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***  4S0V  ***

elNémo ID: 22040500380893449

Job options:

ID        	=	 22040500380893449
JOBID     	=	 4S0V
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 4S0V

HEADER    SIGNALING PROTEIN                       06-JAN-15   4S0V              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN OX2 OREXIN RECEPTOR BOUND TO THE       
TITLE    2 INSOMNIA DRUG SUVOREXANT                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN OREXIN RECEPTOR TYPE 2 FUSION PROTEIN TO P. ABYSII   
COMPND   3 GLYCOGEN SYNTHASE;                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP O43614 RESIDUES 3-254, 294-388, AND UNP Q9V2J8 RESIDUES
COMPND   6 218-413;                                                             
COMPND   7 SYNONYM: OX-2-R, OX2-R, OX2R, HYPOCRETIN RECEPTOR TYPE 2, GLYCOGEN   
COMPND   8 SYNTHASE;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI GE5;            
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   5 GENE: HCRTR2, PAB2292, PYRAB00770;                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: FASTBAC BACULOVIRUS;                  
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    G PROTEIN-COUPLED RECEPTOR, OREXIN NEUROTRANSMITTERS, OREXIN          
KEYWDS   2 RECEPTOR, OREXIN-A, OREXIN-B, SUVOREXANT, N-LINKED GLYCOSYLATION,    
KEYWDS   3 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YIN,P.KOLB,J.C.MOBAREC,D.M.ROSENBAUM                                
REVDAT   4   23-AUG-17 4S0V    1       SOURCE REMARK                            
REVDAT   3   25-MAR-15 4S0V    1       JRNL                                     
REVDAT   2   18-MAR-15 4S0V    1       JRNL                                     
REVDAT   1   14-JAN-15 4S0V    0                                                
SPRSDE     14-JAN-15 4S0V      4RNB                                             
JRNL        AUTH   J.YIN,J.C.MOBAREC,P.KOLB,D.M.ROSENBAUM                       
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN OX2 OREXIN RECEPTOR BOUND TO  
JRNL        TITL 2 THE INSOMNIA DRUG SUVOREXANT.                                
JRNL        REF    NATURE                        V. 519   247 2015              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25533960                                                     
JRNL        DOI    10.1038/NATURE14035                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1839)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18772                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 955                             
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 43.7170 -  4.7589    1.00     3087   162  0.1895 0.2102        
REMARK   3     2  4.7589 -  3.7779    1.00     3018   168  0.1711 0.2290        
REMARK   3     3  3.7779 -  3.3006    1.00     3029   171  0.1953 0.2437        
REMARK   3     4  3.3006 -  2.9989    1.00     3003   156  0.2202 0.2841        
REMARK   3     5  2.9989 -  2.7840    0.92     2758   146  0.2311 0.2691        
REMARK   3     6  2.7840 -  2.6199    0.65     1928   112  0.2329 0.2919        
REMARK   3     7  2.6199 -  2.5000    0.32      994    40  0.2457 0.2862        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           3939                                  
REMARK   3   ANGLE     :  0.745           5331                                  
REMARK   3   CHIRALITY :  0.025            611                                  
REMARK   3   PLANARITY :  0.003            648                                  
REMARK   3   DIHEDRAL  : 12.360           1437                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 50:54)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  54.1433  26.5207  61.3854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7827 T22:   0.7261                                     
REMARK   3      T33:   0.6222 T12:  -0.0884                                     
REMARK   3      T13:  -0.0849 T23:  -0.1524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5733 L22:   1.5019                                     
REMARK   3      L33:   4.0685 L12:  -1.3406                                     
REMARK   3      L13:   2.4012 L23:  -1.8665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0033 S12:  -0.2999 S13:   0.4044                       
REMARK   3      S21:   0.1249 S22:  -0.0290 S23:   0.3229                       
REMARK   3      S31:   0.0657 S32:   0.8761 S33:   0.0510                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 55:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  42.9114  18.3464  37.8261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2395 T22:   0.1739                                     
REMARK   3      T33:   0.2615 T12:   0.0094                                     
REMARK   3      T13:  -0.0408 T23:   0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7113 L22:   2.3959                                     
REMARK   3      L33:   4.5987 L12:   0.0596                                     
REMARK   3      L13:   0.0573 L23:   1.4319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1748 S12:   0.1335 S13:   0.3600                       
REMARK   3      S21:  -0.1194 S22:  -0.2977 S23:   0.4591                       
REMARK   3      S31:  -0.2642 S32:   0.0790 S33:   0.0951                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 86:124)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  44.8382  10.9817  46.5369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1485 T22:   0.2252                                     
REMARK   3      T33:   0.2608 T12:  -0.0087                                     
REMARK   3      T13:   0.0135 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5902 L22:   1.0389                                     
REMARK   3      L33:   4.1422 L12:  -0.7036                                     
REMARK   3      L13:  -0.9380 L23:  -0.8921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0527 S12:  -0.1299 S13:   0.0552                       
REMARK   3      S21:  -0.0086 S22:  -0.0900 S23:   0.1935                       
REMARK   3      S31:  -0.2621 S32:  -0.0433 S33:   0.0266                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 125:156)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6997   2.3116  39.8424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1293 T22:   0.1977                                     
REMARK   3      T33:   0.2436 T12:   0.0323                                     
REMARK   3      T13:  -0.0086 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0526 L22:   1.4177                                     
REMARK   3      L33:   4.5032 L12:   0.3682                                     
REMARK   3      L13:  -1.9058 L23:   0.2164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1570 S12:  -0.0876 S13:  -0.0872                       
REMARK   3      S21:  -0.0870 S22:   0.0211 S23:  -0.1786                       
REMARK   3      S31:  -0.0756 S32:   0.3297 S33:  -0.1102                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 157:168)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  51.1587  -3.7330  21.8609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5549 T22:   0.6739                                     
REMARK   3      T33:   0.6300 T12:   0.0837                                     
REMARK   3      T13:  -0.0520 T23:  -0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4988 L22:   0.6239                                     
REMARK   3      L33:   0.5012 L12:   1.6653                                     
REMARK   3      L13:  -0.7524 L23:  -0.3477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6997 S12:  -0.8659 S13:  -0.9418                       
REMARK   3      S21:  -0.8499 S22:   0.5674 S23:  -0.0502                       
REMARK   3      S31:   0.2777 S32:   0.6708 S33:   0.0532                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 169:206)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6293   0.3098  52.9248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1625 T22:   0.2275                                     
REMARK   3      T33:   0.3020 T12:  -0.0321                                     
REMARK   3      T13:   0.0375 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1427 L22:   2.2363                                     
REMARK   3      L33:   3.7473 L12:  -0.4149                                     
REMARK   3      L13:  -0.2518 L23:   0.8566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0950 S12:  -0.1175 S13:  -0.0982                       
REMARK   3      S21:   0.2434 S22:  -0.1962 S23:   0.4236                       
REMARK   3      S31:   0.4354 S32:   0.1066 S33:   0.1956                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 207:220)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8882   0.8035  64.3297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3928 T22:   0.4823                                     
REMARK   3      T33:   0.3340 T12:   0.0444                                     
REMARK   3      T13:  -0.0897 T23:   0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5317 L22:   6.1611                                     
REMARK   3      L33:   2.1299 L12:  -5.5758                                     
REMARK   3      L13:  -2.8312 L23:   0.8551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0116 S12:  -0.8554 S13:   0.2132                       
REMARK   3      S21:   0.3643 S22:   0.4551 S23:  -0.8422                       
REMARK   3      S31:   0.0113 S32:   0.2012 S33:   0.0382                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 221:252)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1872   2.4894  36.7223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2736 T22:   0.3630                                     
REMARK   3      T33:   0.2829 T12:   0.0962                                     
REMARK   3      T13:   0.0335 T23:   0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3971 L22:   2.3335                                     
REMARK   3      L33:   6.0142 L12:   0.3001                                     
REMARK   3      L13:   0.3854 L23:  -0.4464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:   0.1252 S13:  -0.1344                       
REMARK   3      S21:  -0.2654 S22:   0.0250 S23:  -0.1805                       
REMARK   3      S31:   0.2978 S32:   0.4550 S33:   0.0365                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN A AND (RESID 253:254) OR (RESID 1001: 1012))    
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4489  15.1024   2.9480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5509 T22:   0.4787                                     
REMARK   3      T33:   0.3124 T12:   0.0531                                     
REMARK   3      T13:   0.0812 T23:  -0.0777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4840 L22:   5.6862                                     
REMARK   3      L33:   3.7463 L12:   0.2528                                     
REMARK   3      L13:   0.0814 L23:  -2.8700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0015 S12:  -0.6536 S13:   0.3041                       
REMARK   3      S21:   0.5902 S22:   0.2686 S23:   1.0732                       
REMARK   3      S31:   0.0472 S32:  -0.5921 S33:  -0.0761                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1013:1031)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.5030  11.4582 -17.7986              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3063 T22:   0.2569                                     
REMARK   3      T33:   0.2317 T12:  -0.0670                                     
REMARK   3      T13:   0.0105 T23:  -0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6591 L22:   4.0350                                     
REMARK   3      L33:   4.0781 L12:  -2.0191                                     
REMARK   3      L13:  -1.8966 L23:   0.9885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2262 S12:   0.5537 S13:   0.3664                       
REMARK   3      S21:  -0.4563 S22:  -0.0209 S23:   0.0465                       
REMARK   3      S31:  -0.0107 S32:   0.1254 S33:   0.2046                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1032:1053)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.9179  -4.8110  -4.3800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5993 T22:   0.3313                                     
REMARK   3      T33:   0.2986 T12:   0.0890                                     
REMARK   3      T13:  -0.0111 T23:   0.0725                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0099 L22:   3.0154                                     
REMARK   3      L33:   1.7347 L12:  -1.1395                                     
REMARK   3      L13:  -0.3394 L23:  -1.9594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5026 S12:  -0.6766 S13:  -0.2029                       
REMARK   3      S21:   0.3263 S22:  -0.0923 S23:  -0.6194                       
REMARK   3      S31:   0.4844 S32:   0.4420 S33:   0.4157                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1054:1069)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.2344  -7.9264 -18.4300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7080 T22:   0.0902                                     
REMARK   3      T33:   0.3789 T12:  -0.0328                                     
REMARK   3      T13:   0.1539 T23:  -0.0975                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7684 L22:   6.2111                                     
REMARK   3      L33:   1.1261 L12:   0.1383                                     
REMARK   3      L13:  -0.4952 L23:  -0.5193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4934 S12:   0.8921 S13:  -0.3220                       
REMARK   3      S21:  -0.6056 S22:  -0.1996 S23:   0.3426                       
REMARK   3      S31:   1.2292 S32:   0.0455 S33:   0.0972                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1070:1087)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  81.0025  -5.0721  -7.6087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3520 T22:   0.5308                                     
REMARK   3      T33:   0.6059 T12:   0.3117                                     
REMARK   3      T13:   0.1249 T23:   0.1442                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3292 L22:   2.8743                                     
REMARK   3      L33:   2.3530 L12:  -1.6263                                     
REMARK   3      L13:   0.7880 L23:  -2.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5179 S12:  -0.3250 S13:  -0.5503                       
REMARK   3      S21:   0.4228 S22:  -0.3974 S23:  -0.9302                       
REMARK   3      S31:   0.7418 S32:   1.2697 S33:  -0.5681                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1088:1107)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1556   5.6670  -9.3649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2512 T22:   0.3869                                     
REMARK   3      T33:   0.3538 T12:  -0.0238                                     
REMARK   3      T13:   0.0232 T23:   0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1047 L22:   5.1534                                     
REMARK   3      L33:   3.8327 L12:  -0.2233                                     
REMARK   3      L13:  -0.1527 L23:   3.1557                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0171 S12:  -0.2748 S13:   0.0713                       
REMARK   3      S21:  -0.7739 S22:   0.2874 S23:  -0.7054                       
REMARK   3      S31:  -0.4081 S32:   0.9169 S33:   0.0094                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1108:1121)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8164   0.9472  -4.3766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3626 T22:   0.2957                                     
REMARK   3      T33:   0.1381 T12:   0.0394                                     
REMARK   3      T13:   0.0153 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6844 L22:   2.0340                                     
REMARK   3      L33:   0.3814 L12:   0.5376                                     
REMARK   3      L13:  -0.0726 L23:   0.8378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1927 S12:  -0.3272 S13:   0.3334                       
REMARK   3      S21:   0.0190 S22:   0.0121 S23:   0.2284                       
REMARK   3      S31:   0.8389 S32:   0.5111 S33:   0.0766                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1122:1127)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.3898   1.4947   7.1544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6726 T22:   0.4077                                     
