1007   1645   2507       C  
ATOM   4321  CD1 LEU B 290      -4.689 -23.874  52.758  1.00128.49           C  
ANISOU 4321  CD1 LEU B 290    15302  17067  16451   -883   1905   2462       C  
ATOM   4322  CD2 LEU B 290      -4.825 -25.460  50.815  1.00 97.79           C  
ANISOU 4322  CD2 LEU B 290    11705  12872  12578  -1176   1514   2393       C  
ATOM   4323  N   ARG B 291      -9.947 -24.221  51.470  1.00100.19           N  
ANISOU 4323  N   ARG B 291    11248  13723  13098   -976   1013   3352       N  
ATOM   4324  CA  ARG B 291     -11.242 -24.523  50.877  1.00119.90           C  
ANISOU 4324  CA  ARG B 291    13665  16247  15643  -1047    744   3556       C  
ATOM   4325  C   ARG B 291     -11.958 -23.255  50.426  1.00149.78           C  
ANISOU 4325  C   ARG B 291    17523  20104  19284   -918    750   3607       C  
ATOM   4326  O   ARG B 291     -12.358 -23.136  49.264  1.00162.58           O  
ANISOU 4326  O   ARG B 291    19334  21612  20827   -978    605   3583       O  
ATOM   4327  CB  ARG B 291     -12.100 -25.281  51.888  1.00132.75           C  
ANISOU 4327  CB  ARG B 291    14911  18067  17461  -1065    630   3830       C  
ATOM   4328  CG  ARG B 291     -12.303 -26.758  51.617  1.00141.27           C  
ANISOU 4328  CG  ARG B 291    15931  19043  18702  -1271    397   3904       C  
ATOM   4329  CD  ARG B 291     -13.478 -27.243  52.457  1.00155.99           C  
ANISOU 4329  CD  ARG B 291    17413  21130  20728  -1279    253   4228       C  
ATOM   4330  NE  ARG B 291     -13.875 -28.615  52.160  1.00164.52           N  
ANISOU 4330  NE  ARG B 291    18422  22116  21971  -1485     -7   4338       N  
ATOM   4331  CZ  ARG B 291     -15.098 -29.095  52.364  1.00169.37           C  
ANISOU 4331  CZ  ARG B 291    18778  22869  22707  -1549   -222   4623       C  
ATOM   4332  NH1 ARG B 291     -15.375 -30.357  52.069  1.00171.35           N  
ANISOU 4332  NH1 ARG B 291    18986  23010  23110  -1747   -460   4708       N  
ATOM   4333  NH2 ARG B 291     -16.049 -28.305  52.848  1.00170.46           N  
ANISOU 4333  NH2 ARG B 291    18701  23258  22809  -1413   -206   4824       N  
ATOM   4334  N   ALA B 292     -12.129 -22.293  51.339  1.00144.05           N  
ANISOU 4334  N   ALA B 292    16648  19568  18517   -730    914   3674       N  
ATOM   4335  CA  ALA B 292     -12.846 -21.063  51.009  1.00139.34           C  
ANISOU 4335  CA  ALA B 292    16109  19054  17782   -588    918   3732       C  
ATOM   4336  C   ALA B 292     -12.149 -20.294  49.895  1.00140.12           C  
ANISOU 4336  C   ALA B 292    16593  18948  17700   -589    999   3496       C  
ATOM   4337  O   ALA B 292     -12.783 -19.867  48.924  1.00159.09           O  
ANISOU 4337  O   ALA B 292    19138  21302  20008   -594    877   3522       O  
ATOM   4338  CB  ALA B 292     -12.985 -20.184  52.251  1.00133.92           C  
ANISOU 4338  CB  ALA B 292    15208  18596  17079   -373   1093   3814       C  
ATOM   4339  N   GLU B 293     -10.840 -20.089  50.038  1.00150.39           N  
ANISOU 4339  N   GLU B 293    18057  20137  18945   -582   1210   3267       N  
ATOM   4340  CA  GLU B 293     -10.080 -19.312  49.065  1.00128.71           C  
ANISOU 4340  CA  GLU B 293    15667  17212  16023   -580   1310   3045       C  
ATOM   4341  C   GLU B 293     -10.106 -19.951  47.677  1.00119.37           C  
ANISOU 4341  C   GLU B 293    14707  15839  14810   -746   1123   2973       C  
ATOM   4342  O   GLU B 293     -10.456 -19.292  46.689  1.00124.20           O  
ANISOU 4342  O   GLU B 293    15514  16382  15294   -729   1063   2949       O  
ATOM   4343  CB  GLU B 293      -8.656 -19.144  49.586  1.00114.67           C  
ANISOU 4343  CB  GLU B 293    13984  15374  14210   -558   1562   2828       C  
ATOM   4344  CG  GLU B 293      -7.669 -18.514  48.655  1.00115.87           C  
ANISOU 4344  CG  GLU B 293    14492  15342  14191   -584   1678   2586       C  
ATOM   4345  CD  GLU B 293      -6.395 -18.160  49.384  1.00117.81           C  
ANISOU 4345  CD  GLU B 293    14783  15582  14399   -530   1945   2406       C  
ATOM   4346  OE1 GLU B 293      -6.489 -17.606  50.504  1.00130.77           O  
ANISOU 4346  OE1 GLU B 293    16234  17377  16074   -386   2078   2471       O  
ATOM   4347  OE2 GLU B 293      -5.310 -18.450  48.852  1.00114.38           O  
ANISOU 4347  OE2 GLU B 293    14562  14999  13899   -627   2017   2200       O  
ATOM   4348  N   VAL B 294      -9.730 -21.231  47.579  1.00110.50           N  
ANISOU 4348  N   VAL B 294    13560  14626  13797   -901   1026   2934       N  
ATOM   4349  CA  VAL B 294      -9.746 -21.922  46.288  1.00105.15           C  
ANISOU 4349  CA  VAL B 294    13084  13769  13098  -1052    832   2861       C  
ATOM   4350  C   VAL B 294     -11.144 -21.908  45.681  1.00124.18           C  
ANISOU 4350  C   VAL B 294    15428  16230  15526  -1065    594   3056       C  
ATOM   4351  O   VAL B 294     -11.313 -21.670  44.478  1.00144.45           O  
ANISOU 4351  O   VAL B 294    18217  18681  17986  -1100    495   2990       O  
ATOM   4352  CB  VAL B 294      -9.216 -23.359  46.432  1.00109.37           C  
ANISOU 4352  CB  VAL B 294    13570  14218  13769  -1202    746   2810       C  
ATOM   4353  CG1 VAL B 294      -9.585 -24.172  45.203  1.00101.92           C  
ANISOU 4353  CG1 VAL B 294    12763  13123  12838  -1348    483   2797       C  
ATOM   4354  CG2 VAL B 294      -7.716 -23.351  46.624  1.00109.67           C  
ANISOU 4354  CG2 VAL B 294    13768  14166  13738  -1203    965   2563       C  
ATOM   4355  N   GLU B 295     -12.161 -22.187  46.499  1.00122.39           N  
ANISOU 4355  N   GLU B 295    14886  16185  15430  -1038    498   3301       N  
ATOM   4356  CA  GLU B 295     -13.546 -22.163  46.033  1.00137.78           C  
ANISOU 4356  CA  GLU B 295    16738  18216  17394  -1045    276   3505       C  
ATOM   4357  C   GLU B 295     -13.890 -20.811  45.419  1.00145.34           C  
ANISOU 4357  C   GLU B 295    17867  19191  18166   -911    336   3479       C  
ATOM   4358  O   GLU B 295     -14.516 -20.739  44.355  1.00158.25           O  
ANISOU 4358  O   GLU B 295    19626  20764  19736   -949    174   3501       O  
ATOM   4359  CB  GLU B 295     -14.481 -22.477  47.200  1.00151.89           C  
ANISOU 4359  CB  GLU B 295    18142  20240  19329  -1004    215   3774       C  
ATOM   4360  CG  GLU B 295     -15.959 -22.238  46.962  1.00170.93           C  
ANISOU 4360  CG  GLU B 295    20407  22801  21736   -970     25   4009       C  
ATOM   4361  CD  GLU B 295     -16.772 -22.461  48.227  1.00194.17           C  
ANISOU 4361  CD  GLU B 295    22958  26009  24807   -911     -4   4272       C  
ATOM   4362  OE1 GLU B 295     -17.135 -21.467  48.893  1.00201.49           O  
ANISOU 4362  OE1 GLU B 295    23770  27127  25660   -723    115   4355       O  
ATOM   4363  OE2 GLU B 295     -17.027 -23.636  48.567  1.00202.16           O  
ANISOU 4363  OE2 GLU B 295    23778  27042  25993  -1048   -149   4396       O  
ATOM   4364  N   THR B 296     -13.503 -19.724  46.093  1.00156.27           N  
ANISOU 4364  N   THR B 296    19255  20658  19462   -747    564   3434       N  
ATOM   4365  CA  THR B 296     -13.762 -18.386  45.571  1.00144.40           C  
ANISOU 4365  CA  THR B 296    17925  19161  17778   -611    632   3403       C  
ATOM   4366  C   THR B 296     -13.169 -18.210  44.180  1.00117.23           C  
ANISOU 4366  C   THR B 296    14842  15496  14204   -688    618   3203       C  
ATOM   4367  O   THR B 296     -13.748 -17.525  43.330  1.00101.90           O  
ANISOU 4367  O   THR B 296    13042  13534  12142   -639    550   3222       O  
ATOM   4368  CB  THR B 296     -13.192 -17.337  46.517  1.00142.80           C  
ANISOU 4368  CB  THR B 296    17703  19043  17510   -440    888   3344       C  
ATOM   4369  OG1 THR B 296     -12.929 -17.929  47.796  1.00126.53           O  
ANISOU 4369  OG1 THR B 296    15376  17102  15596   -432    964   3404       O  
ATOM   4370  CG2 THR B 296     -14.180 -16.200  46.683  1.00153.95           C  
ANISOU 4370  CG2 THR B 296    19053  20614  18827   -258    881   3485       C  
ATOM   4371  N   ILE B 297     -11.995 -18.797  43.945  1.00119.01           N  
ANISOU 4371  N   ILE B 297    15216  15562  14440   -797    688   3007       N  
ATOM   4372  CA  ILE B 297     -11.365 -18.716  42.632  1.00113.90           C  
ANISOU 4372  CA  ILE B 297    14897  14716  13665   -871    671   2814       C  
ATOM   4373  C   ILE B 297     -12.181 -19.493  41.603  1.00121.00           C  
ANISOU 4373  C   ILE B 297    15821  15554  14600   -984    394   2886       C  
ATOM   4374  O   ILE B 297     -12.343 -19.054  40.458  1.00138.88           O  
ANISOU 4374  O   ILE B 297    18303  17729  16736   -982    331   2825       O  
ATOM   4375  CB  ILE B 297      -9.913 -19.214  42.725  1.00112.45           C  
ANISOU 4375  CB  ILE B 297    14840  14406  13480   -952    810   2595       C  
ATOM   4376  CG1 ILE B 297      -9.088 -18.277  43.616  1.00115.24           C  
ANISOU 4376  CG1 ILE B 297    15202  14812  13770   -833   1094   2508       C  
ATOM   4377  CG2 ILE B 297      -9.282 -19.237  41.353  1.00111.07           C  
ANISOU 4377  CG2 ILE B 297    14985  14046  13172  -1030    773   2406       C  
ATOM   4378  CD1 ILE B 297      -9.079 -16.830  43.160  1.00117.59           C  
ANISOU 4378  CD1 ILE B 297    15697  15092  13889   -714   1209   2459       C  
ATOM   4379  N   SER B 298     -12.700 -20.662  41.989  1.00110.66           N  
ANISOU 4379  N   SER B 298    14289  14289  13468  -1085    221   3016       N  
ATOM   4380  CA  SER B 298     -13.548 -21.423  41.078  1.00109.91           C  
ANISOU 4380  CA  SER B 298    14195  14143  13422  -1194    -58   3098       C  
ATOM   4381  C   SER B 298     -14.826 -20.651  40.774  1.00120.65           C  
ANISOU 4381  C   SER B 298    15499  15627  14717  -1099   -151   3269       C  
ATOM   4382  O   SER B 298     -15.329 -20.684  39.645  1.00133.68           O  
ANISOU 4382  O   SER B 298    17283  17205  16303  -1137   -311   3262       O  
ATOM   4383  CB  SER B 298     -13.868 -22.798  41.668  1.00121.05           C  
ANISOU 4383  CB  SER B 298    15362  15584  15046  -1323   -222   3221       C  
ATOM   4384  OG  SER B 298     -14.712 -22.695  42.802  1.00148.32           O  
ANISOU 4384  OG  SER B 298    18498  19255  18604  -1257   -221   3455       O  
ATOM   4385  N   LYS B 299     -15.371 -19.961  41.783  1.00116.09           N  
ANISOU 4385  N   LYS B 299    14716  15245  14149   -966    -55   3424       N  
ATOM   4386  CA  LYS B 299     -16.561 -19.140  41.581  1.00122.62           C  
ANISOU 4386  CA  LYS B 299    15486  16210  14893   -850   -127   3584       C  
ATOM   4387  C   LYS B 299     -16.310 -18.008  40.589  1.00117.01           C  
ANISOU 4387  C   LYS B 299    15084  15399  13973   -762    -40   3444       C  
ATOM   4388  O   LYS B 299     -17.248 -17.553  39.923  1.00108.98           O  
ANISOU 4388  O   LYS B 299    14105  14430  12873   -710   -157   3533       O  
ATOM   4389  CB  LYS B 299     -17.036 -18.572  42.921  1.00130.84           C  
ANISOU 4389  CB  LYS B 299    16259  17487  15968   -702    -19   3753       C  
ATOM   4390  CG  LYS B 299     -17.817 -19.551  43.800  1.00141.84           C  
ANISOU 4390  CG  LYS B 299    17294  19048  17551   -765   -164   3980       C  
ATOM   4391  CD  LYS B 299     -19.194 -19.857  43.202  1.00147.53           C  
ANISOU 4391  CD  LYS B 299    17910  19856  18288   -809   -424   4172       C  
ATOM   4392  CE  LYS B 299     -20.004 -20.829  44.064  1.00147.63           C  
ANISOU 4392  CE  LYS B 299    17558  20046  18490   -884   -577   4418       C  
ATOM   4393  NZ  LYS B 299     -21.262 -21.304  43.402  1.00143.23           N  
ANISOU 4393  NZ  LYS B 299    16908  19551  17964   -966   -850   4592       N  
ATOM   4394  N   GLU B 300     -15.066 -17.535  40.477  1.00116.57           N  
ANISOU 4394  N   GLU B 300    15251  15213  13828   -744    162   3231       N  
ATOM   4395  CA  GLU B 300     -14.689 -16.569  39.452  1.00123.17           C  
ANISOU 4395  CA  GLU B 300    16399  15929  14470   -689    240   3086       C  
ATOM   4396  C   GLU B 300     -14.246 -17.238  38.156  1.00122.78           C  
ANISOU 4396  C   GLU B 300    16574  15691  14387   -827    122   2938       C  
ATOM   4397  O   GLU B 300     -13.617 -16.591  37.311  1.00124.52           O  
ANISOU 4397  O   GLU B 300    17070  15791  14452   -805    209   2781       O  
ATOM   4398  CB  GLU B 300     -13.587 -15.636  39.965  1.00132.29           C  
ANISOU 4398  CB  GLU B 300    17683  17047  15533   -599    516   2940       C  
ATOM   4399  CG  GLU B 300     -14.051 -14.644  41.021  1.00146.03           C  
ANISOU 4399  CG  GLU B 300    19270  18962  17254   -420    637   3063       C  
ATOM   4400  CD  GLU B 300     -13.000 -13.593  41.342  1.00151.15           C  
ANISOU 4400  CD  GLU B 300    20088  19550  17792   -328    895   2907       C  
ATOM   4401  OE1 GLU B 300     -11.799 -13.848  41.104  1.00149.11           O  
ANISOU 4401  OE1 GLU B 300    19991  19150  17515   -419   1004   2718       O  
ATOM   4402  OE2 GLU B 300     -13.381 -12.506  41.825  1.00154.90           O  
ANISOU 4402  OE2 GLU B 300    20536  20124  18194   -163    982   2973       O  
ATOM   4403  N   LEU B 301     -14.552 -18.519  37.992  1.00132.80           N  
ANISOU 4403  N   LEU B 301    17729  16934  15795   -964    -80   2986       N  
ATOM   4404  CA  LEU B 301     -14.265 -19.260  36.772  1.00131.33           C  
ANISOU 4404  CA  LEU B 301    17730  16582  15589  -1087   -232   2858       C  
ATOM   4405  C   LEU B 301     -15.452 -20.044  36.243  1.00120.55           C  
ANISOU 4405  C   LEU B 301    16245  15245  14313  -1164   -521   3005       C  
ATOM   4406  O   LEU B 301     -15.442 -20.418  35.064  1.00105.53           O  
ANISOU 4406  O   LEU B 301    14514  13220  12362  -1230   -664   2913       O  
ATOM   4407  CB  LEU B 301     -13.082 -20.216  36.973  1.00132.52           C  
ANISOU 4407  CB  LEU B 301    17922  16614  15815  -1204   -190   2698       C  
ATOM   4408  CG  LEU B 301     -11.731 -19.528  37.145  1.00129.63           C  
ANISOU 4408  CG  LEU B 301    17741  16182  15330  -1154     78   2502       C  
ATOM   4409  CD1 LEU B 301     -10.638 -20.569  37.217  1.00123.69           C  
ANISOU 4409  CD1 LEU B 301    17036  15321  14640  -1271     88   2343       C  
ATOM   4410  CD2 LEU B 301     -11.484 -18.575  35.987  1.00100.61           C  
ANISOU 4410  CD2 LEU B 301    14357  12422  11449  -1097    132   2384       C  
ATOM   4411  N   GLU B 302     -16.474 -20.296  37.064  1.00138.88           N  
ANISOU 4411  N   GLU B 302    18276  17733  16760  -1154   -614   3231       N  
ATOM   4412  CA  GLU B 302     -17.595 -21.133  36.655  1.00145.89           C  
ANISOU 4412  CA  GLU B 302    19024  18657  17749  -1246   -896   3383       C  
ATOM   4413  C   GLU B 302     -18.461 -20.497  35.573  1.00151.96           C  
ANISOU 4413  C   GLU B 302    19913  19442  18384  -1183  -1004   3418       C  
ATOM   4414  O   GLU B 302     -19.145 -21.225  34.844  1.00147.56           O  
ANISOU 4414  O   GLU B 302    19335  18853  17880  -1276  -1245   3469       O  
ATOM   4415  CB  GLU B 302     -18.465 -21.451  37.872  1.00152.49           C  
ANISOU 4415  CB  GLU B 302    19505  19696  18737  -1242   -949   3631       C  
ATOM   4416  CG  GLU B 302     -19.011 -22.870  37.925  1.00157.17           C  
ANISOU 4416  CG  GLU B 302    19910  20280  19526  -1413  -1205   3749       C  
ATOM   4417  CD  GLU B 302     -19.813 -23.130  39.191  1.00154.25           C  
ANISOU 4417  CD  GLU B 302    19178  20130  19298  -1405  -1238   4006       C  
ATOM   4418  OE1 GLU B 302     -20.368 -22.160  39.750  1.00156.04           O  
ANISOU 4418  OE1 GLU B 302    19294  20547  19449  -1253  -1132   4128       O  
ATOM   4419  OE2 GLU B 302     -19.910 -24.302  39.614  1.00156.90           O  
ANISOU 4419  OE2 GLU B 302    19340  20455  19819  -1547  -1377   4090       O  
ATOM   4420  N   LEU B 303     -18.465 -19.176  35.433  1.00162.90           N  
ANISOU 4420  N   LEU B 303    21426  20872  19596  -1028   -842   3393       N  
ATOM   4421  CA  LEU B 303     -19.268 -18.584  34.359  1.00169.66           C  
ANISOU 4421  CA  LEU B 303    22408  21738  20315   -964   -944   3420       C  
ATOM   4422  C   LEU B 303     -18.403 -18.291  33.135  1.00163.20           C  
ANISOU 4422  C   LEU B 303    21928  20728  19352   -971   -893   3190       C  
ATOM   4423  O   LEU B 303     -18.378 -17.193  32.576  1.00162.60           O  
ANISOU 4423  O   LEU B 303    22040  20642  19101   -854   -790   3138       O  
ATOM   4424  CB  LEU B 303     -19.988 -17.336  34.859  1.00178.26           C  
ANISOU 4424  CB  LEU B 303    23427  23006  21298   -782   -837   3554       C  
ATOM   4425  CG  LEU B 303     -20.949 -16.622  33.898  1.00182.47           C  
ANISOU 4425  CG  LEU B 303    24062  23588  21682   -689   -932   3610       C  
ATOM   4426  CD1 LEU B 303     -21.970 -17.597  33.313  1.00182.09           C  
ANISOU 4426  CD1 LEU B 303    23888  23573  21723   -798  -1218   3724       C  
ATOM   4427  CD2 LEU B 303     -21.639 -15.473  34.605  1.00185.55           C  
ANISOU 4427  CD2 LEU B 303    24350  24171  21980   -502   -829   3752       C  
ATOM   4428  N   LEU B 304     -17.622 -19.288  32.741  1.00169.23           N  
ANISOU 4428  N   LEU B 304    22774  21340  20185  -1105   -961   3048       N  
ATOM   4429  CA  LEU B 304     -16.840 -19.224  31.519  1.00155.49           C  
ANISOU 4429  CA  LEU B 304    21331  19430  18316  -1125   -954   2837       C  
ATOM   4430  C   LEU B 304     -17.482 -20.073  30.431  1.00180.43           C  
ANISOU 4430  C   LEU B 304    24517  22529  21510  -1211  -1232   2840       C  
ATOM   4431  O   LEU B 304     -18.384 -20.878  30.675  1.00183.08           O  
ANISOU 4431  O   LEU B 304    24641  22928  21992  -1286  -1435   2990       O  
ATOM   4432  CB  LEU B 304     -15.395 -19.660  31.766  1.00128.30           C  
ANISOU 4432  CB  LEU B 304    17991  15863  14892  -1194   -822   2647       C  
ATOM   4433  CG  LEU B 304     -14.430 -18.505  32.037  1.00118.70           C  
ANISOU 4433  CG  LEU B 304    16937  14634  13532  -1095   -530   2534       C  
ATOM   4434  CD1 LEU B 304     -14.146 -17.739  30.752  1.00114.37           C  
ANISOU 4434  CD1 LEU B 304    16677  13999  12781  -1038   -496   2408       C  
ATOM   4435  CD2 LEU B 304     -14.979 -17.567  33.099  1.00134.34           C  
ANISOU 4435  CD2 LEU B 304    18759  16771  15514   -974   -393   2692       C  
ATOM   4436  N   ASP B 305     -16.994 -19.876  29.212  1.00180.21           N  
ANISOU 4436  N   ASP B 305    24750  22380  21342  -1198  -1243   2672       N  
ATOM   4437  CA  ASP B 305     -17.455 -20.638  28.064  1.00184.42           C  
ANISOU 4437  CA  ASP B 305    25344  22840  21888  -1265  -1498   2636       C  
ATOM   4438  C   ASP B 305     -16.794 -22.012  28.048  1.00177.00           C  
ANISOU 4438  C   ASP B 305    24393  21777  21083  -1410  -1629   2528       C  
ATOM   4439  O   ASP B 305     -15.567 -22.117  28.121  1.00179.98           O  
ANISOU 4439  O   ASP B 305    24901  22062  21422  -1429  -1496   2359       O  
ATOM   4440  CB  ASP B 305     -17.165 -19.867  26.774  1.00193.80           C  
ANISOU 4440  CB  ASP B 305    26812  23959  22864  -1179  -1453   2498       C  
ATOM   4441  CG  ASP B 305     -17.742 -18.454  26.792  1.00201.45           C  
ANISOU 4441  CG  ASP B 305    27817  25035  23688  -1028  -1313   2595       C  
ATOM   4442  OD1 ASP B 305     -18.369 -18.064  27.805  1.00203.93           O  
ANISOU 4442  OD1 ASP B 305    27940  25485  24060   -981  -1255   2763       O  
ATOM   4443  OD2 ASP B 305     -17.590 -17.745  25.776  1.00204.69           O  
ANISOU 4443  OD2 ASP B 305    28447  25401  23925   -951  -1271   2505       O  
ATOM   4444  N   ARG B 306     -17.619 -23.064  27.992  1.00177.34           N  
ANISOU 4444  N   ARG B 306    24274  21823  21283  -1512  -1893   2632       N  
ATOM   4445  CA  ARG B 306     -17.110 -24.433  28.023  1.00167.87           C  
ANISOU 4445  CA  ARG B 306    23050  20503  20230  -1652  -2049   2548       C  
ATOM   4446  C   ARG B 306     -16.003 -24.635  26.993  1.00199.01           C  
ANISOU 4446  C   ARG B 306    27273  24291  24052  -1651  -2043   2290       C  
ATOM   4447  O   ARG B 306     -14.985 -25.277  27.279  1.00195.22           O  
ANISOU 4447  O   ARG B 306    26841  23721  23615  -1712  -2004   2158       O  
ATOM   4448  CB  ARG B 306     -18.257 -25.415  27.783  1.00139.79           C  
ANISOU 4448  CB  ARG B 306    19328  16956  16830  -1754  -2366   2686       C  
ATOM   4449  CG  ARG B 306     -18.896 -25.923  29.054  1.00119.71           C  
ANISOU 4449  CG  ARG B 306    16478  14522  14486  -1832  -2414   2904       C  
ATOM   4450  CD  ARG B 306     -20.392 -26.090  28.879  1.00124.58           C  
ANISOU 4450  CD  ARG B 306    16912  15249  15173  -1860  -2635   3116       C  
ATOM   4451  NE  ARG B 306     -21.089 -26.052  30.160  1.00124.24           N  
ANISOU 4451  NE  ARG B 306    16572  15381  15253  -1875  -2600   3356       N  
ATOM   4452  CZ  ARG B 306     -21.376 -27.127  30.886  1.00127.88           C  
ANISOU 4452  CZ  ARG B 306    16813  15851  15925  -2014  -2750   3483       C  
ATOM   4453  NH1 ARG B 306     -21.031 -28.332  30.452  1.00128.73           N  
ANISOU 4453  NH1 ARG B 306    16976  15789  16148  -2151  -2952   3385       N  
ATOM   4454  NH2 ARG B 306     -22.012 -26.999  32.042  1.00131.60           N  
ANISOU 4454  NH2 ARG B 306    17008  16505  16488  -2010  -2704   3708       N  
ATOM   4455  N   GLU B 307     -16.195 -24.101  25.784  1.00199.67           N  
ANISOU 4455  N   GLU B 307    27537  24351  23977  -1576  -2084   2216       N  
ATOM   4456  CA  GLU B 307     -15.169 -24.189  24.749  1.00196.82           C  
ANISOU 4456  CA  GLU B 307    27438  23868  23475  -1556  -2072   1979       C  
ATOM   4457  C   GLU B 307     -13.858 -23.576  25.229  1.00188.43           C  
ANISOU 4457  C   GLU B 307    26497  22792  22307  -1514  -1778   1852       C  
ATOM   4458  O   GLU B 307     -12.780 -24.141  25.014  1.00191.51           O  
ANISOU 4458  O   GLU B 307    27009  23087  22670  -1553  -1766   1672       O  
ATOM   4459  CB  GLU B 307     -15.653 -23.498  23.474  1.00200.06           C  
ANISOU 4459  CB  GLU B 307    28006  24289  23718  -1459  -2124   1949       C  
ATOM   4460  CG  GLU B 307     -16.782 -24.225  22.758  1.00205.57           C  
ANISOU 4460  CG  GLU B 307    28626  24979  24500  -1502  -2436   2022       C  
ATOM   4461  CD  GLU B 307     -16.346 -25.533  22.131  1.00209.35           C  
ANISOU 4461  CD  GLU B 307    29172  25321  25053  -1593  -2669   1872       C  
ATOM   4462  OE1 GLU B 307     -17.165 -26.476  22.105  1.00215.35           O  
ANISOU 4462  OE1 GLU B 307    29790  26061  25974  -1684  -2933   1960       O  
ATOM   4463  OE2 GLU B 307     -15.189 -25.622  21.673  1.00209.94           O  
ANISOU 4463  OE2 GLU B 307    29437  25309  25020  -1572  -2597   1669       O  
ATOM   4464  N   LEU B 308     -13.933 -22.403  25.868  1.00188.14           N  
ANISOU 4464  N   LEU B 308    26431  22853  22202  -1429  -1543   1940       N  
ATOM   4465  CA  LEU B 308     -12.741 -21.772  26.429  1.00170.25           C  
ANISOU 4465  CA  LEU B 308    24260  20579  19847  -1393  -1260   1835       C  
ATOM   4466  C   LEU B 308     -12.039 -22.680  27.434  1.00163.38           C  
ANISOU 4466  C   LEU B 308    23274  19680  19123  -1488  -1231   1798       C  
ATOM   4467  O   LEU B 308     -10.804 -22.748  27.461  1.00164.32           O  
ANISOU 4467  O   LEU B 308    23524  19741  19170  -1498  -1095   1627       O  
ATOM   4468  CB  LEU B 308     -13.119 -20.451  27.103  1.00160.95           C  
ANISOU 4468  CB  LEU B 308    23030  19515  18610  -1290  -1047   1965       C  
ATOM   4469  CG  LEU B 308     -12.991 -19.112  26.373  1.00163.79           C  
ANISOU 4469  CG  LEU B 308    23596  19883  18752  -1171   -898   1922       C  
ATOM   4470  CD1 LEU B 308     -11.569 -18.871  25.903  1.00168.06           C  
ANISOU 4470  CD1 LEU B 308    24371  20338  19147  -1170   -739   1709       C  
ATOM   4471  CD2 LEU B 308     -13.962 -19.032  25.209  1.00171.10           C  
ANISOU 4471  CD2 LEU B 308    24581  20814  19615  -1131  -1090   1966       C  
ATOM   4472  N   CYS B 309     -12.808 -23.380  28.273  1.00171.51           N  
ANISOU 4472  N   CYS B 309    24055  20757  20352  -1556  -1355   1960       N  
ATOM   4473  CA  CYS B 309     -12.212 -24.295  29.245  1.00157.61           C  
ANISOU 4473  CA  CYS B 309    22172  18971  18742  -1646  -1340   1939       C  
ATOM   4474  C   CYS B 309     -11.423 -25.400  28.553  1.00152.79           C  
ANISOU 4474  C   CYS B 309    21699  18219  18135  -1725  -1487   1748       C  
ATOM   4475  O   CYS B 309     -10.297 -25.716  28.951  1.00152.80           O  
ANISOU 4475  O   CYS B 309    21759  18176  18124  -1750  -1367   1610       O  
ATOM   4476  CB  CYS B 309     -13.297 -24.894  30.140  1.00154.70           C  
ANISOU 4476  CB  CYS B 309    21508  18683  18587  -1711  -1482   2167       C  
ATOM   4477  SG  CYS B 309     -14.075 -23.714  31.256  1.00159.14           S  
ANISOU 4477  SG  CYS B 309    21869  19439  19157  -1608  -1292   2390       S  
ATOM   4478  N   GLN B 310     -12.010 -26.009  27.520  1.00152.78           N  
ANISOU 4478  N   GLN B 310    21749  18153  18147  -1759  -1754   1733       N  
ATOM   4479  CA  GLN B 310     -11.328 -27.082  26.802  1.00145.15           C  
ANISOU 4479  CA  GLN B 310    20917  17052  17180  -1820  -1925   1548       C  
ATOM   4480  C   GLN B 310     -10.069 -26.564  26.115  1.00122.09           C  
ANISOU 4480  C   GLN B 310    18259  14093  14038  -1748  -1756   1320       C  
ATOM   4481  O   GLN B 310      -9.011 -27.202  26.164  1.00120.27           O  
ANISOU 4481  O   GLN B 310    18114  13795  13788  -1781  -1737   1156       O  
ATOM   4482  CB  GLN B 310     -12.282 -27.706  25.782  1.00164.44           C  
ANISOU 4482  CB  GLN B 310    23366  19443  19671  -1853  -2245   1581       C  
ATOM   4483  CG  GLN B 310     -12.395 -29.231  25.837  1.00175.32           C  
ANISOU 4483  CG  GLN B 310    24665  20714  21233  -1978  -2525   1566       C  
ATOM   4484  CD  GLN B 310     -11.137 -29.956  25.382  1.00180.36           C  
ANISOU 4484  CD  GLN B 310    25492  21232  21803  -1989  -2557   1318       C  
ATOM   4485  OE1 GLN B 310     -10.206 -29.347  24.858  1.00181.73           O  
ANISOU 4485  OE1 GLN B 310    25865  21408  21777  -1905  -2390   1150       O  
ATOM   4486  NE2 GLN B 310     -11.115 -31.272  25.570  1.00184.08           N  
ANISOU 4486  NE2 GLN B 310    25902  21604  22437  -2093  -2781   1297       N  
ATOM   4487  N   LEU B 311     -10.168 -25.404  25.463  1.00125.51           N  
ANISOU 4487  N   LEU B 311    18820  14574  14296  -1648  -1634   1313       N  
ATOM   4488  CA  LEU B 311      -9.001 -24.808  24.821  1.00127.54           C  
ANISOU 4488  CA  LEU B 311    19316  14810  14333  -1582  -1461   1119       C  
ATOM   4489  C   LEU B 311      -7.926 -24.454  25.838  1.00133.35           C  
ANISOU 4489  C   LEU B 311    20048  15576  15043  -1584  -1182   1062       C  
ATOM   4490  O   LEU B 311      -6.734 -24.674  25.592  1.00146.09           O  
ANISOU 4490  O   LEU B 311    21809  17151  16549  -1586  -1104    874       O  
ATOM   4491  CB  LEU B 311      -9.420 -23.578  24.017  1.00142.19           C  
ANISOU 4491  CB  LEU B 311    21289  16715  16020  -1479  -1382   1154       C  
ATOM   4492  CG  LEU B 311     -10.374 -23.887  22.861  1.00152.45           C  
ANISOU 4492  CG  LEU B 311    22622  17989  17314  -1462  -1648   1181       C  
ATOM   4493  CD1 LEU B 311     -10.912 -22.611  22.239  1.00159.42           C  
ANISOU 4493  CD1 LEU B 311    23592  18935  18044  -1354  -1553   1248       C  
ATOM   4494  CD2 LEU B 311      -9.705 -24.763  21.806  1.00159.84           C  
ANISOU 4494  CD2 LEU B 311    23719  18834  18180  -1475  -1819    978       C  
ATOM   4495  N   LEU B 312      -8.325 -23.899  26.984  1.00131.73           N  
ANISOU 4495  N   LEU B 312    19672  15451  14928  -1576  -1030   1219       N  
ATOM   4496  CA  LEU B 312      -7.353 -23.581  28.026  1.00121.51           C  
ANISOU 4496  CA  LEU B 312    18355  14191  13624  -1574   -769   1170       C  
ATOM   4497  C   LEU B 312      -6.656 -24.839  28.530  1.00105.71           C  
ANISOU 4497  C   LEU B 312    16299  12133  11732  -1662   -836   1074       C  
ATOM   4498  O   LEU B 312      -5.423 -24.882  28.614  1.00102.55           O  
ANISOU 4498  O   LEU B 312    16015  11715  11233  -1662   -689    905       O  
ATOM   4499  CB  LEU B 312      -8.047 -22.852  29.177  1.00108.39           C  
ANISOU 4499  CB  LEU B 312    16494  12632  12056  -1539   -632   1367       C  
ATOM   4500  CG  LEU B 312      -7.172 -22.475  30.368  1.00107.63           C  
ANISOU 4500  CG  LEU B 312    16343  12584  11969  -1527   -362   1336       C  
ATOM   4501  CD1 LEU B 312      -6.035 -21.583  29.922  1.00108.95           C  
ANISOU 4501  CD1 LEU B 312    16741  12736  11920  -1474   -139   1169       C  
ATOM   4502  CD2 LEU B 312      -8.017 -21.789  31.417  1.00101.53           C  
ANISOU 4502  CD2 LEU B 312    15364  11923  11291  -1476   -268   1542       C  
ATOM   4503  N   LEU B 313      -7.430 -25.897  28.806  1.00104.53           N  
ANISOU 4503  N   LEU B 313    15981  11955  11780  -1740  -1070   1177       N  
ATOM   4504  CA  LEU B 313      -6.858 -27.143  29.314  1.00104.22           C  
ANISOU 4504  CA  LEU B 313    15884  11854  11862  -1826  -1156   1102       C  
ATOM   4505  C   LEU B 313      -5.795 -27.696  28.375  1.00152.64           C  
ANISOU 4505  C   LEU B 313    22246  17896  17855  -1827  -1218    857       C  