REMARK   3      T33:   0.6237 T12:  -0.0482                                     
REMARK   3      T13:  -0.0451 T23:   0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5842 L22:   1.9208                                     
REMARK   3      L33:   6.9009 L12:  -0.3115                                     
REMARK   3      L13:   0.8848 L23:   2.0824                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5588 S12:  -0.5880 S13:  -0.1672                       
REMARK   3      S21:   0.9042 S22:  -0.4147 S23:   0.1123                       
REMARK   3      S31:   0.1911 S32:  -0.7602 S33:   0.2783                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 1128:1182)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.3061  -2.0919  -5.3341              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3308 T22:   0.2855                                     
REMARK   3      T33:   0.3590 T12:  -0.0460                                     
REMARK   3      T13:   0.0748 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2123 L22:   2.7287                                     
REMARK   3      L33:   3.2468 L12:  -1.0506                                     
REMARK   3      L13:   0.5994 L23:   1.6961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0401 S12:  -0.3816 S13:  -0.2659                       
REMARK   3      S21:   0.3202 S22:  -0.2745 S23:   0.5688                       
REMARK   3      S31:   0.6299 S32:  -0.4847 S33:   0.2450                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN A AND (RESID 1183:1196) OR (RESID 294:304))     
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7137  10.2582   6.9053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3435 T22:   0.3994                                     
REMARK   3      T33:   0.2512 T12:   0.0054                                     
REMARK   3      T13:   0.0414 T23:   0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5991 L22:   0.7704                                     
REMARK   3      L33:   3.4917 L12:   0.3748                                     
REMARK   3      L13:   0.8839 L23:   1.7578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2773 S12:   0.1231 S13:   0.1139                       
REMARK   3      S21:  -0.0193 S22:  -0.1442 S23:  -0.0290                       
REMARK   3      S31:  -0.4923 S32:  -0.2171 S33:   0.2366                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 305:340)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  61.9975  10.7862  49.4395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1900 T22:   0.3673                                     
REMARK   3      T33:   0.3083 T12:  -0.0389                                     
REMARK   3      T13:  -0.0173 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8095 L22:   2.6163                                     
REMARK   3      L33:   1.3894 L12:   0.2174                                     
REMARK   3      L13:  -0.7682 L23:  -0.6913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1134 S12:  -0.2731 S13:   0.0903                       
REMARK   3      S21:   0.3497 S22:  -0.2711 S23:  -0.3922                       
REMARK   3      S31:  -0.3538 S32:   0.6439 S33:   0.3697                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 341:381)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  50.4615  19.1727  38.4349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2847 T22:   0.2269                                     
REMARK   3      T33:   0.2718 T12:  -0.0040                                     
REMARK   3      T13:   0.0018 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5420 L22:   1.5576                                     
REMARK   3      L33:   3.2189 L12:   0.0760                                     
REMARK   3      L13:   0.1832 L23:  -0.3129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1773 S12:  -0.1539 S13:   0.1453                       
REMARK   3      S21:  -0.0755 S22:  -0.1464 S23:   0.0835                       
REMARK   3      S31:  -0.4567 S32:  -0.1967 S33:  -0.1169                       
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 4S0V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000088038.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 52                                 
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) : 1.033                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22305                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 4DKL AND 2BFW                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 31% PEG 400, 0.1 M SODIUM CITRATE, 0.2   
REMARK 280  M SODIUM FORMATE, 3%(W/V) HEXANEDIOL, PH 5.9, LIPIDIC CUBIC         
REMARK 280  PHASE (LCP), TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       47.17900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.90950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       47.17900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.90950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     TRP A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     PHE A    39                                                      
REMARK 465     LEU A    40                                                      
REMARK 465     ARG A    41                                                      
REMARK 465     TYR A    42                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     TRP A    44                                                      
REMARK 465     ARG A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     TYR A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     HIS A    49                                                      
REMARK 465     LEU A   160                                                      
REMARK 465     MET A   161                                                      
REMARK 465     PHE A   162                                                      
REMARK 465     LYS A   163                                                      
REMARK 465     PRO A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     LEU A   200                                                      
REMARK 465     ALA A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     THR A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     CYS A   382                                                      
REMARK 465     CYS A   383                                                      
REMARK 465     LEU A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     VAL A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     HIS A   393                                                      
REMARK 465     HIS A   394                                                      
REMARK 465     HIS A   395                                                      
REMARK 465     HIS A   396                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 203    CG   CD   CE   NZ                                   
REMARK 470     HIS A 335    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS A  1061     O    HOH A  4026              2.10            
REMARK 500   OD1  ASN A    90     O    HOH A  4027              2.11            
REMARK 500   O    ILE A  1116     O    HOH A  4012              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  53       17.53     47.19                                   
REMARK 500    TYR A 232      -75.01   -138.51                                   
REMARK 500    GLN A1045      -72.63   -136.82                                   
REMARK 500    PRO A1118       39.26    -88.83                                   
REMARK 500    GLU A1122       86.56   -155.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 2002                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUV A 2001                
DBREF  4S0V A    3   254  UNP    O43614   OX2R_HUMAN       3    254             
DBREF  4S0V A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  4S0V A  294   388  UNP    O43614   OX2R_HUMAN     294    388             
SEQADV 4S0V ASP A   -5  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V TYR A   -4  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V LYS A   -3  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V ASP A   -2  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V ASP A   -1  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V ASP A    0  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V ALA A    1  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V MET A    2  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  389  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  390  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  391  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  392  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  393  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  394  UNP  O43614              EXPRESSION TAG                 
SEQADV 4S0V HIS A  395  UNP  O43614              EXPRESSION TAG                 
SEQRES   1 A  559  ASP TYR LYS ASP ASP ASP ALA MET GLY THR LYS LEU GLU          
SEQRES   2 A  559  ASP SER PRO PRO CYS ARG ASN TRP SER SER ALA SER GLU          
SEQRES   3 A  559  LEU ASN GLU THR GLN GLU PRO PHE LEU ASN PRO THR ASP          
SEQRES   4 A  559  TYR ASP ASP GLU GLU PHE LEU ARG TYR LEU TRP ARG GLU          
SEQRES   5 A  559  TYR LEU HIS PRO LYS GLU TYR GLU TRP VAL LEU ILE ALA          
SEQRES   6 A  559  GLY TYR ILE ILE VAL PHE VAL VAL ALA LEU ILE GLY ASN          
SEQRES   7 A  559  VAL LEU VAL CYS VAL ALA VAL TRP LYS ASN HIS HIS MET          
SEQRES   8 A  559  ARG THR VAL THR ASN TYR PHE ILE VAL ASN LEU SER LEU          
SEQRES   9 A  559  ALA ASP VAL LEU VAL THR ILE THR CYS LEU PRO ALA THR          
SEQRES  10 A  559  LEU VAL VAL ASP ILE THR GLU THR TRP PHE PHE GLY GLN          
SEQRES  11 A  559  SER LEU CYS LYS VAL ILE PRO TYR LEU GLN THR VAL SER          
SEQRES  12 A  559  VAL SER VAL SER VAL LEU THR LEU SER CYS ILE ALA LEU          
SEQRES  13 A  559  ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU MET PHE LYS          
SEQRES  14 A  559  SER THR ALA LYS ARG ALA ARG ASN SER ILE VAL ILE ILE          
SEQRES  15 A  559  TRP ILE VAL SER CYS ILE ILE MET ILE PRO GLN ALA ILE          
SEQRES  16 A  559  VAL MET GLU CYS SER THR VAL PHE PRO GLY LEU ALA ASN          
SEQRES  17 A  559  LYS THR THR LEU PHE THR VAL CYS ASP GLU ARG TRP GLY          
SEQRES  18 A  559  GLY GLU ILE TYR PRO LYS MET TYR HIS ILE CYS PHE PHE          
SEQRES  19 A  559  LEU VAL THR TYR MET ALA PRO LEU CYS LEU MET VAL LEU          
SEQRES  20 A  559  ALA TYR LEU GLN ILE PHE ARG LYS LEU TRP CYS ARG GLN          
SEQRES  21 A  559  GLY ILE ASP CYS SER PHE TRP ASN GLU SER TYR LEU THR          
SEQRES  22 A  559  GLY SER ARG ASP GLU ARG LYS LYS SER LEU LEU SER LYS          
SEQRES  23 A  559  PHE GLY MET ASP GLU GLY VAL THR PHE MET PHE ILE GLY          
SEQRES  24 A  559  ARG PHE ASP ARG GLY GLN LYS GLY VAL ASP VAL LEU LEU          
SEQRES  25 A  559  LYS ALA ILE GLU ILE LEU SER SER LYS LYS GLU PHE GLN          
SEQRES  26 A  559  GLU MET ARG PHE ILE ILE ILE GLY LYS GLY ASP PRO GLU          
SEQRES  27 A  559  LEU GLU GLY TRP ALA ARG SER LEU GLU GLU LYS HIS GLY          
SEQRES  28 A  559  ASN VAL LYS VAL ILE THR GLU MET LEU SER ARG GLU PHE          
SEQRES  29 A  559  VAL ARG GLU LEU TYR GLY SER VAL ASP PHE VAL ILE ILE          
SEQRES  30 A  559  PRO SER TYR PHE GLU PRO PHE GLY LEU VAL ALA LEU GLU          
SEQRES  31 A  559  ALA MET CYS LEU GLY ALA ILE PRO ILE ALA SER ALA VAL          
SEQRES  32 A  559  GLY GLY LEU ARG ASP ILE ILE THR ASN GLU THR GLY ILE          
SEQRES  33 A  559  LEU VAL LYS ALA GLY ASP PRO GLY GLU LEU ALA ASN ALA          
SEQRES  34 A  559  ILE LEU LYS ALA LEU GLU LEU SER ARG SER ASP LEU SER          
SEQRES  35 A  559  LYS PHE ARG GLU ASN CYS LYS LYS ARG ALA MET SER PHE          
SEQRES  36 A  559  SER LYS GLN ILE ARG ALA ARG ARG LYS THR ALA ARG MET          
SEQRES  37 A  559  LEU MET VAL VAL LEU LEU VAL PHE ALA ILE CYS TYR LEU          
SEQRES  38 A  559  PRO ILE SER ILE LEU ASN VAL LEU LYS ARG VAL PHE GLY          
SEQRES  39 A  559  MET PHE ALA HIS THR GLU ASP ARG GLU THR VAL TYR ALA          
SEQRES  40 A  559  TRP PHE THR PHE SER HIS TRP LEU VAL TYR ALA ASN SER          
SEQRES  41 A  559  ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER GLY LYS          
SEQRES  42 A  559  PHE ARG GLU GLU PHE LYS ALA ALA PHE SER CYS CYS CYS          
SEQRES  43 A  559  LEU GLY VAL HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
HET    SUV  A2001      32                                                       
HET    OLA  A2002       8                                                       
HETNAM     SUV [(7R)-4-(5-CHLORO-1,3-BENZOXAZOL-2-YL)-7-METHYL-1,4-             
HETNAM   2 SUV  DIAZEPAN-1-YL][5-METHYL-2-(2H-1,2,3-TRIAZOL-2-YL)               
HETNAM   3 SUV  PHENYL]METHANONE                                                
HETNAM     OLA OLEIC ACID                                                       
HETSYN     SUV SUVOREXANT                                                       
FORMUL   2  SUV    C23 H23 CL N6 O2                                             
FORMUL   3  OLA    C18 H34 O2                                                   
FORMUL   4  HOH   *28(H2 O)                                                     
HELIX    1   1 TYR A   53  ASN A   82  1                                  30    
HELIX    2   2 HIS A   83  ARG A   86  5                                   4    
HELIX    3   3 THR A   87  CYS A  107  1                                  21    
HELIX    4   4 CYS A  107  GLU A  118  1                                  12    
HELIX    5   5 GLY A  123  CYS A  157  1                                  35    
HELIX    6   6 THR A  165  MET A  184  1                                  20    
HELIX    7   7 MET A  184  VAL A  190  1                                   7    
HELIX    8   8 GLU A  217  TYR A  232  1                                  16    
HELIX    9   9 TYR A  232  CYS A  252  1                                  21    
HELIX   10  10 ASN A 1008  LEU A 1012  5                                   5    
HELIX   11  11 SER A 1015  GLY A 1028  1                                  14    
HELIX   12  12 GLY A 1047  SER A 1059  1                                  13    
HELIX   13  13 SER A 1060  GLN A 1065  5                                   6    
HELIX   14  14 ASP A 1076  HIS A 1090  1                                  15    
HELIX   15  15 SER A 1101  GLY A 1110  1                                  10    
HELIX   16  16 GLY A 1125  CYS A 1133  1                                   9    
HELIX   17  17 GLY A 1145  ILE A 1150  1                                   6    
HELIX   18  18 ASP A 1162  ARG A 1178  1                                  17    
HELIX   19  19 LEU A 1181  VAL A  329  1                                  52    
HELIX   20  20 ARG A  339  SER A  368  1                                  30    
HELIX   21  21 SER A  368  PHE A  379  1                                  12    
SHEET    1   A 2 MET A 191  VAL A 196  0                                        
SHEET    2   A 2 PHE A 207  GLU A 212 -1  O  PHE A 207   N  VAL A 196           
SHEET    1   B 6 VAL A1093  ILE A1096  0                                        
SHEET    2   B 6 MET A1067  ILE A1072  1  N  ILE A1071   O  ILE A1096           
SHEET    3   B 6 VAL A1033  PHE A1037  1  N  PHE A1037   O  ILE A1070           
SHEET    4   B 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5   B 6 ILE A1137  SER A1141  1  O  ILE A1139   N  VAL A1115           
SHEET    6   B 6 ILE A1156  VAL A1158  1  O  ILE A1156   N  PRO A1138           
SSBOND   1 CYS A  127    CYS A  210                          1555   1555  2.04  
CISPEP   1 PRO A   50    LYS A   51          0        -2.87                     
SITE     1 AC1 12 THR A 111  VAL A 114  TRP A 120  ILE A 130                    
SITE     2 AC1 12 PRO A 131  GLN A 134  THR A 135  GLN A 187                    
SITE     3 AC1 12 GLU A 212  ILE A 320  ASN A 324  HOH A4025                    
CRYST1   94.358   75.819   96.335  90.00 111.71  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010598  0.000000  0.004220        0.00000                         
SCALE2      0.000000  0.013189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011173        0.00000                         
ATOM      1  N   PRO A  50      52.480  26.848  67.575  1.00 92.84           N  
ANISOU    1  N   PRO A  50    12541  12020  10715   -751   -425  -1950       N  
ATOM      2  CA  PRO A  50      52.585  26.352  66.199  1.00 82.32           C  
ANISOU    2  CA  PRO A  50    11209  10610   9458   -775   -508  -1819       C  
ATOM      3  C   PRO A  50      51.693  27.121  65.224  1.00 77.84           C  
ANISOU    3  C   PRO A  50    10646   9763   9167   -877   -543  -1799       C  