ATOM   4506  O   LEU B 313      -4.727 -28.130  28.823  1.00153.72           O  
ANISOU 4506  O   LEU B 313    22422  18015  17969  -1846  -1117    723       O  
ATOM   4507  CB  LEU B 313      -7.962 -28.177  29.534  1.00105.56           C  
ANISOU 4507  CB  LEU B 313    15861  11993  12256  -1915  -1439   1260       C  
ATOM   4508  CG  LEU B 313      -8.747 -28.036  30.831  1.00120.89           C  
ANISOU 4508  CG  LEU B 313    17524  14034  14374  -1938  -1378   1492       C  
ATOM   4509  CD1 LEU B 313      -9.784 -29.138  30.967  1.00136.55           C  
ANISOU 4509  CD1 LEU B 313    19324  15985  16574  -2042  -1676   1645       C  
ATOM   4510  CD2 LEU B 313      -7.757 -28.093  31.978  1.00114.58           C  
ANISOU 4510  CD2 LEU B 313    16667  13267  13602  -1941  -1149   1435       C  
ATOM   4511  N   GLU B 314      -6.069 -27.695  27.070  1.00150.21           N  
ANISOU 4511  N   GLU B 314    22088  17542  17444  -1797  -1385    793       N  
ATOM   4512  CA  GLU B 314      -5.071 -28.181  26.126  1.00140.03           C  
ANISOU 4512  CA  GLU B 314    21015  16186  16003  -1779  -1451    559       C  
ATOM   4513  C   GLU B 314      -3.853 -27.274  26.115  1.00122.08           C  
ANISOU 4513  C   GLU B 314    18898  13972  13516  -1715  -1152    421       C  
ATOM   4514  O   GLU B 314      -2.712 -27.754  26.074  1.00112.27           O  
ANISOU 4514  O   GLU B 314    17761  12710  12187  -1719  -1106    240       O  
ATOM   4515  CB  GLU B 314      -5.664 -28.288  24.723  1.00154.75           C  
ANISOU 4515  CB  GLU B 314    22996  18005  17795  -1745  -1686    527       C  
ATOM   4516  CG  GLU B 314      -4.755 -29.019  23.743  1.00168.05           C  
ANISOU 4516  CG  GLU B 314    24879  19622  19348  -1724  -1816    292       C  
ATOM   4517  CD  GLU B 314      -5.165 -28.816  22.299  1.00173.99           C  
ANISOU 4517  CD  GLU B 314    25773  20360  19974  -1657  -1980    241       C  
ATOM   4518  OE1 GLU B 314      -6.273 -28.291  22.067  1.00178.90           O  
ANISOU 4518  OE1 GLU B 314    26325  21006  20642  -1642  -2034    396       O  
ATOM   4519  OE2 GLU B 314      -4.383 -29.181  21.395  1.00175.45           O  
ANISOU 4519  OE2 GLU B 314    26136  20519  20007  -1610  -2055     46       O  
ATOM   4520  N   GLY B 315      -4.077 -25.960  26.123  1.00128.45           N  
ANISOU 4520  N   GLY B 315    19725  14851  14230  -1653   -956    503       N  
ATOM   4521  CA  GLY B 315      -2.972 -25.038  26.307  1.00125.49           C  
ANISOU 4521  CA  GLY B 315    19470  14533  13678  -1607   -657    401       C  
ATOM   4522  C   GLY B 315      -2.196 -25.316  27.577  1.00132.24           C  
ANISOU 4522  C   GLY B 315    20226  15414  14607  -1648   -482    369       C  
ATOM   4523  O   GLY B 315      -0.964 -25.333  27.576  1.00144.10           O  
ANISOU 4523  O   GLY B 315    21847  16930  15976  -1641   -340    200       O  
ATOM   4524  N   LEU B 316      -2.910 -25.538  28.686  1.00130.25           N  
ANISOU 4524  N   LEU B 316    19746  15180  14562  -1686   -489    535       N  
ATOM   4525  CA  LEU B 316      -2.243 -25.814  29.956  1.00114.78           C  
ANISOU 4525  CA  LEU B 316    17670  13253  12686  -1717   -323    518       C  
ATOM   4526  C   LEU B 316      -1.423 -27.100  29.893  1.00119.78           C  
ANISOU 4526  C   LEU B 316    18354  13824  13335  -1770   -437    353       C  
ATOM   4527  O   LEU B 316      -0.253 -27.113  30.290  1.00140.39           O  
ANISOU 4527  O   LEU B 316    21027  16461  15855  -1764   -256    211       O  
ATOM   4528  CB  LEU B 316      -3.261 -25.883  31.095  1.00 99.22           C  
ANISOU 4528  CB  LEU B 316    15433  11327  10940  -1742   -339    741       C  
ATOM   4529  CG  LEU B 316      -4.080 -24.622  31.367  1.00 99.21           C  
ANISOU 4529  CG  LEU B 316    15357  11406  10931  -1676   -216    912       C  
ATOM   4530  CD1 LEU B 316      -5.110 -24.912  32.441  1.00 99.37           C  
ANISOU 4530  CD1 LEU B 316    15098  11483  11176  -1702   -278   1131       C  
ATOM   4531  CD2 LEU B 316      -3.189 -23.452  31.752  1.00 97.77           C  
ANISOU 4531  CD2 LEU B 316    15265  11284  10602  -1611    103    840       C  
ATOM   4532  N   GLU B 317      -2.025 -28.200  29.423  1.00120.72           N  
ANISOU 4532  N   GLU B 317    18444  13859  13567  -1820   -741    370       N  
ATOM   4533  CA  GLU B 317      -1.280 -29.455  29.294  1.00131.38           C  
ANISOU 4533  CA  GLU B 317    19857  15136  14926  -1861   -879    207       C  
ATOM   4534  C   GLU B 317       0.023 -29.257  28.527  1.00131.07           C  
ANISOU 4534  C   GLU B 317    20057  15110  14631  -1806   -774    -32       C  
ATOM   4535  O   GLU B 317       1.085 -29.717  28.957  1.00125.92           O  
ANISOU 4535  O   GLU B 317    19445  14469  13929  -1813   -678   -174       O  
ATOM   4536  CB  GLU B 317      -2.126 -30.536  28.618  1.00144.52           C  
ANISOU 4536  CB  GLU B 317    21503  16695  16715  -1911  -1246    242       C  
ATOM   4537  CG  GLU B 317      -1.278 -31.720  28.141  1.00149.60           C  
ANISOU 4537  CG  GLU B 317    22280  17253  17309  -1926  -1411     34       C  
ATOM   4538  CD  GLU B 317      -2.099 -32.894  27.640  1.00155.29           C  
ANISOU 4538  CD  GLU B 317    22966  17854  18184  -1985  -1786     71       C  
ATOM   4539  OE1 GLU B 317      -1.495 -33.872  27.151  1.00153.50           O  
ANISOU 4539  OE1 GLU B 317    22860  17547  17916  -1987  -1957   -101       O  
ATOM   4540  OE2 GLU B 317      -3.344 -32.844  27.731  1.00160.18           O  
ANISOU 4540  OE2 GLU B 317    23438  18461  18961  -2029  -1916    270       O  
ATOM   4541  N   GLY B 318      -0.044 -28.584  27.378  1.00139.15           N  
ANISOU 4541  N   GLY B 318    21240  16145  15485  -1749   -794    -76       N  
ATOM   4542  CA  GLY B 318       1.173 -28.272  26.647  1.00143.20           C  
ANISOU 4542  CA  GLY B 318    21970  16698  15742  -1694   -677   -283       C  
ATOM   4543  C   GLY B 318       2.141 -27.451  27.479  1.00135.75           C  
ANISOU 4543  C   GLY B 318    21030  15845  14702  -1681   -332   -325       C  
ATOM   4544  O   GLY B 318       3.360 -27.602  27.365  1.00141.75           O  
ANISOU 4544  O   GLY B 318    21912  16643  15302  -1664   -226   -507       O  
ATOM   4545  N   VAL B 319       1.608 -26.559  28.316  1.00127.01           N  
ANISOU 4545  N   VAL B 319    19791  14782  13686  -1682   -157   -159       N  
ATOM   4546  CA  VAL B 319       2.455 -25.728  29.165  1.00139.31           C  
ANISOU 4546  CA  VAL B 319    21341  16422  15170  -1668    168   -189       C  
ATOM   4547  C   VAL B 319       3.198 -26.585  30.186  1.00158.67           C  
ANISOU 4547  C   VAL B 319    23703  18883  17701  -1706    232   -268       C  
ATOM   4548  O   VAL B 319       4.371 -26.338  30.484  1.00152.01           O  
ANISOU 4548  O   VAL B 319    22934  18101  16722  -1694    445   -406       O  
ATOM   4549  CB  VAL B 319       1.603 -24.633  29.832  1.00135.39           C  
ANISOU 4549  CB  VAL B 319    20714  15964  14764  -1648    307     13       C  
ATOM   4550  CG1 VAL B 319       2.314 -24.057  31.020  1.00127.90           C  
ANISOU 4550  CG1 VAL B 319    19692  15087  13816  -1641    603      3       C  
ATOM   4551  CG2 VAL B 319       1.307 -23.530  28.830  1.00137.15           C  
ANISOU 4551  CG2 VAL B 319    21081  16196  14832  -1594    336     41       C  
ATOM   4552  N   LEU B 320       2.531 -27.595  30.749  1.00165.50           N  
ANISOU 4552  N   LEU B 320    24404  19693  18786  -1755     52   -179       N  
ATOM   4553  CA  LEU B 320       3.183 -28.436  31.750  1.00164.75           C  
ANISOU 4553  CA  LEU B 320    24216  19605  18778  -1789    107   -243       C  
ATOM   4554  C   LEU B 320       4.359 -29.198  31.150  1.00142.71           C  
ANISOU 4554  C   LEU B 320    21604  16798  15821  -1781     57   -485       C  
ATOM   4555  O   LEU B 320       5.418 -29.318  31.777  1.00136.79           O  
ANISOU 4555  O   LEU B 320    20868  16104  15002  -1775    240   -606       O  
ATOM   4556  CB  LEU B 320       2.169 -29.405  32.350  1.00 95.32           C  
ANISOU 4556  CB  LEU B 320    15219  10748  10251  -1849   -107    -87       C  
ATOM   4557  CG  LEU B 320       0.982 -28.719  33.022  1.00 95.41           C  
ANISOU 4557  CG  LEU B 320    15028  10799  10425  -1851    -66    160       C  
ATOM   4558  CD1 LEU B 320       0.005 -29.744  33.563  1.00 96.27           C  
ANISOU 4558  CD1 LEU B 320    14932  10856  10789  -1921   -294    319       C  
ATOM   4559  CD2 LEU B 320       1.461 -27.787  34.114  1.00 93.74           C  
ANISOU 4559  CD2 LEU B 320    14731  10693  10194  -1812    263    189       C  
ATOM   4560  N   ARG B 321       4.189 -29.721  29.933  1.00138.37           N  
ANISOU 4560  N   ARG B 321    21192  16182  15199  -1771   -192   -560       N  
ATOM   4561  CA  ARG B 321       5.230 -30.485  29.258  1.00143.42           C  
ANISOU 4561  CA  ARG B 321    22008  16814  15671  -1747   -277   -790       C  
ATOM   4562  C   ARG B 321       6.399 -29.622  28.803  1.00143.15           C  
ANISOU 4562  C   ARG B 321    22147  16888  15355  -1692    -41   -944       C  
ATOM   4563  O   ARG B 321       7.444 -30.168  28.436  1.00142.86           O  
ANISOU 4563  O   ARG B 321    22243  16882  15155  -1664    -54  -1143       O  
ATOM   4564  CB  ARG B 321       4.630 -31.208  28.054  1.00155.28           C  
ANISOU 4564  CB  ARG B 321    23602  18222  17177  -1739   -620   -819       C  
ATOM   4565  CG  ARG B 321       3.460 -32.110  28.389  1.00159.36           C  
ANISOU 4565  CG  ARG B 321    23957  18626  17967  -1805   -883   -668       C  
ATOM   4566  CD  ARG B 321       3.020 -32.901  27.168  1.00169.32           C  
ANISOU 4566  CD  ARG B 321    25328  19790  19216  -1793  -1230   -731       C  
ATOM   4567  NE  ARG B 321       1.757 -33.592  27.402  1.00175.28           N  
ANISOU 4567  NE  ARG B 321    25925  20441  20234  -1866  -1483   -558       N  
ATOM   4568  CZ  ARG B 321       1.653 -34.786  27.974  1.00186.65           C  
ANISOU 4568  CZ  ARG B 321    27277  21793  21849  -1929  -1654   -550       C  
ATOM   4569  NH1 ARG B 321       2.743 -35.429  28.369  1.00193.54           N  
ANISOU 4569  NH1 ARG B 321    28210  22668  22658  -1918  -1597   -714       N  
ATOM   4570  NH2 ARG B 321       0.460 -35.337  28.152  1.00191.27           N  
ANISOU 4570  NH2 ARG B 321    27713  22290  22669  -2005  -1884   -375       N  
ATOM   4571  N   ASP B 322       6.250 -28.299  28.818  1.00163.23           N  
ANISOU 4571  N   ASP B 322    19147  21404  21467   1048  -1008   5235       N  
ATOM   4572  CA  ASP B 322       7.286 -27.369  28.372  1.00161.92           C  
ANISOU 4572  CA  ASP B 322    19410  21101  21011   1125   -711   4597       C  
ATOM   4573  C   ASP B 322       7.442 -26.369  29.509  1.00161.24           C  
ANISOU 4573  C   ASP B 322    18802  21897  20565   1349   -495   4500       C  
ATOM   4574  O   ASP B 322       6.655 -25.427  29.622  1.00163.30           O  
ANISOU 4574  O   ASP B 322    19002  22443  20602   1393   -588   4377       O  
ATOM   4575  CB  ASP B 322       6.888 -26.685  27.063  1.00159.09           C  
ANISOU 4575  CB  ASP B 322    19786  20101  20561    986   -857   4143       C  
ATOM   4576  CG  ASP B 322       8.051 -25.977  26.380  1.00154.81           C  
ANISOU 4576  CG  ASP B 322    19800  19225  19794   1019   -565   3495       C  
ATOM   4577  OD1 ASP B 322       9.038 -25.618  27.055  1.00153.50           O  
ANISOU 4577  OD1 ASP B 322    19392  19496  19433   1189   -238   3327       O  
ATOM   4578  OD2 ASP B 322       7.968 -25.776  25.150  1.00155.32           O  
ANISOU 4578  OD2 ASP B 322    20554  18586  19876    868   -668   3153       O  
ATOM   4579  N   GLN B 323       8.491 -26.546  30.314  1.00166.07           N  
ANISOU 4579  N   GLN B 323    19065  22920  21112   1488   -195   4534       N  
ATOM   4580  CA  GLN B 323       8.673 -25.681  31.474  1.00171.07           C  
ANISOU 4580  CA  GLN B 323    19169  24423  21408   1689     17   4480       C  
ATOM   4581  C   GLN B 323       8.892 -24.235  31.045  1.00169.12           C  
ANISOU 4581  C   GLN B 323    19314  24180  20764   1749    168   3841       C  
ATOM   4582  O   GLN B 323       8.331 -23.310  31.645  1.00174.35           O  
ANISOU 4582  O   GLN B 323    19692  25400  21154   1854    178   3783       O  
ATOM   4583  CB  GLN B 323       9.833 -26.189  32.329  1.00178.32           C  
ANISOU 4583  CB  GLN B 323    19687  25725  22342   1805    307   4627       C  
ATOM   4584  CG  GLN B 323       9.867 -25.607  33.733  1.00178.28           C  
ANISOU 4584  CG  GLN B 323    18989  26692  22058   1990    475   4758       C  
ATOM   4585  CD  GLN B 323       8.993 -26.393  34.707  1.00171.15           C  
ANISOU 4585  CD  GLN B 323    17405  26263  21359   2001    277   5436       C  
ATOM   4586  OE1 GLN B 323       7.842 -26.032  34.958  1.00163.82           O  
ANISOU 4586  OE1 GLN B 323    16270  25595  20379   2000     71   5599       O  
ATOM   4587  NE2 GLN B 323       9.541 -27.472  35.259  1.00170.28           N  
ANISOU 4587  NE2 GLN B 323    16942  26270  21488   2016    342   5837       N  
ATOM   4588  N   LEU B 324       9.706 -24.019  30.005  1.00162.74           N  
ANISOU 4588  N   LEU B 324    19167  22750  19918   1685    296   3353       N  
ATOM   4589  CA  LEU B 324       9.948 -22.662  29.518  1.00153.71           C  
ANISOU 4589  CA  LEU B 324    18444  21555  18404   1731    440   2727       C  
ATOM   4590  C   LEU B 324       8.648 -21.986  29.107  1.00158.19           C  
ANISOU 4590  C   LEU B 324    19168  22044  18892   1676    167   2673       C  
ATOM   4591  O   LEU B 324       8.472 -20.781  29.324  1.00160.10           O  
ANISOU 4591  O   LEU B 324    19399  22642  18789   1779    265   2354       O  
ATOM   4592  CB  LEU B 324      10.932 -22.681  28.352  1.00143.53           C  
ANISOU 4592  CB  LEU B 324    17878  19517  17141   1641    577   2254       C  
ATOM   4593  CG  LEU B 324      12.409 -22.848  28.706  1.00147.67           C  
ANISOU 4593  CG  LEU B 324    18330  20176  17600   1737    938   2098       C  
ATOM   4594  CD1 LEU B 324      13.217 -23.133  27.461  1.00149.82           C  
ANISOU 4594  CD1 LEU B 324    19324  19604  17996   1618   1016   1735       C  
ATOM   4595  CD2 LEU B 324      12.932 -21.601  29.394  1.00149.82           C  
ANISOU 4595  CD2 LEU B 324    18406  21090  17427   1907   1224   1733       C  
ATOM   4596  N   ALA B 325       7.735 -22.739  28.488  1.00141.89           N  
ANISOU 4596  N   ALA B 325    17267  19502  17142   1510   -174   2977       N  
ATOM   4597  CA  ALA B 325       6.436 -22.179  28.134  1.00155.24           C  
ANISOU 4597  CA  ALA B 325    19059  21138  18787   1452   -457   2992       C  
ATOM   4598  C   ALA B 325       5.705 -21.672  29.374  1.00167.04           C  
ANISOU 4598  C   ALA B 325    19855  23501  20110   1611   -463   3270       C  
ATOM   4599  O   ALA B 325       5.118 -20.584  29.355  1.00155.39           O  
ANISOU 4599  O   ALA B 325    18430  22232  18378   1673   -485   3034       O  
ATOM   4600  CB  ALA B 325       5.595 -23.221  27.395  1.00156.49           C  
ANISOU 4600  CB  ALA B 325    19424  20699  19336   1238   -828   3356       C  
ATOM   4601  N   LEU B 326       5.723 -22.450  30.461  1.00173.14           N  
ANISOU 4601  N   LEU B 326    19975  24788  21023   1678   -439   3775       N  
ATOM   4602  CA  LEU B 326       5.092 -22.008  31.705  1.00168.05           C  
ANISOU 4602  CA  LEU B 326    18645  24995  20212   1830   -420   4049       C  
ATOM   4603  C   LEU B 326       5.721 -20.727  32.238  1.00164.59           C  
ANISOU 4603  C   LEU B 326    18133  25074  19327   2008    -87   3599       C  
ATOM   4604  O   LEU B 326       5.020 -19.748  32.519  1.00169.40           O  
ANISOU 4604  O   LEU B 326    18623  26046  19696   2092   -104   3487       O  
ATOM   4605  CB  LEU B 326       5.188 -23.106  32.759  1.00163.35           C  
ANISOU 4605  CB  LEU B 326    17392  24834  19838   1866   -418   4640       C  
ATOM   4606  CG  LEU B 326       4.740 -22.656  34.149  1.00162.62           C  
ANISOU 4606  CG  LEU B 326    16568  25675  19546   2034   -339   4902       C  
ATOM   4607  CD1 LEU B 326       3.278 -22.222  34.146  1.00160.86           C  
ANISOU 4607  CD1 LEU B 326    16222  25582  19315   2018   -613   5076       C  
ATOM   4608  CD2 LEU B 326       4.977 -23.763  35.153  1.00169.77           C  
ANISOU 4608  CD2 LEU B 326    16858  26980  20665   2065   -315   5458       C  
ATOM   4609  N   ARG B 327       7.044 -20.731  32.409  1.00177.14           N  
ANISOU 4609  N   ARG B 327    19780  26720  20805   2069    223   3353       N  
ATOM   4610  CA  ARG B 327       7.740 -19.563  32.940  1.00169.32           C  
ANISOU 4610  CA  ARG B 327    18719  26229  19387   2225    555   2927       C  
ATOM   4611  C   ARG B 327       7.506 -18.334  32.069  1.00149.67           C  
ANISOU 4611  C   ARG B 327    16801  23432  16637   2216    562   2360       C  
ATOM   4612  O   ARG B 327       7.251 -17.238  32.582  1.00157.09           O  
ANISOU 4612  O   ARG B 327    17576  24867  17243   2339    683   2158       O  
ATOM   4613  CB  ARG B 327       9.228 -19.875  33.106  1.00180.12           C  
ANISOU 4613  CB  ARG B 327    20119  27601  20719   2263    862   2761       C  
ATOM   4614  CG  ARG B 327       9.504 -20.693  34.375  1.00191.54           C  
ANISOU 4614  CG  ARG B 327    20836  29667  22276   2341    942   3281       C  
ATOM   4615  CD  ARG B 327      10.909 -21.295  34.455  1.00199.38           C  
ANISOU 4615  CD  ARG B 327    21848  30569  23338   2353   1191   3229       C  
ATOM   4616  NE  ARG B 327      11.009 -22.222  35.585  1.00201.12           N  
ANISOU 4616  NE  ARG B 327    21378  31312  23726   2406   1206   3801       N  
ATOM   4617  CZ  ARG B 327      12.129 -22.822  35.981  1.00200.00           C  
ANISOU 4617  CZ  ARG B 327    21055  31283  23654   2444   1418   3894       C  
ATOM   4618  NH1 ARG B 327      13.271 -22.601  35.344  1.00199.52           N  
ANISOU 4618  NH1 ARG B 327    21450  30850  23511   2436   1642   3450       N  
ATOM   4619  NH2 ARG B 327      12.106 -23.642  37.025  1.00198.73           N  
ANISOU 4619  NH2 ARG B 327    20248  31614  23644   2490   1408   4439       N  
ATOM   4620  N   ALA B 328       7.615 -18.490  30.748  1.00149.18           N  
ANISOU 4620  N   ALA B 328    17420  22546  16714   2071    444   2091       N  
ATOM   4621  CA  ALA B 328       7.393 -17.361  29.849  1.00127.17           C  
ANISOU 4621  CA  ALA B 328    15206  19418  13694   2050    436   1555       C  
ATOM   4622  C   ALA B 328       5.979 -16.799  30.001  1.00114.02           C  
ANISOU 4622  C   ALA B 328    13362  17986  11975   2073    202   1718       C  
ATOM   4623  O   ALA B 328       5.796 -15.580  30.084  1.00105.44           O  
ANISOU 4623  O   ALA B 328    12352  17152  10557   2172    316   1369       O  
ATOM   4624  CB  ALA B 328       7.669 -17.774  28.402  1.00126.05           C  
ANISOU 4624  CB  ALA B 328    15809  18330  13754   1867    314   1307       C  
ATOM   4625  N   LEU B 329       4.963 -17.673  30.056  1.00101.05           N  
ANISOU 4625  N   LEU B 329    11470  16270  10655   1984   -122   2254       N  
ATOM   4626  CA  LEU B 329       3.586 -17.194  30.192  1.00116.76           C  
ANISOU 4626  CA  LEU B 329    13271  18474  12619   2002   -357   2445       C  
ATOM   4627  C   LEU B 329       3.397 -16.367  31.454  1.00134.41           C  
ANISOU 4627  C   LEU B 329    14926  21595  14548   2207   -161   2488       C  
ATOM   4628  O   LEU B 329       2.717 -15.335  31.434  1.00126.87           O  
ANISOU 4628  O   LEU B 329    14014  20816  13374   2278   -178   2300       O  
ATOM   4629  CB  LEU B 329       2.606 -18.366  30.200  1.00104.38           C  
ANISOU 4629  CB  LEU B 329    11445  16761  11453   1876   -716   3067       C  
ATOM   4630  CG  LEU B 329       1.158 -17.989  30.541  1.00105.59           C  
ANISOU 4630  CG  LEU B 329    11271  17244  11606   1909   -956   3363       C  
ATOM   4631  CD1 LEU B 329       0.518 -17.205  29.402  1.00186.25           C  
ANISOU 4631  CD1 LEU B 329    22071  26947  21749   1827  -1130   3018       C  
ATOM   4632  CD2 LEU B 329       0.332 -19.220  30.882  1.00108.25           C  
ANISOU 4632  CD2 LEU B 329    11190  17620  12321   1813  -1255   4042       C  
ATOM   4633  N   GLU B 330       3.977 -16.815  32.565  1.00133.10           N  
ANISOU 4633  N   GLU B 330    14212  21994  14367   2301     28   2744       N  
ATOM   4634  CA  GLU B 330       3.848 -16.082  33.817  1.00149.41           C  
ANISOU 4634  CA  GLU B 330    15713  24919  16136   2485    228   2799       C  
ATOM   4635  C   GLU B 330       4.519 -14.714  33.732  1.00153.60           C  
ANISOU 4635  C   GLU B 330    16542  25589  16231   2592    538   2164       C  
ATOM   4636  O   GLU B 330       4.021 -13.736  34.298  1.00163.09           O  
ANISOU 4636  O   GLU B 330    17525  27286  17157   2717    629   2068       O  
ATOM   4637  CB  GLU B 330       4.431 -16.896  34.969  1.00157.81           C  
ANISOU 4637  CB  GLU B 330    16165  26520  17276   2544    367   3193       C  
ATOM   4638  CG  GLU B 330       3.894 -16.477  36.322  1.00170.82           C  
ANISOU 4638  CG  GLU B 330    17120  29051  18733   2695    454   3466       C  
ATOM   4639  CD  GLU B 330       4.868 -15.608  37.087  1.00179.35           C  
ANISOU 4639  CD  GLU B 330    18048  30691  19405   2837    850   3118       C  
ATOM   4640  OE1 GLU B 330       6.080 -15.674  36.792  1.00186.82           O  
ANISOU 4640  OE1 GLU B 330    19274  31423  20287   2818   1054   2810       O  
ATOM   4641  OE2 GLU B 330       4.417 -14.855  37.980  1.00176.76           O  
ANISOU 4641  OE2 GLU B 330    17326  31014  18819   2964    958   3152       O  
ATOM   4642  N   GLU B 331       5.677 -14.629  33.070  1.00156.29           N  
ANISOU 4642  N   GLU B 331    17369  25516  16498   2549    721   1728       N  
ATOM   4643  CA  GLU B 331       6.381 -13.351  33.006  1.00136.85           C  
ANISOU 4643  CA  GLU B 331    15188  23191  13616   2644   1028   1120       C  
ATOM   4644  C   GLU B 331       5.625 -12.347  32.145  1.00130.40           C  
ANISOU 4644  C   GLU B 331    14847  22037  12663   2629    911    767       C  
ATOM   4645  O   GLU B 331       5.461 -11.187  32.533  1.00131.25           O  
ANISOU 4645  O   GLU B 331    14894  22546  12427   2753   1077    495       O  
ATOM   4646  CB  GLU B 331       7.793 -13.551  32.464  1.00143.40           C  
ANISOU 4646  CB  GLU B 331    16430  23634  14423   2593   1240    755       C  
ATOM   4647  CG  GLU B 331       8.826 -13.972  33.492  1.00139.62           C  
ANISOU 4647  CG  GLU B 331    15489  23679  13880   2670   1505    901       C  
ATOM   4648  CD  GLU B 331      10.248 -13.693  33.026  1.00133.65           C  
ANISOU 4648  CD  GLU B 331    15157  22660  12962   2661   1791    398       C  
ATOM   4649  OE1 GLU B 331      10.528 -12.541  32.629  1.00131.14           O  
ANISOU 4649  OE1 GLU B 331    15228  22278  12321   2699   1954   -148       O  
ATOM   4650  OE2 GLU B 331      11.083 -14.624  33.048  1.00132.73           O  
ANISOU 4650  OE2 GLU B 331    14991  22396  13047   2617   1854    551       O  
ATOM   4651  N   ALA B 332       5.179 -12.771  30.960  1.00128.25           N  
ANISOU 4651  N   ALA B 332    15062  21015  12651   2474    631    759       N  
ATOM   4652  CA  ALA B 332       4.405 -11.888  30.091  1.00115.27           C  
ANISOU 4652  CA  ALA B 332    13872  19018  10908   2446    487    462       C  
ATOM   4653  C   ALA B 332       3.129 -11.429  30.785  1.00109.85           C  
ANISOU 4653  C   ALA B 332    12724  18848  10164   2546    359    763       C  
ATOM   4654  O   ALA B 332       2.704 -10.278  30.638  1.00 99.36           O  
ANISOU 4654  O   ALA B 332    11562  17613   8577   2626    414    454       O  
ATOM   4655  CB  ALA B 332       4.079 -12.586  28.775  1.00132.57           C  
ANISOU 4655  CB  ALA B 332    16603  20345  13424   2241    176    494       C  
ATOM   4656  N   LEU B 333       2.521 -12.316  31.572  1.00114.15           N  
ANISOU 4656  N   LEU B 333    12680  19746  10948   2548    201   1371       N  
ATOM   4657  CA  LEU B 333       1.294 -12.030  32.300  1.00117.43           C  
ANISOU 4657  CA  LEU B 333    12598  20671  11349   2639     73   1727       C  
ATOM   4658  C   LEU B 333       1.765 -11.799  33.731  1.00146.74           C  
ANISOU 4658  C   LEU B 333    15696  25232  14827   2806    375   1831       C  
ATOM   4659  O   LEU B 333       1.698 -12.679  34.585  1.00163.15           O  
ANISOU 4659  O   LEU B 333    17226  27686  17078   2815    337   2320       O  
ATOM   4660  CB  LEU B 333       0.335 -13.215  32.188  1.00106.08           C  
ANISOU 4660  CB  LEU B 333    10932  19034  10338   2513   -309   2335       C  
ATOM   4661  CG  LEU B 333      -1.185 -13.113  32.231  1.00106.56           C  
ANISOU 4661  CG  LEU B 333    10765  19199  10525   2512   -608   2692       C  
ATOM   4662  CD1 LEU B 333      -1.773 -14.462  31.840  1.00111.34           C  
ANISOU 4662  CD1 LEU B 333    11317  19410  11579   2330   -973   3205       C  
ATOM   4663  CD2 LEU B 333      -1.658 -12.697  33.592  1.00109.45           C  
ANISOU 4663  CD2 LEU B 333    10437  20429  10719   2694   -472   2952       C  
ATOM   4664  N   GLU B 334       2.195 -10.563  34.004  1.00148.20           N  
ANISOU 4664  N   GLU B 334    15974  25734  14604   2937    676   1368       N  
ATOM   4665  CA  GLU B 334       2.841 -10.268  35.278  1.00159.03           C  
ANISOU 4665  CA  GLU B 334    16850  27869  15706   3077   1001   1375       C  
ATOM   4666  C   GLU B 334       1.827 -10.276  36.409  1.00188.21           C  
ANISOU 4666  C   GLU B 334    19858  32248  19404   3180    940   1853       C  
ATOM   4667  O   GLU B 334       1.858 -11.170  37.262  1.00200.67           O  
ANISOU 4667  O   GLU B 334    20899  34202  21144   3182    913   2325       O  
ATOM   4668  CB  GLU B 334       3.558  -8.913  35.214  1.00148.91           C  
ANISOU 4668  CB  GLU B 334    15891  26713  13976   3173   1338    731       C  
ATOM   4669  CG  GLU B 334       4.756  -8.869  34.271  1.00148.34           C  
ANISOU 4669  CG  GLU B 334    16391  26125  13844   3093   1488    255       C  
ATOM   4670  CD  GLU B 334       5.389  -7.492  34.185  1.00157.13           C  
ANISOU 4670  CD  GLU B 334    18024  27089  14591   3145   1692   -405       C  
ATOM   4671  OE1 GLU B 334       4.798  -6.521  34.703  1.00160.00           O  
ANISOU 4671  OE1 GLU B 334    18554  27385  14853   3104   1918   -768       O  
ATOM   4672  OE2 GLU B 334       6.480  -7.381  33.589  1.00167.91           O  
ANISOU 4672  OE2 GLU B 334    19647  28220  15933   3152   1542   -523       O  
ATOM   4673  N   GLN B 335       0.939  -9.276  36.445  1.00182.96           N  
ANISOU 4673  N   GLN B 335    19198  31758  18559   3272    929   1737       N  
ATOM   4674  CA  GLN B 335      -0.187  -9.325  37.373  1.00187.57           C  
ANISOU 4674  CA  GLN B 335    19171  32903  19194   3359    826   2217       C  
ATOM   4675  C   GLN B 335      -1.468  -8.791  36.756  1.00183.55           C  
ANISOU 4675  C   GLN B 335    18847  32144  18751   3365    588   2236       C  
ATOM   4676  O   GLN B 335      -2.328  -8.270  37.476  1.00175.34           O  
ANISOU 4676  O   GLN B 335    17412  31607  17603   3487    610   2421       O  
ATOM   4677  CB  GLN B 335       0.087  -8.582  38.665  1.00186.83           C  
ANISOU 4677  CB  GLN B 335    18614  33640  18733   3526   1165   2156       C  
ATOM   4678  CG  GLN B 335       0.776  -9.464  39.640  1.00177.40           C  
ANISOU 4678  CG  GLN B 335    16920  32884  17600   3521   1273   2486       C  
ATOM   4679  CD  GLN B 335      -0.162  -9.862  40.733  1.00174.27           C  
ANISOU 4679  CD  GLN B 335    15984  32913  17316   3524   1116   3041       C  
ATOM   4680  OE1 GLN B 335      -0.996  -9.069  41.163  1.00170.97           O  
ANISOU 4680  OE1 GLN B 335    15557  32659  16745   3564   1084   3028       O  
ATOM   4681  NE2 GLN B 335      -0.051 -11.105  41.186  1.00175.29           N  
ANISOU 4681  NE2 GLN B 335    15851  33037  17714   3413    987   3503       N  
ATOM   4682  N   GLY B 336      -1.619  -8.915  35.444  1.00176.40           N  
ANISOU 4682  N   GLY B 336    18529  30475  18021   3234    364   2057       N  
ATOM   4683  CA  GLY B 336      -2.746  -8.306  34.773  1.00188.55           C  
ANISOU 4683  CA  GLY B 336    20302  31746  19592   3236    153   2015       C  
ATOM   4684  C   GLY B 336      -2.421  -6.837  34.631  1.00200.54           C  
ANISOU 4684  C   GLY B 336    22149  33351  20695   3361    439   1416       C  
ATOM   4685  O   GLY B 336      -3.234  -5.965  34.942  1.00198.62           O  
ANISOU 4685  O   GLY B 336    21758  33416  20294   3486    475   1403       O  
ATOM   4686  N   GLN B 337      -1.212  -6.576  34.149  1.00205.72           N  
ANISOU 4686  N   GLN B 337    23261  33724  21180   3324    648    920       N  
ATOM   4687  CA  GLN B 337      -0.641  -5.232  34.084  1.00209.44           C  
ANISOU 4687  CA  GLN B 337    24049  34300  21227   3433    971    313       C  
ATOM   4688  C   GLN B 337       0.087  -5.126  32.746  1.00209.58           C  
ANISOU 4688  C   GLN B 337    24832  33544  21253   3306    946   -170       C  
ATOM   4689  O   GLN B 337      -0.233  -5.854  31.798  1.00215.23           O  
ANISOU 4689  O   GLN B 337    25850  33641  22288   3150    636    -31       O  
ATOM   4690  CB  GLN B 337       0.223  -4.967  35.329  1.00210.07           C  
ANISOU 4690  CB  GLN B 337    23710  35098  21009   3553   1349    244       C  
ATOM   4691  CG  GLN B 337      -0.304  -3.819  36.191  1.00213.44           C  
ANISOU 4691  CG  GLN B 337    23865  35988  21245   3678   1484    170       C  
ATOM   4692  CD  GLN B 337       0.506  -3.597  37.457  1.00215.82           C  
ANISOU 4692  CD  GLN B 337    23891  36402  21707   3570   1532    173       C  
ATOM   4693  OE1 GLN B 337      -0.041  -3.276  38.511  1.00213.45           O  
ANISOU 4693  OE1 GLN B 337    23802  35797  21500   3431   1601    -47       O  
ATOM   4694  NE2 GLN B 337       1.827  -3.699  37.334  1.00220.00           N  
ANISOU 4694  NE2 GLN B 337    23969  37378  22245   3630   1475    457       N  
ATOM   4695  N   SER B 338       1.046  -4.198  32.644  1.00219.93           N  
ANISOU 4695  N   SER B 338    26475  34880  22207   3365   1270   -746       N  
ATOM   4696  CA  SER B 338       1.714  -3.914  31.373  1.00203.78           C  
ANISOU 4696  CA  SER B 338    25182  32122  20122   3260   1275  -1260       C  
ATOM   4697  C   SER B 338       0.719  -3.318  30.384  1.00210.65           C  
ANISOU 4697  C   SER B 338    26468  32529  21041   3232   1043  -1390       C  
ATOM   4698  O   SER B 338       0.227  -4.011  29.489  1.00207.11           O  
ANISOU 4698  O   SER B 338    26274  31503  20913   3082    710  -1205       O  
ATOM   4699  CB  SER B 338       2.385  -5.162  30.786  1.00186.60           C  
ANISOU 4699  CB  SER B 338    23204  29438  18259   3085   1131  -1134       C  
ATOM   4700  OG  SER B 338       3.441  -5.618  31.611  1.00170.52           O  
ANISOU 4700  OG  SER B 338    20781  27825  16186   3114   1346  -1006       O  
ATOM   4701  N   LEU B 339       0.403  -2.031  30.578  1.00216.26           N  
ANISOU 4701  N   LEU B 339    27224  33424  21522   3333   1197  -1665       N  
ATOM   4702  CA  LEU B 339      -0.630  -1.334  29.810  1.00226.52           C  
ANISOU 4702  CA  LEU B 339    28840  34485  22743   3385   1029  -1788       C  
ATOM   4703  C   LEU B 339      -0.498  -1.497  28.299  1.00231.43           C  
ANISOU 4703  C   LEU B 339    30183  34231  23520   3210    811  -2055       C  
ATOM   4704  O   LEU B 339      -1.505  -1.423  27.585  1.00234.26           O  
ANISOU 4704  O   LEU B 339    30731  34232  24045   3156    518  -1934       O  
ATOM   4705  CB  LEU B 339      -0.610   0.153  30.159  1.00229.75           C  
ANISOU 4705  CB  LEU B 339    29253  34683  23360   3250   1183  -1990       C  
ATOM   4706  CG  LEU B 339      -0.904   0.516  31.614  1.00233.31           C  
ANISOU 4706  CG  LEU B 339    29057  35771  23817   3351   1308  -1721       C  
ATOM   4707  CD1 LEU B 339      -1.122   2.012  31.746  1.00234.14           C  
ANISOU 4707  CD1 LEU B 339    29296  35603  24063   3240   1389  -1913       C  
ATOM   4708  CD2 LEU B 339      -2.109  -0.252  32.135  1.00235.27           C  
ANISOU 4708  CD2 LEU B 339    28769  36818  23805   3642   1198  -1246       C  
ATOM   4709  N   GLY B 340       0.709  -1.708  27.783  1.00233.76           N  
ANISOU 4709  N   GLY B 340    30864  34078  23878   3054    926  -2365       N  
ATOM   4710  CA  GLY B 340       0.840  -1.920  26.364  1.00215.92           C  
ANISOU 4710  CA  GLY B 340    29296  31047  21695   2917    734  -2633       C  
ATOM   4711  C   GLY B 340       0.414  -3.344  26.082  1.00208.90           C  
ANISOU 4711  C   GLY B 340    28290  29866  21215   2771    385  -2129       C  
ATOM   4712  O   GLY B 340       0.689  -4.257  26.865  1.00216.90           O  
ANISOU 4712  O   GLY B 340    28834  31201  22376   2769    407  -1756       O  
ATOM   4713  N   PRO B 341      -0.263  -3.564  24.955  1.00213.82           N  
ANISOU 4713  N   PRO B 341    29331  29850  22059   2621     52  -2089       N  
ATOM   4714  CA  PRO B 341      -0.780  -4.909  24.659  1.00205.50           C  
ANISOU 4714  CA  PRO B 341    28165  28483  21434   2447   -306  -1574       C  
ATOM   4715  C   PRO B 341       0.343  -5.929  24.631  1.00199.65           C  
ANISOU 4715  C   PRO B 341    27486  27541  20831   2340   -221  -1561       C  
ATOM   4716  O   PRO B 341       1.319  -5.787  23.890  1.00198.12           O  
ANISOU 4716  O   PRO B 341    27834  26899  20543   2266    -86  -2015       O  
ATOM   4717  CB  PRO B 341      -1.436  -4.740  23.284  1.00207.02           C  
ANISOU 4717  CB  PRO B 341    28959  27949  21751   2291   -614  -1708       C  
ATOM   4718  CG  PRO B 341      -1.792  -3.293  23.208  1.00208.97           C  
ANISOU 4718  CG  PRO B 341    29368  28354  21678   2438   -479  -2078       C  
ATOM   4719  CD  PRO B 341      -0.732  -2.558  23.985  1.00211.09           C  
ANISOU 4719  CD  PRO B 341    29524  29101  21580   2610    -26  -2463       C  
ATOM   4720  N   VAL B 342       0.195  -6.969  25.451  1.00213.58           N  
ANISOU 4720  N   VAL B 342    28684  29642  22825   2336   -297  -1026       N  
ATOM   4721  CA  VAL B 342       1.233  -7.984  25.540  1.00194.27           C  
ANISOU 4721  CA  VAL B 342    26225  27062  20527   2252   -207   -958       C  
ATOM   4722  C   VAL B 342       1.280  -8.751  24.230  1.00202.62           C  
ANISOU 4722  C   VAL B 342    27862  27257  21869   2015   -470   -987       C  
ATOM   4723  O   VAL B 342       0.247  -9.186  23.704  1.00201.44           O  
ANISOU 4723  O   VAL B 342    27773  26793  21972   1891   -829   -679       O  
ATOM   4724  CB  VAL B 342       0.974  -8.922  26.726  1.00154.84           C  
ANISOU 4724  CB  VAL B 342    20478  22633  15723   2302   -245   -349       C  
ATOM   4725  CG1 VAL B 342       2.090  -9.945  26.840  1.00131.50           C  
ANISOU 4725  CG1 VAL B 342    17501  19549  12913   2229   -131   -282       C  
ATOM   4726  CG2 VAL B 342       0.843  -8.120  28.010  1.00141.09           C  
ANISOU 4726  CG2 VAL B 342    18173  21746  13688   2528      8   -317       C  
ATOM   4727  N   GLU B 343       2.475  -8.908  23.694  1.00198.37           N  
ANISOU 4727  N   GLU B 343    27756  26330  21284   1947   -292  -1359       N  
ATOM   4728  CA  GLU B 343       2.625  -9.598  22.429  1.00197.89           C  
ANISOU 4728  CA  GLU B 343    28291  25431  21470   1720   -504  -1436       C  
ATOM   4729  C   GLU B 343       2.551 -11.100  22.659  1.00198.36           C  
ANISOU 4729  C   GLU B 343    28052  25401  21916   1603   -686   -889       C  
ATOM   4730  O   GLU B 343       3.330 -11.633  23.460  1.00200.74           O  
ANISOU 4730  O   GLU B 343    27987  26048  22236   1673   -480   -751       O  
ATOM   4731  CB  GLU B 343       3.932  -9.189  21.777  1.00197.49           C  
ANISOU 4731  CB  GLU B 343    28814  25001  21225   1696   -230  -2041       C  
ATOM   4732  CG  GLU B 343       4.074  -7.668  21.750  1.00201.39           C  
ANISOU 4732  CG  GLU B 343    29520  25696  21304   1838     -3  -2571       C  
ATOM   4733  CD  GLU B 343       3.175  -6.970  20.731  1.00208.09           C  
ANISOU 4733  CD  GLU B 343    30846  26098  22122   1761   -241  -2765       C  
ATOM   4734  OE1 GLU B 343       2.148  -7.542  20.315  1.00214.08           O  
ANISOU 4734  OE1 GLU B 343    31600  26585  23157   1634   -605  -2392       O  
ATOM   4735  OE2 GLU B 343       3.469  -5.812  20.376  1.00209.41           O  
ANISOU 4735  OE2 GLU B 343    31378  26211  21977   1831    -63  -3283       O  
ATOM   4736  N   PRO B 344       1.645 -11.811  21.994  1.00194.71           N  
ANISOU 4736  N   PRO B 344    27729  24491  21763   1422  -1067   -563       N  
ATOM   4737  CA  PRO B 344       1.533 -13.255  22.216  1.00189.28           C  
ANISOU 4737  CA  PRO B 344    26759  23712  21447   1304  -1245    -29       C  
ATOM   4738  C   PRO B 344       2.799 -13.982  21.793  1.00182.56           C  
ANISOU 4738  C   PRO B 344    26240  22429  20696   1211  -1081   -213       C  
ATOM   4739  O   PRO B 344       3.509 -13.565  20.876  1.00183.47           O  
ANISOU 4739  O   PRO B 344    26984  22037  20690   1146   -967   -722       O  
ATOM   4740  CB  PRO B 344       0.333 -13.656  21.348  1.00187.77           C  
ANISOU 4740  CB  PRO B 344    26808  23023  21514   1104  -1683    234       C  
ATOM   4741  CG  PRO B 344       0.220 -12.568  20.326  1.00184.73           C  
ANISOU 4741  CG  PRO B 344    27051  22225  20913   1068  -1702   -288       C  
ATOM   4742  CD  PRO B 344       0.661 -11.317  21.017  1.00183.83           C  
ANISOU 4742  CD  PRO B 344    26766  22677  20403   1312  -1355   -659       C  
ATOM   4743  N   LEU B 345       3.071 -15.087  22.475  1.00177.25           N  
ANISOU 4743  N   LEU B 345    25134  21960  20253   1207  -1068    217       N  
ATOM   4744  CA  LEU B 345       4.223 -15.930  22.205  1.00169.30           C  
ANISOU 4744  CA  LEU B 345    24345  20593  19388   1131   -916    141       C  
ATOM   4745  C   LEU B 345       3.755 -17.263  21.632  1.00162.99           C  
ANISOU 4745  C   LEU B 345    23667  19253  19008    907  -1235    560       C  
ATOM   4746  O   LEU B 345       2.572 -17.605  21.687  1.00138.49           O  
ANISOU 4746  O   LEU B 345    20343  16192  16086    833  -1556    977       O  
ATOM   4747  CB  LEU B 345       5.064 -16.131  23.467  1.00169.78           C  
ANISOU 4747  CB  LEU B 345    23822  21321  19364   1312   -604    274       C  
ATOM   4748  CG  LEU B 345       5.544 -14.791  24.024  1.00161.15           C  
ANISOU 4748  CG  LEU B 345    22632  20759  17838   1517   -282   -156       C  
ATOM   4749  CD1 LEU B 345       6.393 -15.022  25.251  1.00143.75           C  
ANISOU 4749  CD1 LEU B 345    19863  19207  15550   1675     17    -15       C  
ATOM   4750  CD2 LEU B 345       6.311 -14.009  22.960  1.00165.55           C  
ANISOU 4750  CD2 LEU B 345    23934  20782  18185   1471   -125   -828       C  
ATOM   4751  N   ASP B 346       4.698 -18.009  21.064  1.00159.77           N  
ANISOU 4751  N   ASP B 346    23625  18327  18755    796  -1140    441       N  
ATOM   4752  CA  ASP B 346       4.382 -19.271  20.410  1.00173.36           C  
ANISOU 4752  CA  ASP B 346    25554  19452  20862    568  -1412    777       C  
ATOM   4753  C   ASP B 346       4.237 -20.402  21.429  1.00170.50           C  
ANISOU 4753  C   ASP B 346    24522  19499  20763    604  -1456   1402       C  
ATOM   4754  O   ASP B 346       4.547 -20.264  22.617  1.00182.14           O  
ANISOU 4754  O   ASP B 346    25398  21686  22121    802  -1248   1548       O  
ATOM   4755  CB  ASP B 346       5.464 -19.625  19.385  1.00183.69           C  
ANISOU 4755  CB  ASP B 346    27537  20022  22234    437  -1274    397       C  
ATOM   4756  CG  ASP B 346       5.609 -18.579  18.280  1.00190.54           C  
ANISOU 4756  CG  ASP B 346    29118  20417  22861    376  -1247   -219       C  
ATOM   4757  OD1 ASP B 346       4.736 -18.512  17.385  1.00192.04           O  
ANISOU 4757  OD1 ASP B 346    29695  20141  23130    200  -1555   -223       O  
ATOM   4758  OD2 ASP B 346       6.590 -17.806  18.322  1.00190.80           O  
ANISOU 4758  OD2 ASP B 346    29316  20559  22620    503   -920   -695       O  
ATOM   4759  N   GLY B 347       3.747 -21.539  20.942  1.00172.79           N  
ANISOU 4759  N   GLY B 347    24926  19318  21407    398  -1737   1775       N  
ATOM   4760  CA  GLY B 347       3.597 -22.722  21.753  1.00159.23           C  
ANISOU 4760  CA  GLY B 347    22652  17871  19977    397  -1806   2373       C  
ATOM   4761  C   GLY B 347       2.359 -22.707  22.625  1.00140.20           C  
ANISOU 4761  C   GLY B 347    19601  16061  17607    459  -2032   2865       C  
ATOM   4762  O   GLY B 347       1.462 -21.869  22.474  1.00140.51           O  
ANISOU 4762  O   GLY B 347    19667  16223  17499    471  -2191   2786       O  
ATOM   4763  N   PRO B 348       2.289 -23.661  23.555  1.00137.77           N  
ANISOU 4763  N   PRO B 348    18702  16132  17512    500  -2048   3397       N  
ATOM   4764  CA  PRO B 348       1.116 -23.755  24.441  1.00125.68           C  
ANISOU 4764  CA  PRO B 348    16523  15184  16044    555  -2261   3911       C  
ATOM   4765  C   PRO B 348       0.921 -22.553  25.351  1.00124.45           C  
ANISOU 4765  C   PRO B 348    15942  15801  15544    794  -2094   3776       C  
ATOM   4766  O   PRO B 348      -0.194 -22.355  25.852  1.00125.47           O  
ANISOU 4766  O   PRO B 348    15664  16331  15679    830  -2291   4098       O  
ATOM   4767  CB  PRO B 348       1.395 -25.029  25.247  1.00120.01           C  
ANISOU 4767  CB  PRO B 348    15307  14690  15602    563  -2235   4434       C  
ATOM   4768  CG  PRO B 348       2.342 -25.824  24.379  1.00121.03           C  
ANISOU 4768  CG  PRO B 348    15977  14088  15920    416  -2157   4267       C  
ATOM   4769  CD  PRO B 348       3.207 -24.800  23.720  1.00124.46           C  
ANISOU 4769  CD  PRO B 348    16959  14271  16058    468  -1907   3581       C  
ATOM   4770  N   ALA B 349       1.965 -21.761  25.601  1.00126.05           N  
ANISOU 4770  N   ALA B 349    16214  16232  15447    956  -1731   3321       N  
ATOM   4771  CA  ALA B 349       1.796 -20.547  26.394  1.00121.93           C  
ANISOU 4771  CA  ALA B 349    15352  16405  14573   1171  -1559   3143       C  
ATOM   4772  C   ALA B 349       0.882 -19.558  25.682  1.00127.84           C  
ANISOU 4772  C   ALA B 349    16445  16955  15173   1133  -1743   2893       C  
ATOM   4773  O   ALA B 349      -0.051 -19.009  26.282  1.00125.06           O  
ANISOU 4773  O   ALA B 349    15694  17103  14720   1232  -1835   3080       O  
ATOM   4774  CB  ALA B 349       3.158 -19.913  26.675  1.00125.06           C  
ANISOU 4774  CB  ALA B 349    15835  17004  14676   1323  -1137   2670       C  
ATOM   4775  N   GLY B 350       1.141 -19.317  24.393  1.00140.73           N  
ANISOU 4775  N   GLY B 350    18823  17856  16792    989  -1796   2472       N  
ATOM   4776  CA  GLY B 350       0.240 -18.499  23.601  1.00127.53           C  
ANISOU 4776  CA  GLY B 350    17519  15914  15022    921  -2010   2268       C  
ATOM   4777  C   GLY B 350      -1.110 -19.146  23.373  1.00125.85           C  
ANISOU 4777  C   GLY B 350    17176  15543  15099    763  -2437   2773       C  
ATOM   4778  O   GLY B 350      -2.118 -18.448  23.242  1.00125.08           O  
ANISOU 4778  O   GLY B 350    17055  15553  14915    776  -2618   2790       O  
ATOM   4779  N   ALA B 351      -1.153 -20.479  23.313  1.00112.28           N  
ANISOU 4779  N   ALA B 351    15374  13562  13726    610  -2603   3193       N  
ATOM   4780  CA  ALA B 351      -2.437 -21.167  23.231  1.00120.75           C  
ANISOU 4780  CA  ALA B 351    16245  14554  15080    460  -3005   3727       C  
ATOM   4781  C   ALA B 351      -3.287 -20.911  24.471  1.00131.78           C  
ANISOU 4781  C   ALA B 351    16867  16779  16425    635  -3040   4135       C  
ATOM   4782  O   ALA B 351      -4.520 -20.891  24.386  1.00126.60           O  
ANISOU 4782  O   ALA B 351    16066  16166  15873    567  -3349   4439       O  
ATOM   4783  CB  ALA B 351      -2.219 -22.666  23.026  1.00124.35           C  
ANISOU 4783  CB  ALA B 351    16734  14607  15905    274  -3136   4097       C  
ATOM   4784  N   VAL B 352      -2.645 -20.722  25.626  1.00141.79           N  
ANISOU 4784  N   VAL B 352    17631  18709  17535    855  -2727   4152       N  
ATOM   4785  CA  VAL B 352      -3.352 -20.315  26.837  1.00135.87           C  
ANISOU 4785  CA  VAL B 352    16166  18780  16677   1043  -2704   4463       C  
ATOM   4786  C   VAL B 352      -3.692 -18.831  26.798  1.00136.99           C  
ANISOU 4786  C   VAL B 352    16408  19167  16475   1187  -2607   4073       C  
ATOM   4787  O   VAL B 352      -4.809 -18.431  27.144  1.00131.64           O  
ANISOU 4787  O   VAL B 352    15410  18827  15780   1240  -2774   4315       O  
ATOM   4788  CB  VAL B 352      -2.511 -20.665  28.079  1.00120.69           C  
ANISOU 4788  CB  VAL B 352    13686  17470  14701   1212  -2401   4621       C  
ATOM   4789  CG1 VAL B 352      -2.988 -19.881  29.294  1.00118.58           C  
ANISOU 4789  CG1 VAL B 352    12783  18071  14201   1439  -2273   4749       C  
ATOM   4790  CG2 VAL B 352      -2.591 -22.141  28.359  1.00114.12           C  
ANISOU 4790  CG2 VAL B 352    12564  16555  14240   1092  -2562   5176       C  
ATOM   4791  N   LEU B 353      -2.746 -18.000  26.354  1.00146.69           N  
ANISOU 4791  N   LEU B 353    18091  20213  17431   1249  -2337   3466       N  
ATOM   4792  CA  LEU B 353      -2.949 -16.555  26.371  1.00142.60           C  
ANISOU 4792  CA  LEU B 353    17669  19949  16563   1400  -2200   3063       C  
ATOM   4793  C   LEU B 353      -4.086 -16.127  25.451  1.00150.53           C  
ANISOU 4793  C   LEU B 353    19014  20561  17620   1284  -2525   3045       C  
ATOM   4794  O   LEU B 353      -4.734 -15.104  25.700  1.00121.85           O  
ANISOU 4794  O   LEU B 353    15245  17272  13781   1417  -2507   2950       O  
ATOM   4795  CB  LEU B 353      -1.648 -15.849  25.990  1.00124.10           C  
ANISOU 4795  CB  LEU B 353    15793  17419  13940   1463  -1856   2416       C  
ATOM   4796  CG  LEU B 353      -1.623 -14.329  26.129  1.00113.57           C  
ANISOU 4796  CG  LEU B 353    14547  16401  12206   1641  -1637   1952       C  
ATOM   4797  CD1 LEU B 353      -2.178 -13.909  27.480  1.00109.61           C  
ANISOU 4797  CD1 LEU B 353    13310  16774  11565   1849  -1535   2241       C  
ATOM   4798  CD2 LEU B 353      -0.210 -13.812  25.946  1.00120.41           C  
ANISOU 4798  CD2 LEU B 353    15775  17162  12813   1704  -1270   1378       C  
ATOM   4799  N   GLU B 354      -4.340 -16.890  24.385  1.00151.54           N  
ANISOU 4799  N   GLU B 354    19587  19971  18019   1035  -2819   3137       N  
ATOM   4800  CA  GLU B 354      -5.462 -16.594  23.502  1.00161.22           C  
ANISOU 4800  CA  GLU B 354    21119  20816  19322    898  -3162   3175       C  
ATOM   4801  C   GLU B 354      -6.806 -16.747  24.202  1.00155.76           C  
ANISOU 4801  C   GLU B 354    19820  20599  18765    938  -3409   3741       C  
ATOM   4802  O   GLU B 354      -7.794 -16.146  23.763  1.00155.64           O  
ANISOU 4802  O   GLU B 354    19914  20500  18723    912  -3623   3750       O  
ATOM   4803  CB  GLU B 354      -5.421 -17.501  22.269  1.00172.94           C  
ANISOU 4803  CB  GLU B 354    23184  21444  21081    601  -3428   3195       C  
ATOM   4804  CG  GLU B 354      -4.329 -17.159  21.258  1.00177.88           C  
ANISOU 4804  CG  GLU B 354    24557  21464  21567    528  -3249   2578       C  
ATOM   4805  CD  GLU B 354      -4.259 -18.160  20.113  1.00181.70           C  
ANISOU 4805  CD  GLU B 354    25586  21115  22334    228  -3495   2632       C  
ATOM   4806  OE1 GLU B 354      -5.329 -18.603  19.645  1.00185.97           O  
ANISOU 4806  OE1 GLU B 354    26170  21396  23094     46  -3875   2971       O  
ATOM   4807  OE2 GLU B 354      -3.136 -18.511  19.688  1.00180.72           O  
ANISOU 4807  OE2 GLU B 354    25848  20600  22216    171  -3306   2341       O  
ATOM   4808  N   CYS B 355      -6.871 -17.543  25.271  1.00154.21           N  
ANISOU 4808  N   CYS B 355    18985  20893  18715   1000  -3385   4221       N  
ATOM   4809  CA  CYS B 355      -8.127 -17.755  25.976  1.00144.47           C  
ANISOU 4809  CA  CYS B 355    17150  20121  17621   1035  -3613   4782       C  
ATOM   4810  C   CYS B 355      -8.497 -16.599  26.899  1.00136.71           C  
ANISOU 4810  C   CYS B 355    15728  19868  16347   1303  -3414   4711       C  
ATOM   4811  O   CYS B 355      -9.684 -16.415  27.190  1.00143.84           O  
ANISOU 4811  O   CYS B 355    16288  21051  17313   1334  -3619   5051       O  
ATOM   4812  CB  CYS B 355      -8.049 -19.044  26.800  1.00152.94           C  
ANISOU 4812  CB  CYS B 355    17697  21455  18957   1002  -3655   5327       C  
ATOM   4813  SG  CYS B 355      -7.920 -20.575  25.840  1.00160.12           S  
ANISOU 4813  SG  CYS B 355    19006  21558  20274    674  -3949   5573       S  
ATOM   4814  N   LEU B 356      -7.523 -15.814  27.354  1.00140.51           N  
ANISOU 4814  N   LEU B 356    16219  20658  16509   1491  -3019   4279       N  
ATOM   4815  CA  LEU B 356      -7.763 -14.770  28.343  1.00137.25           C  
ANISOU 4815  CA  LEU B 356    15364  20977  15806   1748  -2786   4213       C  
ATOM   4816  C   LEU B 356      -7.842 -13.378  27.739  1.00146.48           C  
ANISOU 4816  C   LEU B 356    16967  22008  16679   1831  -2685   3681       C  
ATOM   4817  O   LEU B 356      -8.039 -12.406  28.476  1.00153.24           O  
ANISOU 4817  O   LEU B 356    17522  23430  17273   2045  -2477   3573       O  
ATOM   4818  CB  LEU B 356      -6.672 -14.799  29.416  1.00118.63           C  
ANISOU 4818  CB  LEU B 356    12647  19156  13271   1912  -2400   4128       C  
ATOM   4819  CG  LEU B 356      -6.565 -16.106  30.197  1.00112.72           C  
ANISOU 4819  CG  LEU B 356    11386  18656  12788   1867  -2457   4670       C  
ATOM   4820  CD1 LEU B 356      -5.339 -16.088  31.090  1.00112.65           C  
ANISOU 4820  CD1 LEU B 356    11127  19089  12586   2009  -2067   4512       C  
ATOM   4821  CD2 LEU B 356      -7.830 -16.334  31.008  1.00114.65           C  
ANISOU 4821  CD2 LEU B 356    10984  19408  13168   1919  -2657   5251       C  
ATOM   4822  N   VAL B 357      -7.716 -13.254  26.424  1.00158.08           N  
ANISOU 4822  N   VAL B 357    19137  22742  18183   1665  -2827   3352       N  
ATOM   4823  CA  VAL B 357      -7.728 -11.941  25.799  1.00161.82           C  
ANISOU 4823  CA  VAL B 357    20060  23049  18375   1738  -2726   2826       C  
ATOM   4824  C   VAL B 357      -8.890 -11.869  24.826  1.00169.38           C  
ANISOU 4824  C   VAL B 357    21307  23549  19499   1584  -3121   2959       C  
ATOM   4825  O   VAL B 357      -9.609 -12.854  24.620  1.00170.83           O  
ANISOU 4825  O   VAL B 357    21367  23531  20009   1412  -3461   3435       O  
ATOM   4826  CB  VAL B 357      -6.393 -11.648  25.096  1.00162.89           C  
ANISOU 4826  CB  VAL B 357    20820  22740  18332   1698  -2484   2214       C  
ATOM   4827  CG1 VAL B 357      -5.248 -11.762  26.083  1.00153.09           C  
ANISOU 4827  CG1 VAL B 357    19262  21971  16936   1842  -2105   2117       C  
ATOM   4828  CG2 VAL B 357      -6.201 -12.600  23.935  1.00172.93           C  
ANISOU 4828  CG2 VAL B 357    22621  23204  19880   1421  -2740   2230       C  
ATOM   4829  N   LEU B 358      -9.079 -10.705  24.227  1.00174.83           N  
ANISOU 4829  N   LEU B 358    22384  24077  19965   1642  -3078   2544       N  
ATOM   4830  CA  LEU B 358     -10.165 -10.452  23.302  1.00184.80           C  
ANISOU 4830  CA  LEU B 358    23936  24938  21343   1517  -3427   2622       C  
ATOM   4831  C   LEU B 358      -9.618 -10.411  21.876  1.00216.13           C  
ANISOU 4831  C   LEU B 358    28737  28074  25307   1313  -3514   2178       C  
ATOM   4832  O   LEU B 358      -8.439 -10.693  21.636  1.00221.55           O  
ANISOU 4832  O   LEU B 358    29743  28498  25939   1264  -3318   1861       O  
ATOM   4833  CB  LEU B 358     -10.868  -9.159  23.716  1.00160.50           C  
ANISOU 4833  CB  LEU B 358    20643  22314  18024   1742  -3321   2521       C  
ATOM   4834  CG  LEU B 358     -11.701  -9.339  24.990  1.00149.14           C  
ANISOU 4834  CG  LEU B 358    18386  21621  16660   1897  -3333   3064       C  
ATOM   4835  CD1 LEU B 358     -12.330  -8.034  25.453  1.00142.97           C  
ANISOU 4835  CD1 LEU B 358    17389  21307  15627   2137  -3183   2945       C  
ATOM   4836  CD2 LEU B 358     -12.758 -10.421  24.802  1.00157.07           C  
ANISOU 4836  CD2 LEU B 358    19163  22461  18054   1706  -3773   3686       C  
ATOM   4837  N   SER B 359     -10.489 -10.077  20.920  1.00201.28           N  
ANISOU 4837  N   SER B 359    27209  25774  23493   1189  -3814   2169       N  
ATOM   4838  CA  SER B 359     -10.059  -9.968  19.529  1.00212.70           C  
ANISOU 4838  CA  SER B 359    29465  26428  24925    988  -3912   1746       C  
ATOM   4839  C   SER B 359      -8.959  -8.924  19.363  1.00221.94           C  
ANISOU 4839  C   SER B 359    31030  27562  25734   1128  -3523   1062       C  
ATOM   4840  O   SER B 359      -8.000  -9.134  18.610  1.00225.76           O  
ANISOU 4840  O   SER B 359    32066  27522  26190    999  -3441    690       O  
ATOM   4841  CB  SER B 359     -11.256  -9.631  18.639  1.00218.04           C  
ANISOU 4841  CB  SER B 359    30393  26755  25696    859  -4286   1859       C  
ATOM   4842  OG  SER B 359     -11.601  -8.260  18.742  1.00219.20           O  
ANISOU 4842  OG  SER B 359    30542  27174  25569   1064  -4145   1582       O  
ATOM   4843  N   SER B 360      -9.077  -7.797  20.071  1.00205.34           N  
ANISOU 4843  N   SER B 360    28653  26015  23352   1391  -3272    890       N  
ATOM   4844  CA  SER B 360      -8.077  -6.735  20.003  1.00211.84           C  
ANISOU 4844  CA  SER B 360    29812  26866  23811   1536  -2890    249       C  
ATOM   4845  C   SER B 360      -6.757  -7.121  20.665  1.00219.52           C  
ANISOU 4845  C   SER B 360    30656  28065  24689   1605  -2545     86       C  
ATOM   4846  O   SER B 360      -5.719  -6.549  20.317  1.00217.91           O  
ANISOU 4846  O   SER B 360    30880  27671  24244   1638  -2273   -465       O  
ATOM   4847  CB  SER B 360      -8.624  -5.449  20.631  1.00221.00           C  
ANISOU 4847  CB  SER B 360    30686  28580  24704   1796  -2716    143       C  
ATOM   4848  OG  SER B 360      -8.850  -5.603  22.021  1.00231.49           O  
ANISOU 4848  OG  SER B 360    31257  30675  26024   1983  -2571    510       O  
ATOM   4849  N   GLY B 361      -6.765  -8.083  21.588  1.00215.11           N  
ANISOU 4849  N   GLY B 361    29524  27894  24313   1622  -2553    554       N  
ATOM   4850  CA  GLY B 361      -5.595  -8.421  22.365  1.00216.95           C  
ANISOU 4850  CA  GLY B 361    29537  28440  24454   1710  -2223    459       C  
ATOM   4851  C   GLY B 361      -5.635  -7.890  23.777  1.00217.52           C  
ANISOU 4851  C   GLY B 361    28946  29382  24321   1974  -1946    574       C  
ATOM   4852  O   GLY B 361      -4.676  -8.104  24.528  1.00212.89           O  
ANISOU 4852  O   GLY B 361    28124  29131  23631   2062  -1657    506       O  
ATOM   4853  N   MET B 362      -6.700  -7.183  24.157  1.00223.84           N  
ANISOU 4853  N   MET B 362    29446  30554  25051   2103  -2016    737       N  
ATOM   4854  CA  MET B 362      -6.801  -6.682  25.524  1.00215.05           C  
ANISOU 4854  CA  MET B 362    27692  30275  23742   2350  -1753    865       C  
ATOM   4855  C   MET B 362      -7.053  -7.820  26.493  1.00208.79           C  
ANISOU 4855  C   MET B 362    26239  29897  23196   2342  -1842   1475       C  
ATOM   4856  O   MET B 362      -7.726  -8.803  26.173  1.00213.35           O  
ANISOU 4856  O   MET B 362    26740  30210  24115   2175  -2192   1919       O  
ATOM   4857  CB  MET B 362      -7.935  -5.665  25.677  1.00214.99           C  
ANISOU 4857  CB  MET B 362    27522  30547  23617   2493  -1807    913       C  
ATOM   4858  CG  MET B 362      -7.474  -4.225  25.796  1.00211.83           C  
ANISOU 4858  CG  MET B 362    27327  30357  22800   2685  -1451    349       C  
ATOM   4859  SD  MET B 362      -5.699  -4.087  25.470  1.00209.26           S  
ANISOU 4859  SD  MET B 362    27504  29766  22238   2652  -1104   -279       S  
ATOM   4860  CE  MET B 362      -5.120  -2.801  26.603  1.00209.31           C  
ANISOU 4860  CE  MET B 362    27231  30526  21772   2939   -595   -646       C  
ATOM   4861  N   LEU B 363      -6.545  -7.656  27.704  1.00210.91           N  
ANISOU 4861  N   LEU B 363    26019  30835  23281   2520  -1527   1502       N  
ATOM   4862  CA  LEU B 363      -6.692  -8.696  28.706  1.00187.61           C  
ANISOU 4862  CA  LEU B 363    22424  28324  20537   2526  -1576   2061       C  
ATOM   4863  C   LEU B 363      -7.936  -8.438  29.541  1.00168.25           C  
ANISOU 4863  C   LEU B 363    19372  26444  18111   2658  -1669   2493       C  
ATOM   4864  O   LEU B 363      -8.393  -7.300  29.681  1.00178.66           O  
ANISOU 4864  O   LEU B 363    20680  28006  19196   2811  -1553   2292       O  
ATOM   4865  CB  LEU B 363      -5.487  -8.781  29.648  1.00183.56           C  
ANISOU 4865  CB  LEU B 363    21645  28266  19833   2635  -1199   1926       C  
ATOM   4866  CG  LEU B 363      -5.036  -7.614  30.538  1.00180.98           C  
ANISOU 4866  CG  LEU B 363    21109  28566  19088   2869   -790   1595       C  
ATOM   4867  CD1 LEU B 363      -3.783  -8.014  31.297  1.00181.65           C  
ANISOU 4867  CD1 LEU B 363    20981  28972  19065   2908   -491   1524       C  
ATOM   4868  CD2 LEU B 363      -4.821  -6.290  29.807  1.00178.95           C  
ANISOU 4868  CD2 LEU B 363    21418  28050  18525   2928   -635    972       C  
ATOM   4869  N   VAL B 364      -8.478  -9.504  30.113  1.00151.57           N  
ANISOU 4869  N   VAL B 364    16753  24550  16287   2601  -1870   3094       N  
ATOM   4870  CA  VAL B 364      -9.631  -9.366  30.992  1.00143.23           C  
ANISOU 4870  CA  VAL B 364    15075  24070  15275   2725  -1952   3547       C  
ATOM   4871  C   VAL B 364      -9.161  -9.702  32.404  1.00160.10           C  
ANISOU 4871  C   VAL B 364    16572  26929  17329   2857  -1696   3779       C  
ATOM   4872  O   VAL B 364      -8.899 -10.877  32.704  1.00165.93           O  
ANISOU 4872  O   VAL B 364    17068  27673  18304   2755  -1792   4136       O  
ATOM   4873  CB  VAL B 364     -10.796 -10.265  30.557  1.00128.31           C  
ANISOU 4873  CB  VAL B 364    13073  21897  13780   2555  -2411   4092       C  
ATOM   4874  CG1 VAL B 364     -12.015 -10.003  31.432  1.00126.55           C  
ANISOU 4874  CG1 VAL B 364    12225  22271  13586   2697  -2482   4532       C  
ATOM   4875  CG2 VAL B 364     -11.134 -10.032  29.093  1.00125.51           C  
ANISOU 4875  CG2 VAL B 364    13398  20779  13513   2390  -2673   3852       C  
ATOM   4876  N   PRO B 365      -9.026  -8.714  33.295  1.00138.74           N  
ANISOU 4876  N   PRO B 365    13975  18575  20164  -1767   1114   3995       N  