ATOM      4  O   PRO A  50      50.566  27.446  65.591  1.00 81.16           O  
ANISOU    4  O   PRO A  50    11076  10021   9742   -863   -473  -1812       O  
ATOM      5  CB  PRO A  50      52.124  24.896  66.317  1.00 80.95           C  
ANISOU    5  CB  PRO A  50    11091  10430   9236   -629   -481  -1680       C  
ATOM      6  CG  PRO A  50      51.225  24.886  67.509  1.00 85.01           C  
ANISOU    6  CG  PRO A  50    11592  10926   9780   -579   -358  -1694       C  
ATOM      7  CD  PRO A  50      51.827  25.873  68.466  1.00 90.12           C  
ANISOU    7  CD  PRO A  50    12213  11720  10310   -605   -315  -1881       C  
ATOM      8  N   LYS A  51      52.171  27.421  64.015  1.00 76.69           N  
ANISOU    8  N   LYS A  51    10483   9583   9071   -962   -644  -1757       N  
ATOM      9  CA  LYS A  51      53.530  27.117  63.561  1.00 77.59           C  
ANISOU    9  CA  LYS A  51    10551   9950   8978   -953   -716  -1716       C  
ATOM     10  C   LYS A  51      53.908  28.081  62.443  1.00 79.95           C  
ANISOU   10  C   LYS A  51    10791  10208   9376  -1108   -812  -1692       C  
ATOM     11  O   LYS A  51      53.033  28.661  61.802  1.00 78.94           O  
ANISOU   11  O   LYS A  51    10693   9816   9486  -1187   -832  -1689       O  
ATOM     12  CB  LYS A  51      53.640  25.670  63.059  1.00 65.27           C  
ANISOU   12  CB  LYS A  51     9057   8443   7298   -768   -739  -1587       C  
ATOM     13  CG  LYS A  51      55.067  25.159  62.918  1.00 65.01           C  
ANISOU   13  CG  LYS A  51     8979   8749   6972   -672   -782  -1552       C  
ATOM     14  CD  LYS A  51      55.816  25.266  64.240  1.00 76.02           C  
ANISOU   14  CD  LYS A  51    10315  10393   8177   -683   -727  -1645       C  
ATOM     15  CE  LYS A  51      57.259  24.812  64.110  1.00 79.00           C  
ANISOU   15  CE  LYS A  51    10616  11144   8257   -588   -768  -1593       C  
ATOM     16  NZ  LYS A  51      57.998  24.937  65.397  1.00 78.70           N  
ANISOU   16  NZ  LYS A  51    10519  11343   8042   -613   -730  -1680       N  
ATOM     17  N   GLU A  52      55.203  28.257  62.196  1.00 79.87           N  
ANISOU   17  N   GLU A  52    10683  10478   9185  -1156   -876  -1652       N  
ATOM     18  CA  GLU A  52      55.612  28.955  60.986  1.00 84.20           C  
ANISOU   18  CA  GLU A  52    11152  11039   9802  -1284   -971  -1564       C  
ATOM     19  C   GLU A  52      55.407  27.998  59.819  1.00 85.67           C  
ANISOU   19  C   GLU A  52    11387  11194   9971  -1105   -979  -1437       C  
ATOM     20  O   GLU A  52      55.025  26.844  60.020  1.00 95.78           O  
ANISOU   20  O   GLU A  52    12775  12434  11184   -908   -942  -1422       O  
ATOM     21  CB  GLU A  52      57.065  29.440  61.058  1.00 87.15           C  
ANISOU   21  CB  GLU A  52    11368  11766   9980  -1402  -1046  -1506       C  
ATOM     22  CG  GLU A  52      58.114  28.364  60.834  1.00 91.30           C  
ANISOU   22  CG  GLU A  52    11815  12668  10205  -1201  -1027  -1387       C  
ATOM     23  CD  GLU A  52      58.537  27.688  62.118  1.00 96.05           C  
ANISOU   23  CD  GLU A  52    12438  13452  10605  -1089   -966  -1465       C  
ATOM     24  OE1 GLU A  52      58.215  28.215  63.202  1.00 99.32           O  
ANISOU   24  OE1 GLU A  52    12896  13752  11090  -1198   -949  -1602       O  
ATOM     25  OE2 GLU A  52      59.189  26.628  62.044  1.00 97.13           O  
ANISOU   25  OE2 GLU A  52    12562  13848  10495   -869   -941  -1393       O  
ATOM     26  N   TYR A  53      55.647  28.491  58.607  1.00 70.28           N  
ANISOU   26  N   TYR A  53     9375   9249   8077  -1173  -1050  -1339       N  
ATOM     27  CA  TYR A  53      55.387  27.763  57.360  1.00 71.99           C  
ANISOU   27  CA  TYR A  53     9667   9397   8291   -998  -1085  -1228       C  
ATOM     28  C   TYR A  53      54.002  27.097  57.298  1.00 72.12           C  
ANISOU   28  C   TYR A  53     9866   9038   8497   -902  -1074  -1259       C  
ATOM     29  O   TYR A  53      53.766  26.233  56.456  1.00 84.50           O  
ANISOU   29  O   TYR A  53    11552  10525  10030   -718  -1133  -1177       O  
ATOM     30  CB  TYR A  53      56.497  26.718  57.092  1.00 67.09           C  
ANISOU   30  CB  TYR A  53     9022   9147   7324   -742  -1097  -1129       C  
ATOM     31  CG  TYR A  53      56.533  25.474  57.972  1.00 70.05           C  
ANISOU   31  CG  TYR A  53     9514   9584   7519   -526  -1061  -1175       C  
ATOM     32  CD1 TYR A  53      55.680  24.400  57.736  1.00 65.46           C  
ANISOU   32  CD1 TYR A  53     9146   8748   6979   -338  -1101  -1165       C  
ATOM     33  CD2 TYR A  53      57.459  25.353  59.004  1.00 78.16           C  
ANISOU   33  CD2 TYR A  53    10445  10924   8328   -517  -1015  -1210       C  
ATOM     34  CE1 TYR A  53      55.718  23.264  58.524  1.00 62.12           C  
ANISOU   34  CE1 TYR A  53     8841   8368   6394   -161  -1098  -1186       C  
ATOM     35  CE2 TYR A  53      57.505  24.215  59.797  1.00 77.67           C  
ANISOU   35  CE2 TYR A  53    10496  10919   8097   -320   -989  -1247       C  
ATOM     36  CZ  TYR A  53      56.633  23.175  59.549  1.00 69.16           C  
ANISOU   36  CZ  TYR A  53     9633   9575   7068   -145  -1033  -1232       C  
ATOM     37  OH  TYR A  53      56.670  22.042  60.328  1.00 68.30           O  
ANISOU   37  OH  TYR A  53     9650   9505   6796     31  -1036  -1249       O  
ATOM     38  N   GLU A  54      53.080  27.522  58.158  1.00 54.70           N  
ANISOU   38  N   GLU A  54     7687   6611   6484  -1018  -1016  -1359       N  
ATOM     39  CA  GLU A  54      51.751  26.920  58.195  1.00 53.91           C  
ANISOU   39  CA  GLU A  54     7713   6204   6567   -953  -1004  -1342       C  
ATOM     40  C   GLU A  54      50.853  27.471  57.092  1.00 53.50           C  
ANISOU   40  C   GLU A  54     7696   5849   6783  -1039  -1060  -1302       C  
ATOM     41  O   GLU A  54      50.151  26.716  56.417  1.00 57.27           O  
ANISOU   41  O   GLU A  54     8289   6126   7346   -941  -1126  -1213       O  
ATOM     42  CB  GLU A  54      51.097  27.138  59.562  1.00 65.34           C  
ANISOU   42  CB  GLU A  54     9146   7593   8087  -1006   -901  -1435       C  
ATOM     43  CG  GLU A  54      49.724  26.488  59.696  1.00 72.33           C  
ANISOU   43  CG  GLU A  54    10111   8222   9149   -952   -883  -1364       C  
ATOM     44  CD  GLU A  54      49.189  26.524  61.115  1.00 79.02           C  
ANISOU   44  CD  GLU A  54    10920   9107   9997   -947   -763  -1418       C  
ATOM     45  OE1 GLU A  54      50.004  26.565  62.061  1.00 82.54           O  
ANISOU   45  OE1 GLU A  54    11328   9791  10241   -921   -708  -1506       O  
ATOM     46  OE2 GLU A  54      47.950  26.514  61.283  1.00 78.44           O  
ANISOU   46  OE2 GLU A  54    10845   8844  10116   -957   -723  -1360       O  
ATOM     47  N   TRP A  55      50.879  28.788  56.910  1.00 35.13           N  
ANISOU   47  N   TRP A  55     5784   3470   4094  -1360   -623   -197       N  
ATOM     48  CA  TRP A  55      50.049  29.435  55.900  1.00 37.11           C  
ANISOU   48  CA  TRP A  55     6067   3515   4518  -1346   -645   -182       C  
ATOM     49  C   TRP A  55      50.467  29.034  54.486  1.00 33.53           C  
ANISOU   49  C   TRP A  55     5449   3219   4073  -1361   -678    -25       C  
ATOM     50  O   TRP A  55      49.622  28.895  53.602  1.00 36.39           O  
ANISOU   50  O   TRP A  55     5787   3476   4562  -1245   -649    -14       O  
ATOM     51  CB  TRP A  55      50.094  30.962  56.059  1.00 44.46           C  
ANISOU   51  CB  TRP A  55     7189   4226   5479  -1521   -770   -215       C  
ATOM     52  CG  TRP A  55      51.471  31.562  55.986  1.00 48.47           C  
ANISOU   52  CG  TRP A  55     7685   4885   5845  -1797   -896   -119       C  
ATOM     53  CD1 TRP A  55      52.299  31.846  57.035  1.00 43.38           C  
ANISOU   53  CD1 TRP A  55     7085   4337   5061  -1948   -947   -167       C  
ATOM     54  CD2 TRP A  55      52.173  31.962  54.802  1.00 52.52           C  
ANISOU   54  CD2 TRP A  55     8136   5485   6333  -1977   -981     26       C  
ATOM     55  NE1 TRP A  55      53.476  32.389  56.575  1.00 45.97           N  
ANISOU   55  NE1 TRP A  55     7353   4827   5288  -2221  -1057    -71       N  
ATOM     56  CE2 TRP A  55      53.423  32.472  55.208  1.00 50.01           C  
ANISOU   56  CE2 TRP A  55     7806   5333   5865  -2253  -1068     50       C  
ATOM     57  CE3 TRP A  55      51.866  31.935  53.437  1.00 51.18           C  
ANISOU   57  CE3 TRP A  55     7926   5276   6243  -1943   -989    131       C  
ATOM     58  CZ2 TRP A  55      54.367  32.951  54.297  1.00 47.76           C  
ANISOU   58  CZ2 TRP A  55     7443   5199   5507  -2478  -1125    172       C  
ATOM     59  CZ3 TRP A  55      52.805  32.409  52.535  1.00 51.94           C  
ANISOU   59  CZ3 TRP A  55     7989   5488   6257  -2183  -1062    264       C  
ATOM     60  CH2 TRP A  55      54.039  32.911  52.969  1.00 49.25           C  
ANISOU   60  CH2 TRP A  55     7609   5339   5766  -2431  -1108    280       C  
ATOM     61  N   VAL A  56      51.766  28.837  54.275  1.00 34.31           N  
ANISOU   61  N   VAL A  56     5424   3587   4027  -1497   -737     83       N  
ATOM     62  CA  VAL A  56      52.263  28.429  52.963  1.00 37.97           C  
ANISOU   62  CA  VAL A  56     5724   4229   4473  -1519   -752    226       C  
ATOM     63  C   VAL A  56      51.913  26.961  52.711  1.00 38.06           C  
ANISOU   63  C   VAL A  56     5611   4367   4484  -1279   -631    237       C  
ATOM     64  O   VAL A  56      51.747  26.534  51.565  1.00 34.93           O  
ANISOU   64  O   VAL A  56     5126   4017   4130  -1220   -610    320       O  
ATOM     65  CB  VAL A  56      53.795  28.655  52.830  1.00 41.10           C  
ANISOU   65  CB  VAL A  56     5990   4918   4708  -1745   -837    313       C  
ATOM     66  CG1 VAL A  56      54.571  27.743  53.766  1.00 46.37           C  
ANISOU   66  CG1 VAL A  56     6534   5861   5223  -1659   -816    275       C  
ATOM     67  CG2 VAL A  56      54.251  28.452  51.395  1.00 49.90           C  
ANISOU   67  CG2 VAL A  56     6962   6189   5808  -1803   -843    452       C  
ATOM     68  N   LEU A  57      51.777  26.199  53.793  1.00 32.65           N  
ANISOU   68  N   LEU A  57     4955   3715   3734  -1148   -549    149       N  
ATOM     69  CA  LEU A  57      51.399  24.794  53.697  1.00 29.85           C  
ANISOU   69  CA  LEU A  57     4550   3436   3355   -934   -421    147       C  
ATOM     70  C   LEU A  57      49.924  24.665  53.339  1.00 33.86           C  
ANISOU   70  C   LEU A  57     5117   3708   4040   -822   -323     70       C  
ATOM     71  O   LEU A  57      49.552  23.893  52.458  1.00 26.40           O  
ANISOU   71  O   LEU A  57     4095   2801   3136   -719   -263    113       O  
ATOM     72  CB  LEU A  57      51.686  24.065  55.009  1.00 27.32           C  
ANISOU   72  CB  LEU A  57     4305   3190   2885   -840   -364     75       C  
ATOM     73  CG  LEU A  57      51.579  22.545  54.921  1.00 36.39           C  
ANISOU   73  CG  LEU A  57     5444   4436   3947   -634   -245     94       C  
ATOM     74  CD1 LEU A  57      52.640  22.012  53.972  1.00 43.98           C  
ANISOU   74  CD1 LEU A  57     6222   5679   4811   -603   -309    227       C  
ATOM     75  CD2 LEU A  57      51.704  21.906  56.296  1.00 41.94           C  
ANISOU   75  CD2 LEU A  57     6303   5143   4490   -537   -186     14       C  
ATOM     76  N   ILE A  58      49.088  25.427  54.035  1.00 40.41           N  
ANISOU   76  N   ILE A  58     6076   4308   4971   -840   -309    -58       N  
ATOM     77  CA  ILE A  58      47.660  25.454  53.758  1.00 35.21           C  
ANISOU   77  CA  ILE A  58     5439   3448   4489   -734   -229   -167       C  
ATOM     78  C   ILE A  58      47.404  25.951  52.340  1.00 37.78           C  
ANISOU   78  C   ILE A  58     5697   3724   4932   -742   -328    -85       C  
ATOM     79  O   ILE A  58      46.643  25.342  51.584  1.00 43.05           O  
ANISOU   79  O   ILE A  58     6287   4382   5687   -629   -270   -101       O  
ATOM     80  CB  ILE A  58      46.914  26.350  54.765  1.00 29.33           C  
ANISOU   80  CB  ILE A  58     4836   2483   3824   -746   -214   -331       C  
ATOM     81  CG1 ILE A  58      47.038  25.774  56.177  1.00 24.78           C  
ANISOU   81  CG1 ILE A  58     4357   1940   3120   -729    -95   -421       C  
ATOM     82  CG2 ILE A  58      45.452  26.498  54.374  1.00 31.36           C  
ANISOU   82  CG2 ILE A  58     5071   2569   4277   -623   -154   -463       C  
ATOM     83  CD1 ILE A  58      46.699  26.766  57.272  1.00 29.40           C  
ANISOU   83  CD1 ILE A  58     5099   2346   3727   -779   -104   -560       C  
ATOM     84  N   ALA A  59      48.059  27.053  51.984  1.00 31.00           N  
ANISOU   84  N   ALA A  59     4889   2834   4057   -892   -478     -2       N  
ATOM     85  CA  ALA A  59      47.910  27.645  50.658  1.00 38.12           C  
ANISOU   85  CA  ALA A  59     5788   3662   5033   -920   -585     89       C  
ATOM     86  C   ALA A  59      48.341  26.671  49.568  1.00 39.41           C  
ANISOU   86  C   ALA A  59     5799   4033   5141   -886   -557    220       C  
ATOM     87  O   ALA A  59      47.607  26.437  48.604  1.00 32.90           O  
ANISOU   87  O   ALA A  59     4939   3152   4411   -782   -560    228       O  
ATOM     88  CB  ALA A  59      48.707  28.933  50.562  1.00 26.33           C  
ANISOU   88  CB  ALA A  59     4418   2102   3482  -1136   -729    166       C  
ATOM     89  N   GLY A  60      49.532  26.102  49.734  1.00 40.34           N  
ANISOU   89  N   GLY A  60     5826   4401   5100   -959   -538    309       N  
ATOM     90  CA  GLY A  60      50.057  25.137  48.784  1.00 36.28           C  
ANISOU   90  CA  GLY A  60     5169   4106   4510   -911   -503    424       C  
ATOM     91  C   GLY A  60      49.160  23.925  48.631  1.00 28.97           C  
ANISOU   91  C   GLY A  60     4203   3166   3636   -707   -378    363       C  
ATOM     92  O   GLY A  60      48.942  23.441  47.520  1.00 36.11           O  
ANISOU   92  O   GLY A  60     5044   4111   4564   -646   -370    425       O  
ATOM     93  N   TYR A  61      48.628  23.439  49.749  1.00 26.30           N  
ANISOU   93  N   TYR A  61     3921   2766   3305   -621   -273    236       N  
ATOM     94  CA  TYR A  61      47.744  22.280  49.725  1.00 21.20           C  
ANISOU   94  CA  TYR A  61     3266   2094   2694   -471   -130    159       C  
ATOM     95  C   TYR A  61      46.437  22.597  49.009  1.00 34.11           C  
ANISOU   95  C   TYR A  61     4883   3558   4520   -419   -136     78       C  
ATOM     96  O   TYR A  61      45.906  21.758  48.286  1.00 44.90           O  
ANISOU   96  O   TYR A  61     6190   4953   5917   -336    -73     71       O  
ATOM     97  CB  TYR A  61      47.467  21.777  51.144  1.00 20.01           C  
ANISOU   97  CB  TYR A  61     3217   1898   2488   -427     -2     34       C  
ATOM     98  CG  TYR A  61      48.348  20.615  51.549  1.00 28.92           C  
ANISOU   98  CG  TYR A  61     4368   3207   3412   -358     62     96       C  
ATOM     99  CD1 TYR A  61      49.593  20.829  52.125  1.00 31.39           C  
ANISOU   99  CD1 TYR A  61     4679   3675   3572   -401    -23    161       C  
ATOM    100  CD2 TYR A  61      47.941  19.305  51.343  1.00 38.06           C  
ANISOU  100  CD2 TYR A  61     5559   4380   4520   -243    198     79       C  
ATOM    101  CE1 TYR A  61      50.404  19.770  52.491  1.00 38.35           C  
ANISOU  101  CE1 TYR A  61     5585   4731   4258   -291     10    205       C  
ATOM    102  CE2 TYR A  61      48.745  18.238  51.706  1.00 42.06           C  
ANISOU  102  CE2 TYR A  61     6132   5026   4822   -144    244    134       C  
ATOM    103  CZ  TYR A  61      49.976  18.478  52.278  1.00 42.21           C  
ANISOU  103  CZ  TYR A  61     6141   5205   4692   -149    141    196       C  
ATOM    104  OH  TYR A  61      50.783  17.425  52.642  1.00 38.99           O  
ANISOU  104  OH  TYR A  61     5801   4944   4070     -6    161    240       O  
ATOM    105  N   ILE A  62      45.925  23.809  49.202  1.00 33.92           N  
ANISOU  105  N   ILE A  62     4916   3359   4615   -458   -224      7       N  
ATOM    106  CA  ILE A  62      44.709  24.232  48.512  1.00 32.30           C  
ANISOU  106  CA  ILE A  62     4686   3001   4585   -373   -268    -83       C  
ATOM    107  C   ILE A  62      44.940  24.323  47.001  1.00 33.73           C  
ANISOU  107  C   ILE A  62     4824   3226   4768   -373   -385     59       C  
ATOM    108  O   ILE A  62      44.163  23.773  46.208  1.00 30.59           O  