ATOM   4877  CA  PRO B 365      -8.582  -9.020  34.665  1.00139.83           C  
ANISOU 4877  CA  PRO B 365    14230  18547  20353  -1672   1289   3874       C  
ATOM   4878  C   PRO B 365      -9.455 -10.039  35.369  1.00145.66           C  
ANISOU 4878  C   PRO B 365    14940  18878  21528  -1386   1513   4022       C  
ATOM   4879  O   PRO B 365      -8.947 -10.838  36.165  1.00147.40           O  
ANISOU 4879  O   PRO B 365    15258  19017  21730  -1346   1616   3898       O  
ATOM   4880  CB  PRO B 365      -8.643  -7.653  35.361  1.00135.93           C  
ANISOU 4880  CB  PRO B 365    13779  17999  19871  -1664   1382   3893       C  
ATOM   4881  CG  PRO B 365      -8.458  -6.671  34.264  1.00129.37           C  
ANISOU 4881  CG  PRO B 365    12904  17470  18780  -1885   1190   3879       C  
ATOM   4882  CD  PRO B 365      -9.155  -7.264  33.068  1.00131.36           C  
ANISOU 4882  CD  PRO B 365    13020  17741  19149  -1845   1063   4060       C  
ATOM   4883  N   GLU B 366     -10.761 -10.016  35.110  1.00133.30           N  
ANISOU 4883  N   GLU B 366    13239  17058  20350  -1195   1618   4274       N  
ATOM   4884  CA  GLU B 366     -11.664 -10.997  35.701  1.00142.99           C  
ANISOU 4884  CA  GLU B 366    14437  17907  21986   -962   1887   4374       C  
ATOM   4885  C   GLU B 366     -11.264 -12.420  35.326  1.00140.81           C  
ANISOU 4885  C   GLU B 366    14193  17697  21610  -1057   1847   4247       C  
ATOM   4886  O   GLU B 366     -11.379 -13.341  36.143  1.00137.98           O  
ANISOU 4886  O   GLU B 366    13908  17092  21427   -937   2077   4201       O  
ATOM   4887  CB  GLU B 366     -13.097 -10.699  35.263  1.00158.79           C  
ANISOU 4887  CB  GLU B 366    16261  19707  24363   -813   1993   4636       C  
ATOM   4888  CG  GLU B 366     -13.671  -9.429  35.878  1.00169.58           C  
ANISOU 4888  CG  GLU B 366    17590  20900  25942   -647   2137   4776       C  
ATOM   4889  CD  GLU B 366     -15.066  -9.110  35.375  1.00174.31           C  
ANISOU 4889  CD  GLU B 366    17990  21332  26908   -509   2233   5046       C  
ATOM   4890  OE1 GLU B 366     -15.386  -9.484  34.227  1.00175.93           O  
ANISOU 4890  OE1 GLU B 366    18080  21695  27072   -623   2062   5135       O  
ATOM   4891  OE2 GLU B 366     -15.839  -8.470  36.120  1.00173.29           O  
ANISOU 4891  OE2 GLU B 366    17820  20924  27097   -297   2493   5165       O  
ATOM   4892  N   LEU B 367     -10.802 -12.622  34.092  1.00136.99           N  
ANISOU 4892  N   LEU B 367    13666  17538  20845  -1280   1591   4178       N  
ATOM   4893  CA  LEU B 367     -10.353 -13.939  33.657  1.00143.29           C  
ANISOU 4893  CA  LEU B 367    14490  18421  21531  -1394   1560   4030       C  
ATOM   4894  C   LEU B 367      -8.883 -14.202  33.955  1.00134.26           C  
ANISOU 4894  C   LEU B 367    13476  17523  20015  -1540   1455   3765       C  
ATOM   4895  O   LEU B 367      -8.499 -15.358  34.168  1.00133.05           O  
ANISOU 4895  O   LEU B 367    13370  17321  19860  -1547   1527   3648       O  
ATOM   4896  CB  LEU B 367     -10.573 -14.092  32.149  1.00161.16           C  
ANISOU 4896  CB  LEU B 367    16643  20921  23670  -1574   1375   4056       C  
ATOM   4897  CG  LEU B 367     -11.991 -13.960  31.592  1.00170.21           C  
ANISOU 4897  CG  LEU B 367    17629  21907  25135  -1492   1444   4309       C  
ATOM   4898  CD1 LEU B 367     -12.063 -14.527  30.180  1.00170.86           C  
ANISOU 4898  CD1 LEU B 367    17627  22224  25066  -1701   1298   4278       C  
ATOM   4899  CD2 LEU B 367     -13.007 -14.629  32.500  1.00173.51           C  
ANISOU 4899  CD2 LEU B 367    18028  21911  25988  -1283   1778   4404       C  
ATOM   4900  N   ALA B 368      -8.053 -13.157  33.973  1.00136.64           N  
ANISOU 4900  N   ALA B 368    13825  18093  19997  -1675   1308   3655       N  
ATOM   4901  CA  ALA B 368      -6.618 -13.345  34.170  1.00123.09           C  
ANISOU 4901  CA  ALA B 368    12200  16671  17898  -1852   1219   3368       C  
ATOM   4902  C   ALA B 368      -6.290 -13.696  35.617  1.00136.19           C  
ANISOU 4902  C   ALA B 368    13966  18130  19652  -1712   1393   3331       C  
ATOM   4903  O   ALA B 368      -5.522 -14.628  35.877  1.00135.54           O  
ANISOU 4903  O   ALA B 368    13926  18118  19456  -1750   1409   3174       O  
ATOM   4904  CB  ALA B 368      -5.856 -12.095  33.735  1.00 90.40           C  
ANISOU 4904  CB  ALA B 368     8075  12895  13376  -2069   1050   3229       C  
ATOM   4905  N   ILE B 369      -6.840 -12.931  36.568  1.00148.43           N  
ANISOU 4905  N   ILE B 369    15556  19437  21404  -1551   1540   3470       N  
ATOM   4906  CA  ILE B 369      -6.472 -13.093  37.979  1.00125.00           C  
ANISOU 4906  CA  ILE B 369    12711  16303  18480  -1437   1721   3428       C  
ATOM   4907  C   ILE B 369      -6.562 -14.545  38.453  1.00109.53           C  
ANISOU 4907  C   ILE B 369    10799  14105  16711  -1290   1886   3446       C  
ATOM   4908  O   ILE B 369      -5.595 -15.033  39.051  1.00120.26           O  
ANISOU 4908  O   ILE B 369    12244  15574  17877  -1339   1892   3305       O  
ATOM   4909  CB  ILE B 369      -7.280 -12.126  38.854  1.00124.24           C  
ANISOU 4909  CB  ILE B 369    12645  15920  18641  -1258   1918   3585       C  
ATOM   4910  CG1 ILE B 369      -6.934 -10.671  38.514  1.00112.37           C  
ANISOU 4910  CG1 ILE B 369    11129  14685  16881  -1451   1770   3519       C  
ATOM   4911  CG2 ILE B 369      -7.041 -12.405  40.333  1.00134.40           C  
ANISOU 4911  CG2 ILE B 369    14083  16983  20001  -1118   2163   3558       C  
ATOM   4912  CD1 ILE B 369      -5.451 -10.398  38.331  1.00105.34           C  
ANISOU 4912  CD1 ILE B 369    10295  14247  15483  -1763   1588   3218       C  
ATOM   4913  N   PRO B 370      -7.663 -15.278  38.232  1.00102.11           N  
ANISOU 4913  N   PRO B 370     9811  12854  16134  -1128   2049   3598       N  
ATOM   4914  CA  PRO B 370      -7.661 -16.701  38.618  1.00103.95           C  
ANISOU 4914  CA  PRO B 370    10115  12879  16502  -1038   2236   3572       C  
ATOM   4915  C   PRO B 370      -6.568 -17.511  37.937  1.00114.77           C  
ANISOU 4915  C   PRO B 370    11467  14570  17569  -1237   2029   3390       C  
ATOM   4916  O   PRO B 370      -6.043 -18.457  38.540  1.00135.66           O  
ANISOU 4916  O   PRO B 370    14207  17140  20199  -1188   2144   3328       O  
ATOM   4917  CB  PRO B 370      -9.058 -17.178  38.204  1.00 91.36           C  
ANISOU 4917  CB  PRO B 370     8444  10985  15282   -930   2431   3716       C  
ATOM   4918  CG  PRO B 370      -9.889 -15.955  38.228  1.00 89.14           C  
ANISOU 4918  CG  PRO B 370     8084  10623  15162   -845   2457   3860       C  
ATOM   4919  CD  PRO B 370      -8.988 -14.865  37.734  1.00 89.54           C  
ANISOU 4919  CD  PRO B 370     8102  11069  14849  -1025   2124   3789       C  
ATOM   4920  N   VAL B 371      -6.222 -17.183  36.691  1.00106.35           N  
ANISOU 4920  N   VAL B 371    10291  13856  16262  -1456   1765   3291       N  
ATOM   4921  CA  VAL B 371      -5.145 -17.896  36.011  1.00111.10           C  
ANISOU 4921  CA  VAL B 371    10857  14789  16566  -1656   1614   3055       C  
ATOM   4922  C   VAL B 371      -3.805 -17.585  36.665  1.00120.38           C  
ANISOU 4922  C   VAL B 371    12075  16247  17416  -1746   1542   2850       C  
ATOM   4923  O   VAL B 371      -2.970 -18.478  36.847  1.00133.32           O  
ANISOU 4923  O   VAL B 371    13707  18005  18942  -1778   1557   2692       O  
ATOM   4924  CB  VAL B 371      -5.143 -17.567  34.509  1.00103.81           C  
ANISOU 4924  CB  VAL B 371     9817  14161  15465  -1863   1413   2968       C  
ATOM   4925  CG1 VAL B 371      -4.006 -18.299  33.815  1.00 97.67           C  
ANISOU 4925  CG1 VAL B 371     8981  13719  14410  -2055   1314   2666       C  
ATOM   4926  CG2 VAL B 371      -6.471 -17.965  33.907  1.00100.03           C  
ANISOU 4926  CG2 VAL B 371     9276  13426  15306  -1787   1498   3169       C  
ATOM   4927  N   VAL B 372      -3.580 -16.321  37.038  1.00109.61           N  
ANISOU 4927  N   VAL B 372    10737  15009  15901  -1791   1482   2834       N  
ATOM   4928  CA  VAL B 372      -2.357 -15.970  37.756  1.00113.82           C  
ANISOU 4928  CA  VAL B 372    11296  15815  16134  -1882   1447   2628       C  
ATOM   4929  C   VAL B 372      -2.257 -16.785  39.034  1.00125.51           C  
ANISOU 4929  C   VAL B 372    12881  17050  17757  -1699   1643   2713       C  
ATOM   4930  O   VAL B 372      -1.167 -17.210  39.440  1.00138.20           O  
ANISOU 4930  O   VAL B 372    14460  18901  19149  -1748   1625   2530       O  
ATOM   4931  CB  VAL B 372      -2.332 -14.462  38.073  1.00111.85           C  
ANISOU 4931  CB  VAL B 372    11083  15659  15755  -1953   1409   2627       C  
ATOM   4932  CG1 VAL B 372      -1.013 -14.075  38.729  1.00114.11           C  
ANISOU 4932  CG1 VAL B 372    11367  16282  15707  -2069   1361   2390       C  
ATOM   4933  CG2 VAL B 372      -2.590 -13.642  36.834  1.00124.52           C  
ANISOU 4933  CG2 VAL B 372    12615  17450  17248  -2098   1244   2617       C  
ATOM   4934  N   TYR B 373      -3.394 -16.996  39.698  1.00113.52           N  
ANISOU 4934  N   TYR B 373    11470  15047  16614  -1455   1862   2984       N  
ATOM   4935  CA  TYR B 373      -3.428 -17.830  40.893  1.00115.29           C  
ANISOU 4935  CA  TYR B 373    11846  14957  17001  -1241   2122   3089       C  
ATOM   4936  C   TYR B 373      -2.960 -19.248  40.582  1.00112.45           C  
ANISOU 4936  C   TYR B 373    11469  14632  16624  -1240   2137   3026       C  
ATOM   4937  O   TYR B 373      -2.039 -19.767  41.225  1.00123.20           O  
ANISOU 4937  O   TYR B 373    12878  16122  17809  -1220   2180   2956       O  
ATOM   4938  CB  TYR B 373      -4.842 -17.824  41.475  1.00120.08           C  
ANISOU 4938  CB  TYR B 373    12560  15026  18040   -981   2435   3314       C  
ATOM   4939  CG  TYR B 373      -4.942 -18.328  42.895  1.00109.20           C  
ANISOU 4939  CG  TYR B 373    11424  13287  16780   -759   2801   3392       C  
ATOM   4940  CD1 TYR B 373      -4.779 -17.458  43.965  1.00108.75           C  
ANISOU 4940  CD1 TYR B 373    11496  13183  16639   -709   2915   3406       C  
ATOM   4941  CD2 TYR B 373      -5.212 -19.660  43.169  1.00108.83           C  
ANISOU 4941  CD2 TYR B 373    11530  12934  16887   -618   3079   3436       C  
ATOM   4942  CE1 TYR B 373      -4.876 -17.899  45.269  1.00126.30           C  
ANISOU 4942  CE1 TYR B 373    14013  15067  18908   -514   3294   3467       C  
ATOM   4943  CE2 TYR B 373      -5.313 -20.112  44.475  1.00128.24           C  
ANISOU 4943  CE2 TYR B 373    14315  15040  19370   -424   3484   3494       C  
ATOM   4944  CZ  TYR B 373      -5.139 -19.228  45.522  1.00140.20           C  
ANISOU 4944  CZ  TYR B 373    15975  16518  20777   -366   3587   3511       C  
ATOM   4945  OH  TYR B 373      -5.234 -19.676  46.822  1.00153.77           O  
ANISOU 4945  OH  TYR B 373    18111  17875  22438   -182   4017   3561       O  
ATOM   4946  N   LEU B 374      -3.587 -19.890  39.590  1.00107.11           N  
ANISOU 4946  N   LEU B 374    10717  13860  16120  -1262   2120   3050       N  
ATOM   4947  CA  LEU B 374      -3.196 -21.245  39.207  1.00 92.57           C  
ANISOU 4947  CA  LEU B 374     8856  12040  14276  -1285   2153   2974       C  
ATOM   4948  C   LEU B 374      -1.755 -21.288  38.714  1.00 99.01           C  
ANISOU 4948  C   LEU B 374     9502  13419  14698  -1502   1916   2668       C  
ATOM   4949  O   LEU B 374      -1.042 -22.271  38.945  1.00109.73           O  
ANISOU 4949  O   LEU B 374    10833  14870  15989  -1469   1977   2576       O  
ATOM   4950  CB  LEU B 374      -4.125 -21.772  38.116  1.00100.68           C  
ANISOU 4950  CB  LEU B 374     9812  12926  15517  -1334   2166   3011       C  
ATOM   4951  CG  LEU B 374      -3.767 -23.144  37.545  1.00108.92           C  
ANISOU 4951  CG  LEU B 374    10822  14009  16555  -1407   2199   2901       C  
ATOM   4952  CD1 LEU B 374      -3.705 -24.183  38.653  1.00105.64           C  
ANISOU 4952  CD1 LEU B 374    10625  13236  16279  -1195   2520   3013       C  
ATOM   4953  CD2 LEU B 374      -4.752 -23.540  36.470  1.00110.35           C  
ANISOU 4953  CD2 LEU B 374    10933  14073  16921  -1493   2222   2928       C  
ATOM   4954  N   LEU B 375      -1.315 -20.238  38.011  1.00105.55           N  
ANISOU 4954  N   LEU B 375    10195  14631  15276  -1706   1690   2469       N  
ATOM   4955  CA  LEU B 375       0.075 -20.169  37.571  1.00120.68           C  
ANISOU 4955  CA  LEU B 375    11907  17081  16866  -1867   1525   2089       C  
ATOM   4956  C   LEU B 375       1.018 -20.188  38.768  1.00134.71           C  
ANISOU 4956  C   LEU B 375    13660  19032  18492  -1767   1576   2010       C  
ATOM   4957  O   LEU B 375       1.986 -20.955  38.803  1.00142.86           O  
ANISOU 4957  O   LEU B 375    14491  20361  19429  -1716   1551   1774       O  
ATOM   4958  CB  LEU B 375       0.297 -18.923  36.713  1.00126.92           C  
ANISOU 4958  CB  LEU B 375    12620  18173  17431  -2042   1319   1963       C  
ATOM   4959  CG  LEU B 375      -0.298 -18.941  35.295  1.00126.87           C  
ANISOU 4959  CG  LEU B 375    12568  18164  17472  -2159   1237   1965       C  
ATOM   4960  CD1 LEU B 375       0.450 -17.982  34.377  1.00135.39           C  
ANISOU 4960  CD1 LEU B 375    13555  19726  18160  -2342   1005   1781       C  
ATOM   4961  CD2 LEU B 375      -0.322 -20.352  34.713  1.00123.09           C  
ANISOU 4961  CD2 LEU B 375    12003  17616  17149  -2158   1308   1865       C  
ATOM   4962  N   GLY B 376       0.751 -19.340  39.764  1.00150.68           N  
ANISOU 4962  N   GLY B 376    15844  20904  20503  -1703   1649   2188       N  
ATOM   4963  CA  GLY B 376       1.514 -19.401  41.003  1.00139.15           C  
ANISOU 4963  CA  GLY B 376    14397  19574  18901  -1583   1745   2166       C  
ATOM   4964  C   GLY B 376       1.459 -20.763  41.670  1.00105.93           C  
ANISOU 4964  C   GLY B 376    10296  15132  14822  -1354   1977   2334       C  
ATOM   4965  O   GLY B 376       2.480 -21.279  42.127  1.00104.29           O  
ANISOU 4965  O   GLY B 376     9915  15287  14422  -1227   2001   2157       O  
ATOM   4966  N   ALA B 377       0.264 -21.359  41.739  1.00 98.46           N  
ANISOU 4966  N   ALA B 377     9611  13587  14214  -1217   2172   2667       N  
ATOM   4967  CA  ALA B 377       0.119 -22.684  42.337  1.00104.99           C  
ANISOU 4967  CA  ALA B 377    10661  14057  15172   -962   2470   2877       C  
ATOM   4968  C   ALA B 377       0.932 -23.744  41.607  1.00120.35           C  
ANISOU 4968  C   ALA B 377    12345  16382  17001  -1003   2392   2642       C  
ATOM   4969  O   ALA B 377       1.457 -24.663  42.245  1.00127.82           O  
ANISOU 4969  O   ALA B 377    13386  17355  17826   -751   2619   2707       O  
ATOM   4970  CB  ALA B 377      -1.353 -23.093  42.369  1.00 81.19           C  
ANISOU 4970  CB  ALA B 377     7922  10344  12581   -816   2734   3132       C  
ATOM   4971  N   LEU B 378       1.067 -23.633  40.286  1.00112.91           N  
ANISOU 4971  N   LEU B 378    11097  15753  16052  -1257   2127   2341       N  
ATOM   4972  CA  LEU B 378       1.823 -24.638  39.545  1.00115.97           C  
ANISOU 4972  CA  LEU B 378    11161  16511  16393  -1273   2062   1995       C  
ATOM   4973  C   LEU B 378       3.317 -24.373  39.602  1.00123.20           C  
ANISOU 4973  C   LEU B 378    11586  18127  17098  -1158   1846   1470       C  
ATOM   4974  O   LEU B 378       4.109 -25.321  39.558  1.00123.87           O  
ANISOU 4974  O   LEU B 378    11305  18528  17233   -853   1799   1148       O  
ATOM   4975  CB  LEU B 378       1.343 -24.706  38.097  1.00109.45           C  
ANISOU 4975  CB  LEU B 378    10244  15662  15681  -1527   1916   1854       C  
ATOM   4976  CG  LEU B 378      -0.104 -25.169  37.957  1.00 96.82           C  
ANISOU 4976  CG  LEU B 378     8974  13424  14389  -1494   2093   2278       C  
ATOM   4977  CD1 LEU B 378      -0.469 -25.248  36.500  1.00105.05           C  
ANISOU 4977  CD1 LEU B 378     9871  14576  15469  -1723   1954   2100       C  
ATOM   4978  CD2 LEU B 378      -0.281 -26.524  38.621  1.00 92.83           C  
ANISOU 4978  CD2 LEU B 378     8695  12521  14056  -1263   2414   2513       C  
ATOM   4979  N   THR B 379       3.721 -23.102  39.687  1.00122.34           N  
ANISOU 4979  N   THR B 379    11424  18261  16798  -1262   1644   1389       N  
ATOM   4980  CA  THR B 379       5.132 -22.789  39.877  1.00139.56           C  
ANISOU 4980  CA  THR B 379    13213  21169  18646  -1057   1325   1035       C  
ATOM   4981  C   THR B 379       5.638 -23.271  41.231  1.00141.96           C  
ANISOU 4981  C   THR B 379    13409  21650  18878   -557   1440   1020       C  
ATOM   4982  O   THR B 379       6.843 -23.493  41.381  1.00147.27           O  
ANISOU 4982  O   THR B 379    13698  23046  19213   -119   1056    618       O  
ATOM   4983  CB  THR B 379       5.385 -21.283  39.736  1.00152.40           C  
ANISOU 4983  CB  THR B 379    14936  23109  19861  -1327   1112   1008       C  
ATOM   4984  OG1 THR B 379       4.518 -20.558  40.621  1.00158.02           O  
ANISOU 4984  OG1 THR B 379    15993  23312  20736  -1397   1357   1378       O  
ATOM   4985  CG2 THR B 379       5.159 -20.821  38.299  1.00153.09           C  
ANISOU 4985  CG2 THR B 379    15075  23261  19832  -1648    958    925       C  
ATOM   4986  N   MET B 380       4.744 -23.423  42.212  1.00140.64           N  
ANISOU 4986  N   MET B 380    13687  20934  18815   -520   1904   1451       N  
ATOM   4987  CA  MET B 380       5.134 -23.943  43.519  1.00120.39           C  
ANISOU 4987  CA  MET B 380    11054  18749  15940    222   2150   1804       C  
ATOM   4988  C   MET B 380       5.492 -25.421  43.451  1.00123.91           C  
ANISOU 4988  C   MET B 380    11095  19776  16211   1277   2208   2080       C  
ATOM   4989  O   MET B 380       6.339 -25.893  44.219  1.00157.50           O  
ANISOU 4989  O   MET B 380    15260  24814  19769   2742   1938   1950       O  
ATOM   4990  CB  MET B 380       3.996 -23.729  44.519  1.00107.31           C  
ANISOU 4990  CB  MET B 380    10256  16193  14325    108   2717   2606       C  
ATOM   4991  CG  MET B 380       4.415 -23.564  45.967  1.00119.05           C  
ANISOU 4991  CG  MET B 380    11947  17981  15307    963   3130   3288       C  
ATOM   4992  SD  MET B 380       5.337 -22.039  46.232  1.00124.79           S  
ANISOU 4992  SD  MET B 380    12177  19549  15690    594   2574   2562       S  
ATOM   4993  CE  MET B 380       4.943 -21.711  47.948  1.00148.21           C  
ANISOU 4993  CE  MET B 380    16084  21998  18232   1100   3225   3410       C  
ATOM   4994  N   LEU B 381       4.853 -26.163  42.551  1.00108.92           N  
ANISOU 4994  N   LEU B 381     9314  17294  14778    860   2355   2118       N  
ATOM   4995  CA  LEU B 381       5.075 -27.591  42.409  1.00 95.31           C  
ANISOU 4995  CA  LEU B 381     7384  15819  13012   1989   2494   2339       C  
ATOM   4996  C   LEU B 381       6.359 -27.865  41.627  1.00109.53           C  
ANISOU 4996  C   LEU B 381     8495  18601  14518   2320   1446   1139       C  
ATOM   4997  O   LEU B 381       6.950 -26.976  41.008  1.00118.55           O  
ANISOU 4997  O   LEU B 381     9473  19788  15783   1442    991    509       O  
ATOM   4998  CB  LEU B 381       3.874 -28.256  41.734  1.00 98.13           C  
ANISOU 4998  CB  LEU B 381     8252  15043  13990   1198   3052   2832       C  
ATOM   4999  CG  LEU B 381       2.592 -28.286  42.573  1.00111.12           C  
ANISOU 4999  CG  LEU B 381    11195  15208  15817    922   3824   3749       C  
ATOM   5000  CD1 LEU B 381       1.384 -28.766  41.774  1.00109.53           C  
ANISOU 5000  CD1 LEU B 381    11490  14190  15935    138   3666   3512       C  
ATOM   5001  CD2 LEU B 381       2.805 -29.153  43.802  1.00129.19           C  
ANISOU 5001  CD2 LEU B 381    15007  16618  17464   2258   4038   4108       C  
ATOM   5002  N   SER B 382       6.789 -29.121  41.663  1.00100.40           N  
ANISOU 5002  N   SER B 382     7571  17572  13003   3689   1107    884       N  
ATOM   5003  CA  SER B 382       7.993 -29.545  40.967  1.00131.32           C  
ANISOU 5003  CA  SER B 382    11061  22215  16619   3991    174   -186       C  
ATOM   5004  C   SER B 382       7.653 -30.029  39.559  1.00162.99           C  
ANISOU 5004  C   SER B 382    14714  25892  21325   3021    330   -248       C  
ATOM   5005  O   SER B 382       6.489 -30.212  39.200  1.00162.71           O  
ANISOU 5005  O   SER B 382    14723  25180  21918   2346   1052    376       O  
ATOM   5006  CB  SER B 382       8.702 -30.646  41.758  1.00136.15           C  
ANISOU 5006  CB  SER B 382    12530  22805  16397   6024   -482   -618       C  
ATOM   5007  OG  SER B 382       8.143 -31.916  41.470  1.00131.94           O  
ANISOU 5007  OG  SER B 382    12915  21179  16038   6434   -241   -339       O  
ATOM   5008  N   GLU B 383       8.697 -30.237  38.752  1.00157.09           N  
ANISOU 5008  N   GLU B 383    13783  25538  20366   2925   -276   -960       N  
ATOM   5009  CA  GLU B 383       8.488 -30.675  37.374  1.00164.85           C  
ANISOU 5009  CA  GLU B 383    14609  26116  21909   2152   -159   -939       C  
ATOM   5010  C   GLU B 383       7.868 -32.069  37.323  1.00155.94           C  
ANISOU 5010  C   GLU B 383    13447  24857  20946   2942     39   -854       C  
ATOM   5011  O   GLU B 383       6.953 -32.321  36.532  1.00153.68           O  
ANISOU 5011  O   GLU B 383    13061  23954  21376   2102    571   -442       O  
ATOM   5012  CB  GLU B 383       9.794 -30.650  36.585  1.00186.26           C  
ANISOU 5012  CB  GLU B 383    17274  29330  24167   2091   -685  -1621       C  
ATOM   5013  CG  GLU B 383       9.594 -31.137  35.156  1.00203.51           C  
ANISOU 5013  CG  GLU B 383    19301  31463  26559   1553   -581  -1724       C  
ATOM   5014  CD  GLU B 383      10.693 -30.699  34.216  1.00225.00           C  
ANISOU 5014  CD  GLU B 383    21896  35067  28528   1333   -826  -2599       C  
ATOM   5015  OE1 GLU B 383      11.874 -30.911  34.553  1.00241.34           O  
ANISOU 5015  OE1 GLU B 383    23890  37826  29982   2026  -1229  -3369       O  
ATOM   5016  OE2 GLU B 383      10.375 -30.125  33.151  1.00227.55           O  
ANISOU 5016  OE2 GLU B 383    22254  35365  28840    564   -571  -2553       O  
ATOM   5017  N   THR B 384       8.391 -33.003  38.125  1.00163.52           N  
ANISOU 5017  N   THR B 384    14866  26053  21211   4723   -422  -1265       N  
ATOM   5018  CA  THR B 384       7.815 -34.346  38.172  1.00138.88           C  
ANISOU 5018  CA  THR B 384    12588  22067  18113   5743   -181  -1048       C  
ATOM   5019  C   THR B 384       6.325 -34.285  38.472  1.00137.82           C  
ANISOU 5019  C   THR B 384    13393  20497  18474   4762    915    130       C  
ATOM   5020  O   THR B 384       5.532 -35.047  37.907  1.00145.78           O  
ANISOU 5020  O   THR B 384    14820  20665  19905   4269   1455    504       O  
ATOM   5021  CB  THR B 384       8.529 -35.192  39.227  1.00136.66           C  
ANISOU 5021  CB  THR B 384    13794  21231  16900   7586   -828  -1384       C  
ATOM   5022  OG1 THR B 384       9.930 -35.247  38.933  1.00138.04           O  
ANISOU 5022  OG1 THR B 384    13335  22549  16566   7989  -1768  -2421       O  
ATOM   5023  CG2 THR B 384       7.964 -36.608  39.261  1.00140.63           C  
ANISOU 5023  CG2 THR B 384    15904  20195  17332   8138   -525  -1044       C  
ATOM   5024  N   GLN B 385       5.930 -33.383  39.369  1.00149.41           N  
ANISOU 5024  N   GLN B 385    15194  21696  19880   4455   1270    695       N  
ATOM   5025  CA  GLN B 385       4.513 -33.160  39.617  1.00150.58           C  
ANISOU 5025  CA  GLN B 385    15999  20669  20547   3411   2333   1765       C  
ATOM   5026  C   GLN B 385       3.828 -32.579  38.384  1.00149.66           C  
ANISOU 5026  C   GLN B 385    14403  21111  21352   1805   2862   2006       C  
ATOM   5027  O   GLN B 385       2.674 -32.913  38.092  1.00141.19           O  
ANISOU 5027  O   GLN B 385    13727  19116  20803    982   3669   2687       O  
ATOM   5028  CB  GLN B 385       4.345 -32.245  40.827  1.00139.91           C  
ANISOU 5028  CB  GLN B 385    15201  19052  18907   3468   2539   2223       C  
ATOM   5029  CG  GLN B 385       4.884 -32.851  42.107  1.00132.46           C  
ANISOU 5029  CG  GLN B 385    15888  17400  17040   5009   2092   2099       C  
ATOM   5030  CD  GLN B 385       5.091 -31.828  43.191  1.00122.56           C  
ANISOU 5030  CD  GLN B 385    14813  16349  15405   5162   2041   2268       C  
ATOM   5031  OE1 GLN B 385       5.533 -30.712  42.929  1.00105.46           O  
ANISOU 5031  OE1 GLN B 385    11267  15423  13378   4621   1831   1971       O  
ATOM   5032  NE2 GLN B 385       4.762 -32.198  44.420  1.00140.33           N  
ANISOU 5032  NE2 GLN B 385    18819  17356  17145   5858   2261   2747       N  
ATOM   5033  N   HIS B 386       4.528 -31.719  37.640  1.00147.93           N  
ANISOU 5033  N   HIS B 386    13109  22016  21081   1151   2162   1115       N  
ATOM   5034  CA  HIS B 386       3.969 -31.183  36.401  1.00138.00           C  
ANISOU 5034  CA  HIS B 386    12171  20388  19875   -291   2005    318       C  
ATOM   5035  C   HIS B 386       3.671 -32.294  35.404  1.00136.78           C  
ANISOU 5035  C   HIS B 386    11921  20250  19798   -448   2079    228       C  
ATOM   5036  O   HIS B 386       2.570 -32.366  34.847  1.00141.09           O  
ANISOU 5036  O   HIS B 386    13050  20353  20203  -1123   2283    660       O  
ATOM   5037  CB  HIS B 386       4.929 -30.166  35.787  1.00142.38           C  
ANISOU 5037  CB  HIS B 386    12442  20890  20766   -362   1484     21       C  
ATOM   5038  CG  HIS B 386       5.062 -28.905  36.579  1.00138.96           C  
ANISOU 5038  CG  HIS B 386    12159  20623  20018   -432   1432    201       C  
ATOM   5039  ND1 HIS B 386       6.110 -28.026  36.406  1.00133.28           N  
ANISOU 5039  ND1 HIS B 386    11264  20549  18829   -364    931    125       N  
ATOM   5040  CD2 HIS B 386       4.278 -28.373  37.546  1.00129.86           C  
ANISOU 5040  CD2 HIS B 386    11467  19304  18569   -620   1782    513       C  
ATOM   5041  CE1 HIS B 386       5.965 -27.007  37.233  1.00130.05           C  
ANISOU 5041  CE1 HIS B 386    11070  20131  18212   -467   1029    277       C  
ATOM   5042  NE2 HIS B 386       4.862 -27.193  37.936  1.00128.57           N  
ANISOU 5042  NE2 HIS B 386    11243  19368  18240   -592   1536    537       N  
ATOM   5043  N   LYS B 387       4.652 -33.167  35.157  1.00130.79           N  
ANISOU 5043  N   LYS B 387    10427  19809  19457    430   1796    -50       N  
ATOM   5044  CA  LYS B 387       4.450 -34.255  34.207  1.00118.72           C  
ANISOU 5044  CA  LYS B 387     8781  18331  17997    342   1862   -185       C  
ATOM   5045  C   LYS B 387       3.321 -35.176  34.648  1.00125.34           C  
ANISOU 5045  C   LYS B 387    10173  18163  19288    492   2884   1127       C  
ATOM   5046  O   LYS B 387       2.459 -35.547  33.843  1.00118.43           O  
ANISOU 5046  O   LYS B 387     9762  16848  18387   -429   3038   1218       O  
ATOM   5047  CB  LYS B 387       5.745 -35.045  34.027  1.00108.40           C  
ANISOU 5047  CB  LYS B 387     6942  17537  16709   1602   1252   -377       C  
ATOM   5048  CG  LYS B 387       6.854 -34.280  33.327  1.00110.83           C  
ANISOU 5048  CG  LYS B 387     7306  18083  16723   1169    529   -619       C  
ATOM   5049  CD  LYS B 387       7.682 -35.216  32.453  1.00130.86           C  
ANISOU 5049  CD  LYS B 387     9657  21137  18927   1546     76  -1284       C  
ATOM   5050  CE  LYS B 387       9.074 -34.661  32.186  1.00144.75           C  
ANISOU 5050  CE  LYS B 387    11459  23529  20009   1623   -524  -1950       C  
ATOM   5051  NZ  LYS B 387       9.894 -35.571  31.331  1.00161.52           N  
ANISOU 5051  NZ  LYS B 387    13431  26112  21827   1974   -884  -2692       N  
ATOM   5052  N   LEU B 388       3.314 -35.562  35.924  1.00130.80           N  
ANISOU 5052  N   LEU B 388    12195  17880  19623   1577   3066   1524       N  
ATOM   5053  CA  LEU B 388       2.234 -36.403  36.424  1.00126.43           C  
ANISOU 5053  CA  LEU B 388    13304  15652  19082   1509   3844   2270       C  
ATOM   5054  C   LEU B 388       0.892 -35.688  36.356  1.00133.71           C  
ANISOU 5054  C   LEU B 388    13955  16158  20690     36   4840   3181       C  
ATOM   5055  O   LEU B 388      -0.138 -36.329  36.122  1.00136.52           O  
ANISOU 5055  O   LEU B 388    15202  15644  21027   -449   5023   3320       O  
ATOM   5056  CB  LEU B 388       2.534 -36.864  37.850  1.00128.08           C  
ANISOU 5056  CB  LEU B 388    15349  14865  18452   2896   3624   2363       C  
ATOM   5057  CG  LEU B 388       3.605 -37.952  37.958  1.00136.69           C  
ANISOU 5057  CG  LEU B 388    17197  15910  18830   4473   2782   1591       C  
ATOM   5058  CD1 LEU B 388       3.763 -38.409  39.398  1.00149.75           C  
ANISOU 5058  CD1 LEU B 388    20816  16437  19644   5786   2634   1798       C  
ATOM   5059  CD2 LEU B 388       3.278 -39.127  37.047  1.00138.76           C  
ANISOU 5059  CD2 LEU B 388    17756  15635  19331   4275   3022   1478       C  
ATOM   5060  N   LEU B 389       0.876 -34.367  36.570  1.00142.12           N  
ANISOU 5060  N   LEU B 389    14709  17894  21394   -379   4123   2884       N  
ATOM   5061  CA  LEU B 389      -0.378 -33.626  36.461  1.00143.69           C  
ANISOU 5061  CA  LEU B 389    15581  18012  21004  -1176   3546   2564       C  
ATOM   5062  C   LEU B 389      -0.870 -33.566  35.020  1.00148.60           C  