ANISOU  108  O   ILE A  62     4350   2829   4445   -272   -368     20       O  
ATOM    109  CB  ILE A  62      44.202  25.587  49.041  1.00 24.76           C  
ANISOU  109  CB  ILE A  62     3834   1838   3735   -382   -360   -187       C  
ATOM    110  CG1 ILE A  62      43.663  25.430  50.462  1.00 28.00           C  
ANISOU  110  CG1 ILE A  62     4279   2192   4166   -356   -219   -367       C  
ATOM    111  CG2 ILE A  62      43.111  26.138  48.143  1.00 23.15           C  
ANISOU  111  CG2 ILE A  62     3609   1495   3694   -262   -462   -259       C  
ATOM    112  CD1 ILE A  62      43.222  26.731  51.091  1.00 25.36           C  
ANISOU  112  CD1 ILE A  62     4060   1657   3917   -351   -297   -482       C  
ATOM    113  N   ILE A  63      46.013  25.011  46.613  1.00 23.08           N  
ANISOU  113  N   ILE A  63     3528   1918   3325   -504   -498    214       N  
ATOM    114  CA  ILE A  63      46.387  25.135  45.205  1.00 26.65           C  
ANISOU  114  CA  ILE A  63     3969   2419   3740   -538   -595    364       C  
ATOM    115  C   ILE A  63      46.514  23.766  44.543  1.00 35.62           C  
ANISOU  115  C   ILE A  63     4981   3740   4814   -461   -497    415       C  
ATOM    116  O   ILE A  63      45.884  23.496  43.513  1.00 36.22           O  
ANISOU  116  O   ILE A  63     5028   3788   4945   -378   -528    421       O  
ATOM    117  CB  ILE A  63      47.719  25.888  45.033  1.00 25.84           C  
ANISOU  117  CB  ILE A  63     3923   2392   3503   -743   -678    518       C  
ATOM    118  CG1 ILE A  63      47.619  27.299  45.611  1.00 33.32           C  
ANISOU  118  CG1 ILE A  63     5041   3124   4494   -843   -783    473       C  
ATOM    119  CG2 ILE A  63      48.111  25.947  43.563  1.00 22.70           C  
ANISOU  119  CG2 ILE A  63     3526   2055   3045   -795   -747    670       C  
ATOM    120  CD1 ILE A  63      46.581  28.159  44.935  1.00 44.25           C  
ANISOU  120  CD1 ILE A  63     6562   4248   6003   -751   -908    431       C  
ATOM    121  N   VAL A  64      47.329  22.908  45.151  1.00 32.49           N  
ANISOU  121  N   VAL A  64     4529   3526   4288   -475   -391    446       N  
ATOM    122  CA  VAL A  64      47.546  21.560  44.646  1.00 22.07           C  
ANISOU  122  CA  VAL A  64     3131   2371   2881   -386   -292    491       C  
ATOM    123  C   VAL A  64      46.228  20.808  44.535  1.00 21.88           C  
ANISOU  123  C   VAL A  64     3096   2247   2968   -259   -205    358       C  
ATOM    124  O   VAL A  64      45.971  20.164  43.528  1.00 37.11           O  
ANISOU  124  O   VAL A  64     4985   4221   4894   -200   -195    391       O  
ATOM    125  CB  VAL A  64      48.523  20.769  45.543  1.00 23.60           C  
ANISOU  125  CB  VAL A  64     3306   2746   2914   -373   -201    513       C  
ATOM    126  CG1 VAL A  64      48.427  19.277  45.266  1.00 19.95           C  
ANISOU  126  CG1 VAL A  64     2828   2379   2373   -234    -78    511       C  
ATOM    127  CG2 VAL A  64      49.944  21.260  45.330  1.00 26.92           C  
ANISOU  127  CG2 VAL A  64     3667   3357   3203   -495   -283    646       C  
ATOM    128  N   PHE A  65      45.392  20.911  45.563  1.00 22.16           N  
ANISOU  128  N   PHE A  65     3166   2157   3098   -234   -136    197       N  
ATOM    129  CA  PHE A  65      44.101  20.226  45.587  1.00 29.55           C  
ANISOU  129  CA  PHE A  65     4069   3020   4140   -153    -30     35       C  
ATOM    130  C   PHE A  65      43.226  20.619  44.394  1.00 27.91           C  
ANISOU  130  C   PHE A  65     3794   2743   4068    -99   -142      5       C  
ATOM    131  O   PHE A  65      42.773  19.761  43.623  1.00 27.64           O  
ANISOU  131  O   PHE A  65     3705   2758   4039    -49   -100    -13       O  
ATOM    132  CB  PHE A  65      43.374  20.527  46.904  1.00 27.63           C  
ANISOU  132  CB  PHE A  65     3862   2659   3976   -159     59   -146       C  
ATOM    133  CG  PHE A  65      42.014  19.897  47.013  1.00 20.32           C  
ANISOU  133  CG  PHE A  65     2877   1681   3162   -112    190   -343       C  
ATOM    134  CD1 PHE A  65      41.875  18.581  47.429  1.00 21.65           C  
ANISOU  134  CD1 PHE A  65     3088   1900   3237   -124    385   -394       C  
ATOM    135  CD2 PHE A  65      40.872  20.627  46.720  1.00 23.11           C  
ANISOU  135  CD2 PHE A  65     3140   1937   3705    -59    119   -491       C  
ATOM    136  CE1 PHE A  65      40.624  18.000  47.535  1.00 27.30           C  
ANISOU  136  CE1 PHE A  65     3747   2579   4047   -130    526   -590       C  
ATOM    137  CE2 PHE A  65      39.617  20.052  46.824  1.00 32.44           C  
ANISOU  137  CE2 PHE A  65     4221   3114   4992    -33    245   -701       C  
ATOM    138  CZ  PHE A  65      39.493  18.737  47.232  1.00 27.63           C  
ANISOU  138  CZ  PHE A  65     3646   2565   4289    -92    459   -752       C  
ATOM    139  N   VAL A  66      43.007  21.921  44.240  1.00 28.23           N  
ANISOU  139  N   VAL A  66     3864   2660   4204   -103   -297     -2       N  
ATOM    140  CA  VAL A  66      42.148  22.429  43.176  1.00 33.72           C  
ANISOU  140  CA  VAL A  66     4527   3267   5019    -17   -440    -40       C  
ATOM    141  C   VAL A  66      42.697  22.099  41.787  1.00 35.44           C  
ANISOU  141  C   VAL A  66     4748   3574   5142    -26   -517    132       C  
ATOM    142  O   VAL A  66      41.975  21.576  40.927  1.00 40.06           O  
ANISOU  142  O   VAL A  66     5266   4177   5775     56   -536     83       O  
ATOM    143  CB  VAL A  66      41.955  23.951  43.294  1.00 31.50           C  
ANISOU  143  CB  VAL A  66     4344   2807   4818     -4   -608    -59       C  
ATOM    144  CG1 VAL A  66      41.132  24.471  42.127  1.00 30.65           C  
ANISOU  144  CG1 VAL A  66     4238   2604   4805    120   -786    -86       C  
ATOM    145  CG2 VAL A  66      41.288  24.297  44.620  1.00 37.00           C  
ANISOU  145  CG2 VAL A  66     5033   3411   5615     27   -530   -255       C  
ATOM    146  N   VAL A  67      43.979  22.390  41.578  1.00 22.45           N  
ANISOU  146  N   VAL A  67     3172   2001   3356   -134   -553    320       N  
ATOM    147  CA  VAL A  67      44.605  22.159  40.279  1.00 29.28           C  
ANISOU  147  CA  VAL A  67     4049   2963   4112   -161   -610    486       C  
ATOM    148  C   VAL A  67      44.634  20.674  39.907  1.00 35.57           C  
ANISOU  148  C   VAL A  67     4763   3915   4839   -103   -478    488       C  
ATOM    149  O   VAL A  67      44.384  20.314  38.756  1.00 36.64           O  
ANISOU  149  O   VAL A  67     4889   4075   4956    -55   -523    527       O  
ATOM    150  CB  VAL A  67      46.035  22.724  40.244  1.00 29.92           C  
ANISOU  150  CB  VAL A  67     4190   3133   4046   -320   -641    663       C  
ATOM    151  CG1 VAL A  67      46.742  22.323  38.960  1.00 25.57           C  
ANISOU  151  CG1 VAL A  67     3630   2723   3361   -356   -654    821       C  
ATOM    152  CG2 VAL A  67      45.998  24.237  40.379  1.00 40.38           C  
ANISOU  152  CG2 VAL A  67     5654   4271   5419   -403   -787    677       C  
ATOM    153  N   ALA A  68      44.923  19.814  40.879  1.00 26.35           N  
ANISOU  153  N   ALA A  68     3566   2831   3614   -100   -319    442       N  
ATOM    154  CA  ALA A  68      44.956  18.374  40.633  1.00 31.95           C  
ANISOU  154  CA  ALA A  68     4251   3653   4236    -38   -186    436       C  
ATOM    155  C   ALA A  68      43.566  17.855  40.292  1.00 35.94           C  
ANISOU  155  C   ALA A  68     4717   4074   4865     28   -155    277       C  
ATOM    156  O   ALA A  68      43.394  17.105  39.326  1.00 49.99           O  
ANISOU  156  O   ALA A  68     6486   5905   6601     68   -146    300       O  
ATOM    157  CB  ALA A  68      45.516  17.629  41.835  1.00 16.37           C  
ANISOU  157  CB  ALA A  68     2311   1751   2159    -34    -37    414       C  
ATOM    158  N   LEU A  69      42.578  18.263  41.084  1.00 30.33           N  
ANISOU  158  N   LEU A  69     3975   3247   4302     34   -137    103       N  
ATOM    159  CA  LEU A  69      41.207  17.816  40.866  1.00 36.85           C  
ANISOU  159  CA  LEU A  69     4718   4027   5257     78    -99    -88       C  
ATOM    160  C   LEU A  69      40.705  18.223  39.479  1.00 35.88           C  
ANISOU  160  C   LEU A  69     4547   3887   5199    142   -280    -70       C  
ATOM    161  O   LEU A  69      40.388  17.361  38.640  1.00 34.03           O  
ANISOU  161  O   LEU A  69     4285   3713   4933    162   -259    -85       O  
ATOM    162  CB  LEU A  69      40.283  18.375  41.947  1.00 32.19           C  
ANISOU  162  CB  LEU A  69     4075   3339   4817     77    -57   -289       C  
ATOM    163  CG  LEU A  69      38.957  17.631  42.101  1.00 35.39           C  
ANISOU  163  CG  LEU A  69     4371   3749   5327     77     68   -526       C  
ATOM    164  CD1 LEU A  69      39.210  16.206  42.560  1.00 39.96           C  
ANISOU  164  CD1 LEU A  69     5035   4383   5766     -1    295   -530       C  
ATOM    165  CD2 LEU A  69      38.036  18.355  43.066  1.00 39.19           C  
ANISOU  165  CD2 LEU A  69     4770   4156   5964     91     95   -738       C  
ATOM    166  N   ILE A  70      40.653  19.534  39.242  1.00 28.31           N  
ANISOU  166  N   ILE A  70     3611   2834   4313    175   -465    -37       N  
ATOM    167  CA  ILE A  70      40.174  20.065  37.967  1.00 28.76           C  
ANISOU  167  CA  ILE A  70     3668   2844   4414    258   -666    -16       C  
ATOM    168  C   ILE A  70      40.970  19.490  36.798  1.00 31.72           C  
ANISOU  168  C   ILE A  70     4108   3316   4630    229   -685    171       C  
ATOM    169  O   ILE A  70      40.398  19.025  35.812  1.00 33.27           O  
ANISOU  169  O   ILE A  70     4270   3540   4832    289   -744    135       O  
ATOM    170  CB  ILE A  70      40.258  21.608  37.914  1.00 36.67           C  
ANISOU  170  CB  ILE A  70     4774   3696   5463    290   -863     36       C  
ATOM    171  CG1 ILE A  70      39.512  22.239  39.094  1.00 34.90           C  
ANISOU  171  CG1 ILE A  70     4500   3372   5389    337   -845   -155       C  
ATOM    172  CG2 ILE A  70      39.707  22.128  36.592  1.00 30.72           C  
ANISOU  172  CG2 ILE A  70     4066   2873   4733    402  -1086     54       C  
ATOM    173  CD1 ILE A  70      38.046  21.880  39.156  1.00 45.96           C  
ANISOU  173  CD1 ILE A  70     5720   4789   6953    454   -831   -418       C  
ATOM    174  N   GLY A  71      42.292  19.512  36.931  1.00 21.29           N  
ANISOU  174  N   GLY A  71     2866   2064   3160    138   -632    355       N  
ATOM    175  CA  GLY A  71      43.186  19.058  35.882  1.00 22.57           C  
ANISOU  175  CA  GLY A  71     3080   2339   3154    107   -634    533       C  
ATOM    176  C   GLY A  71      42.984  17.612  35.475  1.00 31.00           C  
ANISOU  176  C   GLY A  71     4106   3512   4161    151   -511    491       C  
ATOM    177  O   GLY A  71      42.805  17.315  34.291  1.00 27.23           O  
ANISOU  177  O   GLY A  71     3652   3059   3636    187   -579    531       O  
ATOM    178  N   ASN A  72      43.008  16.705  36.446  1.00 17.72           N  
ANISOU  178  N   ASN A  72     2396   1874   2463    143   -331    411       N  
ATOM    179  CA  ASN A  72      42.875  15.287  36.126  1.00 28.96           C  
ANISOU  179  CA  ASN A  72     3835   3368   3801    173   -200    374       C  
ATOM    180  C   ASN A  72      41.466  14.943  35.642  1.00 34.23           C  
ANISOU  180  C   ASN A  72     4438   3974   4592    200   -231    195       C  
ATOM    181  O   ASN A  72      41.293  14.100  34.744  1.00 38.05           O  
ANISOU  181  O   ASN A  72     4948   4503   5006    219   -217    194       O  
ATOM    182  CB  ASN A  72      43.259  14.430  37.331  1.00 27.72           C  
ANISOU  182  CB  ASN A  72     3722   3242   3570    161     -5    336       C  
ATOM    183  CG  ASN A  72      44.750  14.474  37.622  1.00 34.13           C  
ANISOU  183  CG  ASN A  72     4575   4173   4219    165     20    507       C  
ATOM    184  OD1 ASN A  72      45.545  13.832  36.935  1.00 47.56           O  
ANISOU  184  OD1 ASN A  72     6312   5994   5765    211     47    618       O  
ATOM    185  ND2 ASN A  72      45.136  15.235  38.640  1.00 28.05           N  
ANISOU  185  ND2 ASN A  72     3789   3386   3480    121      9    513       N  
ATOM    186  N   VAL A  73      40.463  15.608  36.215  1.00 33.20           N  
ANISOU  186  N   VAL A  73     4216   3757   4643    203   -279     29       N  
ATOM    187  CA  VAL A  73      39.096  15.443  35.725  1.00 22.27           C  
ANISOU  187  CA  VAL A  73     2720   2351   3390    235   -339   -167       C  
ATOM    188  C   VAL A  73      39.009  15.863  34.254  1.00 28.29           C  
ANISOU  188  C   VAL A  73     3499   3117   4132    309   -554    -85       C  
ATOM    189  O   VAL A  73      38.378  15.181  33.439  1.00 31.41           O  
ANISOU  189  O   VAL A  73     3858   3554   4523    325   -579   -166       O  
ATOM    190  CB  VAL A  73      38.087  16.247  36.570  1.00 19.99           C  
ANISOU  190  CB  VAL A  73     2304   1992   3300    257   -373   -368       C  
ATOM    191  CG1 VAL A  73      36.760  16.387  35.843  1.00 21.52           C  
ANISOU  191  CG1 VAL A  73     2345   2197   3635    332   -511   -562       C  
ATOM    192  CG2 VAL A  73      37.884  15.577  37.919  1.00 27.86           C  
ANISOU  192  CG2 VAL A  73     3285   2991   4309    165   -130   -499       C  
ATOM    193  N   LEU A  74      39.668  16.966  33.911  1.00 30.40           N  
ANISOU  193  N   LEU A  74     3848   3335   4367    337   -706     78       N  
ATOM    194  CA  LEU A  74      39.692  17.441  32.528  1.00 34.74           C  
ANISOU  194  CA  LEU A  74     4474   3865   4861    398   -909    182       C  
ATOM    195  C   LEU A  74      40.471  16.504  31.614  1.00 33.49           C  
ANISOU  195  C   LEU A  74     4401   3811   4512    363   -839    327       C  
ATOM    196  O   LEU A  74      40.175  16.412  30.425  1.00 28.92           O  
ANISOU  196  O   LEU A  74     3864   3238   3884    412   -963    348       O  
ATOM    197  CB  LEU A  74      40.288  18.846  32.439  1.00 21.39           C  
ANISOU  197  CB  LEU A  74     2904   2072   3150    398  -1061    330       C  
ATOM    198  CG  LEU A  74      39.395  20.000  32.889  1.00 30.68           C  
ANISOU  198  CG  LEU A  74     4053   3105   4498    491  -1218    197       C  
ATOM    199  CD1 LEU A  74      39.940  21.315  32.358  1.00 39.02           C  
ANISOU  199  CD1 LEU A  74     5313   4029   5485    493  -1405    366       C  
ATOM    200  CD2 LEU A  74      37.958  19.786  32.441  1.00 25.27           C  
ANISOU  200  CD2 LEU A  74     3232   2423   3948    628  -1333    -26       C  
ATOM    201  N   VAL A  75      41.477  15.828  32.162  1.00 22.69           N  
ANISOU  201  N   VAL A  75     3067   2529   3026    298   -650    421       N  
ATOM    202  CA  VAL A  75      42.221  14.835  31.393  1.00 24.33           C  
ANISOU  202  CA  VAL A  75     3349   2847   3046    294   -562    534       C  
ATOM    203  C   VAL A  75      41.282  13.706  30.989  1.00 26.38           C  
ANISOU  203  C   VAL A  75     3584   3114   3323    319   -512    380       C  
ATOM    204  O   VAL A  75      41.163  13.354  29.800  1.00 36.01           O  
ANISOU  204  O   VAL A  75     4858   4362   4461    350   -585    412       O  
ATOM    205  CB  VAL A  75      43.408  14.263  32.191  1.00 26.79           C  
ANISOU  205  CB  VAL A  75     3688   3260   3232    263   -375    629       C  
ATOM    206  CG1 VAL A  75      43.985  13.046  31.489  1.00 20.90           C  
ANISOU  206  CG1 VAL A  75     3016   2623   2301    302   -269    694       C  
ATOM    207  CG2 VAL A  75      44.478  15.328  32.390  1.00 40.67           C  
ANISOU  207  CG2 VAL A  75     5459   5054   4940    207   -428    788       C  
ATOM    208  N   CYS A  76      40.599  13.159  31.990  1.00 28.36           N  
ANISOU  208  N   CYS A  76     3766   3336   3672    287   -384    205       N  
ATOM    209  CA  CYS A  76      39.637  12.087  31.756  1.00 28.30           C  
ANISOU  209  CA  CYS A  76     3734   3332   3686    261   -312     28       C  
ATOM    210  C   CYS A  76      38.542  12.498  30.769  1.00 38.08           C  
ANISOU  210  C   CYS A  76     4878   4559   5031    302   -516    -88       C  
ATOM    211  O   CYS A  76      38.206  11.740  29.858  1.00 43.95           O  
ANISOU  211  O   CYS A  76     5655   5338   5706    299   -535   -130       O  
ATOM    212  CB  CYS A  76      39.017  11.642  33.079  1.00 29.28           C  
ANISOU  212  CB  CYS A  76     3801   3419   3906    184   -136   -154       C  
ATOM    213  SG  CYS A  76      40.233  11.021  34.259  1.00 44.76           S  
ANISOU  213  SG  CYS A  76     5912   5384   5713    164     89    -35       S  
ATOM    214  N   VAL A  77      37.996  13.698  30.950  1.00 34.02           N  
ANISOU  214  N   VAL A  77     4261   3992   4673    357   -682   -147       N  
ATOM    215  CA  VAL A  77      36.965  14.213  30.049  1.00 39.70           C  
ANISOU  215  CA  VAL A  77     4892   4702   5489    444   -916   -263       C  
ATOM    216  C   VAL A  77      37.487  14.329  28.616  1.00 40.94           C  
ANISOU  216  C   VAL A  77     5199   4866   5490    501  -1071    -85       C  
ATOM    217  O   VAL A  77      36.818  13.921  27.660  1.00 35.04           O  
ANISOU  217  O   VAL A  77     4434   4155   4727    535  -1180   -172       O  
ATOM    218  CB  VAL A  77      36.446  15.591  30.520  1.00 40.43           C  
ANISOU  218  CB  VAL A  77     4895   4716   5750    537  -1082   -334       C  
ATOM    219  CG1 VAL A  77      35.604  16.252  29.438  1.00 38.26           C  
ANISOU  219  CG1 VAL A  77     4586   4421   5530    683  -1374   -407       C  
ATOM    220  CG2 VAL A  77      35.649  15.442  31.805  1.00 41.73           C  
ANISOU  220  CG2 VAL A  77     4880   4894   6082    490   -940   -567       C  
ATOM    221  N   ALA A  78      38.691  14.877  28.481  1.00 35.38           N  
ANISOU  221  N   ALA A  78     4643   4139   4662    494  -1073    156       N  
ATOM    222  CA  ALA A  78      39.327  15.055  27.182  1.00 34.29           C  
ANISOU  222  CA  ALA A  78     4669   4010   4351    520  -1187    342       C  
ATOM    223  C   ALA A  78      39.465  13.731  26.445  1.00 41.05           C  
ANISOU  223  C   ALA A  78     5577   4956   5063    495  -1082    343       C  
ATOM    224  O   ALA A  78      39.135  13.635  25.262  1.00 42.49           O  
ANISOU  224  O   ALA A  78     5829   5144   5172    542  -1223    348       O  
ATOM    225  CB  ALA A  78      40.692  15.712  27.345  1.00 29.89           C  
ANISOU  225  CB  ALA A  78     4231   3450   3673    462  -1137    577       C  
ATOM    226  N   VAL A  79      39.951  12.709  27.143  1.00 33.15           N  
ANISOU  226  N   VAL A  79     4572   4014   4008    431   -842    337       N  
ATOM    227  CA  VAL A  79      40.121  11.408  26.502  1.00 33.31           C  
ANISOU  227  CA  VAL A  79     4683   4097   3876    418   -731    334       C  
ATOM    228  C   VAL A  79      38.774  10.746  26.191  1.00 36.93           C  
ANISOU  228  C   VAL A  79     5065   4545   4423    399   -777    100       C  
ATOM    229  O   VAL A  79      38.594  10.151  25.127  1.00 32.28           O  
ANISOU  229  O   VAL A  79     4557   3982   3725    411   -829     91       O  
ATOM    230  CB  VAL A  79      40.970  10.464  27.373  1.00 30.07           C  
ANISOU  230  CB  VAL A  79     4328   3731   3368    385   -473    378       C  
ATOM    231  CG1 VAL A  79      40.915   9.035  26.843  1.00 24.88           C  
ANISOU  231  CG1 VAL A  79     3788   3097   2567    381   -354    328       C  
ATOM    232  CG2 VAL A  79      42.407  10.956  27.434  1.00 30.69           C  
ANISOU  232  CG2 VAL A  79     4462   3878   3319    406   -434    602       C  
ATOM    233  N   TRP A  80      37.823  10.870  27.110  1.00 29.05           N  
ANISOU  233  N   TRP A  80     3903   3520   3616    360   -756   -100       N  
ATOM    234  CA  TRP A  80      36.555  10.156  26.988  1.00 24.32           C  
ANISOU  234  CA  TRP A  80     3192   2944   3104    298   -755   -356       C  
ATOM    235  C   TRP A  80      35.611  10.742  25.937  1.00 31.52           C  
ANISOU  235  C   TRP A  80     4007   3880   4089    381  -1039   -460       C  
ATOM    236  O   TRP A  80      34.870  10.003  25.288  1.00 37.97           O  
ANISOU  236  O   TRP A  80     4791   4747   4888    338  -1075   -612       O  
ATOM    237  CB  TRP A  80      35.849  10.111  28.345  1.00 33.66           C  
ANISOU  237  CB  TRP A  80     4214   4115   4461    211   -618   -555       C  
ATOM    238  CG  TRP A  80      36.468   9.137  29.306  1.00 41.61           C  
ANISOU  238  CG  TRP A  80     5348   5092   5370    110   -327   -521       C  
ATOM    239  CD1 TRP A  80      37.273   8.079  28.994  1.00 38.11           C  
ANISOU  239  CD1 TRP A  80     5121   4642   4718     93   -187   -403       C  
ATOM    240  CD2 TRP A  80      36.339   9.134  30.735  1.00 36.99           C  
ANISOU  240  CD2 TRP A  80     4711   4471   4873     34   -152   -609       C  
ATOM    241  NE1 TRP A  80      37.649   7.415  30.137  1.00 36.34           N  
ANISOU  241  NE1 TRP A  80     4996   4371   4442     27     51   -410       N  
ATOM    242  CE2 TRP A  80      37.091   8.044  31.220  1.00 37.72           C  
ANISOU  242  CE2 TRP A  80     5015   4526   4792    -22     79   -530       C  
ATOM    243  CE3 TRP A  80      35.660   9.946  31.649  1.00 38.74           C  
ANISOU  243  CE3 TRP A  80     4745   4685   5290     21   -170   -751       C  
ATOM    244  CZ2 TRP A  80      37.182   7.744  32.579  1.00 29.14           C  
ANISOU  244  CZ2 TRP A  80     3975   3385   3712    -98    285   -580       C  
ATOM    245  CZ3 TRP A  80      35.753   9.648  32.999  1.00 41.63           C  
ANISOU  245  CZ3 TRP A  80     5142   5008   5669    -71     52   -804       C  
ATOM    246  CH2 TRP A  80      36.508   8.555  33.450  1.00 36.47           C  
ANISOU  246  CH2 TRP A  80     4718   4308   4830   -134    274   -715       C  
ATOM    247  N   LYS A  81      35.639  12.060  25.762  1.00 30.11           N  
ANISOU  247  N   LYS A  81     3804   3659   3978    504  -1251   -382       N  
ATOM    248  CA  LYS A  81      34.663  12.715  24.892  1.00 32.04           C  
ANISOU  248  CA  LYS A  81     3963   3912   4297    626  -1549   -500       C  
ATOM    249  C   LYS A  81      35.160  12.926  23.465  1.00 40.82           C  
ANISOU  249  C   LYS A  81     5287   5001   5220    707  -1729   -314       C  
ATOM    250  O   LYS A  81      34.364  13.173  22.560  1.00 55.34           O  
ANISOU  250  O   LYS A  81     7100   6857   7070    808  -1975   -414       O  
ATOM    251  CB  LYS A  81      34.236  14.054  25.497  1.00 42.30           C  
ANISOU  251  CB  LYS A  81     5149   5151   5772    744  -1704   -554       C  
ATOM    252  CG  LYS A  81      33.577  13.905  26.859  1.00 63.50           C  
ANISOU  252  CG  LYS A  81     7605   7873   8651    673  -1541   -774       C  
ATOM    253  CD  LYS A  81      32.543  12.783  26.833  1.00 74.99           C  
ANISOU  253  CD  LYS A  81     8878   9451  10165    562  -1451  -1049       C  
ATOM    254  CE  LYS A  81      32.294  12.206  28.219  1.00 67.33           C  
ANISOU  254  CE  LYS A  81     7783   8505   9293    399  -1162  -1201       C  
ATOM    255  NZ  LYS A  81      31.486  10.956  28.152  1.00 55.35           N  
ANISOU  255  NZ  LYS A  81     6162   7089   7779    225  -1022  -1435       N  
ATOM    256  N   ASN A  82      36.469  12.828  23.261  1.00 38.66           N  
ANISOU  256  N   ASN A  82     5221   4703   4765    666  -1607    -57       N  
ATOM    257  CA  ASN A  82      37.035  12.967  21.924  1.00 36.48           C  
ANISOU  257  CA  ASN A  82     5163   4415   4282    714  -1731    125       C  
ATOM    258  C   ASN A  82      37.709  11.674  21.484  1.00 41.43           C  
ANISOU  258  C   ASN A  82     5909   5113   4719    631  -1530    194       C  
ATOM    259  O   ASN A  82      38.651  11.207  22.126  1.00 35.29           O  
ANISOU  259  O   ASN A  82     5169   4362   3876    566  -1293    298       O  
ATOM    260  CB  ASN A  82      38.024  14.130  21.880  1.00 33.34           C  
ANISOU  260  CB  ASN A  82     4922   3939   3807    736  -1782    369       C  
ATOM    261  CG  ASN A  82      37.455  15.394  22.487  1.00 40.25           C  
ANISOU  261  CG  ASN A  82     5715   4716   4863    815  -1940    304       C  
ATOM    262  OD1 ASN A  82      37.702  15.698  23.655  1.00 50.69           O  
ANISOU  262  OD1 ASN A  82     6948   6017   6297    773  -1826    299       O  
ATOM    263  ND2 ASN A  82      36.680  16.133  21.702  1.00 33.24           N  
ANISOU  263  ND2 ASN A  82     4850   3774   4006    904  -2117    230       N  
ATOM    264  N   HIS A  83      37.223  11.096  20.390  1.00 31.77           N  
ANISOU  264  N   HIS A  83     4753   3920   3399    652  -1635    127       N  
ATOM    265  CA  HIS A  83      37.652   9.763  19.982  1.00 36.18           C  
ANISOU  265  CA  HIS A  83     5428   4532   3786    583  -1451    141       C  
ATOM    266  C   HIS A  83      39.081   9.730  19.450  1.00 40.34           C  
ANISOU  266  C   HIS A  83     6166   5080   4080    594  -1341    405       C  
ATOM    267  O   HIS A  83      39.763   8.712  19.564  1.00 41.36           O  
ANISOU  267  O   HIS A  83     6377   5255   4082    560  -1121    446       O  
ATOM    268  CB  HIS A  83      36.703   9.196  18.928  1.00 29.57           C  
ANISOU  268  CB  HIS A  83     4609   3722   2903    593  -1610    -17       C  
ATOM    269  CG  HIS A  83      36.816   7.714  18.755  1.00 50.59           C  
ANISOU  269  CG  HIS A  83     7367   6417   5438    499  -1411    -83       C  
ATOM    270  ND1 HIS A  83      36.274   6.821  19.654  1.00 59.62           N  
ANISOU  270  ND1 HIS A  83     8404   7565   6684    380  -1233   -275       N  
ATOM    271  CD2 HIS A  83      37.415   6.968  17.797  1.00 50.42           C  
ANISOU  271  CD2 HIS A  83     7568   6410   5180    505  -1355     15       C  
ATOM    272  CE1 HIS A  83      36.530   5.589  19.254  1.00 60.58           C  
ANISOU  272  CE1 HIS A  83     8701   7684   6634    318  -1084   -289       C  
ATOM    273  NE2 HIS A  83      37.220   5.649  18.130  1.00 53.58           N  
ANISOU  273  NE2 HIS A  83     8005   6808   5544    404  -1157   -119       N  
ATOM    274  N   HIS A  84      39.537  10.835  18.869  1.00 41.70           N  
ANISOU  274  N   HIS A  84     6434   5222   4187    641  -1485    574       N  
ATOM    275  CA  HIS A  84      40.898  10.893  18.344  1.00 37.96           C  
ANISOU  275  CA  HIS A  84     6017   4821   3587    574  -1261    763       C  
ATOM    276  C   HIS A  84      41.916  10.852  19.485  1.00 39.87           C  
ANISOU  276  C   HIS A  84     6177   5120   3852    526  -1043    851       C  
ATOM    277  O   HIS A  84      43.112  10.649  19.262  1.00 49.33           O  
ANISOU  277  O   HIS A  84     7351   6428   4962    472   -852    966       O  
ATOM    278  CB  HIS A  84      41.096  12.146  17.481  1.00 34.76           C  
ANISOU  278  CB  HIS A  84     5640   4383   3182    560  -1346    859       C  
ATOM    279  CG  HIS A  84      41.033  13.428  18.249  1.00 42.98           C  
ANISOU  279  CG  HIS A  84     6617   5347   4364    557  -1413    882       C  
ATOM    280  ND1 HIS A  84      42.150  14.014  18.808  1.00 48.28           N  
ANISOU  280  ND1 HIS A  84     7251   6063   5030    483  -1251   1012       N  
ATOM    281  CD2 HIS A  84      39.992  14.239  18.554  1.00 33.62           C  
ANISOU  281  CD2 HIS A  84     5395   4049   3329    627  -1627    776       C  
ATOM    282  CE1 HIS A  84      41.797  15.130  19.424  1.00 51.91           C  
ANISOU  282  CE1 HIS A  84     7690   6417   5615    492  -1360    994       C  
ATOM    283  NE2 HIS A  84      40.494  15.287  19.284  1.00 48.69           N  
ANISOU  283  NE2 HIS A  84     7280   5912   5309    586  -1582    853       N  
ATOM    284  N   MET A  85      41.428  11.031  20.709  1.00 28.18           N  
ANISOU  284  N   MET A  85     4631   3578   2497    550  -1093    778       N  
ATOM    285  CA  MET A  85      42.261  10.943  21.899  1.00 28.40           C  
ANISOU  285  CA  MET A  85     4595   3649   2545    518   -902    839       C  
ATOM    286  C   MET A  85      42.450   9.500  22.349  1.00 32.70           C  
ANISOU  286  C   MET A  85     5152   4246   3026    524   -682    763       C  
ATOM    287  O   MET A  85      43.238   9.227  23.251  1.00 43.30           O  
ANISOU  287  O   MET A  85     6465   5639   4347    523   -508    812       O  
ATOM    288  CB  MET A  85      41.649  11.758  23.041  1.00 31.56           C  
ANISOU  288  CB  MET A  85     4843   3969   3179    502   -965    747       C  
ATOM    289  CG  MET A  85      41.502  13.235  22.745  1.00 39.72           C  
ANISOU  289  CG  MET A  85     5902   4919   4271    515  -1178    821       C  
ATOM    290  SD  MET A  85      43.101  14.043  22.615  1.00 41.68           S  
ANISOU  290  SD  MET A  85     6146   5262   4426    415   -989   1017       S  
ATOM    291  CE  MET A  85      43.802  13.635  24.213  1.00 37.11           C  
ANISOU  291  CE  MET A  85     5475   4744   3882    385   -814   1035       C  
ATOM    292  N   ARG A  86      41.728   8.575  21.725  1.00 30.87           N  
ANISOU  292  N   ARG A  86     4470   3628   3630   1499  -1090   -322       N  
ATOM    293  CA  ARG A  86      41.720   7.195  22.199  1.00 35.31           C  
ANISOU  293  CA  ARG A  86     5094   4143   4179   1284  -1131   -364       C  
ATOM    294  C   ARG A  86      42.901   6.390  21.685  1.00 36.28           C  
ANISOU  294  C   ARG A  86     5474   4081   4232   1340  -1081   -302       C  
ATOM    295  O   ARG A  86      42.820   5.718  20.658  1.00 44.86           O  
ANISOU  295  O   ARG A  86     6738   5110   5198   1380  -1163   -331       O  
ATOM    296  CB  ARG A  86      40.407   6.511  21.821  1.00 36.21           C  
ANISOU  296  CB  ARG A  86     5152   4385   4220   1143  -1299   -475       C  
ATOM    297  CG  ARG A  86      39.214   7.141  22.512  1.00 57.54           C  
ANISOU  297  CG  ARG A  86     7571   7307   6983   1073  -1337   -517       C  
ATOM    298  CD  ARG A  86      37.963   6.294  22.406  1.00 74.32           C  
ANISOU  298  CD  ARG A  86     9601   9591   9047    860  -1495   -615       C  
ATOM    299  NE  ARG A  86      36.843   6.940  23.084  1.00 84.29           N  
ANISOU  299  NE  ARG A  86    10568  11097  10361    823  -1518   -630       N  
ATOM    300  CZ  ARG A  86      36.635   6.885  24.396  1.00 79.99           C  
ANISOU  300  CZ  ARG A  86     9883  10590   9920    682  -1449   -620       C  
ATOM    301  NH1 ARG A  86      37.471   6.209  25.174  1.00 74.01           N  
ANISOU  301  NH1 ARG A  86     9247   9648   9225    561  -1358   -602       N  
ATOM    302  NH2 ARG A  86      35.592   7.506  24.930  1.00 78.27           N  
ANISOU  302  NH2 ARG A  86     9403  10605   9729    685  -1464   -620       N  
ATOM    303  N   THR A  87      44.002   6.473  22.421  1.00 39.30           N  
ANISOU  303  N   THR A  87     5874   4382   4674   1351   -942   -211       N  
ATOM    304  CA  THR A  87      45.170   5.642  22.180  1.00 25.99           C  
ANISOU  304  CA  THR A  87     4404   2554   2917   1408   -868   -127       C  
ATOM    305  C   THR A  87      45.476   4.870  23.458  1.00 30.08           C  
ANISOU  305  C   THR A  87     4898   3054   3479   1240   -798   -114       C  
ATOM    306  O   THR A  87      44.970   5.214  24.528  1.00 23.78           O  
ANISOU  306  O   THR A  87     3905   2346   2784   1104   -790   -153       O  
ATOM    307  CB  THR A  87      46.394   6.479  21.758  1.00 30.01           C  
ANISOU  307  CB  THR A  87     4855   3113   3433   1446   -679    -18       C  
ATOM    308  OG1 THR A  87      46.806   7.318  22.845  1.00 37.59           O  
ANISOU  308  OG1 THR A  87     5645   4127   4511   1386   -584     31       O  
ATOM    309  CG2 THR A  87      46.057   7.346  20.555  1.00 22.68           C  
ANISOU  309  CG2 THR A  87     3908   2240   2471   1529   -691    -38       C  
ATOM    310  N   VAL A  88      46.293   3.827  23.345  1.00 30.99           N  
ANISOU  310  N   VAL A  88     5224   3053   3500   1271   -740    -52       N  
ATOM    311  CA  VAL A  88      46.679   3.026  24.502  1.00 30.19           C  
ANISOU  311  CA  VAL A  88     5131   2929   3412   1152   -655    -23       C  
ATOM    312  C   VAL A  88      47.355   3.904  25.553  1.00 31.55           C  
ANISOU  312  C   VAL A  88     5096   3195   3698   1154   -549     54       C  
ATOM    313  O   VAL A  88      47.020   3.852  26.750  1.00 43.62           O  
ANISOU  313  O   VAL A  88     6483   4782   5307   1001   -528     18       O  
ATOM    314  CB  VAL A  88      47.617   1.876  24.092  1.00 24.86           C  
ANISOU  314  CB  VAL A  88     4740   2121   2586   1253   -576     63       C  
ATOM    315  CG1 VAL A  88      48.130   1.142  25.314  1.00 28.59           C  
ANISOU  315  CG1 VAL A  88     5223   2580   3058   1183   -465    118       C  
ATOM    316  CG2 VAL A  88      46.895   0.917  23.166  1.00 24.27           C  
ANISOU  316  CG2 VAL A  88     4919   1922   2382   1215   -685    -29       C  
ATOM    317  N   THR A  89      48.294   4.723  25.085  1.00 26.82           N  