ANISOU 5062  C   LEU B 389    15829  18900  21731  -1590   3212   2254       C  
ATOM   5063  O   LEU B 389      -2.064 -33.750  34.762  1.00155.42           O  
ANISOU 5063  O   LEU B 389    17015  19247  22789  -1713   3372   2429       O  
ATOM   5064  CB  LEU B 389      -0.215 -32.213  37.020  1.00130.43           C  
ANISOU 5064  CB  LEU B 389    13731  16648  19177  -1157   3258   2504       C  
ATOM   5065  CG  LEU B 389      -0.353 -32.052  38.532  1.00119.48           C  
ANISOU 5065  CG  LEU B 389    12985  14662  17748   -763   3666   2997       C  
ATOM   5066  CD1 LEU B 389      -0.181 -30.598  38.929  1.00104.09           C  
ANISOU 5066  CD1 LEU B 389    10771  13132  15646   -842   3312   2842       C  
ATOM   5067  CD2 LEU B 389      -1.698 -32.574  38.975  1.00125.75           C  
ANISOU 5067  CD2 LEU B 389    14609  14556  18613   -779   3988   3226       C  
ATOM   5068  N   ALA B 390       0.034 -33.315  34.068  1.00139.31           N  
ANISOU 5068  N   ALA B 390    13966  18580  20384  -1738   2804   1738       N  
ATOM   5069  CA  ALA B 390      -0.348 -33.354  32.660  1.00127.13           C  
ANISOU 5069  CA  ALA B 390    12229  17238  18838  -2090   2600   1514       C  
ATOM   5070  C   ALA B 390      -0.812 -34.748  32.265  1.00150.63           C  
ANISOU 5070  C   ALA B 390    15413  19809  22012  -2152   2882   1651       C  
ATOM   5071  O   ALA B 390      -1.759 -34.904  31.484  1.00167.27           O  
ANISOU 5071  O   ALA B 390    17654  21679  24221  -2389   2916   1722       O  
ATOM   5072  CB  ALA B 390       0.823 -32.912  31.786  1.00106.69           C  
ANISOU 5072  CB  ALA B 390     8991  15609  15937  -2207   2210    814       C  
ATOM   5073  N   GLU B 391      -0.144 -35.774  32.793  1.00143.12           N  
ANISOU 5073  N   GLU B 391    14475  18823  21082  -1896   3135   1656       N  
ATOM   5074  CA  GLU B 391      -0.579 -37.147  32.579  1.00146.16           C  
ANISOU 5074  CA  GLU B 391    15267  18574  21694  -1931   3574   1873       C  
ATOM   5075  C   GLU B 391      -1.966 -37.368  33.171  1.00147.73           C  
ANISOU 5075  C   GLU B 391    16406  17769  21956  -2003   3942   2315       C  
ATOM   5076  O   GLU B 391      -2.837 -37.979  32.541  1.00141.50           O  
ANISOU 5076  O   GLU B 391    15811  16660  21291  -2226   4087   2322       O  
ATOM   5077  CB  GLU B 391       0.437 -38.105  33.201  1.00153.66           C  
ANISOU 5077  CB  GLU B 391    15894  18777  23711  -1013   4644   2256       C  
ATOM   5078  CG  GLU B 391       1.752 -38.209  32.437  1.00151.95           C  
ANISOU 5078  CG  GLU B 391    14263  19813  23659   -521   4088   1434       C  
ATOM   5079  CD  GLU B 391       2.639 -39.329  32.947  1.00151.93           C  
ANISOU 5079  CD  GLU B 391    15452  19310  22963   1128   3535    877       C  
ATOM   5080  OE1 GLU B 391       2.164 -40.138  33.772  1.00148.97           O  
ANISOU 5080  OE1 GLU B 391    16918  17479  22206   1703   3901   1298       O  
ATOM   5081  OE2 GLU B 391       3.813 -39.396  32.527  1.00150.57           O  
ANISOU 5081  OE2 GLU B 391    14466  20205  22539   1862   2674    -23       O  
ATOM   5082  N   ALA B 392      -2.186 -36.883  34.396  1.00151.79           N  
ANISOU 5082  N   ALA B 392    17412  17867  22392  -1747   4123   2607       N  
ATOM   5083  CA  ALA B 392      -3.498 -37.018  35.016  1.00163.72           C  
ANISOU 5083  CA  ALA B 392    19604  18634  23967  -1714   4480   2838       C  
ATOM   5084  C   ALA B 392      -4.553 -36.191  34.292  1.00177.92           C  
ANISOU 5084  C   ALA B 392    20912  20719  25969  -1967   4280   2690       C  
ATOM   5085  O   ALA B 392      -5.726 -36.575  34.273  1.00184.66           O  
ANISOU 5085  O   ALA B 392    22061  21188  26914  -2085   4581   2742       O  
ATOM   5086  CB  ALA B 392      -3.426 -36.626  36.492  1.00159.92           C  
ANISOU 5086  CB  ALA B 392    19738  17741  23284  -1353   4671   3110       C  
ATOM   5087  N   LEU B 393      -4.154 -35.088  33.654  1.00168.54           N  
ANISOU 5087  N   LEU B 393    19081  20193  24765  -2058   3790   2511       N  
ATOM   5088  CA  LEU B 393      -5.114 -34.290  32.896  1.00172.57           C  
ANISOU 5088  CA  LEU B 393    19329  20901  25340  -2255   3602   2453       C  
ATOM   5089  C   LEU B 393      -5.565 -35.020  31.639  1.00170.23           C  
ANISOU 5089  C   LEU B 393    18895  20717  25067  -2564   3595   2316       C  
ATOM   5090  O   LEU B 393      -6.750 -34.981  31.285  1.00165.00           O  
ANISOU 5090  O   LEU B 393    18283  19914  24496  -2717   3722   2372       O  
ATOM   5091  CB  LEU B 393      -4.520 -32.927  32.547  1.00175.90           C  
ANISOU 5091  CB  LEU B 393    19339  21899  25597  -2269   3138   2318       C  
ATOM   5092  CG  LEU B 393      -4.452 -31.934  33.707  1.00179.17           C  
ANISOU 5092  CG  LEU B 393    19870  22197  26010  -2014   3134   2482       C  
ATOM   5093  CD1 LEU B 393      -3.520 -30.794  33.358  1.00177.50           C  
ANISOU 5093  CD1 LEU B 393    19315  22579  25547  -2069   2710   2285       C  
ATOM   5094  CD2 LEU B 393      -5.840 -31.406  34.046  1.00181.21           C  
ANISOU 5094  CD2 LEU B 393    20289  22110  26452  -1971   3323   2663       C  
ATOM   5095  N   GLU B 394      -4.635 -35.682  30.947  1.00175.38           N  
ANISOU 5095  N   GLU B 394    19337  21673  25626  -2670   3452   2122       N  
ATOM   5096  CA  GLU B 394      -4.996 -36.428  29.747  1.00181.96           C  
ANISOU 5096  CA  GLU B 394    20044  22628  26464  -2968   3450   1992       C  
ATOM   5097  C   GLU B 394      -5.898 -37.611  30.072  1.00188.86           C  
ANISOU 5097  C   GLU B 394    21413  22837  27508  -3016   3952   2151       C  
ATOM   5098  O   GLU B 394      -6.747 -37.983  29.254  1.00193.49           O  
ANISOU 5098  O   GLU B 394    21961  23426  28131  -3284   4022   2117       O  
ATOM   5099  CB  GLU B 394      -3.734 -36.917  29.036  1.00185.94           C  
ANISOU 5099  CB  GLU B 394    20188  23629  26833  -3037   3213   1718       C  
ATOM   5100  CG  GLU B 394      -3.935 -37.260  27.572  1.00188.70           C  
ANISOU 5100  CG  GLU B 394    20258  24350  27089  -3361   3050   1540       C  
ATOM   5101  CD  GLU B 394      -3.212 -38.535  27.179  1.00188.79           C  
ANISOU 5101  CD  GLU B 394    20173  24387  27171  -3385   3126   1403       C  
ATOM   5102  OE1 GLU B 394      -2.057 -38.725  27.616  1.00185.46           O  
ANISOU 5102  OE1 GLU B 394    19550  24200  26717  -3172   3048   1263       O  
ATOM   5103  OE2 GLU B 394      -3.804 -39.355  26.445  1.00191.66           O  
ANISOU 5103  OE2 GLU B 394    20625  24566  27632  -3598   3279   1416       O  
ATOM   5104  N   SER B 395      -5.733 -38.211  31.253  1.00186.28           N  
ANISOU 5104  N   SER B 395    21633  21933  27210  -2778   4335   2323       N  
ATOM   5105  CA  SER B 395      -6.552 -39.337  31.680  1.00191.64           C  
ANISOU 5105  CA  SER B 395    23001  21901  27914  -2822   4885   2448       C  
ATOM   5106  C   SER B 395      -7.673 -38.942  32.638  1.00201.47           C  
ANISOU 5106  C   SER B 395    24629  22746  29174  -2741   5205   2599       C  
ATOM   5107  O   SER B 395      -8.489 -39.798  32.995  1.00207.67           O  
ANISOU 5107  O   SER B 395    26016  22975  29913  -2823   5690   2648       O  
ATOM   5108  CB  SER B 395      -5.666 -40.410  32.329  1.00191.71           C  
ANISOU 5108  CB  SER B 395    23670  21394  27778  -2603   5165   2563       C  
ATOM   5109  OG  SER B 395      -4.974 -39.900  33.455  1.00192.67           O  
ANISOU 5109  OG  SER B 395    24055  21394  27755  -2241   5136   2740       O  
ATOM   5110  N   GLN B 396      -7.728 -37.677  33.063  1.00195.38           N  
ANISOU 5110  N   GLN B 396    22853  20038  31345   -658  -6204   1366       N  
ATOM   5111  CA  GLN B 396      -8.804 -37.121  33.889  1.00197.49           C  
ANISOU 5111  CA  GLN B 396    22922  20217  31898   -749  -6147   1551       C  
ATOM   5112  C   GLN B 396      -8.920 -37.787  35.262  1.00207.41           C  
ANISOU 5112  C   GLN B 396    23968  21343  33495   -858  -6189   1792       C  
ATOM   5113  O   GLN B 396      -9.975 -37.705  35.903  1.00205.90           O  
ANISOU 5113  O   GLN B 396    23484  21040  33708   -963  -6147   2079       O  
ATOM   5114  CB  GLN B 396     -10.154 -37.140  33.164  1.00193.74           C  
ANISOU 5114  CB  GLN B 396    22201  19684  31726   -816  -6155   1756       C  
ATOM   5115  CG  GLN B 396     -10.093 -36.525  31.779  1.00186.98           C  
ANISOU 5115  CG  GLN B 396    21530  18939  30576   -721  -6125   1553       C  
ATOM   5116  CD  GLN B 396     -11.430 -35.977  31.327  1.00182.28           C  
ANISOU 5116  CD  GLN B 396    20752  18302  30204   -771  -6085   1698       C  
ATOM   5117  OE1 GLN B 396     -11.759 -34.821  31.600  1.00176.32           O  
ANISOU 5117  OE1 GLN B 396    20040  17574  29381   -751  -5962   1631       O  
ATOM   5118  NE2 GLN B 396     -12.223 -36.812  30.663  1.00185.76           N  
ANISOU 5118  NE2 GLN B 396    20978  18670  30932   -838  -6192   1908       N  
ATOM   5119  N   THR B 397      -7.865 -38.451  35.736  1.00200.33           N  
ANISOU 5119  N   THR B 397    23185  20453  32477   -838  -6257   1716       N  
ATOM   5120  CA  THR B 397      -7.880 -39.073  37.064  1.00201.24           C  
ANISOU 5120  CA  THR B 397    23108  20440  32915   -943  -6301   1955       C  
ATOM   5121  C   THR B 397      -7.330 -38.087  38.102  1.00196.72           C  
ANISOU 5121  C   THR B 397    22759  19886  32101   -899  -6205   1795       C  
ATOM   5122  O   THR B 397      -6.287 -38.289  38.730  1.00205.23           O  
ANISOU 5122  O   THR B 397    24073  20980  32926   -862  -6182   1652       O  
ATOM   5123  CB  THR B 397      -7.099 -40.384  37.051  1.00201.70           C  
ANISOU 5123  CB  THR B 397    23151  20473  33012   -958  -6429   1984       C  
ATOM   5124  OG1 THR B 397      -6.944 -40.868  38.390  1.00212.05           O  
ANISOU 5124  OG1 THR B 397    24314  21669  34588  -1050  -6464   2193       O  
ATOM   5125  CG2 THR B 397      -5.726 -40.209  36.414  1.00195.33           C  
ANISOU 5125  CG2 THR B 397    22722  19819  31676   -804  -6427   1606       C  
ATOM   5126  N   LEU B 398      -8.083 -37.000  38.291  1.00210.68           N  
ANISOU 5126  N   LEU B 398    24695  21635  33717   -908  -5819   1768       N  
ATOM   5127  CA  LEU B 398      -7.677 -35.886  39.143  1.00178.18           C  
ANISOU 5127  CA  LEU B 398    21094  17526  29080   -854  -5338   1530       C  
ATOM   5128  C   LEU B 398      -8.449 -35.802  40.455  1.00181.29           C  
ANISOU 5128  C   LEU B 398    21551  17725  29606   -926  -4879   1820       C  
ATOM   5129  O   LEU B 398      -8.273 -34.830  41.197  1.00182.03           O  
ANISOU 5129  O   LEU B 398    22091  17789  29282   -860  -4429   1666       O  
ATOM   5130  CB  LEU B 398      -7.825 -34.559  38.399  1.00151.12           C  
ANISOU 5130  CB  LEU B 398    17905  14220  25294   -771  -5162   1259       C  
ATOM   5131  CG  LEU B 398      -6.622 -34.036  37.621  1.00134.48           C  
ANISOU 5131  CG  LEU B 398    16066  12315  22714   -620  -5296    883       C  
ATOM   5132  CD1 LEU B 398      -6.770 -34.386  36.165  1.00142.33           C  
ANISOU 5132  CD1 LEU B 398    16764  13391  23923   -561  -5721    922       C  
ATOM   5133  CD2 LEU B 398      -6.499 -32.535  37.800  1.00122.16           C  
ANISOU 5133  CD2 LEU B 398    14946  10829  20640   -565  -4827    606       C  
ATOM   5134  N   LEU B 399      -9.283 -36.791  40.774  1.00174.91           N  
ANISOU 5134  N   LEU B 399    20321  16782  29354  -1031  -4952   2271       N  
ATOM   5135  CA  LEU B 399     -10.098 -36.724  41.982  1.00173.86           C  
ANISOU 5135  CA  LEU B 399    20229  16473  29358  -1040  -4481   2654       C  
ATOM   5136  C   LEU B 399      -9.578 -37.614  43.099  1.00183.93           C  
ANISOU 5136  C   LEU B 399    21549  17637  30698  -1036  -4408   2885       C  
ATOM   5137  O   LEU B 399      -9.773 -37.287  44.274  1.00188.27           O  
ANISOU 5137  O   LEU B 399    22384  18070  31081   -934  -3940   3096       O  
ATOM   5138  CB  LEU B 399     -11.554 -37.096  41.670  1.00163.88           C  
ANISOU 5138  CB  LEU B 399    18449  15147  28670  -1125  -4510   3098       C  
ATOM   5139  CG  LEU B 399     -12.340 -36.122  40.785  1.00148.77           C  
ANISOU 5139  CG  LEU B 399    16498  13299  26728  -1113  -4464   2976       C  
ATOM   5140  CD1 LEU B 399     -13.591 -36.769  40.196  1.00145.51           C  
ANISOU 5140  CD1 LEU B 399    15473  12861  26952  -1208  -4684   3379       C  
ATOM   5141  CD2 LEU B 399     -12.706 -34.874  41.571  1.00149.77           C  
ANISOU 5141  CD2 LEU B 399    17059  13359  26487  -1012  -3864   2949       C  
ATOM   5142  N   GLY B 400      -8.920 -38.719  42.765  1.00186.62           N  
ANISOU 5142  N   GLY B 400    21636  18013  31257  -1109  -4848   2875       N  
ATOM   5143  CA  GLY B 400      -8.336 -39.586  43.758  1.00179.68           C  
ANISOU 5143  CA  GLY B 400    20803  17036  30433  -1106  -4801   3075       C  
ATOM   5144  C   GLY B 400      -7.318 -38.846  44.604  1.00167.78           C  
ANISOU 5144  C   GLY B 400    19910  15523  28316   -962  -4498   2778       C  
ATOM   5145  O   GLY B 400      -7.459 -38.735  45.826  1.00177.93           O  
ANISOU 5145  O   GLY B 400    21451  16680  29472   -842  -4071   3050       O  
ATOM   5146  N   PRO B 401      -6.272 -38.310  43.966  1.00159.05           N  
ANISOU 5146  N   PRO B 401    19056  14576  26798   -923  -4708   2248       N  
ATOM   5147  CA  PRO B 401      -5.296 -37.504  44.721  1.00153.38           C  
ANISOU 5147  CA  PRO B 401    18918  13878  25483   -782  -4418   1930       C  
ATOM   5148  C   PRO B 401      -5.890 -36.262  45.360  1.00151.04           C  
ANISOU 5148  C   PRO B 401    19017  13507  24865   -664  -3844   1940       C  
ATOM   5149  O   PRO B 401      -5.395 -35.823  46.406  1.00157.53           O  
ANISOU 5149  O   PRO B 401    20289  14256  25309   -508  -3482   1899       O  
ATOM   5150  CB  PRO B 401      -4.244 -37.141  43.661  1.00143.28           C  
ANISOU 5150  CB  PRO B 401    17720  12842  23877   -751  -4784   1420       C  
ATOM   5151  CG  PRO B 401      -4.932 -37.348  42.342  1.00147.25           C  
ANISOU 5151  CG  PRO B 401    17799  13431  24718   -820  -5123   1477       C  
ATOM   5152  CD  PRO B 401      -5.861 -38.493  42.564  1.00147.81           C  
ANISOU 5152  CD  PRO B 401    17401  13339  25423   -955  -5223   1968       C  
ATOM   5153  N   LEU B 402      -6.929 -35.674  44.763  1.00143.49           N  
ANISOU 5153  N   LEU B 402    17916  12562  24040   -705  -3744   2001       N  
ATOM   5154  CA  LEU B 402      -7.584 -34.525  45.381  1.00144.45           C  
ANISOU 5154  CA  LEU B 402    18401  12596  23888   -580  -3180   2057       C  
ATOM   5155  C   LEU B 402      -8.163 -34.907  46.738  1.00156.63           C  
ANISOU 5155  C   LEU B 402    20024  13948  25539   -434  -2798   2606       C  
ATOM   5156  O   LEU B 402      -7.838 -34.297  47.762  1.00166.47           O  
ANISOU 5156  O   LEU B 402    21776  15124  26350   -212  -2378   2608       O  
ATOM   5157  CB  LEU B 402      -8.675 -33.970  44.463  1.00141.72           C  
ANISOU 5157  CB  LEU B 402    17812  12294  23743   -658  -3183   2084       C  
ATOM   5158  CG  LEU B 402      -9.559 -32.895  45.106  1.00140.25           C  
ANISOU 5158  CG  LEU B 402    17930  11995  23362   -531  -2604   2237       C  
ATOM   5159  CD1 LEU B 402      -8.723 -31.688  45.511  1.00130.31           C  
ANISOU 5159  CD1 LEU B 402    17310  10764  21438   -395  -2242   1801       C  
ATOM   5160  CD2 LEU B 402     -10.698 -32.476  44.185  1.00144.68           C  
ANISOU 5160  CD2 LEU B 402    18177  12594  24200   -620  -2644   2311       C  
ATOM   5161  N   GLU B 403      -9.051 -35.908  46.754  1.00157.23           N  
ANISOU 5161  N   GLU B 403    19592  13970  26179   -517  -2934   3115       N  
ATOM   5162  CA  GLU B 403      -9.623 -36.389  48.008  1.00165.34           C  
ANISOU 5162  CA  GLU B 403    20614  14888  27318   -343  -2612   3723       C  
ATOM   5163  C   GLU B 403      -8.530 -36.795  48.985  1.00164.78           C  
ANISOU 5163  C   GLU B 403    20889  14783  26936   -172  -2551   3731       C  
ATOM   5164  O   GLU B 403      -8.634 -36.542  50.191  1.00175.17           O  
ANISOU 5164  O   GLU B 403    22549  16059  27947    125  -2158   4045       O  
ATOM   5165  CB  GLU B 403     -10.554 -37.574  47.741  1.00180.54           C  
ANISOU 5165  CB  GLU B 403    21851  16805  29940   -500  -2849   4225       C  
ATOM   5166  CG  GLU B 403     -11.716 -37.280  46.808  1.00191.94           C  
ANISOU 5166  CG  GLU B 403    22892  18287  31749   -641  -2928   4287       C  
ATOM   5167  CD  GLU B 403     -12.957 -36.804  47.543  1.00204.30           C  
ANISOU 5167  CD  GLU B 403    24430  19821  33375   -483  -2466   4772       C  
ATOM   5168  OE1 GLU B 403     -12.849 -36.442  48.733  1.00209.25           O  
ANISOU 5168  OE1 GLU B 403    25456  20420  33630   -226  -2066   4975       O  
ATOM   5169  OE2 GLU B 403     -14.047 -36.801  46.934  1.00207.75           O  
ANISOU 5169  OE2 GLU B 403    24430  20282  34222   -589  -2522   4967       O  
ATOM   5170  N   LEU B 404      -7.474 -37.436  48.479  1.00163.81           N  
ANISOU 5170  N   LEU B 404    20671  14704  26866   -323  -2965   3407       N  
ATOM   5171  CA  LEU B 404      -6.366 -37.842  49.334  1.00149.87           C  
ANISOU 5171  CA  LEU B 404    19206  12913  24824   -167  -2942   3386       C  
ATOM   5172  C   LEU B 404      -5.719 -36.634  49.998  1.00142.71           C  
ANISOU 5172  C   LEU B 404    18970  12010  23243     97  -2554   3080       C  
ATOM   5173  O   LEU B 404      -5.687 -36.526  51.228  1.00160.12           O  
ANISOU 5173  O   LEU B 404    21520  14173  25144    435  -2197   3409       O  
ATOM   5174  CB  LEU B 404      -5.338 -38.613  48.509  1.00134.56           C  
ANISOU 5174  CB  LEU B 404    17031  11047  23047   -394  -3493   3018       C  
ATOM   5175  CG  LEU B 404      -4.036 -38.961  49.218  1.00140.47           C  
ANISOU 5175  CG  LEU B 404    18080  11789  23502   -267  -3532   2883       C  
ATOM   5176  CD1 LEU B 404      -4.312 -39.924  50.368  1.00144.65           C  
ANISOU 5176  CD1 LEU B 404    18535  12215  24210    -86  -3351   3537       C  
ATOM   5177  CD2 LEU B 404      -3.071 -39.551  48.215  1.00137.71           C  
ANISOU 5177  CD2 LEU B 404    17488  11557  23278   -491  -4112   2461       C  
ATOM   5178  N   VAL B 405      -5.225 -35.694  49.188  1.00124.16           N  
ANISOU 5178  N   VAL B 405    16794   9754  20627    -17  -2624   2472       N  
ATOM   5179  CA  VAL B 405      -4.565 -34.510  49.729  1.00129.16           C  
ANISOU 5179  CA  VAL B 405    18006  10408  20663    195  -2247   2124       C  
ATOM   5180  C   VAL B 405      -5.528 -33.708  50.597  1.00157.22           C  
ANISOU 5180  C   VAL B 405    21892  13855  23990    487  -1669   2488       C  
ATOM   5181  O   VAL B 405      -5.142 -33.165  51.640  1.00171.70           O  
ANISOU 5181  O   VAL B 405    24202  15661  25374    834  -1271   2546       O  
ATOM   5182  CB  VAL B 405      -3.985 -33.658  48.586  1.00121.04           C  
ANISOU 5182  CB  VAL B 405    17000   9569  19420     -4  -2453   1446       C  
ATOM   5183  CG1 VAL B 405      -3.499 -32.323  49.114  1.00113.93           C  
ANISOU 5183  CG1 VAL B 405    16602   8706  17979    172  -1998   1098       C  
ATOM   5184  CG2 VAL B 405      -2.859 -34.406  47.895  1.00116.25           C  
ANISOU 5184  CG2 VAL B 405    16170   9135  18867   -163  -3041   1125       C  
ATOM   5185  N   GLY B 406      -6.796 -33.630  50.187  1.00145.27           N  
ANISOU 5185  N   GLY B 406    20114  12310  22774    384  -1640   2758       N  
ATOM   5186  CA  GLY B 406      -7.779 -32.909  50.984  1.00161.85           C  
ANISOU 5186  CA  GLY B 406    22500  14345  24651    648  -1194   3122       C  
ATOM   5187  C   GLY B 406      -7.940 -33.489  52.375  1.00183.71           C  
ANISOU 5187  C   GLY B 406    25398  17109  27294    988  -1065   3716       C  
ATOM   5188  O   GLY B 406      -7.890 -32.766  53.373  1.00192.11           O  
ANISOU 5188  O   GLY B 406    26992  18179  27822   1330   -798   3802       O  
ATOM   5189  N   SER B 407      -8.150 -34.804  52.460  1.00179.57           N  
ANISOU 5189  N   SER B 407    24371  16609  27249    894  -1320   4136       N  
ATOM   5190  CA  SER B 407      -8.295 -35.441  53.763  1.00187.25           C  
ANISOU 5190  CA  SER B 407    25370  17649  28128   1206  -1226   4731       C  
ATOM   5191  C   SER B 407      -7.004 -35.378  54.569  1.00176.22           C  
ANISOU 5191  C   SER B 407    24503  16289  26162   1523  -1206   4558       C  
ATOM   5192  O   SER B 407      -7.051 -35.278  55.800  1.00182.48           O  
ANISOU 5192  O   SER B 407    25571  17192  26570   1889  -1093   4913       O  
ATOM   5193  CB  SER B 407      -8.737 -36.888  53.589  1.00201.78           C  
ANISOU 5193  CB  SER B 407    26530  19506  30632   1006  -1479   5181       C  
ATOM   5194  OG  SER B 407      -9.981 -36.971  52.918  1.00214.19           O  
ANISOU 5194  OG  SER B 407    27583  21067  32732    766  -1490   5392       O  
ATOM   5195  N   LEU B 408      -5.848 -35.445  53.903  1.00195.81           N  
ANISOU 5195  N   LEU B 408    27049  18732  28618   1372  -1363   4024       N  
ATOM   5196  CA  LEU B 408      -4.579 -35.340  54.617  1.00159.17           C  
ANISOU 5196  CA  LEU B 408    22831  14156  23490   1693  -1282   3851       C  
ATOM   5197  C   LEU B 408      -4.389 -33.951  55.213  1.00157.64           C  
ANISOU 5197  C   LEU B 408    23277  13992  22627   2063   -852   3644       C  
ATOM   5198  O   LEU B 408      -4.052 -33.815  56.394  1.00153.38           O  
ANISOU 5198  O   LEU B 408    23057  13681  21537   2456   -814   3792       O  
ATOM   5199  CB  LEU B 408      -3.420 -35.680  53.682  1.00130.96           C  
ANISOU 5199  CB  LEU B 408    19023  10570  20164   1342  -1601   3287       C  
ATOM   5200  CG  LEU B 408      -3.374 -37.103  53.133  1.00119.82           C  
ANISOU 5200  CG  LEU B 408    17073   9132  19324   1015  -2096   3432       C  
ATOM   5201  CD1 LEU B 408      -2.023 -37.372  52.495  1.00108.27           C  
ANISOU 5201  CD1 LEU B 408    15546   7706  17886    771  -2493   2851       C  
ATOM   5202  CD2 LEU B 408      -3.697 -38.127  54.207  1.00123.61           C  
ANISOU 5202  CD2 LEU B 408    17452   9647  19866   1297  -2063   4144       C  
ATOM   5203  N   LEU B 409      -4.607 -32.906  54.408  1.00163.95           N  
ANISOU 5203  N   LEU B 409    24119  14718  23456   1845   -625   3209       N  
ATOM   5204  CA  LEU B 409      -4.462 -31.540  54.906  1.00157.30           C  
ANISOU 5204  CA  LEU B 409    23464  14148  22153   2032   -111   2930       C  
ATOM   5205  C   LEU B 409      -5.516 -31.212  55.954  1.00171.10           C  
ANISOU 5205  C   LEU B 409    25707  15860  23443   2071   -898   3199       C  
ATOM   5206  O   LEU B 409      -5.253 -30.431  56.877  1.00174.63           O  
ANISOU 5206  O   LEU B 409    25569  16276  24505   2014  -1267   3570       O  
ATOM   5207  CB  LEU B 409      -4.538 -30.543  53.747  1.00131.66           C  
ANISOU 5207  CB  LEU B 409    19913  10814  19299   1632     64   2408       C  
ATOM   5208  CG  LEU B 409      -3.404 -30.579  52.718  1.00110.64           C  
ANISOU 5208  CG  LEU B 409    17072   8051  16915   1220   -381   1709       C  
ATOM   5209  CD1 LEU B 409      -3.615 -29.544  51.617  1.00122.40           C  
ANISOU 5209  CD1 LEU B 409    18502   9620  18383    883   -418   1124       C  
ATOM   5210  CD2 LEU B 409      -2.068 -30.372  53.395  1.00108.37           C  
ANISOU 5210  CD2 LEU B 409    16785   7906  16487   1297   -550   1341       C  
ATOM   5211  N   GLU B 410      -6.715 -31.781  55.815  1.00155.50           N  
ANISOU 5211  N   GLU B 410    23427  13712  21943   2028   -822   3805       N  
ATOM   5212  CA  GLU B 410      -7.762 -31.579  56.809  1.00170.16           C  
ANISOU 5212  CA  GLU B 410    25050  15666  23935   2117   -814   4461       C  
ATOM   5213  C   GLU B 410      -7.369 -32.196  58.145  1.00179.15           C  
ANISOU 5213  C   GLU B 410    25994  17050  25024   2423   -818   5048       C  
ATOM   5214  O   GLU B 410      -7.593 -31.601  59.206  1.00192.51           O  
ANISOU 5214  O   GLU B 410    27460  19055  26632   2682   -411   5546       O  
ATOM   5215  CB  GLU B 410      -9.074 -32.180  56.302  1.00179.50           C  
ANISOU 5215  CB  GLU B 410    25645  16861  25694   1964   -566   4898       C  
ATOM   5216  CG  GLU B 410     -10.298 -31.878  57.147  1.00196.10           C  
ANISOU 5216  CG  GLU B 410    27410  19178  27920   2083   -242   5513       C  
ATOM   5217  CD  GLU B 410     -11.546 -32.552  56.608  1.00212.01           C  
ANISOU 5217  CD  GLU B 410    28793  21183  30579   1913   -110   5922       C  
ATOM   5218  OE1 GLU B 410     -11.423 -33.377  55.677  1.00215.90           O  
ANISOU 5218  OE1 GLU B 410    29016  21540  31477   1675   -338   5795       O  
ATOM   5219  OE2 GLU B 410     -12.651 -32.255  57.109  1.00219.69           O  
ANISOU 5219  OE2 GLU B 410    29469  22310  31692   2003    217   6377       O  
ATOM   5220  N   GLN B 411      -6.784 -33.393  58.109  1.00184.50           N  
ANISOU 5220  N   GLN B 411    26689  17706  25708   2492  -1017   5074       N  
ATOM   5221  CA  GLN B 411      -6.346 -34.094  59.307  1.00173.14           C  
ANISOU 5221  CA  GLN B 411    25014  16531  24240   2785  -1042   5657       C  
ATOM   5222  C   GLN B 411      -5.011 -33.596  59.847  1.00174.52           C  
ANISOU 5222  C   GLN B 411    25368  16814  24127   3011  -1163   5538       C  
ATOM   5223  O   GLN B 411      -4.658 -33.944  60.978  1.00182.25           O  
ANISOU 5223  O   GLN B 411    26148  18190  24910   3341  -1026   6079       O  
ATOM   5224  CB  GLN B 411      -6.241 -35.595  59.013  1.00170.41           C  
ANISOU 5224  CB  GLN B 411    24501  16143  24105   2735  -1207   5738       C  
ATOM   5225  CG  GLN B 411      -7.570 -36.329  59.015  1.00178.82           C  
ANISOU 5225  CG  GLN B 411    24927  17267  25750   2591  -1015   6342       C  
ATOM   5226  CD  GLN B 411      -7.421 -37.807  58.707  1.00188.87           C  
ANISOU 5226  CD  GLN B 411    25739  18496  27527   2457  -1189   6584       C  
ATOM   5227  OE1 GLN B 411      -6.388 -38.249  58.202  1.00186.40           O  
ANISOU 5227  OE1 GLN B 411    25539  18077  27207   2393  -1415   6223       O  
ATOM   5228  NE2 GLN B 411      -8.457 -38.580  59.012  1.00197.13           N  
ANISOU 5228  NE2 GLN B 411    26215  19636  29048   2397  -1071   7207       N  
ATOM   5229  N   SER B 412      -4.282 -32.769  59.099  1.00161.73           N  
ANISOU 5229  N   SER B 412    24024  14931  22493   2846  -1363   4869       N  
ATOM   5230  CA  SER B 412      -2.938 -32.356  59.482  1.00176.67           C  
ANISOU 5230  CA  SER B 412    25800  17009  24316   3056  -1290   4754       C  
ATOM   5231  C   SER B 412      -2.880 -30.974  60.126  1.00210.03           C  
ANISOU 5231  C   SER B 412    30510  21627  27664   3582   -414   4589       C  
ATOM   5232  O   SER B 412      -1.790 -30.405  60.230  1.00201.33           O  
ANISOU 5232  O   SER B 412    30077  20625  25794   3916   -282   3923       O  
ATOM   5233  CB  SER B 412      -2.002 -32.403  58.270  1.00155.80           C  
ANISOU 5233  CB  SER B 412    22737  14201  22260   2741  -1179   4116       C  
ATOM   5234  OG  SER B 412      -2.310 -31.379  57.346  1.00143.45           O  
ANISOU 5234  OG  SER B 412    21290  12419  20793   2500   -898   3492       O  
ATOM   5235  N   ALA B 413      -4.018 -30.412  60.546  1.00203.28           N  
ANISOU 5235  N   ALA B 413    29580  20964  26695   3672     80   4990       N  
ATOM   5236  CA  ALA B 413      -3.944 -29.117  61.216  1.00208.26           C  
ANISOU 5236  CA  ALA B 413    30816  21970  26343   4204    889   4799       C  
ATOM   5237  C   ALA B 413      -3.557 -29.311  62.683  1.00219.62           C  
ANISOU 5237  C   ALA B 413    32392  24150  26905   4842   1239   5350       C  
ATOM   5238  O   ALA B 413      -4.075 -30.213  63.347  1.00225.96           O  
ANISOU 5238  O   ALA B 413    32617  25213  28026   4825   1145   6129       O  
ATOM   5239  CB  ALA B 413      -5.280 -28.380  61.126  1.00210.88           C  
ANISOU 5239  CB  ALA B 413    30954  22283  26887   4064   1346   5020       C  
ATOM   5240  N   PRO B 414      -2.641 -28.480  63.218  1.00222.33           N  
ANISOU 5240  N   PRO B 414    33257  25084  26135   5100   1522   4598       N  
ATOM   5241  CA  PRO B 414      -1.934 -27.389  62.533  1.00215.03           C  
ANISOU 5241  CA  PRO B 414    32824  24106  24772   4835   1554   3241       C  
ATOM   5242  C   PRO B 414      -0.776 -27.856  61.654  1.00208.92           C  
ANISOU 5242  C   PRO B 414    32179  22949  24253   4526    840   2437       C  
ATOM   5243  O   PRO B 414      -0.188 -28.905  61.921  1.00223.00           O  
ANISOU 5243  O   PRO B 414    33737  24822  26170   4605    388   2761       O  
ATOM   5244  CB  PRO B 414      -1.417 -26.537  63.692  1.00219.28           C  
ANISOU 5244  CB  PRO B 414    33633  25654  24030   5126   2088   2780       C  
ATOM   5245  CG  PRO B 414      -1.203 -27.517  64.792  1.00226.08           C  
ANISOU 5245  CG  PRO B 414    34172  27070  24658   5465   1980   3600       C  
ATOM   5246  CD  PRO B 414      -2.280 -28.558  64.645  1.00228.42           C  
ANISOU 5246  CD  PRO B 414    33982  26816  25993   5510   1821   4894       C  
ATOM   5247  N   TRP B 415      -0.441 -27.060  60.634  1.00224.90           N  