ANISOU  317  N   THR A  89     4437   2651   3101   1253   -460    144       N  
ATOM    318  CA  THR A  89      48.988   5.689  25.929  1.00 40.89           C  
ANISOU  318  CA  THR A  89     6033   4526   4976   1223   -368    211       C  
ATOM    319  C   THR A  89      48.007   6.544  26.723  1.00 34.20           C  
ANISOU  319  C   THR A  89     5038   3709   4246   1166   -437    127       C  
ATOM    320  O   THR A  89      48.152   6.709  27.932  1.00 34.72           O  
ANISOU  320  O   THR A  89     4977   3836   4378   1053   -385    130       O  
ATOM    321  CB  THR A  89      49.894   6.615  25.092  1.00 38.57           C  
ANISOU  321  CB  THR A  89     5673   4300   4680   1246   -283    278       C  
ATOM    322  OG1 THR A  89      50.881   5.832  24.410  1.00 51.70           O  
ANISOU  322  OG1 THR A  89     7427   5975   6242   1278   -209    342       O  
ATOM    323  CG2 THR A  89      50.587   7.635  25.983  1.00 34.95           C  
ANISOU  323  CG2 THR A  89     5071   3906   4304   1208   -213    340       C  
ATOM    324  N   ASN A  90      46.996   7.068  26.037  1.00 27.40           N  
ANISOU  324  N   ASN A  90     4154   2857   3399   1193   -530     42       N  
ATOM    325  CA  ASN A  90      46.023   7.953  26.667  1.00 28.23           C  
ANISOU  325  CA  ASN A  90     4082   3048   3597   1114   -561    -36       C  
ATOM    326  C   ASN A  90      45.071   7.240  27.623  1.00 30.85           C  
ANISOU  326  C   ASN A  90     4318   3435   3967    932   -609   -122       C  
ATOM    327  O   ASN A  90      44.622   7.833  28.600  1.00 36.52           O  
ANISOU  327  O   ASN A  90     4885   4227   4767    855   -586   -151       O  
ATOM    328  CB  ASN A  90      45.222   8.692  25.599  1.00 26.49           C  
ANISOU  328  CB  ASN A  90     3862   2850   3354   1235   -638    -83       C  
ATOM    329  CG  ASN A  90      45.968   9.886  25.037  1.00 27.89           C  
ANISOU  329  CG  ASN A  90     4055   3013   3530   1334   -536     -6       C  
ATOM    330  OD1 ASN A  90      47.117  10.140  25.400  1.00 36.02           O  
ANISOU  330  OD1 ASN A  90     5080   4027   4579   1286   -422     79       O  
ATOM    331  ND2 ASN A  90      45.320  10.625  24.144  1.00 24.04           N  
ANISOU  331  ND2 ASN A  90     3559   2563   3011   1408   -557    -36       N  
ATOM    332  N   TYR A  91      44.753   5.979  27.340  1.00 29.32           N  
ANISOU  332  N   TYR A  91     4233   3198   3708    862   -668   -160       N  
ATOM    333  CA  TYR A  91      43.967   5.175  28.271  1.00 20.64           C  
ANISOU  333  CA  TYR A  91     3066   2137   2640    668   -694   -228       C  
ATOM    334  C   TYR A  91      44.744   5.013  29.575  1.00 27.48           C  
ANISOU  334  C   TYR A  91     3889   2999   3554    610   -576   -169       C  
ATOM    335  O   TYR A  91      44.208   5.210  30.680  1.00 41.11           O  
ANISOU  335  O   TYR A  91     5461   4800   5360    497   -560   -205       O  
ATOM    336  CB  TYR A  91      43.635   3.804  27.678  1.00 23.60           C  
ANISOU  336  CB  TYR A  91     3624   2430   2913    588   -761   -274       C  
ATOM    337  CG  TYR A  91      42.454   3.786  26.729  1.00 39.28           C  
ANISOU  337  CG  TYR A  91     5594   4475   4853    549   -911   -369       C  
ATOM    338  CD1 TYR A  91      41.182   4.137  27.165  1.00 42.25           C  
ANISOU  338  CD1 TYR A  91     5751   5011   5291    428   -986   -444       C  
ATOM    339  CD2 TYR A  91      42.606   3.387  25.405  1.00 36.23           C  
ANISOU  339  CD2 TYR A  91     5411   4006   4348    640   -977   -377       C  
ATOM    340  CE1 TYR A  91      40.097   4.112  26.304  1.00 50.65           C  
ANISOU  340  CE1 TYR A  91     6769   6179   6297    390  -1129   -521       C  
ATOM    341  CE2 TYR A  91      41.526   3.358  24.536  1.00 38.28           C  
ANISOU  341  CE2 TYR A  91     5648   4347   4550    596  -1126   -468       C  
ATOM    342  CZ  TYR A  91      40.274   3.722  24.991  1.00 47.02           C  
ANISOU  342  CZ  TYR A  91     6508   5641   5717    466  -1205   -538       C  
ATOM    343  OH  TYR A  91      39.195   3.696  24.136  1.00 39.33           O  
ANISOU  343  OH  TYR A  91     5479   4796   4669    420  -1360   -619       O  
ATOM    344  N   PHE A  92      46.018   4.660  29.431  1.00 19.25           N  
ANISOU  344  N   PHE A  92     2976   1887   2451    704   -491    -71       N  
ATOM    345  CA  PHE A  92      46.912   4.552  30.576  1.00 22.17           C  
ANISOU  345  CA  PHE A  92     3297   2287   2842    678   -379      3       C  
ATOM    346  C   PHE A  92      46.969   5.867  31.352  1.00 24.01           C  
ANISOU  346  C   PHE A  92     3338   2611   3173    652   -348      4       C  
ATOM    347  O   PHE A  92      46.878   5.885  32.584  1.00 19.25           O  
ANISOU  347  O   PHE A  92     2627   2064   2623    551   -307    -10       O  
ATOM    348  CB  PHE A  92      48.310   4.147  30.117  1.00 24.60           C  
ANISOU  348  CB  PHE A  92     3747   2551   3047    823   -295    132       C  
ATOM    349  CG  PHE A  92      48.474   2.670  29.901  1.00 37.23           C  
ANISOU  349  CG  PHE A  92     5564   4051   4529    842   -269    154       C  
ATOM    350  CD1 PHE A  92      47.960   1.765  30.813  1.00 42.30           C  
ANISOU  350  CD1 PHE A  92     6225   4673   5174    704   -251    104       C  
ATOM    351  CD2 PHE A  92      49.137   2.185  28.786  1.00 37.82           C  
ANISOU  351  CD2 PHE A  92     5850   4040   4478   1005   -251    228       C  
ATOM    352  CE1 PHE A  92      48.104   0.404  30.620  1.00 40.49           C  
ANISOU  352  CE1 PHE A  92     6243   4323   4820    719   -209    123       C  
ATOM    353  CE2 PHE A  92      49.286   0.824  28.588  1.00 28.76           C  
ANISOU  353  CE2 PHE A  92     4954   2775   3198   1036   -213    249       C  
ATOM    354  CZ  PHE A  92      48.768  -0.066  29.504  1.00 31.38           C  
ANISOU  354  CZ  PHE A  92     5323   3071   3529    887   -189    194       C  
ATOM    355  N   ILE A  93      47.108   6.964  30.615  1.00 25.06           N  
ANISOU  355  N   ILE A  93     3455   2746   3320    749   -362     18       N  
ATOM    356  CA  ILE A  93      47.142   8.301  31.197  1.00 25.58           C  
ANISOU  356  CA  ILE A  93     3398   2863   3457    730   -326     14       C  
ATOM    357  C   ILE A  93      45.869   8.585  31.996  1.00 24.17           C  
ANISOU  357  C   ILE A  93     3094   2739   3349    635   -365    -82       C  
ATOM    358  O   ILE A  93      45.921   9.170  33.082  1.00 33.23           O  
ANISOU  358  O   ILE A  93     4152   3928   4547    567   -314    -88       O  
ATOM    359  CB  ILE A  93      47.335   9.370  30.100  1.00 28.02           C  
ANISOU  359  CB  ILE A  93     3756   3136   3753    861   -329     40       C  
ATOM    360  CG1 ILE A  93      48.783   9.355  29.602  1.00 27.21           C  
ANISOU  360  CG1 ILE A  93     3734   3010   3593    940   -258    163       C  
ATOM    361  CG2 ILE A  93      46.975  10.746  30.613  1.00 23.18           C  
ANISOU  361  CG2 ILE A  93     3063   2545   3200    841   -299      7       C  
ATOM    362  CD1 ILE A  93      49.035  10.249  28.411  1.00 21.30           C  
ANISOU  362  CD1 ILE A  93     3059   2213   2822   1078   -251    201       C  
ATOM    363  N   VAL A  94      44.731   8.147  31.466  1.00 18.13           N  
ANISOU  363  N   VAL A  94     2323   1988   2576    628   -456   -153       N  
ATOM    364  CA  VAL A  94      43.463   8.268  32.177  1.00 23.99           C  
ANISOU  364  CA  VAL A  94     2925   2817   3372    543   -495   -228       C  
ATOM    365  C   VAL A  94      43.522   7.523  33.498  1.00 23.71           C  
ANISOU  365  C   VAL A  94     2837   2801   3371    403   -446   -230       C  
ATOM    366  O   VAL A  94      43.127   8.059  34.532  1.00 27.33           O  
ANISOU  366  O   VAL A  94     3180   3319   3885    358   -410   -249       O  
ATOM    367  CB  VAL A  94      42.283   7.735  31.348  1.00 25.27           C  
ANISOU  367  CB  VAL A  94     3073   3029   3501    527   -612   -294       C  
ATOM    368  CG1 VAL A  94      41.081   7.453  32.240  1.00 20.30           C  
ANISOU  368  CG1 VAL A  94     2283   2513   2918    395   -642   -350       C  
ATOM    369  CG2 VAL A  94      41.917   8.730  30.280  1.00 30.37           C  
ANISOU  369  CG2 VAL A  94     3718   3704   4117    684   -657   -299       C  
ATOM    370  N   ASN A  95      44.021   6.289  33.462  1.00 18.23           N  
ANISOU  370  N   ASN A  95     2247   2048   2631    354   -433   -207       N  
ATOM    371  CA  ASN A  95      44.205   5.519  34.692  1.00 21.06           C  
ANISOU  371  CA  ASN A  95     2583   2414   3005    247   -367   -196       C  
ATOM    372  C   ASN A  95      45.027   6.294  35.724  1.00 28.25           C  
ANISOU  372  C   ASN A  95     3420   3366   3949    260   -280   -149       C  
ATOM    373  O   ASN A  95      44.662   6.385  36.908  1.00 37.19           O  
ANISOU  373  O   ASN A  95     4450   4551   5129    183   -245   -172       O  
ATOM    374  CB  ASN A  95      44.874   4.182  34.381  1.00 18.21           C  
ANISOU  374  CB  ASN A  95     2400   1963   2557    247   -337   -154       C  
ATOM    375  CG  ASN A  95      44.875   3.242  35.566  1.00 25.35           C  
ANISOU  375  CG  ASN A  95     3305   2865   3460    146   -265   -148       C  
ATOM    376  OD1 ASN A  95      43.824   2.773  36.000  1.00 30.44           O  
ANISOU  376  OD1 ASN A  95     3900   3526   4141     16   -294   -213       O  
ATOM    377  ND2 ASN A  95      46.060   2.951  36.090  1.00 27.04           N  
ANISOU  377  ND2 ASN A  95     3572   3077   3625    209   -166    -61       N  
ATOM    378  N   LEU A  96      46.128   6.868  35.251  1.00 24.06           N  
ANISOU  378  N   LEU A  96     2940   2816   3384    350   -246    -81       N  
ATOM    379  CA  LEU A  96      47.000   7.695  36.080  1.00 24.66           C  
ANISOU  379  CA  LEU A  96     2955   2941   3472    337   -176    -36       C  
ATOM    380  C   LEU A  96      46.232   8.848  36.735  1.00 25.21           C  
ANISOU  380  C   LEU A  96     2930   3041   3610    298   -180   -100       C  
ATOM    381  O   LEU A  96      46.344   9.085  37.944  1.00 22.63           O  
ANISOU  381  O   LEU A  96     2537   2759   3303    226   -134   -107       O  
ATOM    382  CB  LEU A  96      48.155   8.234  35.232  1.00 21.98           C  
ANISOU  382  CB  LEU A  96     2679   2587   3084    424   -151     46       C  
ATOM    383  CG  LEU A  96      49.368   8.825  35.946  1.00 30.52           C  
ANISOU  383  CG  LEU A  96     3710   3742   4144    382    -79    118       C  
ATOM    384  CD1 LEU A  96      49.906   7.842  36.960  1.00 28.15           C  
ANISOU  384  CD1 LEU A  96     3372   3521   3804    339    -29    162       C  
ATOM    385  CD2 LEU A  96      50.439   9.176  34.932  1.00 40.03           C  
ANISOU  385  CD2 LEU A  96     4973   4944   5294    465    -56    214       C  
ATOM    386  N   SER A  97      45.441   9.551  35.929  1.00 30.12           N  
ANISOU  386  N   SER A  97     3557   3639   4248    365   -230   -141       N  
ATOM    387  CA  SER A  97      44.650  10.677  36.414  1.00 29.79           C  
ANISOU  387  CA  SER A  97     3458   3619   4243    376   -221   -189       C  
ATOM    388  C   SER A  97      43.589  10.248  37.423  1.00 30.01           C  
ANISOU  388  C   SER A  97     3375   3716   4312    308   -228   -237       C  
ATOM    389  O   SER A  97      43.262  10.997  38.340  1.00 27.38           O  
ANISOU  389  O   SER A  97     2999   3406   3998    299   -185   -256       O  
ATOM    390  CB  SER A  97      43.985  11.406  35.244  1.00 21.26           C  
ANISOU  390  CB  SER A  97     2411   2520   3149    502   -265   -208       C  
ATOM    391  OG  SER A  97      44.936  12.141  34.498  1.00 29.78           O  
ANISOU  391  OG  SER A  97     3594   3526   4194    569   -231   -160       O  
ATOM    392  N   LEU A  98      43.050   9.046  37.244  1.00 25.43           N  
ANISOU  392  N   LEU A  98     2767   3161   3736    256   -277   -255       N  
ATOM    393  CA  LEU A  98      42.061   8.509  38.171  1.00 26.19           C  
ANISOU  393  CA  LEU A  98     2752   3327   3870    170   -278   -290       C  
ATOM    394  C   LEU A  98      42.701   8.228  39.526  1.00 29.82           C  
ANISOU  394  C   LEU A  98     3201   3788   4343     99   -196   -268       C  
ATOM    395  O   LEU A  98      42.138   8.572  40.570  1.00 26.29           O  
ANISOU  395  O   LEU A  98     2669   3392   3927     76   -160   -286       O  
ATOM    396  CB  LEU A  98      41.425   7.235  37.610  1.00 25.71           C  
ANISOU  396  CB  LEU A  98     2694   3277   3797     94   -345   -314       C  
ATOM    397  CG  LEU A  98      40.495   7.420  36.407  1.00 31.69           C  
ANISOU  397  CG  LEU A  98     3422   4084   4533    139   -446   -349       C  
ATOM    398  CD1 LEU A  98      39.958   6.082  35.927  1.00 24.72           C  
ANISOU  398  CD1 LEU A  98     2569   3202   3623     13   -516   -382       C  
ATOM    399  CD2 LEU A  98      39.354   8.366  36.749  1.00 27.42           C  
ANISOU  399  CD2 LEU A  98     2726   3672   4020    193   -455   -368       C  
ATOM    400  N   ALA A  99      43.877   7.604  39.505  1.00 28.12           N  
ANISOU  400  N   ALA A  99     3069   3529   4087     85   -162   -220       N  
ATOM    401  CA  ALA A  99      44.627   7.370  40.738  1.00 24.67           C  
ANISOU  401  CA  ALA A  99     2616   3119   3639     39    -85   -188       C  
ATOM    402  C   ALA A  99      44.927   8.694  41.444  1.00 33.79           C  
ANISOU  402  C   ALA A  99     3737   4299   4802     44    -51   -196       C  
ATOM    403  O   ALA A  99      44.781   8.815  42.673  1.00 25.01           O  
ANISOU  403  O   ALA A  99     2573   3229   3702      1     -7   -210       O  
ATOM    404  CB  ALA A  99      45.918   6.619  40.445  1.00 20.82           C  
ANISOU  404  CB  ALA A  99     2217   2614   3080     63    -50   -115       C  
ATOM    405  N   ASP A 100      45.335   9.688  40.656  1.00 31.83           N  
ANISOU  405  N   ASP A 100     3543   4014   4538     95    -67   -187       N  
ATOM    406  CA  ASP A 100      45.646  11.009  41.194  1.00 32.64           C  
ANISOU  406  CA  ASP A 100     3666   4105   4629     82    -30   -199       C  
ATOM    407  C   ASP A 100      44.422  11.687  41.818  1.00 29.15           C  
ANISOU  407  C   ASP A 100     3191   3667   4219    110    -20   -256       C  
ATOM    408  O   ASP A 100      44.531  12.324  42.866  1.00 22.79           O  
ANISOU  408  O   ASP A 100     2398   2863   3397     73     27   -273       O  
ATOM    409  CB  ASP A 100      46.245  11.896  40.102  1.00 35.18           C  
ANISOU  409  CB  ASP A 100     4077   4366   4924    129    -38   -175       C  
ATOM    410  CG  ASP A 100      47.684  11.528  39.779  1.00 58.71           C  
ANISOU  410  CG  ASP A 100     7080   7373   7856     96    -22    -98       C  
ATOM    411  OD1 ASP A 100      48.369  10.974  40.665  1.00 57.60           O  
ANISOU  411  OD1 ASP A 100     6889   7311   7687     28      7    -66       O  
ATOM    412  OD2 ASP A 100      48.131  11.795  38.643  1.00 74.68           O  
ANISOU  412  OD2 ASP A 100     9163   9354   9858    154    -34    -59       O  
ATOM    413  N   VAL A 101      43.264  11.547  41.178  1.00 19.72           N  
ANISOU  413  N   VAL A 101     1953   2486   3052    181    -64   -279       N  
ATOM    414  CA  VAL A 101      42.016  12.076  41.727  1.00 28.36           C  
ANISOU  414  CA  VAL A 101     2988   3625   4163    237    -49   -310       C  
ATOM    415  C   VAL A 101      41.688  11.385  43.047  1.00 29.71           C  
ANISOU  415  C   VAL A 101     3071   3857   4361    163    -15   -315       C  
ATOM    416  O   VAL A 101      41.298  12.031  44.025  1.00 35.20           O  
ANISOU  416  O   VAL A 101     3762   4566   5047    189     38   -327       O  
ATOM    417  CB  VAL A 101      40.832  11.897  40.745  1.00 23.17           C  
ANISOU  417  CB  VAL A 101     2258   3029   3517    317   -114   -319       C  
ATOM    418  CG1 VAL A 101      39.504  12.112  41.457  1.00 24.78           C  
ANISOU  418  CG1 VAL A 101     2345   3338   3732    366    -95   -328       C  
ATOM    419  CG2 VAL A 101      40.962  12.848  39.572  1.00 25.30           C  
ANISOU  419  CG2 VAL A 101     2622   3244   3747    437   -129   -313       C  
ATOM    420  N   LEU A 102      41.857  10.065  43.063  1.00 26.44           N  
ANISOU  420  N   LEU A 102     2612   3467   3968     83    -34   -303       N  
ATOM    421  CA  LEU A 102      41.635   9.266  44.261  1.00 33.74           C  
ANISOU  421  CA  LEU A 102     3469   4437   4912     14     11   -300       C  