ANISOU 5247  N   TRP B 415    34571  24562  26320   4186    763   1388       N  
ATOM   5248  CA  TRP B 415       0.536 -27.419  59.615  1.00198.29           C  
ANISOU 5248  CA  TRP B 415    31347  20689  23306   3839    105    591       C  
ATOM   5249  C   TRP B 415       1.980 -27.095  59.995  1.00191.82           C  
ANISOU 5249  C   TRP B 415    30841  20486  21554   3878    -10   -442       C  
ATOM   5250  O   TRP B 415       2.824 -26.954  59.103  1.00194.32           O  
ANISOU 5250  O   TRP B 415    31419  20441  21975   3566   -404  -1403       O  
ATOM   5251  CB  TRP B 415       0.180 -26.743  58.290  1.00177.48           C  
ANISOU 5251  CB  TRP B 415    28932  17299  21205   3429     63    -23       C  
ATOM   5252  CG  TRP B 415      -1.121 -27.224  57.751  1.00164.41           C  
ANISOU 5252  CG  TRP B 415    26505  15368  20593   3091     27    885       C  
ATOM   5253  CD1 TRP B 415      -1.570 -28.511  57.739  1.00165.45           C  
ANISOU 5253  CD1 TRP B 415    25915  15375  21573   2969   -320   1811       C  
ATOM   5254  CD2 TRP B 415      -2.143 -26.438  57.132  1.00149.75           C  
ANISOU 5254  CD2 TRP B 415    24345  13466  19088   2766    321    862       C  
ATOM   5255  NE1 TRP B 415      -2.812 -28.576  57.160  1.00162.72           N  
ANISOU 5255  NE1 TRP B 415    24841  14891  22096   2590   -293   2303       N  
ATOM   5256  CE2 TRP B 415      -3.187 -27.315  56.776  1.00154.83           C  
ANISOU 5256  CE2 TRP B 415    24114  13920  20793   2494     69   1751       C  
ATOM   5257  CE3 TRP B 415      -2.278 -25.077  56.847  1.00130.64           C  
ANISOU 5257  CE3 TRP B 415    22191  11246  16199   2641    724    178       C  
ATOM   5258  CZ2 TRP B 415      -4.350 -26.875  56.150  1.00143.94           C  
ANISOU 5258  CZ2 TRP B 415    22253  12472  19966   2177    121   1926       C  
ATOM   5259  CZ3 TRP B 415      -3.433 -24.642  56.226  1.00123.29           C  
ANISOU 5259  CZ3 TRP B 415    20786  10231  15826   2353    854    439       C  
ATOM   5260  CH2 TRP B 415      -4.453 -25.538  55.885  1.00125.97           C  
ANISOU 5260  CH2 TRP B 415    20357  10325  17180   2153    532   1281       C  
ATOM   5261  N   GLN B 416       2.291 -26.971  61.288  1.00196.26           N  
ANISOU 5261  N   GLN B 416    31388  21972  21208   4244    321   -277       N  
ATOM   5262  CA  GLN B 416       3.670 -26.680  61.669  1.00175.85           C  
ANISOU 5262  CA  GLN B 416    29083  20004  17730   4276    198  -1242       C  
ATOM   5263  C   GLN B 416       4.141 -27.564  62.822  1.00175.22           C  
ANISOU 5263  C   GLN B 416    28719  20610  17249   4621     64   -610       C  
ATOM   5264  O   GLN B 416       5.136 -27.234  63.477  1.00192.57           O  
ANISOU 5264  O   GLN B 416    31112  23538  18518   4745    114  -1241       O  
ATOM   5265  CB  GLN B 416       3.885 -25.197  62.028  1.00163.10           C  
ANISOU 5265  CB  GLN B 416    27614  19002  15356   4148    747  -2011       C  
ATOM   5266  CG  GLN B 416       2.673 -24.454  62.560  1.00167.53           C  
ANISOU 5266  CG  GLN B 416    28333  19737  15585   4429   1504  -1561       C  
ATOM   5267  CD  GLN B 416       1.749 -23.983  61.457  1.00160.54           C  
ANISOU 5267  CD  GLN B 416    27485  18048  15466   4137   1596  -1570       C  
ATOM   5268  OE1 GLN B 416       2.087 -24.057  60.275  1.00157.55           O  
ANISOU 5268  OE1 GLN B 416    26779  17181  15901   3552   1058  -1904       O  
ATOM   5269  NE2 GLN B 416       0.575 -23.493  61.838  1.00164.62           N  
ANISOU 5269  NE2 GLN B 416    28091  18589  15867   4397   2250  -1022       N  
ATOM   5270  N   GLU B 417       3.456 -28.678  63.082  1.00155.17           N  
ANISOU 5270  N   GLU B 417    25719  17855  15383   4775   -104    619       N  
ATOM   5271  CA  GLU B 417       3.849 -29.628  64.116  1.00149.08           C  
ANISOU 5271  CA  GLU B 417    24641  17659  14342   5101   -266   1315       C  
ATOM   5272  C   GLU B 417       3.756 -31.028  63.532  1.00131.35           C  
ANISOU 5272  C   GLU B 417    22011  14713  13183   4990   -889   2030       C  
ATOM   5273  O   GLU B 417       2.685 -31.442  63.078  1.00130.27           O  
ANISOU 5273  O   GLU B 417    21626  13944  13926   4913   -889   2815       O  
ATOM   5274  CB  GLU B 417       2.970 -29.504  65.367  1.00170.10           C  
ANISOU 5274  CB  GLU B 417    27117  20958  16557   5504    338   2256       C  
ATOM   5275  CG  GLU B 417       3.523 -28.547  66.413  1.00177.41           C  
ANISOU 5275  CG  GLU B 417    28340  22901  16166   5730    827   1671       C  
ATOM   5276  CD  GLU B 417       3.205 -28.971  67.834  1.00185.70           C  
ANISOU 5276  CD  GLU B 417    29121  24723  16713   6173   1138   2647       C  
ATOM   5277  OE1 GLU B 417       3.053 -30.187  68.081  1.00189.35           O  
ANISOU 5277  OE1 GLU B 417    29176  25061  17707   6319    803   3597       O  
ATOM   5278  OE2 GLU B 417       3.119 -28.082  68.708  1.00187.06           O  
ANISOU 5278  OE2 GLU B 417    29500  25628  15948   6370   1729   2452       O  
ATOM   5279  N   ARG B 418       4.874 -31.746  63.547  1.00112.13           N  
ANISOU 5279  N   ARG B 418    19526  12394  10683   4980  -1407   1760       N  
ATOM   5280  CA  ARG B 418       4.948 -33.106  63.026  1.00126.47           C  
ANISOU 5280  CA  ARG B 418    20996  13583  13474   4877  -2013   2364       C  
ATOM   5281  C   ARG B 418       3.895 -33.994  63.681  1.00152.98           C  
ANISOU 5281  C   ARG B 418    23883  16934  17307   5156  -1876   3827       C  
ATOM   5282  O   ARG B 418       3.933 -34.229  64.893  1.00193.82           O  
ANISOU 5282  O   ARG B 418    28891  22866  21887   5543  -1645   4398       O  
ATOM   5283  CB  ARG B 418       6.356 -33.649  63.282  1.00135.50           C  
ANISOU 5283  CB  ARG B 418    22154  15101  14231   4931  -2467   1903       C  
ATOM   5284  CG  ARG B 418       6.798 -34.838  62.448  1.00137.97           C  
ANISOU 5284  CG  ARG B 418    22255  14681  15487   4710  -3159   2055       C  
ATOM   5285  CD  ARG B 418       8.321 -34.930  62.503  1.00147.27           C  
ANISOU 5285  CD  ARG B 418    23601  16220  16135   4684  -3539   1180       C  
ATOM   5286  NE  ARG B 418       8.854 -36.186  61.985  1.00154.11           N  
ANISOU 5286  NE  ARG B 418    24219  16556  17779   4565  -4171   1443       N  
ATOM   5287  CZ  ARG B 418      10.143 -36.402  61.742  1.00160.27           C  
ANISOU 5287  CZ  ARG B 418    25122  17405  18368   4464  -4596    689       C  
ATOM   5288  NH1 ARG B 418      11.033 -35.443  61.969  1.00166.94           N  
ANISOU 5288  NH1 ARG B 418    26331  18837  18263   4461  -4467   -383       N  
ATOM   5289  NH2 ARG B 418      10.545 -37.577  61.277  1.00156.18           N  
ANISOU 5289  NH2 ARG B 418    24361  16368  18611   4363  -5138   1008       N  
ATOM   5290  N   SER B 419       2.952 -34.491  62.877  1.00140.97           N  
ANISOU 5290  N   SER B 419    22147  14558  16857   4954  -2016   4435       N  
ATOM   5291  CA  SER B 419       1.882 -35.347  63.378  1.00151.61           C  
ANISOU 5291  CA  SER B 419    22867  15892  18844   4945  -1892   5650       C  
ATOM   5292  C   SER B 419       1.538 -36.419  62.355  1.00169.73           C  
ANISOU 5292  C   SER B 419    24612  17401  22479   4240  -2466   5795       C  
ATOM   5293  O   SER B 419       1.287 -36.110  61.186  1.00183.68           O  
ANISOU 5293  O   SER B 419    26170  18747  24872   3859  -2273   5428       O  
ATOM   5294  CB  SER B 419       0.631 -34.519  63.707  1.00141.74           C  
ANISOU 5294  CB  SER B 419    21618  14775  17462   5003  -1267   5983       C  
ATOM   5295  OG  SER B 419      -0.530 -35.330  63.746  1.00148.05           O  
ANISOU 5295  OG  SER B 419    21876  15312  19063   4629  -1361   6622       O  
ATOM   5296  N   THR B 420       1.535 -37.675  62.803  1.00166.23           N  
ANISOU 5296  N   THR B 420    24124  16948  22087   4293  -2813   6120       N  
ATOM   5297  CA  THR B 420       1.230 -38.797  61.924  1.00177.00           C  
ANISOU 5297  CA  THR B 420    25565  17958  23731   4254  -2651   5903       C  
ATOM   5298  C   THR B 420      -0.246 -38.813  61.538  1.00191.50           C  
ANISOU 5298  C   THR B 420    27263  19557  25941   3943  -2395   6063       C  
ATOM   5299  O   THR B 420      -1.127 -38.548  62.361  1.00196.52           O  
ANISOU 5299  O   THR B 420    27702  20410  26557   3961  -2252   6586       O  
ATOM   5300  CB  THR B 420       1.615 -40.120  62.593  1.00180.73           C  
ANISOU 5300  CB  THR B 420    25753  18653  24265   4375  -2873   6327       C  
ATOM   5301  OG1 THR B 420       0.740 -40.377  63.699  1.00188.16           O  
ANISOU 5301  OG1 THR B 420    26383  19899  25211   4415  -2752   7050       O  
ATOM   5302  CG2 THR B 420       3.055 -40.072  63.093  1.00182.04           C  
ANISOU 5302  CG2 THR B 420    26004  19162  23998   4672  -3183   6191       C  
ATOM   5303  N   MET B 421      -0.506 -39.138  60.273  1.00190.88           N  
ANISOU 5303  N   MET B 421    27094  19174  26257   3614  -2209   5679       N  
ATOM   5304  CA  MET B 421      -1.834 -39.248  59.683  1.00197.83           C  
ANISOU 5304  CA  MET B 421    27818  19867  27481   3279  -2032   5726       C  
ATOM   5305  C   MET B 421      -2.216 -40.715  59.503  1.00217.01           C  
ANISOU 5305  C   MET B 421    29787  22260  30405   3059  -2132   6045       C  
ATOM   5306  O   MET B 421      -1.421 -41.627  59.745  1.00221.05           O  
ANISOU 5306  O   MET B 421    30181  22849  30959   3145  -2320   6139       O  
ATOM   5307  CB  MET B 421      -1.900 -38.486  58.358  1.00182.90           C  
ANISOU 5307  CB  MET B 421    26030  17747  25715   2960  -1812   5092       C  
ATOM   5308  CG  MET B 421      -1.269 -37.101  58.404  1.00179.78           C  
ANISOU 5308  CG  MET B 421    25954  17359  24994   3145  -1634   4756       C  
ATOM   5309  SD  MET B 421      -2.433 -35.837  58.967  1.00184.15           S  
ANISOU 5309  SD  MET B 421    26841  17891  25236   3211  -1580   4890       S  
ATOM   5310  CE  MET B 421      -2.264 -35.937  60.750  1.00195.06           C  
ANISOU 5310  CE  MET B 421    28031  19650  26432   3516  -1890   5679       C  
ATOM   5311  N   SER B 422      -3.461 -40.935  59.072  1.00222.36           N  
ANISOU 5311  N   SER B 422    30041  22812  31635   2734  -2039   6330       N  
ATOM   5312  CA  SER B 422      -4.043 -42.269  59.004  1.00236.39           C  
ANISOU 5312  CA  SER B 422    31197  24552  34068   2501  -2134   6833       C  
ATOM   5313  C   SER B 422      -4.346 -42.721  57.579  1.00239.54           C  
ANISOU 5313  C   SER B 422    31147  24686  35181   1947  -2299   6592       C  
ATOM   5314  O   SER B 422      -3.861 -43.776  57.166  1.00238.89           O  
ANISOU 5314  O   SER B 422    30753  24516  35499   1723  -2562   6591       O  
ATOM   5315  CB  SER B 422      -5.318 -42.319  59.851  1.00244.74           C  
ANISOU 5315  CB  SER B 422    31997  25774  35218   2622  -1892   7488       C  
ATOM   5316  OG  SER B 422      -6.306 -41.470  59.298  1.00242.66           O  
ANISOU 5316  OG  SER B 422    31686  25413  35103   2438  -1700   7388       O  
ATOM   5317  N   LEU B 423      -5.135 -41.945  56.811  1.00239.81           N  
ANISOU 5317  N   LEU B 423    31124  24613  35382   1710  -2197   6378       N  
ATOM   5318  CA  LEU B 423      -5.815 -42.404  55.596  1.00246.95           C  
ANISOU 5318  CA  LEU B 423    31480  25354  36997   1210  -2381   6304       C  
ATOM   5319  C   LEU B 423      -4.961 -43.245  54.653  1.00268.29           C  
ANISOU 5319  C   LEU B 423    33926  27932  40079    852  -2799   5950       C  
ATOM   5320  O   LEU B 423      -3.869 -42.830  54.239  1.00255.38           O  
ANISOU 5320  O   LEU B 423    32592  26264  38175    805  -2949   5378       O  
ATOM   5321  CB  LEU B 423      -6.384 -41.237  54.785  1.00222.76           C  
ANISOU 5321  CB  LEU B 423    28518  22223  33899   1042  -2277   5918       C  
ATOM   5322  CG  LEU B 423      -7.913 -41.119  54.908  1.00212.42           C  
ANISOU 5322  CG  LEU B 423    26864  20953  32893   1018  -2055   6395       C  
ATOM   5323  CD1 LEU B 423      -8.345 -40.771  56.361  1.00211.67           C  
ANISOU 5323  CD1 LEU B 423    27011  21043  32371   1467  -1696   6902       C  
ATOM   5324  CD2 LEU B 423      -8.566 -40.202  53.839  1.00205.56           C  
ANISOU 5324  CD2 LEU B 423    25933  20008  32164    765  -2037   6029       C  
ATOM   5325  N   PRO B 424      -5.446 -44.428  54.288  1.00262.19           N  
ANISOU 5325  N   PRO B 424    32570  27103  39947    586  -3005   6274       N  
ATOM   5326  CA  PRO B 424      -4.747 -45.265  53.320  1.00264.57           C  
ANISOU 5326  CA  PRO B 424    32572  27299  40652    220  -3450   5950       C  
ATOM   5327  C   PRO B 424      -5.231 -44.979  51.909  1.00260.31           C  
ANISOU 5327  C   PRO B 424    31719  26709  40480   -176  -3713   5559       C  
ATOM   5328  O   PRO B 424      -6.367 -44.521  51.712  1.00259.88           O  
ANISOU 5328  O   PRO B 424    31496  26672  40575   -208  -3549   5733       O  
ATOM   5329  CB  PRO B 424      -5.127 -46.686  53.759  1.00274.45           C  
ANISOU 5329  CB  PRO B 424    33355  28541  42381    195  -3503   6572       C  
ATOM   5330  CG  PRO B 424      -6.480 -46.532  54.385  1.00278.25           C  
ANISOU 5330  CG  PRO B 424    33658  29108  42958    354  -3158   7151       C  
ATOM   5331  CD  PRO B 424      -6.622 -45.104  54.862  1.00272.58           C  
ANISOU 5331  CD  PRO B 424    33465  28478  41625    645  -2831   6990       C  
ATOM   5332  N   PRO B 425      -4.390 -45.225  50.899  1.00265.82           N  
ANISOU 5332  N   PRO B 425    30076  34412  36513   -516  -2025   3144       N  
ATOM   5333  CA  PRO B 425      -4.844 -45.046  49.509  1.00253.90           C  
ANISOU 5333  CA  PRO B 425    29423  32342  34706   -365  -2347   2944       C  
ATOM   5334  C   PRO B 425      -5.802 -46.134  49.056  1.00256.35           C  
ANISOU 5334  C   PRO B 425    29787  32529  35085   -514  -2820   2984       C  
ATOM   5335  O   PRO B 425      -6.652 -45.876  48.194  1.00251.82           O  
ANISOU 5335  O   PRO B 425    29660  31707  34313   -409  -3272   2818       O  
ATOM   5336  CB  PRO B 425      -3.537 -45.083  48.708  1.00238.34           C  
ANISOU 5336  CB  PRO B 425    28209  29784  32564   -324  -1849   2943       C  
ATOM   5337  CG  PRO B 425      -2.625 -45.924  49.536  1.00236.62           C  
ANISOU 5337  CG  PRO B 425    27523  29731  32652   -526  -1394   3196       C  
ATOM   5338  CD  PRO B 425      -2.997 -45.697  50.978  1.00250.61           C  
ANISOU 5338  CD  PRO B 425    28301  32245  34674   -610  -1435   3315       C  
ATOM   5339  N   GLY B 426      -5.675 -47.348  49.595  1.00255.03           N  
ANISOU 5339  N   GLY B 426    29194  32511  35195   -767  -2743   3211       N  
ATOM   5340  CA  GLY B 426      -6.628 -48.398  49.272  1.00263.72           C  
ANISOU 5340  CA  GLY B 426    30274  33553  36373   -923  -3213   3268       C  
ATOM   5341  C   GLY B 426      -8.047 -48.018  49.654  1.00272.84           C  
ANISOU 5341  C   GLY B 426    30949  35169  37550   -891  -3782   3173       C  
ATOM   5342  O   GLY B 426      -9.000 -48.337  48.939  1.00278.95           O  
ANISOU 5342  O   GLY B 426    32013  35746  38229   -888  -4270   3099       O  
ATOM   5343  N   LEU B 427      -8.205 -47.341  50.798  1.00281.58           N  
ANISOU 5343  N   LEU B 427    31301  36897  38790   -878  -3720   3168       N  
ATOM   5344  CA  LEU B 427      -9.512 -46.814  51.187  1.00262.35           C  
ANISOU 5344  CA  LEU B 427    28384  34914  36382   -821  -4220   3026       C  
ATOM   5345  C   LEU B 427     -10.090 -45.908  50.109  1.00271.26           C  
ANISOU 5345  C   LEU B 427    30171  35659  37237   -546  -4565   2762       C  
ATOM   5346  O   LEU B 427     -11.312 -45.866  49.925  1.00277.86           O  
ANISOU 5346  O   LEU B 427    30886  36611  38078   -518  -5114   2655       O  
ATOM   5347  CB  LEU B 427      -9.405 -46.063  52.517  1.00237.43           C  
ANISOU 5347  CB  LEU B 427    24402  32433  33379   -830  -4005   3019       C  
ATOM   5348  CG  LEU B 427     -10.658 -45.543  53.243  1.00223.24           C  
ANISOU 5348  CG  LEU B 427    21917  31236  31668   -813  -4403   2854       C  
ATOM   5349  CD1 LEU B 427     -10.957 -44.084  52.897  1.00218.59           C  
ANISOU 5349  CD1 LEU B 427    21531  30596  30926   -486  -4551   2575       C  
ATOM   5350  CD2 LEU B 427     -11.889 -46.423  52.997  1.00222.64           C  
ANISOU 5350  CD2 LEU B 427    21908  31142  31544   -911  -4812   2755       C  
ATOM   5351  N   LEU B 428      -9.237 -45.174  49.396  1.00254.62           N  
ANISOU 5351  N   LEU B 428    28757  33095  34894   -356  -4270   2661       N  
ATOM   5352  CA  LEU B 428      -9.713 -44.325  48.311  1.00252.94           C  
ANISOU 5352  CA  LEU B 428    29235  32465  34405   -127  -4608   2429       C  
ATOM   5353  C   LEU B 428     -10.052 -45.168  47.087  1.00252.96           C  
ANISOU 5353  C   LEU B 428    29965  31891  34257   -208  -4903   2445       C  
ATOM   5354  O   LEU B 428     -11.194 -45.167  46.616  1.00256.75           O  
ANISOU 5354  O   LEU B 428    30544  32314  34696   -179  -5474   2353       O  
ATOM   5355  CB  LEU B 428      -8.670 -43.256  47.968  1.00248.89           C  
ANISOU 5355  CB  LEU B 428    29229  31671  33669     71  -4201   2322       C  
ATOM   5356  CG  LEU B 428      -8.798 -41.947  48.753  1.00242.96           C  
ANISOU 5356  CG  LEU B 428    27993  31365  32957    261  -4176   2180       C  
ATOM   5357  CD1 LEU B 428      -8.460 -42.128  50.230  1.00238.31           C  
ANISOU 5357  CD1 LEU B 428    26461  31436  32652    126  -3828   2328       C  
ATOM   5358  CD2 LEU B 428      -7.950 -40.866  48.127  1.00239.96           C  
ANISOU 5358  CD2 LEU B 428    28282  30598  32293    470  -3913   2052       C  
ATOM   5359  N   GLY B 429      -9.069 -45.885  46.553  1.00257.05           N  
ANISOU 5359  N   GLY B 429    31000  31970  34699   -314  -4520   2555       N  
ATOM   5360  CA  GLY B 429      -9.338 -46.807  45.468  1.00255.15           C  
ANISOU 5360  CA  GLY B 429    31403  31207  34336   -429  -4753   2580       C  
ATOM   5361  C   GLY B 429      -8.142 -46.983  44.561  1.00249.95           C  
ANISOU 5361  C   GLY B 429    31574  29928  33465   -441  -4299   2565       C  
ATOM   5362  O   GLY B 429      -8.081 -47.919  43.758  1.00252.33           O  
ANISOU 5362  O   GLY B 429    32383  29791  33700   -579  -4338   2606       O  
ATOM   5363  N   ASN B 430      -7.180 -46.078  44.700  1.00257.03           N  
ANISOU 5363  N   ASN B 430    32603  30799  34257   -303  -3855   2497       N  
ATOM   5364  CA  ASN B 430      -6.015 -46.051  43.834  1.00240.97           C  
ANISOU 5364  CA  ASN B 430    31367  28199  31992   -298  -3403   2444       C  
ATOM   5365  C   ASN B 430      -5.065 -47.202  44.158  1.00231.72           C  
ANISOU 5365  C   ASN B 430    30036  26961  31047   -483  -2918   2628       C  
ATOM   5366  O   ASN B 430      -4.996 -47.683  45.293  1.00230.21           O  
ANISOU 5366  O   ASN B 430    29039  27240  31188   -580  -2794   2810       O  
ATOM   5367  CB  ASN B 430      -5.293 -44.714  44.008  1.00231.48           C  
ANISOU 5367  CB  ASN B 430    30269  27055  30629    -99  -3084   2332       C  
ATOM   5368  CG  ASN B 430      -6.080 -43.546  43.432  1.00234.99           C  
ANISOU 5368  CG  ASN B 430    31067  27405  30814     86  -3551   2126       C  
ATOM   5369  OD1 ASN B 430      -7.289 -43.644  43.212  1.00240.17           O  
ANISOU 5369  OD1 ASN B 430    31654  28112  31489     84  -4137   2082       O  
ATOM   5370  ND2 ASN B 430      -5.403 -42.425  43.217  1.00236.08           N  
ANISOU 5370  ND2 ASN B 430    31561  27413  30725    243  -3309   2007       N  
ATOM   5371  N   SER B 431      -4.335 -47.651  43.138  1.00226.53           N  
ANISOU 5371  N   SER B 431    30156  25702  30213   -548  -2654   2572       N  
ATOM   5372  CA  SER B 431      -3.278 -48.632  43.338  1.00225.28           C  
ANISOU 5372  CA  SER B 431    29929  25396  30273   -695  -2141   2708       C  
ATOM   5373  C   SER B 431      -2.065 -47.944  43.944  1.00230.21           C  
ANISOU 5373  C   SER B 431    30369  26160  30941   -602  -1545   2731       C  
ATOM   5374  O   SER B 431      -1.696 -46.836  43.544  1.00233.59           O  
ANISOU 5374  O   SER B 431    31224  26452  31077   -441  -1409   2576       O  
ATOM   5375  CB  SER B 431      -2.901 -49.311  42.020  1.00223.25           C  
ANISOU 5375  CB  SER B 431    30569  24442  29815   -797  -2039   2602       C  
ATOM   5376  OG  SER B 431      -1.807 -50.202  42.186  1.00217.85           O  
ANISOU 5376  OG  SER B 431    29826  23580  29366   -921  -1514   2702       O  
ATOM   5377  N   TRP B 432      -1.445 -48.605  44.908  1.00221.92           N  
ANISOU 5377  N   TRP B 432    28688  25376  30256   -716  -1206   2938       N  
ATOM   5378  CA  TRP B 432      -0.347 -48.036  45.667  1.00216.90           C  
ANISOU 5378  CA  TRP B 432    27743  24947  29722   -654   -663   3011       C  
ATOM   5379  C   TRP B 432       0.950 -48.761  45.336  1.00220.26           C  
ANISOU 5379  C   TRP B 432    28483  24945  30262   -751    -99   3056       C  
ATOM   5380  O   TRP B 432       1.004 -49.628  44.454  1.00230.61           O  
ANISOU 5380  O   TRP B 432    30298  25778  31544   -853   -118   2996       O  
ATOM   5381  CB  TRP B 432      -0.658 -48.087  47.163  1.00213.21           C  
ANISOU 5381  CB  TRP B 432    26230  25180  29598   -724   -725   3223       C  
ATOM   5382  CG  TRP B 432       0.207 -47.186  47.999  1.00207.47           C  
ANISOU 5382  CG  TRP B 432    25158  24760  28912   -632   -280   3277       C  
ATOM   5383  CD1 TRP B 432       1.032 -47.564  49.017  1.00202.68           C  
ANISOU 5383  CD1 TRP B 432    23958  24418  28633   -758    124   3504       C  
ATOM   5384  CD2 TRP B 432       0.354 -45.767  47.869  1.00204.65           C  
ANISOU 5384  CD2 TRP B 432    25048  24453  28257   -406   -203   3112       C  
ATOM   5385  NE1 TRP B 432       1.668 -46.468  49.544  1.00196.54           N  
ANISOU 5385  NE1 TRP B 432    23037  23869  27772   -627    456   3494       N  
ATOM   5386  CE2 TRP B 432       1.270 -45.352  48.857  1.00197.46           C  
ANISOU 5386  CE2 TRP B 432    23661  23861  27504   -403    265   3251       C  
ATOM   5387  CE3 TRP B 432      -0.207 -44.805  47.024  1.00208.61           C  
ANISOU 5387  CE3 TRP B 432    26124  24756  28382   -217   -508   2871       C  
ATOM   5388  CZ2 TRP B 432       1.637 -44.020  49.022  1.00196.39           C  
ANISOU 5388  CZ2 TRP B 432    23610  23857  27152   -209    448   3150       C  
ATOM   5389  CZ3 TRP B 432       0.161 -43.483  47.188  1.00207.00           C  
ANISOU 5389  CZ3 TRP B 432    25997  24675  27979    -25   -342   2770       C  
ATOM   5390  CH2 TRP B 432       1.073 -43.103  48.181  1.00201.76           C  
ANISOU 5390  CH2 TRP B 432    24853  24338  27469    -17    138   2906       C  
ATOM   5391  N   GLY B 433       2.001 -48.400  46.047  1.00205.25           N  
ANISOU 5391  N   GLY B 433    26275  23210  28501   -722    409   3154       N  
ATOM   5392  CA  GLY B 433       3.312 -48.921  45.729  1.00208.18           C  
ANISOU 5392  CA  GLY B 433    26950  23169  28981   -785    981   3171       C  
ATOM   5393  C   GLY B 433       4.153 -47.798  45.158  1.00206.30           C  
ANISOU 5393  C   GLY B 433    27314  22684  28388   -616   1360   2988       C  
ATOM   5394  O   GLY B 433       3.659 -46.941  44.413  1.00198.17           O  
ANISOU 5394  O   GLY B 433    26825  21519  26953   -487   1111   2785       O  
ATOM   5395  N   GLU B 434       5.422 -47.771  45.556  1.00211.39           N  
ANISOU 5395  N   GLU B 434    27836  23289  29195   -624   1948   3074       N  
ATOM   5396  CA  GLU B 434       6.364 -46.773  45.071  1.00206.71           C  
ANISOU 5396  CA  GLU B 434    27786  22466  28286   -485   2370   2922       C  
ATOM   5397  C   GLU B 434       6.347 -46.733  43.553  1.00204.59           C  
ANISOU 5397  C   GLU B 434    28525  21596  27613   -473   2324   2640       C  
ATOM   5398  O   GLU B 434       6.640 -47.734  42.891  1.00210.00           O  
ANISOU 5398  O   GLU B 434    29548  21853  28391   -604   2454   2582       O  
ATOM   5399  CB  GLU B 434       7.769 -47.111  45.569  1.00207.66           C  
ANISOU 5399  CB  GLU B 434    27677  22519  28704   -543   3018   3060       C  
ATOM   5400  CG  GLU B 434       8.838 -46.122  45.142  1.00213.22           C  
ANISOU 5400  CG  GLU B 434    28898  23011  29105   -415   3500   2923       C  
ATOM   5401  CD  GLU B 434      10.242 -46.625  45.423  1.00219.51           C  
ANISOU 5401  CD  GLU B 434    29568  23627  30209   -489   4142   3029       C  
ATOM   5402  OE1 GLU B 434      10.764 -46.368  46.527  1.00219.70           O  
ANISOU 5402  OE1 GLU B 434    28962  24027  30485   -485   4386   3252       O  
ATOM   5403  OE2 GLU B 434      10.822 -47.286  44.532  1.00223.79           O  
ANISOU 5403  OE2 GLU B 434    30638  23643  30748   -562   4402   2883       O  
ATOM   5404  N   GLY B 435       6.009 -45.572  43.002  1.00203.10           N  
ANISOU 5404  N   GLY B 435    28819  21370  26980   -331   2132   2462       N  
ATOM   5405  CA  GLY B 435       5.787 -45.416  41.579  1.00184.67           C  
ANISOU 5405  CA  GLY B 435    27437  18516  24213   -348   1972   2203       C  
ATOM   5406  C   GLY B 435       4.383 -44.988  41.210  1.00176.54           C  
ANISOU 5406  C   GLY B 435    26558  17570  22948   -296   1272   2119       C  
ATOM   5407  O   GLY B 435       4.184 -44.444  40.114  1.00182.14           O  
ANISOU 5407  O   GLY B 435    28060  17916  23227   -282   1099   1909       O  
ATOM   5408  N   ALA B 436       3.398 -45.218  42.077  1.00191.87           N  
ANISOU 5408  N   ALA B 436    27770  19974  25159   -283    854   2273       N  
ATOM   5409  CA  ALA B 436       2.053 -44.748  41.793  1.00167.26           C  
ANISOU 5409  CA  ALA B 436    24736  16963  21852   -217    185   2190       C  
ATOM   5410  C   ALA B 436       2.057 -43.221  41.734  1.00163.61           C  
ANISOU 5410  C   ALA B 436    24487  16608  21069    -23    117   2067       C  
ATOM   5411  O   ALA B 436       2.873 -42.572  42.397  1.00168.59           O  
ANISOU 5411  O   ALA B 436    24848  17468  21741     72    520   2123       O  
ATOM   5412  CB  ALA B 436       1.076 -45.236  42.861  1.00145.11           C  
ANISOU 5412  CB  ALA B 436    21022  14694  19419   -245   -194   2375       C  
ATOM   5413  N   PRO B 437       1.175 -42.619  40.929  1.00148.38           N  
ANISOU 5413  N   PRO B 437    23059  14498  18822     32   -398   1906       N  
ATOM   5414  CA  PRO B 437       1.213 -41.153  40.797  1.00154.39           C  
ANISOU 5414  CA  PRO B 437    24078  15307  19276    211   -485   1780       C  
ATOM   5415  C   PRO B 437       1.090 -40.439  42.129  1.00165.69           C  
ANISOU 5415  C   PRO B 437    24650  17363  20941    374   -470   1888       C  
ATOM   5416  O   PRO B 437       1.806 -39.461  42.371  1.00171.00           O  
ANISOU 5416  O   PRO B 437    25374  18123  21477    498   -174   1858       O  
ATOM   5417  CB  PRO B 437       0.028 -40.854  39.868  1.00158.30           C  
ANISOU 5417  CB  PRO B 437    25079  15558  19511    214  -1168   1634       C  
ATOM   5418  CG  PRO B 437      -0.160 -42.105  39.087  1.00162.80           C  
ANISOU 5418  CG  PRO B 437    26035  15736  20087      3  -1236   1631       C  
ATOM   5419  CD  PRO B 437       0.172 -43.226  40.037  1.00156.82           C  
ANISOU 5419  CD  PRO B 437    24542  15263  19781    -79   -917   1831       C  
ATOM   5420  N   ALA B 438       0.203 -40.914  43.008  1.00167.06           N  
ANISOU 5420  N   ALA B 438    24034  17983  21458    359   -778   2010       N  
ATOM   5421  CA  ALA B 438       0.040 -40.288  44.316  1.00158.21           C  
ANISOU 5421  CA  ALA B 438    22057  17487  20568    478   -760   2100       C  
ATOM   5422  C   ALA B 438       1.302 -40.419  45.164  1.00162.46           C  
ANISOU 5422  C   ALA B 438    22208  18225  21295    442    -88   2265       C  
ATOM   5423  O   ALA B 438       1.678 -39.478  45.870  1.00165.06           O  
ANISOU 5423  O   ALA B 438    22223  18874  21619    570    108   2281       O  
ATOM   5424  CB  ALA B 438      -1.156 -40.895  45.046  1.00152.55           C  
ANISOU 5424  CB  ALA B 438    20587  17201  20174    418  -1209   2190       C  
ATOM   5425  N   TRP B 439       1.956 -41.584  45.133  1.00173.41           N  
ANISOU 5425  N   TRP B 439    23590  19428  22872    266    259   2394       N  
ATOM   5426  CA  TRP B 439       3.199 -41.752  45.884  1.00168.08           C  
ANISOU 5426  CA  TRP B 439    22574  18888  22399    219    893   2560       C  
ATOM   5427  C   TRP B 439       4.243 -40.727  45.461  1.00159.02           C  
ANISOU 5427  C   TRP B 439    21979  17509  20933    346   1302   2454       C  
ATOM   5428  O   TRP B 439       4.725 -39.935  46.279  1.00154.13           O  
ANISOU 5428  O   TRP B 439    20979  17232  20350    443   1553   2526       O  
ATOM   5429  CB  TRP B 439       3.743 -43.171  45.697  1.00174.08           C  
ANISOU 5429  CB  TRP B 439    23370  19368  23404     15   1165   2677       C  
ATOM   5430  CG  TRP B 439       5.050 -43.426  46.414  1.00175.92           C  
ANISOU 5430  CG  TRP B 439    23270  19683  23887    -48   1804   2856       C  
ATOM   5431  CD1 TRP B 439       6.248 -42.803  46.186  1.00178.10           C  
ANISOU 5431  CD1 TRP B 439    23926  19753  23992     28   2324   2810       C  
ATOM   5432  CD2 TRP B 439       5.299 -44.397  47.436  1.00173.72           C  
ANISOU 5432  CD2 TRP B 439    22235  19690  24081   -217   1975   3116       C  
ATOM   5433  NE1 TRP B 439       7.213 -43.305  47.018  1.00175.47           N  
ANISOU 5433  NE1 TRP B 439    23101  19561  24008    -70   2806   3027       N  
ATOM   5434  CE2 TRP B 439       6.660 -44.290  47.793  1.00170.21           C  
ANISOU 5434  CE2 TRP B 439    21738  19188  23746   -227   2595   3221       C  
ATOM   5435  CE3 TRP B 439       4.506 -45.344  48.088  1.00176.38           C  
ANISOU 5435  CE3 TRP B 439    21932  20326  24757   -376   1648   3279       C  
ATOM   5436  CZ2 TRP B 439       7.240 -45.092  48.772  1.00168.88           C  
ANISOU 5436  CZ2 TRP B 439    20903  19233  24032   -392   2880   3489       C  
ATOM   5437  CZ3 TRP B 439       5.083 -46.137  49.062  1.00175.73           C  
ANISOU 5437  CZ3 TRP B 439    21197  20468  25106   -552   1928   3543       C  
ATOM   5438  CH2 TRP B 439       6.436 -46.006  49.395  1.00177.10           C  
ANISOU 5438  CH2 TRP B 439    21334  20559  25396   -559   2531   3649       C  
ATOM   5439  N   VAL B 440       4.619 -40.740  44.180  1.00147.78           N  
ANISOU 5439  N   VAL B 440    21462  15505  19182    327   1380   2283       N  
ATOM   5440  CA  VAL B 440       5.688 -39.861  43.713  1.00148.77           C  
ANISOU 5440  CA  VAL B 440    22156  15382  18986    409   1797   2181       C  
ATOM   5441  C   VAL B 440       5.291 -38.402  43.886  1.00156.34           C  
ANISOU 5441  C   VAL B 440    23128  16578  19695    610   1536   2089       C  
ATOM   5442  O   VAL B 440       6.127 -37.548  44.205  1.00158.14           O  
ANISOU 5442  O   VAL B 440    23372  16908  19808    709   1897   2105       O  
ATOM   5443  CB  VAL B 440       6.043 -40.189  42.253  1.00147.99           C  
ANISOU 5443  CB  VAL B 440    23045  14624  18559    308   1879   1990       C  
ATOM   5444  CG1 VAL B 440       7.205 -39.326  41.787  1.00148.52           C  
ANISOU 5444  CG1 VAL B 440    23689  14451  18290    362   2342   1887       C  
ATOM   5445  CG2 VAL B 440       6.365 -41.667  42.115  1.00143.61           C  
ANISOU 5445  CG2 VAL B 440    22430  13840  18296    116   2111   2065       C  
ATOM   5446  N   LEU B 441       4.012 -38.095  43.675  1.00150.50           N  
ANISOU 5446  N   LEU B 441    22380  15919  18883    675    896   1990       N  
ATOM   5447  CA  LEU B 441       3.524 -36.738  43.885  1.00150.75           C  
ANISOU 5447  CA  LEU B 441    22356  16182  18738    874    587   1891       C  
ATOM   5448  C   LEU B 441       3.791 -36.274  45.315  1.00156.01           C  
ANISOU 5448  C   LEU B 441    22155  17448  19673    966    829   2041       C  
ATOM   5449  O   LEU B 441       4.348 -35.194  45.535  1.00157.64           O  
ANISOU 5449  O   LEU B 441    22435  17753  19710   1103   1029   2009       O  
ATOM   5450  CB  LEU B 441       2.032 -36.676  43.572  1.00146.15           C  
ANISOU 5450  CB  LEU B 441    21750  15629  18150    913   -154   1783       C  
ATOM   5451  CG  LEU B 441       1.501 -35.388  42.959  1.00136.19           C  
ANISOU 5451  CG  LEU B 441    20962  14227  16556   1075   -594   1587       C  
ATOM   5452  CD1 LEU B 441       2.249 -35.107  41.667  1.00130.24           C  
ANISOU 5452  CD1 LEU B 441    21259  12871  15354   1012   -425   1461       C  
ATOM   5453  CD2 LEU B 441       0.025 -35.545  42.687  1.00131.29           C  
ANISOU 5453  CD2 LEU B 441    20253  13622  16009   1086  -1316   1506       C  
ATOM   5454  N   LEU B 442       3.381 -37.079  46.303  1.00169.62           N  
ANISOU 5454  N   LEU B 442    23055  19585  21808    874    799   2208       N  
ATOM   5455  CA  LEU B 442       3.571 -36.715  47.706  1.00147.55           C  
ANISOU 5455  CA  LEU B 442    19399  17387  19276    911   1013   2358       C  
ATOM   5456  C   LEU B 442       5.046 -36.595  48.079  1.00142.27           C  
ANISOU 5456  C   LEU B 442    18742  16700  18615    885   1706   2498       C  
ATOM   5457  O   LEU B 442       5.427 -35.668  48.803  1.00130.87           O  
ANISOU 5457  O   LEU B 442    16999  15577  17149    993   1901   2535       O  
ATOM   5458  CB  LEU B 442       2.859 -37.722  48.606  1.00125.47           C  
ANISOU 5458  CB  LEU B 442    15774  15002  16897    756    836   2516       C  
ATOM   5459  CG  LEU B 442       1.343 -37.665  48.434  1.00116.14           C  
ANISOU 5459  CG  LEU B 442    14450  13949  15729    805    142   2378       C  
ATOM   5460  CD1 LEU B 442       0.678 -38.707  49.300  1.00121.95           C  
ANISOU 5460  CD1 LEU B 442    14387  15093  16855    623    -19   2538       C  
ATOM   5461  CD2 LEU B 442       0.842 -36.270  48.778  1.00119.43           C  
ANISOU 5461  CD2 LEU B 442    14690  14658  16028   1022   -108   2225       C  
ATOM   5462  N   ASP B 443       5.889 -37.532  47.626  1.00143.91           N  
ANISOU 5462  N   ASP B 443    19266  16541  18874    739   2088   2576       N  
ATOM   5463  CA  ASP B 443       7.312 -37.459  47.964  1.00149.73           C  
ANISOU 5463  CA  ASP B 443    20004  17238  19648    710   2751   2710       C  
ATOM   5464  C   ASP B 443       7.928 -36.169  47.444  1.00160.24           C  
ANISOU 5464  C   ASP B 443    21938  18387  20561    879   2919   2567       C  
ATOM   5465  O   ASP B 443       8.810 -35.587  48.087  1.00169.97           O  
ANISOU 5465  O   ASP B 443    22960  19817  21802    927   3339   2677       O  
ATOM   5466  CB  ASP B 443       8.071 -38.663  47.402  1.00153.65           C  
ANISOU 5466  CB  ASP B 443    20815  17299  20267    538   3100   2765       C  
ATOM   5467  CG  ASP B 443       9.405 -38.901  48.109  1.00159.50           C  
ANISOU 5467  CG  ASP B 443    21243  18119  21241    464   3752   2975       C  
ATOM   5468  OD1 ASP B 443       9.399 -39.382  49.266  1.00159.92           O  
ANISOU 5468  OD1 ASP B 443    20484  18587  21690    359   3831   3210       O  
ATOM   5469  OD2 ASP B 443      10.461 -38.619  47.501  1.00161.34           O  
ANISOU 5469  OD2 ASP B 443    22044  17995  21263    492   4179   2907       O  
ATOM   5470  N   GLU B 444       7.479 -35.713  46.274  1.00157.26           N  
ANISOU 5470  N   GLU B 444    22323  17623  19805    951   2582   2333       N  
ATOM   5471  CA  GLU B 444       7.946 -34.439  45.744  1.00149.54           C  
ANISOU 5471  CA  GLU B 444    21939  16476  18405   1097   2652   2192       C  
ATOM   5472  C   GLU B 444       7.491 -33.278  46.618  1.00136.47           C  
ANISOU 5472  C   GLU B 444    19789  15304  16759   1279   2439   2197       C  
ATOM   5473  O   GLU B 444       8.209 -32.280  46.738  1.00116.01           O  
ANISOU 5473  O   GLU B 444    17370  12751  13956   1389   2696   2188       O  
ATOM   5474  CB  GLU B 444       7.443 -34.256  44.310  1.00152.53           C  
ANISOU 5474  CB  GLU B 444    23220  16342  18391   1093   2259   1952       C  
ATOM   5475  CG  GLU B 444       8.180 -35.078  43.255  1.00151.34           C  
ANISOU 5475  CG  GLU B 444    23773  15638  18091    919   2578   1888       C  
ATOM   5476  CD  GLU B 444       9.649 -34.721  43.121  1.00150.59           C  
ANISOU 5476  CD  GLU B 444    24023  15374  17819    907   3229   1905       C  
ATOM   5477  OE1 GLU B 444       9.967 -33.515  43.133  1.00147.77           O  
ANISOU 5477  OE1 GLU B 444    23880  15087  17180   1038   3263   1855       O  
ATOM   5478  OE2 GLU B 444      10.485 -35.642  42.984  1.00151.37           O  
ANISOU 5478  OE2 GLU B 444    24188  15260  18067    767   3699   1962       O  
ATOM   5479  N   CYS B 445       6.314 -33.394  47.246  1.00124.99           N  
ANISOU 5479  N   CYS B 445    17711  14226  15552   1308   1982   2203       N  
ATOM   5480  CA  CYS B 445       5.851 -32.364  48.172  1.00139.64           C  
ANISOU 5480  CA  CYS B 445    19005  16580  17473   1467   1801   2190       C  
ATOM   5481  C   CYS B 445       6.750 -32.260  49.400  1.00149.50           C  
ANISOU 5481  C   CYS B 445    19621  18247  18935   1435   2344   2409       C  
ATOM   5482  O   CYS B 445       6.840 -31.191  50.014  1.00145.29           O  
ANISOU 5482  O   CYS B 445    18839  18022  18340   1575   2380   2394       O  
ATOM   5483  CB  CYS B 445       4.411 -32.650  48.600  1.00156.89           C  
ANISOU 5483  CB  CYS B 445    20612  19087  19910   1471   1231   2140       C  
ATOM   5484  SG  CYS B 445       3.246 -32.796  47.231  1.00180.34           S  
ANISOU 5484  SG  CYS B 445    24261  21591  22670   1495    537   1909       S  
ATOM   5485  N   GLY B 446       7.419 -33.349  49.771  1.00161.25           N  
ANISOU 5485  N   GLY B 446    20843  19742  20684   1246   2754   2617       N  
ATOM   5486  CA  GLY B 446       8.358 -33.325  50.876  1.00161.44           C  
ANISOU 5486  CA  GLY B 446    20314  20108  20917   1181   3281   2853       C  
ATOM   5487  C   GLY B 446       7.980 -34.270  51.999  1.00162.18           C  
ANISOU 5487  C   GLY B 446    19501  20648  21471    993   3276   3062       C  
ATOM   5488  O   GLY B 446       8.511 -34.168  53.110  1.00160.52           O  
ANISOU 5488  O   GLY B 446    18689  20836  21467    918   3608   3266       O  
ATOM   5489  N   LEU B 447       7.052 -35.184  51.725  1.00173.01           N  
ANISOU 5489  N   LEU B 447    20775  21962  22997    895   2885   3023       N  
ATOM   5490  CA  LEU B 447       6.562 -36.139  52.710  1.00140.63           C  
ANISOU 5490  CA  LEU B 447    15845  18275  19314    690   2798   3210       C  
ATOM   5491  C   LEU B 447       7.226 -37.498  52.521  1.00155.87           C  
ANISOU 5491  C   LEU B 447    17832  19914  21476    479   3088   3390       C  
ATOM   5492  O   LEU B 447       7.442 -37.949  51.391  1.00161.61           O  
ANISOU 5492  O   LEU B 447    19255  20097  22054    488   3097   3283       O  
ATOM   5493  CB  LEU B 447       5.042 -36.290  52.622  1.00120.57           C  
ANISOU 5493  CB  LEU B 447    13082  15908  16821    708   2148   3060       C  
ATOM   5494  CG  LEU B 447       4.210 -35.012  52.774  1.00124.17           C  
ANISOU 5494  CG  LEU B 447    13438  16635  17107    923   1776   2847       C  
ATOM   5495  CD1 LEU B 447       2.718 -35.325  52.840  1.00121.05           C  
ANISOU 5495  CD1 LEU B 447    12687  16461  16847    904   1161   2729       C  
ATOM   5496  CD2 LEU B 447       4.653 -34.234  54.001  1.00132.31           C  
ANISOU 5496  CD2 LEU B 447    13856  18186  18230    937   2081   2953       C  
ATOM   5497  N   GLU B 448       7.556 -38.142  53.638  1.00170.15           N  
ANISOU 5497  N   GLU B 448    18906  22084  23659    273   3320   3659       N  
ATOM   5498  CA  GLU B 448       8.149 -39.472  53.610  1.00172.79           C  
ANISOU 5498  CA  GLU B 448    19178  22183  24292     56   3562   3852       C  
ATOM   5499  C   GLU B 448       7.058 -40.523  53.460  1.00174.88           C  
ANISOU 5499  C   GLU B 448    19241  22463  24740    -79   3087   3839       C  
ATOM   5500  O   GLU B 448       6.067 -40.511  54.198  1.00174.16           O  
ANISOU 5500  O   GLU B 448    18539  22857  24777   -145   2723   3862       O  
ATOM   5501  CB  GLU B 448       8.952 -39.747  54.881  1.00171.19           C  
ANISOU 5501  CB  GLU B 448    18747  22201  24097    -40   3388   3640       C  
ATOM   5502  CG  GLU B 448      10.296 -39.053  54.939  1.00178.44           C  
ANISOU 5502  CG  GLU B 448    20095  22941  24763     70   3566   3428       C  
ATOM   5503  CD  GLU B 448      10.246 -37.763  55.724  1.00187.28           C  
ANISOU 5503  CD  GLU B 448    21122  24388  25649    155   3399   3258       C  
ATOM   5504  OE1 GLU B 448       9.142 -37.362  56.151  1.00192.20           O  
ANISOU 5504  OE1 GLU B 448    21374  25364  26289    159   3186   3284       O  
ATOM   5505  OE2 GLU B 448      11.315 -37.154  55.919  1.00189.54           O  
ANISOU 5505  OE2 GLU B 448    21695  24575  25748    207   3453   3083       O  
ATOM   5506  N   LEU B 449       7.253 -41.426  52.494  1.00181.89           N  
ANISOU 5506  N   LEU B 449    20643  22830  25639   -129   3092   3792       N  
ATOM   5507  CA  LEU B 449       6.266 -42.502  52.209  1.00184.13           C  
ANISOU 5507  CA  LEU B 449    20783  23079  26098   -270   2665   3799       C  
ATOM   5508  C   LEU B 449       6.862 -43.870  52.559  1.00183.67           C  
ANISOU 5508  C   LEU B 449    20350  22969  26467   -526   2913   4063       C  
ATOM   5509  O   LEU B 449       8.067 -44.079  52.312  1.00185.47           O  
ANISOU 5509  O   LEU B 449    20674  22984  26811   -565   3422   4181       O  
ATOM   5510  CB  LEU B 449       5.873 -42.436  50.729  1.00179.52           C  
ANISOU 5510  CB  LEU B 449    21054  21933  25223   -164   2403   3545       C  
ATOM   5511  CG  LEU B 449       5.129 -41.171  50.303  1.00174.26           C  
ANISOU 5511  CG  LEU B 449    21064  21053  24096     71   2135   3252       C  
ATOM   5512  CD1 LEU B 449       4.921 -41.146  48.796  1.00169.86           C  
ANISOU 5512  CD1 LEU B 449    20074  20952  23514    145   1585   3174       C  
ATOM   5513  CD2 LEU B 449       3.796 -41.056  51.027  1.00177.22           C  
ANISOU 5513  CD2 LEU B 449    21837  21299  24201    231   2551   3183       C  
ATOM   5514  N   GLY B 450       6.028 -44.753  53.114  1.00184.01           N  
ANISOU 5514  N   GLY B 450    19953  23209  26754   -707   2527   4157       N  
ATOM   5515  CA  GLY B 450       6.403 -46.097  53.491  1.00185.07           C  
ANISOU 5515  CA  GLY B 450    19737  23274  27307   -968   2634   4398       C  
ATOM   5516  C   GLY B 450       5.376 -47.026  52.887  1.00195.01           C  
ANISOU 5516  C   GLY B 450    21134  24366  28596  -1044   2142   4322       C  
ATOM   5517  O   GLY B 450       4.573 -46.595  52.055  1.00200.86           O  
ANISOU 5517  O   GLY B 450    22346  24956  29014   -881   1801   4078       O  
ATOM   5518  N   GLU B 451       5.377 -48.293  53.285  1.00195.21           N  
ANISOU 5518  N   GLU B 451    20761  24404  29004  -1297   2077   4536       N  
ATOM   5519  CA  GLU B 451       4.423 -49.257  52.761  1.00216.53           C  
ANISOU 5519  CA  GLU B 451    23564  26954  31753  -1391   1607   4492       C  
ATOM   5520  C   GLU B 451       3.284 -49.554  53.730  1.00230.28           C  
ANISOU 5520  C   GLU B 451    24523  29312  33660  -1578   1136   4629       C  
ATOM   5521  O   GLU B 451       2.523 -50.500  53.499  1.00231.97           O  
ANISOU 5521  O   GLU B 451    24686  29469  33982  -1711    746   4657       O  
ATOM   5522  CB  GLU B 451       5.143 -50.543  52.353  1.00217.91           C  
ANISOU 5522  CB  GLU B 451    23931  26640  32225  -1542   1809   4598       C  
ATOM   5523  CG  GLU B 451       5.544 -50.581  50.874  1.00218.25           C  
ANISOU 5523  CG  GLU B 451    24945  25974  32006  -1374   1967   4334       C  
ATOM   5524  CD  GLU B 451       6.858 -49.875  50.570  1.00215.03           C  
ANISOU 5524  CD  GLU B 451    24950  25274  31477  -1228   2568   4256       C  
ATOM   5525  OE1 GLU B 451       7.176 -48.876  51.244  1.00213.65           O  
ANISOU 5525  OE1 GLU B 451    24511  25451  31217  -1144   2765   4306       O  
ATOM   5526  OE2 GLU B 451       7.567 -50.310  49.637  1.00216.82           O  
ANISOU 5526  OE2 GLU B 451    25781  24919  31682  -1201   2848   4130       O  
ATOM   5527  N   ASP B 452       3.149 -48.777  54.806  1.00232.18           N  
ANISOU 5527  N   ASP B 452    24254  30125  33841  -1563   1139   4640       N  
ATOM   5528  CA  ASP B 452       2.041 -48.922  55.744  1.00229.21           C  
ANISOU 5528  CA  ASP B 452    23538  30259  33292  -1600    649   4480       C  
ATOM   5529  C   ASP B 452       1.285 -47.595  55.870  1.00231.55           C  
ANISOU 5529  C   ASP B 452    23657  30934  33388  -1455    495   4345       C  
ATOM   5530  O   ASP B 452       1.630 -46.592  55.239  1.00234.36           O  
ANISOU 5530  O   ASP B 452    24167  31169  33711  -1295    726   4370       O  
ATOM   5531  CB  ASP B 452       2.549 -49.387  57.114  1.00222.57           C  
ANISOU 5531  CB  ASP B 452    22793  29575  32197  -1598    686   4244       C  
ATOM   5532  CG  ASP B 452       4.056 -49.299  57.238  1.00216.20           C  
ANISOU 5532  CG  ASP B 452    22303  28494  31348  -1502   1106   4193       C  
ATOM   5533  OD1 ASP B 452       4.753 -49.960  56.439  1.00215.79           O  
ANISOU 5533  OD1 ASP B 452    22415  28023  31551  -1533   1315   4352       O  
ATOM   5534  OD2 ASP B 452       4.541 -48.560  58.121  1.00211.20           O  
ANISOU 5534  OD2 ASP B 452    21785  28036  30427  -1403   1215   3961       O  
ATOM   5535  N   THR B 453       0.231 -47.598  56.699  1.00232.70           N  
ANISOU 5535  N   THR B 453    23610  31480  33325  -1476    121   4119       N  
ATOM   5536  CA  THR B 453      -0.649 -46.437  56.807  1.00231.04           C  
ANISOU 5536  CA  THR B 453    23237  31610  32940  -1334    -91   3925       C  
ATOM   5537  C   THR B 453      -0.225 -45.444  57.891  1.00241.25           C  
ANISOU 5537  C   THR B 453    24662  33096  33907  -1215    163   3617       C  
ATOM   5538  O   THR B 453      -0.147 -44.245  57.601  1.00236.55           O  
ANISOU 5538  O   THR B 453    24059  32577  33241  -1037    251   3574       O  
ATOM   5539  CB  THR B 453      -2.111 -46.861  57.024  1.00217.90           C  
ANISOU 5539  CB  THR B 453    21366  30204  31223  -1413   -596   3773       C  
ATOM   5540  OG1 THR B 453      -2.699 -46.041  58.046  1.00212.09           O  
ANISOU 5540  OG1 THR B 453    20592  29799  30194  -1326   -616   3382       O  
ATOM   5541  CG2 THR B 453      -2.215 -48.334  57.405  1.00214.54           C  
ANISOU 5541  CG2 THR B 453    20968  29689  30859  -1623   -684   3832       C  
ATOM   5542  N   PRO B 454       0.070 -45.866  59.130  1.00238.76           N  
ANISOU 5542  N   PRO B 454    24473  32834  33411  -1305    260   3396       N  
ATOM   5543  CA  PRO B 454       0.488 -44.881  60.137  1.00233.62           C  
ANISOU 5543  CA  PRO B 454    23962  32297  32506  -1222    454   3094       C  
ATOM   5544  C   PRO B 454       1.834 -44.250  59.830  1.00232.65           C  
ANISOU 5544  C   PRO B 454    24092  31956  32348  -1104    812   3187       C  
ATOM   5545  O   PRO B 454       2.296 -43.402  60.605  1.00230.77           O  
ANISOU 5545  O   PRO B 454    24005  31771  31907  -1043    954   2950       O  
ATOM   5546  CB  PRO B 454       0.552 -45.705  61.438  1.00231.47           C  
ANISOU 5546  CB  PRO B 454    23733  32066  32150  -1370    429   2987       C  
ATOM   5547  CG  PRO B 454       0.839 -47.070  60.993  1.00232.93           C  
ANISOU 5547  CG  PRO B 454    23963  32039  32499  -1487    398   3152       C  
ATOM   5548  CD  PRO B 454       0.107 -47.234  59.688  1.00236.54           C  
ANISOU 5548  CD  PRO B 454    24224  32479  33172  -1482    189   3412       C  
ATOM   5549  N   HIS B 455       2.470 -44.639  58.720  1.00239.58           N  
ANISOU 5549  N   HIS B 455    25045  32549  33437  -1077    973   3505       N  
ATOM   5550  CA  HIS B 455       3.805 -44.164  58.393  1.00219.62           C  
ANISOU 5550  CA  HIS B 455    22821  29752  30874   -962   1361   3564       C  
ATOM   5551  C   HIS B 455       3.809 -42.700  57.986  1.00206.27           C  
ANISOU 5551  C   HIS B 455    21163  28145  29065   -763   1497   3537       C  
ATOM   5552  O   HIS B 455       4.853 -42.046  58.098  1.00206.70           O  
ANISOU 5552  O   HIS B 455    21511  28058  28966   -660   1779   3458       O  
ATOM   5553  CB  HIS B 455       4.419 -45.012  57.275  1.00214.03           C  
ANISOU 5553  CB  HIS B 455    22235  28632  30454   -993   1568   3865       C  
ATOM   5554  CG  HIS B 455       5.821 -45.453  57.559  1.00206.19           C  
ANISOU 5554  CG  HIS B 455    21570  27357  29415   -989   1836   3794       C  
ATOM   5555  ND1 HIS B 455       6.187 -46.781  57.600  1.00204.98           N  
ANISOU 5555  ND1 HIS B 455    21443  27002  29438  -1115   1807   3864       N  
ATOM   5556  CD2 HIS B 455       6.948 -44.744  57.815  1.00200.99           C  
ANISOU 5556  CD2 HIS B 455    21212  26598  28559   -871   2087   3641       C  
ATOM   5557  CE1 HIS B 455       7.477 -46.874  57.870  1.00202.35           C  
ANISOU 5557  CE1 HIS B 455    21385  26474  29025  -1064   2025   3753       C  
ATOM   5558  NE2 HIS B 455       7.963 -45.652  58.005  1.00201.74           N  
ANISOU 5558  NE2 HIS B 455    21482  26455  28715   -926   2182   3614       N  
ATOM   5559  N   VAL B 456       2.683 -42.173  57.501  1.00216.45           N  
ANISOU 5559  N   VAL B 456    22160  29663  30418   -693   1263   3584       N  
ATOM   5560  CA  VAL B 456       2.679 -40.790  57.051  1.00199.92           C  
ANISOU 5560  CA  VAL B 456    20073  27658  28230   -463   1377   3575       C  
ATOM   5561  C   VAL B 456       2.944 -39.894  58.248  1.00188.39           C  
ANISOU 5561  C   VAL B 456    18749  26371  26460   -432   1405   3219       C  
ATOM   5562  O   VAL B 456       2.304 -40.024  59.298  1.00188.97           O  
ANISOU 5562  O   VAL B 456    18708  26652  26440   -551   1174   2942       O  
ATOM   5563  CB  VAL B 456       1.345 -40.445  56.374  1.00196.53           C  
ANISOU 5563  CB  VAL B 456    19251  27472  27948   -357    968   3634       C  
ATOM   5564  CG1 VAL B 456       0.216 -41.143  57.084  1.00200.65           C  
ANISOU 5564  CG1 VAL B 456    19552  28232  28453   -532    516   3427       C  
ATOM   5565  CG2 VAL B 456       1.118 -38.934  56.378  1.00190.54           C  
ANISOU 5565  CG2 VAL B 456    18557  26880  26958    -83    919   3414       C  
ATOM   5566  N   CYS B 457       3.882 -38.978  58.085  1.00172.16           N  
ANISOU 5566  N   CYS B 457    16969  24183  24260   -282   1712   3211       N  
ATOM   5567  CA  CYS B 457       4.166 -37.889  59.005  1.00167.55           C  
ANISOU 5567  CA  CYS B 457    16520  23719  23424   -236   1732   2908       C  
ATOM   5568  C   CYS B 457       3.865 -36.582  58.288  1.00163.57           C  
ANISOU 5568  C   CYS B 457    15955  23332  22862     29   1781   2959       C  
ATOM   5569  O   CYS B 457       3.248 -36.564  57.225  1.00175.67           O  
ANISOU 5569  O   CYS B 457    17275  24916  24556    184   1722   3186       O  
ATOM   5570  CB  CYS B 457       5.611 -37.964  59.501  1.00174.82           C  
ANISOU 5570  CB  CYS B 457    17838  24376  24208   -293   1970   2820       C  
ATOM   5571  SG  CYS B 457       6.146 -39.626  59.951  1.00186.07           S  
ANISOU 5571  SG  CYS B 457    19331  25617  25748   -514   1942   2847       S  
ATOM   5572  N   TRP B 458       4.286 -35.476  58.893  1.00156.06           N  
ANISOU 5572  N   TRP B 458    15178  22421  21698     95   1853   2736       N  
ATOM   5573  CA  TRP B 458       3.986 -34.178  58.317  1.00156.92           C  
ANISOU 5573  CA  TRP B 458    15233  22664  21726    374   1874   2747       C  
ATOM   5574  C   TRP B 458       5.183 -33.267  58.516  1.00166.77           C  
ANISOU 5574  C   TRP B 458    16895  23725  22746    442   2151   2671       C  
ATOM   5575  O   TRP B 458       5.707 -33.166  59.627  1.00186.30           O  
ANISOU 5575  O   TRP B 458    19521  26147  25118    260   2112   2422       O  
ATOM   5576  CB  TRP B 458       2.734 -33.571  58.955  1.00151.12           C  
ANISOU 5576  CB  TRP B 458    14164  22258  20996    385   1499   2449       C  
ATOM   5577  CG  TRP B 458       2.555 -32.139  58.636  1.00147.43           C  
ANISOU 5577  CG  TRP B 458    13679  21920  20417    673   1475   2365       C  
ATOM   5578  CD1 TRP B 458       2.994 -31.065  59.351  1.00141.13           C  
ANISOU 5578  CD1 TRP B 458    13068  21105  19450    678   1567   2139       C  
ATOM   5579  CD2 TRP B 458       1.882 -31.617  57.491  1.00145.57           C  
ANISOU 5579  CD2 TRP B 458    13235  21830  20245   1050   1285   2496       C  
ATOM   5580  NE1 TRP B 458       2.632 -29.901  58.714  1.00137.97           N  
ANISOU 5580  NE1 TRP B 458    12590  20848  18984   1017   1485   2124       N  
ATOM   5581  CE2 TRP B 458       1.946 -30.216  57.570  1.00144.33           C  
ANISOU 5581  CE2 TRP B 458    13164  21756  19917   1290   1284   2323       C  
ATOM   5582  CE3 TRP B 458       1.229 -32.204  56.404  1.00136.16           C  
ANISOU 5582  CE3 TRP B 458    12327  20344  19063   1137    927   2483       C  
ATOM   5583  CZ2 TRP B 458       1.382 -29.390  56.598  1.00145.23           C  
ANISOU 5583  CZ2 TRP B 458    13661  21654  19866   1622    911   2126       C  
ATOM   5584  CZ3 TRP B 458       0.669 -31.386  55.445  1.00139.27           C  
ANISOU 5584  CZ3 TRP B 458    13289  20404  19222   1407    521   2208       C  
ATOM   5585  CH2 TRP B 458       0.747 -29.993  55.548  1.00142.89           C  
ANISOU 5585  CH2 TRP B 458    13833  20942  19518   1644    506   2034       C  
ATOM   5586  N   GLU B 459       5.607 -32.602  57.447  1.00145.93           N  
ANISOU 5586  N   GLU B 459    14469  20958  20020    718   2428   2865       N  
ATOM   5587  CA  GLU B 459       6.698 -31.665  57.624  1.00154.29           C  
ANISOU 5587  CA  GLU B 459    15951  21835  20837    776   2629   2759       C  
ATOM   5588  C   GLU B 459       6.209 -30.239  57.416  1.00163.58           C  
ANISOU 5588  C   GLU B 459    17058  23225  21871   1065   2585   2686       C  
ATOM   5589  O   GLU B 459       5.400 -29.986  56.518  1.00166.98           O  
ANISOU 5589  O   GLU B 459    17290  23809  22345   1386   2566   2814       O  
ATOM   5590  CB  GLU B 459       7.851 -31.948  56.651  1.00166.21           C  
ANISOU 5590  CB  GLU B 459    17979  22911  22262    853   3029   2940       C  
ATOM   5591  CG  GLU B 459       8.353 -33.382  56.659  1.00179.49           C  
ANISOU 5591  CG  GLU B 459    19727  24357  24114    625   3071   3008       C  
ATOM   5592  CD  GLU B 459       8.839 -33.818  58.028  1.00183.51           C  
ANISOU 5592  CD  GLU B 459    20160  24931  24634    352   2815   2755       C  
ATOM   5593  OE1 GLU B 459       8.487 -34.938  58.456  1.00186.48           O  
ANISOU 5593  OE1 GLU B 459    20319  25363  25172    171   2668   2762       O  
ATOM   5594  OE2 GLU B 459       9.566 -33.037  58.679  1.00181.25           O  
ANISOU 5594  OE2 GLU B 459    20060  24629  24179    324   2769   2547       O  
ATOM   5595  N   PRO B 460       6.691 -29.287  58.217  1.00164.30           N  
ANISOU 5595  N   PRO B 460    17303  23318  21805   1002   2529   2457       N  
ATOM   5596  CA  PRO B 460       6.227 -27.903  58.051  1.00176.18           C  
ANISOU 5596  CA  PRO B 460    18743  25019  23180   1282   2462   2366       C  
ATOM   5597  C   PRO B 460       6.769 -27.254  56.793  1.00198.93           C  
ANISOU 5597  C   PRO B 460    22036  27717  25830   1667   2802   2556       C  
ATOM   5598  O   PRO B 460       6.129 -26.345  56.250  1.00192.17           O  
ANISOU 5598  O   PRO B 460    21235  26938  24844   2010   2625   2445       O  
ATOM   5599  CB  PRO B 460       6.735 -27.212  59.322  1.00163.50           C  
ANISOU 5599  CB  PRO B 460    17250  23375  21500   1044   2353   2081       C  
ATOM   5600  CG  PRO B 460       7.929 -28.007  59.713  1.00158.14           C  
ANISOU 5600  CG  PRO B 460    16875  22399  20813    784   2461   2081       C  
ATOM   5601  CD  PRO B 460       7.661 -29.426  59.317  1.00163.11           C  
ANISOU 5601  CD  PRO B 460    17373  22996  21607    704   2490   2250       C  
ATOM   5602  N   GLN B 461       7.940 -27.688  56.319  1.00178.94           N  
ANISOU 5602  N   GLN B 461    20029  24773  23186   1577   3120   2677       N  
ATOM   5603  CA  GLN B 461       8.487 -27.126  55.092  1.00188.32           C  
ANISOU 5603  CA  GLN B 461    21880  25636  24037   1879   3480   2775       C  
ATOM   5604  C   GLN B 461       7.644 -27.540  53.900  1.00177.83           C  
ANISOU 5604  C   GLN B 461    21081  23879  22605   1931   2983   2568       C  
ATOM   5605  O   GLN B 461       7.616 -26.839  52.882  1.00186.79           O  
ANISOU 5605  O   GLN B 461    22951  24615  23404   2099   2764   2380       O  
ATOM   5606  CB  GLN B 461       9.933 -27.575  54.896  1.00198.99           C  
ANISOU 5606  CB  GLN B 461    23763  26513  25333   1646   3651   2758       C  
ATOM   5607  CG  GLN B 461      10.831 -27.309  56.084  1.00206.48           C  
ANISOU 5607  CG  GLN B 461    24578  27492  26383   1362   3387   2542       C  
ATOM   5608  CD  GLN B 461      10.734 -28.391  57.145  1.00211.01           C  
ANISOU 5608  CD  GLN B 461    24746  28206  27223   1042   3162   2469       C  
ATOM   5609  OE1 GLN B 461      10.125 -29.441  56.927  1.00214.64           O  
ANISOU 5609  OE1 GLN B 461    24996  28709  27851    999   3191   2601       O  
ATOM   5610  NE2 GLN B 461      11.332 -28.139  58.301  1.00211.19           N  
ANISOU 5610  NE2 GLN B 461    24699  28274  27268    865   2966   2313       N  
ATOM   5611  N   ALA B 462       6.951 -28.672  54.014  1.00182.94           N  
ANISOU 5611  N   ALA B 462    21373  24605  23532   1770   2785   2609       N  
ATOM   5612  CA  ALA B 462       6.081 -29.176  52.967  1.00147.21           C  
ANISOU 5612  CA  ALA B 462    17280  19710  18945   1789   2301   2437       C  
ATOM   5613  C   ALA B 462       4.705 -28.542  53.000  1.00130.66           C  
ANISOU 5613  C   ALA B 462    14953  17812  16878   1943   1672   2191       C  
ATOM   5614  O   ALA B 462       3.769 -29.088  52.407  1.00123.16           O  
ANISOU 5614  O   ALA B 462    14128  16688  15978   1923   1220   2078       O  
ATOM   5615  CB  ALA B 462       5.957 -30.698  53.076  1.00135.59           C  
ANISOU 5615  CB  ALA B 462    15528  18225  17763   1544   2361   2600       C  
ATOM   5616  N   GLN B 463       4.557 -27.418  53.702  1.00138.19           N  
ANISOU 5616  N   GLN B 463    15552  19129  17825   2091   1633   2105       N  
ATOM   5617  CA  GLN B 463       3.276 -26.721  53.737  1.00144.68           C  
ANISOU 5617  CA  GLN B 463    16144  20126  18702   2260   1038   1842       C  
ATOM   5618  C   GLN B 463       2.899 -26.225  52.346  1.00149.93           C  