ATOM    422  C   LEU A 102      42.445   9.787  45.446  1.00 36.00           C  
ANISOU  422  C   LEU A 102     3796   4716   5167     -4     76   -295       C  
ATOM    423  O   LEU A 102      41.885  10.152  46.492  1.00 35.66           O  
ANISOU  423  O   LEU A 102     3717   4704   5130     11    121   -309       O  
ATOM    424  CB  LEU A 102      41.987   7.802  43.991  1.00 29.37           C  
ANISOU  424  CB  LEU A 102     2930   3871   4358    -61      0   -280       C  
ATOM    425  CG  LEU A 102      42.022   6.876  45.209  1.00 32.79           C  
ANISOU  425  CG  LEU A 102     3333   4331   4796   -124     68   -265       C  
ATOM    426  CD1 LEU A 102      40.658   6.822  45.886  1.00 27.00           C  
ANISOU  426  CD1 LEU A 102     2482   3663   4112   -145     83   -284       C  
ATOM    427  CD2 LEU A 102      42.485   5.484  44.808  1.00 30.19           C  
ANISOU  427  CD2 LEU A 102     3078   3956   4437   -173     76   -238       C  
ATOM    428  N   VAL A 103      43.764   9.833  45.273  1.00 22.41           N  
ANISOU  428  N   VAL A 103     2145   2968   3402    -35     80   -271       N  
ATOM    429  CA  VAL A 103      44.644  10.253  46.358  1.00 27.45           C  
ANISOU  429  CA  VAL A 103     2808   3630   3991    -82    127   -266       C  
ATOM    430  C   VAL A 103      44.437  11.737  46.700  1.00 34.94           C  
ANISOU  430  C   VAL A 103     3827   4533   4916    -64    144   -306       C  
ATOM    431  O   VAL A 103      44.647  12.155  47.839  1.00 27.43           O  
ANISOU  431  O   VAL A 103     2899   3596   3925    -99    184   -324       O  
ATOM    432  CB  VAL A 103      46.133   9.980  46.013  1.00 23.83           C  
ANISOU  432  CB  VAL A 103     2382   3198   3474   -124    124   -214       C  
ATOM    433  CG1 VAL A 103      46.589  10.819  44.826  1.00 28.13           C  
ANISOU  433  CG1 VAL A 103     2997   3686   4006   -109     89   -205       C  
ATOM    434  CG2 VAL A 103      47.024  10.222  47.223  1.00 19.06           C  
ANISOU  434  CG2 VAL A 103     1769   2669   2805   -191    162   -205       C  
ATOM    435  N   THR A 104      43.998  12.525  45.722  1.00 31.75           N  
ANISOU  435  N   THR A 104     3478   4066   4520      3    121   -319       N  
ATOM    436  CA  THR A 104      43.721  13.939  45.958  1.00 31.66           C  
ANISOU  436  CA  THR A 104     3580   3983   4466     46    157   -351       C  
ATOM    437  C   THR A 104      42.516  14.122  46.881  1.00 38.65           C  
ANISOU  437  C   THR A 104     4431   4896   5358    125    200   -370       C  
ATOM    438  O   THR A 104      42.550  14.926  47.815  1.00 40.82           O  
ANISOU  438  O   THR A 104     4803   5129   5577    126    253   -395       O  
ATOM    439  CB  THR A 104      43.468  14.692  44.635  1.00 26.47           C  
ANISOU  439  CB  THR A 104     3000   3255   3804    136    139   -349       C  
ATOM    440  OG1 THR A 104      44.662  14.677  43.842  1.00 41.35           O  
ANISOU  440  OG1 THR A 104     4932   5108   5673     67    114   -322       O  
ATOM    441  CG2 THR A 104      43.066  16.135  44.900  1.00 21.30           C  
ANISOU  441  CG2 THR A 104     2500   2507   3087    211    200   -376       C  
ATOM    442  N   ILE A 105      41.455  13.368  46.619  1.00 30.55           N  
ANISOU  442  N   ILE A 105     3271   3945   4390    185    178   -355       N  
ATOM    443  CA  ILE A 105      40.233  13.487  47.406  1.00 33.66           C  
ANISOU  443  CA  ILE A 105     3599   4401   4790    272    221   -351       C  
ATOM    444  C   ILE A 105      40.359  12.859  48.793  1.00 33.17           C  
ANISOU  444  C   ILE A 105     3487   4380   4734    208    265   -350       C  
ATOM    445  O   ILE A 105      39.962  13.463  49.792  1.00 24.57           O  
ANISOU  445  O   ILE A 105     2443   3287   3605    269    327   -356       O  
ATOM    446  CB  ILE A 105      39.036  12.842  46.679  1.00 32.42           C  
ANISOU  446  CB  ILE A 105     3283   4350   4686    326    177   -328       C  
ATOM    447  CG1 ILE A 105      38.695  13.631  45.415  1.00 40.91           C  
ANISOU  447  CG1 ILE A 105     4403   5408   5733    440    144   -325       C  
ATOM    448  CG2 ILE A 105      37.825  12.770  47.595  1.00 30.93           C  
ANISOU  448  CG2 ILE A 105     2981   4268   4505    396    227   -304       C  
ATOM    449  CD1 ILE A 105      37.506  13.080  44.658  1.00 50.60           C  
ANISOU  449  CD1 ILE A 105     5461   6774   6989    486     85   -304       C  
ATOM    450  N   THR A 106      40.922  11.656  48.860  1.00 37.74           N  
ANISOU  450  N   THR A 106     3996   4993   5349    104    243   -338       N  
ATOM    451  CA  THR A 106      40.860  10.883  50.099  1.00 38.14           C  
ANISOU  451  CA  THR A 106     3985   5097   5408     67    293   -327       C  
ATOM    452  C   THR A 106      42.043  11.063  51.053  1.00 42.94           C  
ANISOU  452  C   THR A 106     4674   5691   5950      8    323   -338       C  
ATOM    453  O   THR A 106      41.912  10.810  52.250  1.00 46.30           O  
ANISOU  453  O   THR A 106     5078   6154   6359     15    377   -336       O  
ATOM    454  CB  THR A 106      40.732   9.381  49.799  1.00 32.69           C  
ANISOU  454  CB  THR A 106     3199   4450   4773     -2    277   -300       C  
ATOM    455  OG1 THR A 106      41.909   8.926  49.118  1.00 29.01           O  
ANISOU  455  OG1 THR A 106     2791   3947   4283    -59    243   -291       O  
ATOM    456  CG2 THR A 106      39.509   9.114  48.935  1.00 21.08           C  
ANISOU  456  CG2 THR A 106     1631   3023   3357     17    236   -294       C  
ATOM    457  N   CYS A 107      43.191  11.497  50.543  1.00 32.24           N  
ANISOU  457  N   CYS A 107     3400   4299   4550    -51    289   -346       N  
ATOM    458  CA  CYS A 107      44.410  11.473  51.352  1.00 28.21           C  
ANISOU  458  CA  CYS A 107     2924   3829   3966   -133    301   -345       C  
ATOM    459  C   CYS A 107      44.994  12.850  51.651  1.00 26.40           C  
ANISOU  459  C   CYS A 107     2832   3546   3654   -185    299   -387       C  
ATOM    460  O   CYS A 107      45.405  13.124  52.781  1.00 25.82           O  
ANISOU  460  O   CYS A 107     2798   3503   3508   -232    322   -410       O  
ATOM    461  CB  CYS A 107      45.469  10.611  50.664  1.00 32.07           C  
ANISOU  461  CB  CYS A 107     3373   4367   4446   -185    270   -298       C  
ATOM    462  SG  CYS A 107      44.943   8.909  50.394  1.00 39.12           S  
ANISOU  462  SG  CYS A 107     4175   5288   5402   -148    288   -253       S  
ATOM    463  N   LEU A 108      45.041  13.704  50.634  1.00 30.77           N  
ANISOU  463  N   LEU A 108     3472   4014   4206   -183    274   -399       N  
ATOM    464  CA  LEU A 108      45.597  15.051  50.767  1.00 25.41           C  
ANISOU  464  CA  LEU A 108     2963   3250   3440   -255    282   -441       C  
ATOM    465  C   LEU A 108      45.051  15.845  51.975  1.00 27.71           C  
ANISOU  465  C   LEU A 108     3379   3485   3664   -224    336   -490       C  
ATOM    466  O   LEU A 108      45.842  16.395  52.750  1.00 45.69           O  
ANISOU  466  O   LEU A 108     5758   5758   5846   -346    338   -526       O  
ATOM    467  CB  LEU A 108      45.367  15.825  49.461  1.00 22.02           C  
ANISOU  467  CB  LEU A 108     2627   2712   3028   -206    272   -441       C  
ATOM    468  CG  LEU A 108      45.866  17.263  49.300  1.00 24.03           C  
ANISOU  468  CG  LEU A 108     3100   2838   3194   -278    296   -478       C  
ATOM    469  CD1 LEU A 108      46.213  17.518  47.848  1.00 24.60           C  
ANISOU  469  CD1 LEU A 108     3198   2856   3291   -273    272   -449       C  
ATOM    470  CD2 LEU A 108      44.823  18.271  49.769  1.00 27.77           C  
ANISOU  470  CD2 LEU A 108     3746   3190   3617   -155    365   -518       C  
ATOM    471  N   PRO A 109      43.713  15.907  52.153  1.00 26.83           N  
ANISOU  471  N   PRO A 109     3261   3346   3589    -63    381   -487       N  
ATOM    472  CA  PRO A 109      43.223  16.717  53.279  1.00 31.28           C  
ANISOU  472  CA  PRO A 109     3970   3847   4067     -5    446   -523       C  
ATOM    473  C   PRO A 109      43.645  16.163  54.638  1.00 37.19           C  
ANISOU  473  C   PRO A 109     4671   4681   4777    -70    455   -535       C  
ATOM    474  O   PRO A 109      44.085  16.921  55.513  1.00 37.22           O  
ANISOU  474  O   PRO A 109     4840   4633   4669   -136    473   -584       O  
ATOM    475  CB  PRO A 109      41.697  16.657  53.125  1.00 24.44           C  
ANISOU  475  CB  PRO A 109     3041   2992   3252    202    494   -486       C  
ATOM    476  CG  PRO A 109      41.462  16.236  51.710  1.00 34.91           C  
ANISOU  476  CG  PRO A 109     4249   4348   4665    229    443   -453       C  
ATOM    477  CD  PRO A 109      42.597  15.327  51.383  1.00 28.13           C  
ANISOU  477  CD  PRO A 109     3292   3547   3849     70    376   -447       C  
ATOM    478  N   ALA A 110      43.505  14.850  54.802  1.00 39.35           N  
ANISOU  478  N   ALA A 110     4742   5078   5132    -53    445   -491       N  
ATOM    479  CA  ALA A 110      43.919  14.172  56.024  1.00 31.66           C  
ANISOU  479  CA  ALA A 110     3708   4201   4122    -90    462   -489       C  
ATOM    480  C   ALA A 110      45.377  14.481  56.331  1.00 30.73           C  
ANISOU  480  C   ALA A 110     3651   4125   3901   -260    416   -519       C  
ATOM    481  O   ALA A 110      45.733  14.776  57.472  1.00 45.57           O  
ANISOU  481  O   ALA A 110     5602   6032   5681   -304    428   -554       O  
ATOM    482  CB  ALA A 110      43.706  12.669  55.899  1.00 22.60           C  
ANISOU  482  CB  ALA A 110     2360   3157   3068    -60    467   -430       C  
ATOM    483  N   THR A 111      46.210  14.427  55.297  1.00 20.58           N  
ANISOU  483  N   THR A 111     2330   2859   2629   -356    360   -500       N  
ATOM    484  CA  THR A 111      47.633  14.697  55.435  1.00 21.01           C  
ANISOU  484  CA  THR A 111     2402   2996   2585   -532    311   -508       C  
ATOM    485  C   THR A 111      47.885  16.133  55.869  1.00 29.93           C  
ANISOU  485  C   THR A 111     3753   4018   3599   -646    309   -585       C  
ATOM    486  O   THR A 111      48.746  16.388  56.707  1.00 26.18           O  
ANISOU  486  O   THR A 111     3312   3628   3008   -789    281   -616       O  
ATOM    487  CB  THR A 111      48.384  14.427  54.125  1.00 22.56           C  
ANISOU  487  CB  THR A 111     2523   3230   2820   -591    265   -457       C  
ATOM    488  OG1 THR A 111      48.161  13.070  53.722  1.00 28.99           O  
ANISOU  488  OG1 THR A 111     3177   4119   3719   -487    274   -390       O  
ATOM    489  CG2 THR A 111      49.874  14.656  54.312  1.00 30.01           C  
ANISOU  489  CG2 THR A 111     3442   4309   3650   -776    218   -445       C  
ATOM    490  N   LEU A 112      47.135  17.073  55.300  1.00 32.73           N  
ANISOU  490  N   LEU A 112     4274   4191   3970   -584    341   -616       N  
ATOM    491  CA  LEU A 112      47.254  18.466  55.719  1.00 31.61           C  
ANISOU  491  CA  LEU A 112     4407   3902   3704   -674    362   -691       C  
ATOM    492  C   LEU A 112      46.933  18.612  57.208  1.00 37.71           C  
ANISOU  492  C   LEU A 112     5271   4675   4383   -642    397   -737       C  
ATOM    493  O   LEU A 112      47.695  19.228  57.964  1.00 37.53           O  
ANISOU  493  O   LEU A 112     5387   4650   4222   -816    372   -798       O  
ATOM    494  CB  LEU A 112      46.337  19.366  54.893  1.00 24.75           C  
ANISOU  494  CB  LEU A 112     3715   2834   2856   -544    419   -699       C  
ATOM    495  CG  LEU A 112      46.338  20.829  55.343  1.00 37.70           C  
ANISOU  495  CG  LEU A 112     5703   4275   4345   -605    470   -774       C  
ATOM    496  CD1 LEU A 112      47.727  21.435  55.190  1.00 44.42           C  
ANISOU  496  CD1 LEU A 112     6657   5119   5102   -903    417   -815       C  
ATOM    497  CD2 LEU A 112      45.304  21.642  54.581  1.00 34.31           C  
ANISOU  497  CD2 LEU A 112     5452   3662   3920   -407    552   -764       C  
ATOM    498  N   VAL A 113      45.811  18.030  57.623  1.00 34.61           N  
ANISOU  498  N   VAL A 113     4797   4295   4060   -430    451   -705       N  
ATOM    499  CA  VAL A 113      45.389  18.100  59.021  1.00 33.45           C  
ANISOU  499  CA  VAL A 113     4729   4148   3832   -358    498   -734       C  
ATOM    500  C   VAL A 113      46.427  17.500  59.968  1.00 32.82           C  
ANISOU  500  C   VAL A 113     4549   4241   3681   -497    446   -747       C  
ATOM    501  O   VAL A 113      46.783  18.110  60.973  1.00 34.84           O  
ANISOU  501  O   VAL A 113     4969   4476   3793   -581    443   -811       O  
ATOM    502  CB  VAL A 113      44.048  17.381  59.242  1.00 29.85           C  
ANISOU  502  CB  VAL A 113     4142   3722   3479   -115    568   -673       C  
ATOM    503  CG1 VAL A 113      43.683  17.397  60.719  1.00 33.59           C  
ANISOU  503  CG1 VAL A 113     4690   4208   3866    -30    624   -691       C  
ATOM    504  CG2 VAL A 113      42.955  18.033  58.415  1.00 31.36           C  
ANISOU  504  CG2 VAL A 113     4419   3786   3711     48    622   -651       C  
ATOM    505  N   VAL A 114      46.907  16.304  59.641  1.00 32.92           N  
ANISOU  505  N   VAL A 114     4306   4426   3776   -512    411   -684       N  
ATOM    506  CA  VAL A 114      47.907  15.628  60.462  1.00 32.60           C  
ANISOU  506  CA  VAL A 114     4143   4586   3658   -605    371   -674       C  
ATOM    507  C   VAL A 114      49.214  16.414  60.528  1.00 42.79           C  
ANISOU  507  C   VAL A 114     5517   5936   4805   -859    292   -724       C  
ATOM    508  O   VAL A 114      49.779  16.595  61.603  1.00 48.83           O  
ANISOU  508  O   VAL A 114     6324   6797   5431   -954    264   -767       O  
ATOM    509  CB  VAL A 114      48.197  14.208  59.935  1.00 31.35           C  
ANISOU  509  CB  VAL A 114     3728   4585   3598   -548    366   -582       C  
ATOM    510  CG1 VAL A 114      49.368  13.585  60.681  1.00 27.41           C  
ANISOU  510  CG1 VAL A 114     3107   4318   2988   -627    332   -556       C  
ATOM    511  CG2 VAL A 114      46.961  13.343  60.068  1.00 28.16           C  
ANISOU  511  CG2 VAL A 114     3243   4143   3315   -344    444   -537       C  
ATOM    512  N   ASP A 115      49.688  16.890  59.381  1.00 38.54           N  
ANISOU  512  N   ASP A 115     5001   5350   4294   -978    254   -717       N  
ATOM    513  CA  ASP A 115      50.944  17.631  59.337  1.00 40.07           C  
ANISOU  513  CA  ASP A 115     5255   5613   4357  -1252    180   -753       C  
ATOM    514  C   ASP A 115      50.834  18.974  60.053  1.00 43.37           C  
ANISOU  514  C   ASP A 115     5986   5860   4631  -1380    186   -865       C  
ATOM    515  O   ASP A 115      51.838  19.531  60.496  1.00 46.77           O  
ANISOU  515  O   ASP A 115     6482   6376   4913  -1635    121   -914       O  
ATOM    516  CB  ASP A 115      51.397  17.843  57.892  1.00 35.98           C  
ANISOU  516  CB  ASP A 115     4699   5063   3907  -1335    156   -710       C  
ATOM    517  CG  ASP A 115      51.934  16.573  57.259  1.00 48.06           C  
ANISOU  517  CG  ASP A 115     5942   6801   5516  -1269    135   -599       C  
ATOM    518  OD1 ASP A 115      52.083  15.564  57.982  1.00 55.43           O  
ANISOU  518  OD1 ASP A 115     6714   7913   6433  -1183    140   -557       O  
ATOM    519  OD2 ASP A 115      52.221  16.585  56.043  1.00 44.42           O  
ANISOU  519  OD2 ASP A 115     5438   6320   5121  -1291    123   -550       O  
ATOM    520  N   ILE A 116      49.616  19.490  60.172  1.00 41.13           N  
ANISOU  520  N   ILE A 116     5905   5344   4377  -1204    267   -900       N  
ATOM    521  CA  ILE A 116      49.398  20.740  60.892  1.00 45.15           C  
ANISOU  521  CA  ILE A 116     6765   5657   4732  -1278    297  -1001       C  
ATOM    522  C   ILE A 116      49.276  20.521  62.405  1.00 44.36           C  
ANISOU  522  C   ILE A 116     6701   5631   4523  -1232    301  -1041       C  
ATOM    523  O   ILE A 116      49.862  21.260  63.200  1.00 42.35           O  
ANISOU  523  O   ILE A 116     6647   5358   4088  -1428    262  -1128       O  
ATOM    524  CB  ILE A 116      48.136  21.465  60.377  1.00 40.58           C  
ANISOU  524  CB  ILE A 116     6415   4804   4200  -1068    400  -1005       C  
ATOM    525  CG1 ILE A 116      48.430  22.154  59.046  1.00 49.55           C  
ANISOU  525  CG1 ILE A 116     7647   5814   5366  -1171    399  -1001       C  
ATOM    526  CG2 ILE A 116      47.649  22.493  61.382  1.00 51.50           C  