ANISOU 5618  C   GLN B 463    17683  20220  19063   2430    587   1625       C  
ATOM   5619  O   GLN B 463       1.874 -26.624  51.784  1.00168.62           O  
ANISOU 5619  O   GLN B 463    20142  22431  21496   2432     79   1493       O  
ATOM   5620  CB  GLN B 463       3.331 -25.571  54.744  1.00153.50           C  
ANISOU 5620  CB  GLN B 463    16747  21711  19864   2386   1143   1782       C  
ATOM   5621  CG  GLN B 463       2.171 -24.595  54.660  1.00162.08           C  
ANISOU 5621  CG  GLN B 463    17714  22896  20975   2614    551   1469       C  
ATOM   5622  CD  GLN B 463       2.298 -23.464  55.664  1.00170.16           C  
ANISOU 5622  CD  GLN B 463    18235  24371  22046   2735    696   1399       C  
ATOM   5623  OE1 GLN B 463       1.483 -22.539  55.683  1.00176.71           O  
ANISOU 5623  OE1 GLN B 463    18771  25478  22893   2627   1239   1605       O  
ATOM   5624  NE2 GLN B 463       3.321 -23.532  56.506  1.00168.14           N  
ANISOU 5624  NE2 GLN B 463    17878  24182  21827   2955    204   1108       N  
ATOM   5625  N   GLY B 464       3.717 -25.334  51.783  1.00137.48           N  
ANISOU 5625  N   GLY B 464    16761  18332  17145   2556    750   1593       N  
ATOM   5626  CA  GLY B 464       3.466 -24.734  50.485  1.00133.68           C  
ANISOU 5626  CA  GLY B 464    17146  17311  16335   2690    334   1400       C  
ATOM   5627  C   GLY B 464       3.235 -25.720  49.355  1.00135.73           C  
ANISOU 5627  C   GLY B 464    17993  17082  16498   2555    142   1395       C  
ATOM   5628  O   GLY B 464       2.218 -25.652  48.661  1.00148.80           O  
ANISOU 5628  O   GLY B 464    19893  18516  18129   2612   -451   1220       O  
ATOM   5629  N   ARG B 465       4.190 -26.631  49.156  1.00132.53           N  
ANISOU 5629  N   ARG B 465    17823  16490  16043   2372    643   1584       N  
ATOM   5630  CA  ARG B 465       4.091 -27.639  48.105  1.00123.09           C  
ANISOU 5630  CA  ARG B 465    17190  14825  14756   2221    538   1582       C  
ATOM   5631  C   ARG B 465       2.770 -28.404  48.178  1.00123.97           C  
ANISOU 5631  C   ARG B 465    16888  15063  15151   2167     37   1526       C  
ATOM   5632  O   ARG B 465       2.053 -28.535  47.179  1.00136.25           O  
ANISOU 5632  O   ARG B 465    18951  16243  16575   2166   -441   1388       O  
ATOM   5633  CB  ARG B 465       5.263 -28.606  48.252  1.00131.60           C  
ANISOU 5633  CB  ARG B 465    18289  15829  15884   2030   1198   1804       C  
ATOM   5634  CG  ARG B 465       6.612 -28.108  47.769  1.00134.21           C  
ANISOU 5634  CG  ARG B 465    19265  15854  15875   2037   1684   1843       C  
ATOM   5635  CD  ARG B 465       7.403 -29.299  47.257  1.00134.62           C  
ANISOU 5635  CD  ARG B 465    19647  15569  15932   1830   2102   1958       C  
ATOM   5636  NE  ARG B 465       8.645 -28.937  46.592  1.00136.06           N  
ANISOU 5636  NE  ARG B 465    20540  15388  15768   1810   2544   1957       N  
ATOM   5637  CZ  ARG B 465       8.782 -28.935  45.275  1.00150.30           C  
ANISOU 5637  CZ  ARG B 465    23244  16651  17213   1754   2435   1806       C  
ATOM   5638  NH1 ARG B 465       9.936 -28.600  44.717  1.00164.93           N  
ANISOU 5638  NH1 ARG B 465    25711  18208  18745   1716   2863   1797       N  
ATOM   5639  NH2 ARG B 465       7.750 -29.272  44.517  1.00155.15           N  
ANISOU 5639  NH2 ARG B 465    24141  17026  17783   1718   1892   1663       N  
ATOM   5640  N   MET B 466       2.434 -28.913  49.366  1.00128.14           N  
ANISOU 5640  N   MET B 466    16496  16129  16062   2100    134   1639       N  
ATOM   5641  CA  MET B 466       1.232 -29.726  49.530  1.00132.75           C  
ANISOU 5641  CA  MET B 466    16628  16883  16928   2019   -297   1608       C  
ATOM   5642  C   MET B 466      -0.032 -28.926  49.231  1.00131.74           C  
ANISOU 5642  C   MET B 466    16503  16762  16790   2202   -988   1357       C  
ATOM   5643  O   MET B 466      -0.893 -29.366  48.460  1.00147.32           O  
ANISOU 5643  O   MET B 466    18761  18462  18752   2173  -1466   1265       O  
ATOM   5644  CB  MET B 466       1.185 -30.294  50.949  1.00133.82           C  
ANISOU 5644  CB  MET B 466    15752  17643  17451   1891    -38   1778       C  
ATOM   5645  CG  MET B 466       2.058 -31.521  51.165  1.00131.75           C  
ANISOU 5645  CG  MET B 466    15404  17337  17316   1651    466   2040       C  
ATOM   5646  SD  MET B 466       1.332 -33.000  50.442  1.00142.94           S  
ANISOU 5646  SD  MET B 466    16995  18462  18852   1467    141   2066       S  
ATOM   5647  CE  MET B 466      -0.196 -33.093  51.372  1.00142.92           C  
ANISOU 5647  CE  MET B 466    16054  19061  19188   1455   -383   1992       C  
ATOM   5648  N   CYS B 467      -0.165 -27.748  49.848  1.00 97.02           N  
ANISOU 5648  N   CYS B 467    11777  12671  12416   2388  -1057   1243       N  
ATOM   5649  CA  CYS B 467      -1.347 -26.919  49.632  1.00111.30           C  
ANISOU 5649  CA  CYS B 467    13530  14493  14266   2579  -1715    989       C  
ATOM   5650  C   CYS B 467      -1.483 -26.490  48.177  1.00128.95           C  
ANISOU 5650  C   CYS B 467    16760  16074  16160   2655  -2116    855       C  
ATOM   5651  O   CYS B 467      -2.585 -26.524  47.616  1.00127.98           O  
ANISOU 5651  O   CYS B 467    16753  15781  16094   2695  -2727    710       O  
ATOM   5652  CB  CYS B 467      -1.307 -25.701  50.553  1.00121.41           C  
ANISOU 5652  CB  CYS B 467    14312  16191  15626   2765  -1652    886       C  
ATOM   5653  SG  CYS B 467      -1.251 -26.118  52.298  1.00148.25           S  
ANISOU 5653  SG  CYS B 467    16520  20394  19415   2638  -1229   1023       S  
ATOM   5654  N   ALA B 468      -0.378 -26.076  47.550  1.00115.66           N  
ANISOU 5654  N   ALA B 468    15806  14022  14117   2657  -1790    904       N  
ATOM   5655  CA  ALA B 468      -0.428 -25.672  46.148  1.00126.62           C  
ANISOU 5655  CA  ALA B 468    18183  14785  15141   2678  -2147    788       C  
ATOM   5656  C   ALA B 468      -0.880 -26.820  45.253  1.00129.76           C  
ANISOU 5656  C   ALA B 468    18981  14815  15508   2491  -2370    815       C  
ATOM   5657  O   ALA B 468      -1.655 -26.614  44.310  1.00148.87           O  
ANISOU 5657  O   ALA B 468    21899  16863  17803   2508  -2952    679       O  
ATOM   5658  CB  ALA B 468       0.937 -25.150  45.703  1.00128.08           C  
ANISOU 5658  CB  ALA B 468    19042  14685  14936   2665  -1675    852       C  
ATOM   5659  N   LEU B 469      -0.386 -28.031  45.518  1.00114.54           N  
ANISOU 5659  N   LEU B 469    16862  12964  13695   2300  -1923    996       N  
ATOM   5660  CA  LEU B 469      -0.868 -29.203  44.798  1.00107.20           C  
ANISOU 5660  CA  LEU B 469    16206  11739  12785   2119  -2127   1027       C  
ATOM   5661  C   LEU B 469      -2.370 -29.374  44.994  1.00108.31           C  
ANISOU 5661  C   LEU B 469    15864  12080  13208   2168  -2774    929       C  
ATOM   5662  O   LEU B 469      -3.106 -29.643  44.037  1.00136.56           O  
ANISOU 5662  O   LEU B 469    19920  15279  16686   2114  -3264    849       O  
ATOM   5663  CB  LEU B 469      -0.109 -30.448  45.254  1.00 98.31           C  
ANISOU 5663  CB  LEU B 469    14803  10736  11815   1924  -1540   1241       C  
ATOM   5664  CG  LEU B 469      -0.611 -31.779  44.700  1.00115.17           C  
ANISOU 5664  CG  LEU B 469    17082  12640  14037   1729  -1714   1292       C  
ATOM   5665  CD1 LEU B 469      -0.461 -31.796  43.187  1.00127.58           C  
ANISOU 5665  CD1 LEU B 469    19729  13534  15211   1648  -1884   1192       C  
ATOM   5666  CD2 LEU B 469       0.149 -32.936  45.324  1.00122.48           C  
ANISOU 5666  CD2 LEU B 469    17615  13740  15183   1554  -1142   1508       C  
ATOM   5667  N   TYR B 470      -2.841 -29.244  46.239  1.00100.83           N  
ANISOU 5667  N   TYR B 470    13960  11735  12614   2249  -2776    934       N  
ATOM   5668  CA  TYR B 470      -4.278 -29.300  46.494  1.00103.39           C  
ANISOU 5668  CA  TYR B 470    13767  12295  13220   2307  -3384    812       C  
ATOM   5669  C   TYR B 470      -5.028 -28.236  45.698  1.00116.77           C  
ANISOU 5669  C   TYR B 470    15922  13671  14774   2487  -4025    587       C  
ATOM   5670  O   TYR B 470      -6.043 -28.529  45.056  1.00130.58           O  
ANISOU 5670  O   TYR B 470    17851  15197  16568   2462  -4594    508       O  
ATOM   5671  CB  TYR B 470      -4.571 -29.140  47.987  1.00105.95           C  
ANISOU 5671  CB  TYR B 470    13005  13339  13911   2362  -3242    818       C  
ATOM   5672  CG  TYR B 470      -6.054 -29.007  48.262  1.00109.50           C  
ANISOU 5672  CG  TYR B 470    12910  14050  14647   2446  -3872    644       C  
ATOM   5673  CD1 TYR B 470      -6.866 -30.132  48.337  1.00103.35           C  
ANISOU 5673  CD1 TYR B 470    11796  13391  14082   2286  -4103    704       C  
ATOM   5674  CD2 TYR B 470      -6.649 -27.758  48.420  1.00109.48           C  
ANISOU 5674  CD2 TYR B 470    12734  14154  14708   2684  -4250    412       C  
ATOM   5675  CE1 TYR B 470      -8.224 -30.020  48.570  1.00104.36           C  
ANISOU 5675  CE1 TYR B 470    11424  13757  14471   2357  -4677    540       C  
ATOM   5676  CE2 TYR B 470      -8.008 -27.637  48.652  1.00104.17           C  
ANISOU 5676  CE2 TYR B 470    11551  13704  14325   2765  -4826    233       C  
ATOM   5677  CZ  TYR B 470      -8.789 -28.772  48.727  1.00106.72           C  
ANISOU 5677  CZ  TYR B 470    11543  14158  14848   2598  -5030    298       C  
ATOM   5678  OH  TYR B 470     -10.139 -28.658  48.962  1.00117.04           O  
ANISOU 5678  OH  TYR B 470    12327  15697  16445   2672  -5596    116       O  
ATOM   5679  N   ALA B 471      -4.557 -26.986  45.748  1.00124.68           N  
ANISOU 5679  N   ALA B 471    17105  14647  15621   2665  -3965    491       N  
ATOM   5680  CA  ALA B 471      -5.226 -25.910  45.019  1.00120.58           C  
ANISOU 5680  CA  ALA B 471    17018  13811  14987   2834  -4596    283       C  
ATOM   5681  C   ALA B 471      -5.224 -26.187  43.523  1.00118.67           C  
ANISOU 5681  C   ALA B 471    17811  12880  14398   2700  -4884    287       C  
ATOM   5682  O   ALA B 471      -6.246 -26.019  42.848  1.00123.93           O  
ANISOU 5682  O   ALA B 471    18716  13282  15091   2728  -5553    167       O  
ATOM   5683  CB  ALA B 471      -4.568 -24.567  45.316  1.00119.97           C  
ANISOU 5683  CB  ALA B 471    17008  13802  14774   3025  -4429    204       C  
ATOM   5684  N   SER B 472      -4.066 -26.573  42.981  1.00113.26           N  
ANISOU 5684  N   SER B 472    17761  11891  13383   2544  -4384    417       N  
ATOM   5685  CA  SER B 472      -3.976 -26.921  41.567  1.00118.11           C  
ANISOU 5685  CA  SER B 472    19372  11864  13642   2368  -4581    417       C  
ATOM   5686  C   SER B 472      -5.018 -27.966  41.196  1.00122.43           C  
ANISOU 5686  C   SER B 472    19850  12309  14359   2237  -4995    432       C  
ATOM   5687  O   SER B 472      -5.752 -27.813  40.213  1.00134.03           O  
ANISOU 5687  O   SER B 472    21867  13363  15696   2195  -5588    344       O  
ATOM   5688  CB  SER B 472      -2.572 -27.440  41.258  1.00117.42           C  
ANISOU 5688  CB  SER B 472    19780  11573  13262   2195  -3872    553       C  
ATOM   5689  OG  SER B 472      -1.588 -26.472  41.569  1.00117.73           O  
ANISOU 5689  OG  SER B 472    19912  11696  13124   2308  -3491    550       O  
ATOM   5690  N   LEU B 473      -5.086 -29.046  41.973  1.00110.43           N  
ANISOU 5690  N   LEU B 473    17669  11160  13129   2153  -4698    558       N  
ATOM   5691  CA  LEU B 473      -6.071 -30.090  41.719  1.00112.66           C  
ANISOU 5691  CA  LEU B 473    17822  11396  13589   2024  -5071    589       C  
ATOM   5692  C   LEU B 473      -7.492 -29.542  41.815  1.00115.18           C  
ANISOU 5692  C   LEU B 473    17777  11839  14146   2176  -5822    435       C  
ATOM   5693  O   LEU B 473      -8.328 -29.788  40.939  1.00118.48           O  
ANISOU 5693  O   LEU B 473    18608  11900  14509   2103  -6378    391       O  
ATOM   5694  CB  LEU B 473      -5.858 -31.248  42.694  1.00110.29           C  
ANISOU 5694  CB  LEU B 473    16784  11538  13582   1913  -4617    757       C  
ATOM   5695  CG  LEU B 473      -4.619 -32.097  42.392  1.00108.72           C  
ANISOU 5695  CG  LEU B 473    17006  11109  13195   1719  -3969    913       C  
ATOM   5696  CD1 LEU B 473      -4.552 -33.310  43.300  1.00127.44           C  
ANISOU 5696  CD1 LEU B 473    18648  13876  15895   1589  -3634   1088       C  
ATOM   5697  CD2 LEU B 473      -4.604 -32.523  40.937  1.00111.68           C  
ANISOU 5697  CD2 LEU B 473    18380  10820  13232   1550  -4165    884       C  
ATOM   5698  N   ALA B 474      -7.786 -28.797  42.882  1.00113.78           N  
ANISOU 5698  N   ALA B 474    16816  12166  14249   2382  -5847    347       N  
ATOM   5699  CA  ALA B 474      -9.146 -28.313  43.090  1.00119.40           C  
ANISOU 5699  CA  ALA B 474    17067  13046  15253   2534  -6526    178       C  
ATOM   5700  C   ALA B 474      -9.581 -27.330  42.006  1.00119.42           C  
ANISOU 5700  C   ALA B 474    17802  12521  15052   2629  -7143     27       C  
ATOM   5701  O   ALA B 474     -10.776 -27.227  41.710  1.00122.52           O  
ANISOU 5701  O   ALA B 474    18099  12825  15627   2680  -7812    -81       O  
ATOM   5702  CB  ALA B 474      -9.271 -27.669  44.470  1.00133.38           C  
ANISOU 5702  CB  ALA B 474    17858  15469  17353   2723  -6364     87       C  
ATOM   5703  N   LEU B 475      -8.643 -26.580  41.415  1.00118.87           N  
ANISOU 5703  N   LEU B 475    18454  12098  14614   2644  -6954     20       N  
ATOM   5704  CA  LEU B 475      -9.031 -25.643  40.362  1.00122.11           C  
ANISOU 5704  CA  LEU B 475    19594  11989  14815   2697  -7568   -107       C  
ATOM   5705  C   LEU B 475      -9.251 -26.337  39.020  1.00145.35           C  
ANISOU 5705  C   LEU B 475    23418  14333  17473   2448  -7871    -39       C  
ATOM   5706  O   LEU B 475     -10.179 -25.984  38.282  1.00158.19           O  
ANISOU 5706  O   LEU B 475    25374  15623  19109   2452  -8588   -127       O  
ATOM   5707  CB  LEU B 475      -7.989 -24.534  40.229  1.00120.57           C  
ANISOU 5707  CB  LEU B 475    19846  11650  14316   2787  -7297   -142       C  
ATOM   5708  CG  LEU B 475      -7.988 -23.494  41.348  1.00118.65           C  
ANISOU 5708  CG  LEU B 475    18860  11886  14334   3066  -7221   -262       C  
ATOM   5709  CD1 LEU B 475      -6.972 -22.402  41.053  1.00117.50           C  
ANISOU 5709  CD1 LEU B 475    19282  11523  13840   3134  -7015   -283       C  
ATOM   5710  CD2 LEU B 475      -9.377 -22.905  41.520  1.00121.54           C  
ANISOU 5710  CD2 LEU B 475    18761  12346  15074   3256  -7975   -458       C  
ATOM   5711  N   LEU B 476      -8.411 -27.317  38.682  1.00141.58           N  
ANISOU 5711  N   LEU B 476    23334  13706  16753   2220  -7343    113       N  
ATOM   5712  CA  LEU B 476      -8.550 -28.001  37.397  1.00133.50           C  
ANISOU 5712  CA  LEU B 476    23177  12113  15435   1958  -7577    167       C  
ATOM   5713  C   LEU B 476      -9.803 -28.866  37.348  1.00146.20           C  
ANISOU 5713  C   LEU B 476    24458  13768  17325   1895  -8063    189       C  
ATOM   5714  O   LEU B 476     -10.487 -28.911  36.319  1.00166.69           O  
ANISOU 5714  O   LEU B 476    27649  15904  19783   1773  -8639    166       O  
ATOM   5715  CB  LEU B 476      -7.309 -28.846  37.109  1.00125.02           C  
ANISOU 5715  CB  LEU B 476    22548  10887  14068   1740  -6849    296       C  
ATOM   5716  CG  LEU B 476      -5.960 -28.127  37.120  1.00122.48           C  
ANISOU 5716  CG  LEU B 476    22586  10510  13441   1768  -6295    293       C  
ATOM   5717  CD1 LEU B 476      -4.807 -29.084  36.833  1.00120.99           C  
ANISOU 5717  CD1 LEU B 476    22783  10167  13019   1544  -5585    407       C  
ATOM   5718  CD2 LEU B 476      -5.974 -26.996  36.115  1.00126.03           C  
ANISOU 5718  CD2 LEU B 476    23868  10483  13534   1758  -6742    181       C  
ATOM   5719  N   SER B 477     -10.106 -29.572  38.440  1.00138.73           N  
ANISOU 5719  N   SER B 477    22582  13370  16760   1952  -7842    245       N  
ATOM   5720  CA  SER B 477     -11.272 -30.452  38.469  1.00129.07           C  
ANISOU 5720  CA  SER B 477    20996  12240  15805   1881  -8270    278       C  
ATOM   5721  C   SER B 477     -12.569 -29.704  38.179  1.00134.80           C  
ANISOU 5721  C   SER B 477    21651  12855  16711   2017  -9118    132       C  
ATOM   5722  O   SER B 477     -13.479 -30.258  37.553  1.00143.83           O  
ANISOU 5722  O   SER B 477    23000  13755  17891   1898  -9627    157       O  
ATOM   5723  CB  SER B 477     -11.368 -31.159  39.824  1.00127.14           C  
ANISOU 5723  CB  SER B 477    19687  12671  15948   1926  -7902    348       C  
ATOM   5724  OG  SER B 477     -11.508 -30.234  40.893  1.00138.56           O  
ANISOU 5724  OG  SER B 477    20367  14612  17667   2173  -7874    229       O  
ATOM   5725  N   GLY B 478     -12.683 -28.455  38.633  1.00132.21           N  
ANISOU 5725  N   GLY B 478    21021  12696  16516   2265  -9291    -23       N  
ATOM   5726  CA  GLY B 478     -13.929 -27.728  38.437  1.00135.54           C  
ANISOU 5726  CA  GLY B 478    21291  13029  17179   2414 -10102   -178       C  
ATOM   5727  C   GLY B 478     -14.261 -27.459  36.979  1.00157.29           C  
ANISOU 5727  C   GLY B 478    25065  15062  19634   2273 -10699   -179       C  
ATOM   5728  O   GLY B 478     -15.422 -27.551  36.571  1.00168.59           O  
ANISOU 5728  O   GLY B 478    26484  16326  21246   2260 -11382   -216       O  
ATOM   5729  N   LEU B 479     -13.255 -27.124  36.172  1.00152.47           N  
ANISOU 5729  N   LEU B 479    25353  14018  18560   2145 -10459   -136       N  
ATOM   5730  CA  LEU B 479     -13.488 -26.780  34.773  1.00148.78           C  
ANISOU 5730  CA  LEU B 479    25907  12860  17763   1971 -11015   -137       C  
ATOM   5731  C   LEU B 479     -13.367 -27.960  33.807  1.00155.13           C  
ANISOU 5731  C   LEU B 479    27419  13267  18257   1626 -10940     11       C  
ATOM   5732  O   LEU B 479     -13.709 -27.804  32.629  1.00180.55           O  
ANISOU 5732  O   LEU B 479    31465  15919  21218   1436 -11455     22       O  
ATOM   5733  CB  LEU B 479     -12.559 -25.636  34.342  1.00142.47           C  
ANISOU 5733  CB  LEU B 479    25745  11778  16608   1996 -10899   -194       C  
ATOM   5734  CG  LEU B 479     -11.085 -25.614  34.736  1.00138.48           C  
ANISOU 5734  CG  LEU B 479    25328  11449  15839   1986 -10028   -144       C  
ATOM   5735  CD1 LEU B 479     -10.249 -26.278  33.670  1.00139.00           C  
ANISOU 5735  CD1 LEU B 479    26374  11045  15395   1647  -9703    -36       C  
ATOM   5736  CD2 LEU B 479     -10.632 -24.183  34.958  1.00137.67           C  
ANISOU 5736  CD2 LEU B 479    25267  11368  15673   2190 -10063   -258       C  
ATOM   5737  N   SER B 480     -12.898 -29.126  34.258  1.00141.82           N  
ANISOU 5737  N   SER B 480    25444  11848  16593   1526 -10335    126       N  
ATOM   5738  CA  SER B 480     -12.745 -30.278  33.370  1.00149.88           C  
ANISOU 5738  CA  SER B 480    27117  12495  17335   1203 -10228    251       C  
ATOM   5739  C   SER B 480     -13.989 -31.169  33.356  1.00173.59           C  
ANISOU 5739  C   SER B 480    29778  15558  20621   1141 -10708    310       C  
ATOM   5740  O   SER B 480     -14.595 -31.378  32.300  1.00170.62           O  
ANISOU 5740  O   SER B 480    30056  14699  20074    943 -11235    341       O  
ATOM   5741  CB  SER B 480     -11.508 -31.089  33.779  1.00148.84           C  
ANISOU 5741  CB  SER B 480    26921  12556  17074   1111  -9321    343       C  
ATOM   5742  OG  SER B 480     -11.161 -32.054  32.797  1.00158.39           O  
ANISOU 5742  OG  SER B 480    28897  13329  17955    791  -9163    429       O  
ATOM   5743  N   GLN B 481     -14.381 -31.701  34.515  1.00188.42           N  
ANISOU 5743  N   GLN B 481    30647  18026  22918   1286 -10540    333       N  
ATOM   5744  CA  GLN B 481     -15.560 -32.566  34.598  1.00187.01           C  
ANISOU 5744  CA  GLN B 481    30072  17965  23019   1229 -10975    392       C  
ATOM   5745  C   GLN B 481     -16.214 -32.550  35.983  1.00179.93           C  
ANISOU 5745  C   GLN B 481    27954  17772  22638   1466 -10990    338       C  
ATOM   5746  O   GLN B 481     -15.553 -32.737  37.006  1.00171.81           O  
ANISOU 5746  O   GLN B 481    26312  17227  21739   1547 -10382    359       O  
ATOM   5747  CB  GLN B 481     -15.195 -34.004  34.209  1.00188.88           C  
ANISOU 5747  CB  GLN B 481    30633  18057  23078    948 -10616    557       C  
ATOM   5748  CG  GLN B 481     -14.029 -34.603  34.989  1.00183.17           C  
ANISOU 5748  CG  GLN B 481    29566  17678  22353    937  -9740    630       C  
ATOM   5749  CD  GLN B 481     -14.473 -35.544  36.097  1.00176.73           C  
ANISOU 5749  CD  GLN B 481    27765  17445  21940    972  -9588    717       C  
ATOM   5750  OE1 GLN B 481     -15.633 -35.539  36.508  1.00183.47           O  
ANISOU 5750  OE1 GLN B 481    28032  18565  23114   1066 -10093    687       O  
ATOM   5751  NE2 GLN B 481     -13.547 -36.364  36.579  1.00166.31           N  
ANISOU 5751  NE2 GLN B 481    26258  16320  20611    881  -8899    827       N  
TER    5752      GLN B 481                                                      
ATOM   5753  N   MET C   1       8.938 -47.280  10.952  1.00224.53           N  
ANISOU 5753  N   MET C   1    29595  23788  31930   2747   3287   1441       N  
ATOM   5754  CA  MET C   1       7.809 -46.396  10.691  1.00219.42           C  
ANISOU 5754  CA  MET C   1    28975  23368  31025   2571   3317   1185       C  
ATOM   5755  C   MET C   1       8.278 -44.959  10.483  1.00218.33           C  
ANISOU 5755  C   MET C   1    28695  23458  30801   2582   2996   1093       C  
ATOM   5756  O   MET C   1       8.511 -44.223  11.441  1.00222.23           O  
ANISOU 5756  O   MET C   1    29253  24090  31095   2655   2716   1201       O  
ATOM   5757  CB  MET C   1       6.797 -46.460  11.841  1.00218.00           C  
ANISOU 5757  CB  MET C   1    29057  23250  30523   2518   3344   1229       C  
ATOM   5758  CG  MET C   1       5.528 -45.649  11.606  1.00212.12           C  
ANISOU 5758  CG  MET C   1    28328  22722  29547   2341   3397    928       C  
ATOM   5759  SD  MET C   1       4.381 -45.675  13.003  1.00205.57           S  
ANISOU 5759  SD  MET C   1    27783  21977  28349   2244   3436    924       S  
ATOM   5760  CE  MET C   1       5.288 -44.726  14.222  1.00199.56           C  
ANISOU 5760  CE  MET C   1    27055  21360  27409   2375   2987   1161       C  
ATOM   5761  N   GLY C   2       8.425 -44.565   9.219  1.00207.22           N  
ANISOU 5761  N   GLY C   2    27105  22088  29539   2490   3049    891       N  
ATOM   5762  CA  GLY C   2       8.764 -43.189   8.908  1.00203.66           C  
ANISOU 5762  CA  GLY C   2    26551  21834  28995   2468   2780    780       C  
ATOM   5763  C   GLY C   2       7.514 -42.333   8.906  1.00199.26           C  
ANISOU 5763  C   GLY C   2    26075  21464  28172   2345   2757    585       C  
ATOM   5764  O   GLY C   2       6.481 -42.723   8.350  1.00204.13           O  
ANISOU 5764  O   GLY C   2    26719  22069  28771   2220   3000    416       O  
ATOM   5765  N   SER C   3       7.604 -41.162   9.537  1.00185.93           N  
ANISOU 5765  N   SER C   3    24409  19950  26288   2383   2466    590       N  
ATOM   5766  CA  SER C   3       6.458 -40.266   9.650  1.00173.48           C  
ANISOU 5766  CA  SER C   3    22892  18541  24481   2289   2407    398       C  
ATOM   5767  C   SER C   3       5.884 -39.959   8.273  1.00169.56           C  
ANISOU 5767  C   SER C   3    22309  18070  24046   2158   2511    157       C  
ATOM   5768  O   SER C   3       6.598 -39.488   7.384  1.00179.48           O  
ANISOU 5768  O   SER C   3    23456  19324  25413   2133   2427    121       O  
ATOM   5769  CB  SER C   3       6.870 -38.979  10.360  1.00173.07           C  
ANISOU 5769  CB  SER C   3    22834  18655  24270   2346   2077    429       C  
ATOM   5770  OG  SER C   3       7.650 -39.269  11.507  1.00179.16           O  
ANISOU 5770  OG  SER C   3    23655  19415  25003   2468   1956    671       O  
ATOM   5771  N   ALA C   4       4.591 -40.242   8.103  1.00163.15           N  
ANISOU 5771  N   ALA C   4    21552  17289  23150   2061   2696    -20       N  
ATOM   5772  CA  ALA C   4       3.951 -40.055   6.806  1.00159.53           C  
ANISOU 5772  CA  ALA C   4    21014  16867  22734   1935   2798   -249       C  
ATOM   5773  C   ALA C   4       4.044 -38.608   6.334  1.00162.59           C  
ANISOU 5773  C   ALA C   4    21354  17380  23042   1922   2508   -347       C  
ATOM   5774  O   ALA C   4       4.342 -38.348   5.161  1.00177.06           O  
ANISOU 5774  O   ALA C   4    23113  19203  24960   1842   2501   -419       O  
ATOM   5775  CB  ALA C   4       2.491 -40.505   6.877  1.00157.19           C  
ANISOU 5775  CB  ALA C   4    20774  16615  22334   1847   3014   -449       C  
ATOM   5776  N   PHE C   5       3.776 -37.648   7.227  1.00155.42           N  
ANISOU 5776  N   PHE C   5    20500  16586  21968   1982   2276   -358       N  
ATOM   5777  CA  PHE C   5       3.876 -36.244   6.836  1.00144.21           C  
ANISOU 5777  CA  PHE C   5    19050  15259  20483   1978   2002   -442       C  
ATOM   5778  C   PHE C   5       5.270 -35.915   6.315  1.00151.59           C  
ANISOU 5778  C   PHE C   5    19930  16142  21525   1990   1888   -318       C  
ATOM   5779  O   PHE C   5       5.419 -35.078   5.419  1.00166.09           O  
ANISOU 5779  O   PHE C   5    21749  18000  23359   1926   1763   -404       O  
ATOM   5780  CB  PHE C   5       3.515 -35.342   8.012  1.00130.62           C  
ANISOU 5780  CB  PHE C   5    17379  13653  18598   2040   1796   -463       C  
ATOM   5781  CG  PHE C   5       3.501 -33.880   7.673  1.00113.96           C  
ANISOU 5781  CG  PHE C   5    15249  11618  16432   2040   1527   -564       C  
ATOM   5782  CD1 PHE C   5       2.494 -33.367   6.867  1.00112.84           C  
ANISOU 5782  CD1 PHE C   5    15095  11508  16270   1986   1488   -776       C  
ATOM   5783  CD2 PHE C   5       4.477 -33.024   8.143  1.00123.21           C  
ANISOU 5783  CD2 PHE C   5    16415  12825  17574   2097   1312   -454       C  
ATOM   5784  CE1 PHE C   5       2.457 -32.028   6.550  1.00116.89           C  
ANISOU 5784  CE1 PHE C   5    15613  12059  16742   1997   1231   -854       C  
ATOM   5785  CE2 PHE C   5       4.446 -31.681   7.825  1.00127.19           C  
ANISOU 5785  CE2 PHE C   5    16920  13375  18031   2089   1086   -550       C  
ATOM   5786  CZ  PHE C   5       3.429 -31.185   7.029  1.00121.13           C  
ANISOU 5786  CZ  PHE C   5    16161  12610  17252   2044   1041   -740       C  
ATOM   5787  N   GLU C   6       6.298 -36.552   6.876  1.00143.83           N  
ANISOU 5787  N   GLU C   6    18927  15088  20635   2069   1922   -125       N  
ATOM   5788  CA  GLU C   6       7.647 -36.436   6.332  1.00153.22           C  
ANISOU 5788  CA  GLU C   6    20034  16219  21965   2069   1861    -48       C  
ATOM   5789  C   GLU C   6       7.747 -37.115   4.975  1.00149.73           C  
ANISOU 5789  C   GLU C   6    19523  15676  21694   1939   2078   -133       C  
ATOM   5790  O   GLU C   6       8.098 -36.486   3.971  1.00154.03           O  
ANISOU 5790  O   GLU C   6    20037  16229  22258   1827   2015   -228       O  
ATOM   5791  CB  GLU C   6       8.653 -37.065   7.299  1.00174.02           C  
ANISOU 5791  CB  GLU C   6    22641  18800  24679   2205   1841    165       C  
ATOM   5792  CG  GLU C   6       9.224 -36.163   8.375  1.00189.01           C  
ANISOU 5792  CG  GLU C   6    24554  20817  26443   2307   1572    257       C  
ATOM   5793  CD  GLU C   6      10.224 -35.141   7.849  1.00199.75           C  
ANISOU 5793  CD  GLU C   6    25839  22224  27832   2278   1395    202       C  
ATOM   5794  OE1 GLU C   6      10.121 -34.709   6.680  1.00200.69           O  
ANISOU 5794  OE1 GLU C   6    25948  22319  27987   2150   1424     58       O  
ATOM   5795  OE2 GLU C   6      11.140 -34.784   8.620  1.00205.14           O  
ANISOU 5795  OE2 GLU C   6    26481  22972  28492   2372   1231    301       O  
ATOM   5796  N   ARG C   7       7.451 -38.416   4.945  1.00155.84           N  
ANISOU 5796  N   ARG C   7    20280  16346  22584   1932   2348   -103       N  
ATOM   5797  CA  ARG C   7       7.602 -39.230   3.744  1.00152.38           C  
ANISOU 5797  CA  ARG C   7    19754  15807  22337   1797   2601   -186       C  
ATOM   5798  C   ARG C   7       6.924 -38.585   2.536  1.00151.93           C  
ANISOU 5798  C   ARG C   7    19699  15833  22194   1622   2595   -388       C  
ATOM   5799  O   ARG C   7       7.485 -38.579   1.432  1.00159.99           O  
ANISOU 5799  O   ARG C   7    20650  16819  23321   1476   2656   -460       O  
ATOM   5800  CB  ARG C   7       7.067 -40.635   4.020  1.00152.90           C  
ANISOU 5800  CB  ARG C   7    19831  15765  22501   1814   2906   -149       C  
ATOM   5801  CG  ARG C   7       7.052 -41.589   2.843  1.00157.80           C  
ANISOU 5801  CG  ARG C   7    20350  16285  23322   1659   3222   -259       C  
ATOM   5802  CD  ARG C   7       7.360 -42.994   3.370  1.00164.47           C  
ANISOU 5802  CD  ARG C   7    21181  16944  24366   1744   3465   -121       C  
ATOM   5803  NE  ARG C   7       8.105 -43.831   2.433  1.00161.23           N  
ANISOU 5803  NE  ARG C   7    20610  16452  24199   1612   3653   -154       N  
ATOM   5804  CZ  ARG C   7       7.582 -44.862