ANISOU  526  CG2 ILE A 116     8164   5989   5414  -1036    464  -1089       C  
ATOM    527  CD1 ILE A 116      47.261  22.942  58.506  1.00 59.94           C  
ANISOU  527  CD1 ILE A 116     9200   6877   6696   -952    506   -998       C  
ATOM    528  N   THR A 117      48.531  19.492  62.796  1.00 34.04           N  
ANISOU  528  N   THR A 117     5204   4411   3318   -985    347   -977       N  
ATOM    529  CA  THR A 117      48.183  19.280  64.198  1.00 30.81           C  
ANISOU  529  CA  THR A 117     4843   4042   2820   -879    379  -1002       C  
ATOM    530  C   THR A 117      49.020  18.202  64.885  1.00 31.48           C  
ANISOU  530  C   THR A 117     4666   4418   2876   -927    320   -968       C  
ATOM    531  O   THR A 117      49.041  18.124  66.114  1.00 31.30           O  
ANISOU  531  O   THR A 117     4696   4458   2738   -894    326  -1002       O  
ATOM    532  CB  THR A 117      46.699  18.896  64.340  1.00 34.59           C  
ANISOU  532  CB  THR A 117     5305   4425   3413   -555    492   -946       C  
ATOM    533  OG1 THR A 117      46.462  17.646  63.680  1.00 28.86           O  
ANISOU  533  OG1 THR A 117     4262   3834   2869   -447    499   -848       O  
ATOM    534  CG2 THR A 117      45.811  19.967  63.723  1.00 31.70           C  
ANISOU  534  CG2 THR A 117     5195   3802   3048   -456    564   -963       C  
ATOM    535  N   GLU A 118      49.691  17.374  64.088  1.00 39.81           N  
ANISOU  535  N   GLU A 118     5454   5650   4022   -981    274   -895       N  
ATOM    536  CA  GLU A 118      50.488  16.248  64.586  1.00 39.65           C  
ANISOU  536  CA  GLU A 118     5174   5921   3971   -981    239   -835       C  
ATOM    537  C   GLU A 118      49.655  15.259  65.403  1.00 43.03           C  
ANISOU  537  C   GLU A 118     5511   6382   4455   -720    326   -787       C  
ATOM    538  O   GLU A 118      50.185  14.550  66.258  1.00 48.72           O  
ANISOU  538  O   GLU A 118     6108   7310   5093   -691    318   -761       O  
ATOM    539  CB  GLU A 118      51.672  16.746  65.419  1.00 43.29           C  
ANISOU  539  CB  GLU A 118     5677   6555   4216  -1221    145   -898       C  
ATOM    540  CG  GLU A 118      52.582  17.712  64.681  1.00 52.97           C  
ANISOU  540  CG  GLU A 118     6984   7770   5371  -1525     59   -942       C  
ATOM    541  CD  GLU A 118      53.861  18.005  65.439  1.00 73.82           C  
ANISOU  541  CD  GLU A 118     9590  10662   7797  -1794    -50   -985       C  
ATOM    542  OE1 GLU A 118      54.124  17.323  66.452  1.00 78.01           O  
ANISOU  542  OE1 GLU A 118     9992  11411   8239  -1716    -63   -966       O  
ATOM    543  OE2 GLU A 118      54.603  18.919  65.021  1.00 82.98           O  
ANISOU  543  OE2 GLU A 118    10849  11811   8869  -2090   -121  -1034       O  
ATOM    544  N   THR A 119      48.353  15.217  65.134  1.00 39.22           N  
ANISOU  544  N   THR A 119     5084   5712   4106   -529    415   -767       N  
ATOM    545  CA  THR A 119      47.457  14.265  65.784  1.00 44.43           C  
ANISOU  545  CA  THR A 119     5647   6394   4841   -294    510   -709       C  
ATOM    546  C   THR A 119      46.503  13.638  64.772  1.00 43.41           C  
ANISOU  546  C   THR A 119     5401   6184   4911   -162    569   -636       C  
ATOM    547  O   THR A 119      46.357  14.129  63.652  1.00 43.74           O  
ANISOU  547  O   THR A 119     5477   6120   5022   -216    541   -642       O  
ATOM    548  CB  THR A 119      46.626  14.924  66.910  1.00 48.63           C  
ANISOU  548  CB  THR A 119     6387   6800   5288   -175    574   -759       C  
ATOM    549  OG1 THR A 119      45.918  16.052  66.387  1.00 54.01           O  
ANISOU  549  OG1 THR A 119     7283   7257   5982   -163    595   -801       O  
ATOM    550  CG2 THR A 119      47.522  15.377  68.055  1.00 49.56           C  
ANISOU  550  CG2 THR A 119     6620   7015   5194   -296    515   -835       C  
ATOM    551  N   TRP A 120      45.854  12.550  65.176  1.00 34.28           N  
ANISOU  551  N   TRP A 120     4112   5079   3835      3    650   -567       N  
ATOM    552  CA  TRP A 120      44.897  11.865  64.317  1.00 28.94           C  
ANISOU  552  CA  TRP A 120     3318   4342   3333    103    703   -500       C  
ATOM    553  C   TRP A 120      43.490  11.970  64.904  1.00 31.07           C  
ANISOU  553  C   TRP A 120     3630   4524   3651    280    802   -480       C  
ATOM    554  O   TRP A 120      43.189  11.355  65.925  1.00 32.33           O  
ANISOU  554  O   TRP A 120     3750   4742   3791    388    876   -447       O  
ATOM    555  CB  TRP A 120      45.299  10.398  64.132  1.00 22.97           C  
ANISOU  555  CB  TRP A 120     2376   3718   2635    123    726   -423       C  
ATOM    556  CG  TRP A 120      44.463   9.665  63.125  1.00 23.57           C  
ANISOU  556  CG  TRP A 120     2349   3732   2875    169    761   -366       C  
ATOM    557  CD1 TRP A 120      43.406   8.841  63.379  1.00 26.89           C  
ANISOU  557  CD1 TRP A 120     2695   4133   3389    280    854   -312       C  
ATOM    558  CD2 TRP A 120      44.613   9.697  61.701  1.00 20.80           C  
ANISOU  558  CD2 TRP A 120     1964   3338   2603     90    700   -360       C  
ATOM    559  NE1 TRP A 120      42.888   8.356  62.202  1.00 20.74           N  
ANISOU  559  NE1 TRP A 120     1838   3307   2735    254    844   -279       N  
ATOM    560  CE2 TRP A 120      43.614   8.865  61.157  1.00 27.87           C  
ANISOU  560  CE2 TRP A 120     2769   4191   3630    151    750   -309       C  
ATOM    561  CE3 TRP A 120      45.497  10.343  60.835  1.00 23.84           C  
ANISOU  561  CE3 TRP A 120     2387   3719   2953    -35    609   -389       C  
ATOM    562  CZ2 TRP A 120      43.474   8.667  59.784  1.00 31.48           C  
ANISOU  562  CZ2 TRP A 120     3182   4601   4177    101    703   -295       C  
ATOM    563  CZ3 TRP A 120      45.358  10.144  59.473  1.00 32.54           C  
ANISOU  563  CZ3 TRP A 120     3443   4768   4151    -63    575   -366       C  
ATOM    564  CH2 TRP A 120      44.354   9.313  58.961  1.00 26.45           C  
ANISOU  564  CH2 TRP A 120     2592   3955   3504      9    618   -323       C  
ATOM    565  N   PHE A 121      42.635  12.756  64.254  1.00 43.25           N  
ANISOU  565  N   PHE A 121     5248   5941   5245    324    810   -488       N  
ATOM    566  CA  PHE A 121      41.287  13.014  64.757  1.00 41.57           C  
ANISOU  566  CA  PHE A 121     5071   5670   5055    509    907   -453       C  
ATOM    567  C   PHE A 121      40.291  11.977  64.269  1.00 39.08           C  
ANISOU  567  C   PHE A 121     4543   5408   4899    586    962   -364       C  
ATOM    568  O   PHE A 121      39.221  11.800  64.852  1.00 41.19           O  
ANISOU  568  O   PHE A 121     4766   5691   5194    733   1055   -307       O  
ATOM    569  CB  PHE A 121      40.817  14.405  64.337  1.00 39.32           C  
ANISOU  569  CB  PHE A 121     4983   5242   4716    552    906   -491       C  
ATOM    570  CG  PHE A 121      41.642  15.519  64.905  1.00 49.47           C  
ANISOU  570  CG  PHE A 121     6532   6440   5826    463    868   -585       C  
ATOM    571  CD1 PHE A 121      41.350  16.048  66.151  1.00 49.62           C  
ANISOU  571  CD1 PHE A 121     6733   6410   5712    571    930   -609       C  
ATOM    572  CD2 PHE A 121      42.708  16.040  64.192  1.00 49.76           C  
ANISOU  572  CD2 PHE A 121     6645   6443   5819    260    771   -648       C  
ATOM    573  CE1 PHE A 121      42.108  17.075  66.677  1.00 50.46           C  
ANISOU  573  CE1 PHE A 121     7109   6424   5638    460    889   -707       C  
ATOM    574  CE2 PHE A 121      43.470  17.067  64.711  1.00 53.88           C  
ANISOU  574  CE2 PHE A 121     7415   6887   6169    133    733   -740       C  
ATOM    575  CZ  PHE A 121      43.169  17.586  65.956  1.00 57.24           C  
ANISOU  575  CZ  PHE A 121     8039   7254   6456    224    788   -775       C  
ATOM    576  N   PHE A 122      40.650  11.298  63.189  1.00 38.49           N  
ANISOU  576  N   PHE A 122     4342   5363   4918    477    905   -348       N  
ATOM    577  CA  PHE A 122      39.752  10.350  62.551  1.00 40.44           C  
ANISOU  577  CA  PHE A 122     4412   5649   5307    501    938   -278       C  
ATOM    578  C   PHE A 122      39.800   9.009  63.271  1.00 46.15           C  
ANISOU  578  C   PHE A 122     5028   6448   6059    510   1009   -227       C  
ATOM    579  O   PHE A 122      40.523   8.852  64.252  1.00 65.52           O  
ANISOU  579  O   PHE A 122     7536   8937   8419    525   1031   -242       O  
ATOM    580  CB  PHE A 122      40.120  10.218  61.078  1.00 37.63           C  
ANISOU  580  CB  PHE A 122     4007   5272   5019    386    849   -290       C  
ATOM    581  CG  PHE A 122      40.578  11.514  60.469  1.00 39.84           C  
ANISOU  581  CG  PHE A 122     4431   5469   5236    349    779   -351       C  
ATOM    582  CD1 PHE A 122      39.693  12.568  60.308  1.00 38.43           C  
ANISOU  582  CD1 PHE A 122     4339   5224   5039    457    803   -354       C  
ATOM    583  CD2 PHE A 122      41.899  11.691  60.088  1.00 50.94           C  
ANISOU  583  CD2 PHE A 122     5896   6870   6587    216    702   -394       C  
ATOM    584  CE1 PHE A 122      40.111  13.769  59.762  1.00 40.28           C  
ANISOU  584  CE1 PHE A 122     4746   5356   5203    426    759   -409       C  
ATOM    585  CE2 PHE A 122      42.325  12.889  59.540  1.00 51.26           C  
ANISOU  585  CE2 PHE A 122     6084   6825   6568    159    649   -447       C  
ATOM    586  CZ  PHE A 122      41.428  13.930  59.377  1.00 45.05           C  
ANISOU  586  CZ  PHE A 122     5413   5939   5764    262    681   -460       C  
ATOM    587  N   GLY A 123      39.021   8.047  62.799  1.00 40.83           N  
ANISOU  587  N   GLY A 123     4214   5800   5500    496   1047   -167       N  
ATOM    588  CA  GLY A 123      38.885   6.792  63.515  1.00 48.30           C  
ANISOU  588  CA  GLY A 123     5089   6791   6471    511   1142   -111       C  
ATOM    589  C   GLY A 123      40.072   5.857  63.398  1.00 45.52           C  
ANISOU  589  C   GLY A 123     4755   6456   6084    438   1131   -112       C  
ATOM    590  O   GLY A 123      41.121   6.217  62.863  1.00 37.52           O  
ANISOU  590  O   GLY A 123     3795   5444   5016    375   1043   -154       O  
ATOM    591  N   GLN A 124      39.899   4.649  63.924  1.00 47.87           N  
ANISOU  591  N   GLN A 124     5036   6766   6386    443   1200    -65       N  
ATOM    592  CA  GLN A 124      40.851   3.564  63.736  1.00 45.19           C  
ANISOU  592  CA  GLN A 124     4737   6432   6001    396   1198    -49       C  
ATOM    593  C   GLN A 124      40.794   3.099  62.286  1.00 37.85           C  
ANISOU  593  C   GLN A 124     3769   5455   5157    295   1170    -35       C  
ATOM    594  O   GLN A 124      41.824   2.882  61.626  1.00 42.64           O  
ANISOU  594  O   GLN A 124     4406   6068   5728    265   1142    -36       O  
ATOM    595  CB  GLN A 124      40.527   2.404  64.682  1.00 50.15           C  
ANISOU  595  CB  GLN A 124     5407   7047   6601    426   1266     -8       C  
ATOM    596  CG  GLN A 124      41.639   2.042  65.644  1.00 59.92           C  
ANISOU  596  CG  GLN A 124     6727   8324   7715    490   1277    -11       C  
ATOM    597  CD  GLN A 124      42.736   1.220  64.996  1.00 67.00           C  
ANISOU  597  CD  GLN A 124     7670   9228   8558    463   1265     11       C  
ATOM    598  OE1 GLN A 124      42.595   0.752  63.866  1.00 82.79           O  
ANISOU  598  OE1 GLN A 124     9660  11183  10614    398   1267     32       O  
ATOM    599  NE2 GLN A 124      43.837   1.038  65.713  1.00 58.95           N  
ANISOU  599  NE2 GLN A 124     6706   8269   7425    521   1256     17       N  
ATOM    600  N   SER A 125      39.562   2.959  61.805  1.00 28.36           N  
ANISOU  600  N   SER A 125     3561   4091   3124   -774    168    200       N  
ATOM    601  CA  SER A 125      39.296   2.487  60.460  1.00 29.43           C  
ANISOU  601  CA  SER A 125     3631   4135   3415   -651    127    239       C  
ATOM    602  C   SER A 125      39.983   3.361  59.429  1.00 37.31           C  
ANISOU  602  C   SER A 125     4591   5099   4484   -594    130    172       C  
ATOM    603  O   SER A 125      40.672   2.849  58.563  1.00 30.35           O  
ANISOU  603  O   SER A 125     3663   4206   3663   -521     30    209       O  
ATOM    604  CB  SER A 125      37.793   2.441  60.193  1.00 29.06           C  
ANISOU  604  CB  SER A 125     3559   4034   3447   -627    227    237       C  
ATOM    605  OG  SER A 125      37.189   1.386  60.918  1.00 42.98           O  
ANISOU  605  OG  SER A 125     5356   5813   5160   -689    219    306       O  
ATOM    606  N   LEU A 126      39.807   4.674  59.529  1.00 40.22           N  
ANISOU  606  N   LEU A 126     5000   5440   4844   -629    267     74       N  
ATOM    607  CA  LEU A 126      40.428   5.583  58.572  1.00 30.21           C  
ANISOU  607  CA  LEU A 126     3731   4114   3634   -589    305     10       C  
ATOM    608  C   LEU A 126      41.947   5.578  58.717  1.00 39.48           C  
ANISOU  608  C   LEU A 126     4886   5384   4729   -671    209    -22       C  
ATOM    609  O   LEU A 126      42.673   5.785  57.739  1.00 33.34           O  
ANISOU  609  O   LEU A 126     4072   4583   4011   -628    179    -40       O  
ATOM    610  CB  LEU A 126      39.877   6.997  58.737  1.00 27.11           C  
ANISOU  610  CB  LEU A 126     3429   3634   3236   -605    511    -82       C  
ATOM    611  CG  LEU A 126      38.422   7.152  58.294  1.00 29.81           C  
ANISOU  611  CG  LEU A 126     3749   3909   3669   -465    611    -41       C  
ATOM    612  CD1 LEU A 126      37.935   8.573  58.509  1.00 26.62           C  
ANISOU  612  CD1 LEU A 126     3457   3403   3255   -441    839   -118       C  
ATOM    613  CD2 LEU A 126      38.265   6.741  56.839  1.00 35.16           C  
ANISOU  613  CD2 LEU A 126     4334   4561   4463   -316    529     25       C  
ATOM    614  N   CYS A 127      42.422   5.325  59.936  1.00 20.95           N  
ANISOU  614  N   CYS A 127     2551   3172   2237   -789    161    -26       N  
ATOM    615  CA  CYS A 127      43.852   5.181  60.182  1.00 21.63           C  
ANISOU  615  CA  CYS A 127     2574   3424   2220   -859     45    -43       C  
ATOM    616  C   CYS A 127      44.384   3.980  59.409  1.00 36.51           C  
ANISOU  616  C   CYS A 127     4366   5329   4179   -709   -115     76       C  
ATOM    617  O   CYS A 127      45.546   3.963  59.006  1.00 33.03           O  
ANISOU  617  O   CYS A 127     3841   4988   3720   -702   -193     61       O  
ATOM    618  CB  CYS A 127      44.137   5.041  61.682  1.00 28.64           C  
ANISOU  618  CB  CYS A 127     3479   4492   2910   -995     10    -47       C  
ATOM    619  SG  CYS A 127      45.857   4.651  62.153  1.00 52.27           S  
ANISOU  619  SG  CYS A 127     6340   7788   5731  -1054   -169    -33       S  
ATOM    620  N   LYS A 128      43.534   2.980  59.193  1.00 20.30           N  
ANISOU  620  N   LYS A 128     2329   3180   2205   -600   -146    183       N  
ATOM    621  CA  LYS A 128      43.901   1.887  58.293  1.00 28.15           C  
ANISOU  621  CA  LYS A 128     3274   4134   3289   -459   -253    276       C  
ATOM    622  C   LYS A 128      43.771   2.309  56.825  1.00 30.06           C  
ANISOU  622  C   LYS A 128     3487   4258   3676   -389   -213    228       C  
ATOM    623  O   LYS A 128      44.702   2.160  56.033  1.00 43.64           O  
ANISOU  623  O   LYS A 128     5147   6000   5434   -329   -273    226       O  
ATOM    624  CB  LYS A 128      43.029   0.653  58.542  1.00 35.96           C  
ANISOU  624  CB  LYS A 128     4320   5043   4301   -405   -274    389       C  
ATOM    625  CG  LYS A 128      42.822   0.301  60.004  1.00 53.90           C  
ANISOU  625  CG  LYS A 128     6655   7398   6427   -478   -277    446       C  
ATOM    626  CD  LYS A 128      44.094  -0.203  60.640  1.00 46.25           C  
ANISOU  626  CD  LYS A 128     5652   6594   5325   -438   -400    524       C  
ATOM    627  CE  LYS A 128      44.015  -1.692  60.927  1.00 29.39           C  
ANISOU  627  CE  LYS A 128     3593   4403   3170   -327   -454    691       C  
ATOM    628  NZ  LYS A 128      45.240  -2.168  61.622  1.00 27.98           N  
ANISOU  628  NZ  LYS A 128     3375   4417   2840   -243   -573    796       N  
ATOM    629  N   VAL A 129      42.607   2.855  56.490  1.00 17.96           N  
ANISOU  629  N   VAL A 129     1991   2622   2210   -388   -105    193       N  
ATOM    630  CA  VAL A 129      42.169   3.077  55.115  1.00 25.66           C  
ANISOU  630  CA  VAL A 129     2943   3500   3307   -296    -72    180       C  
ATOM    631  C   VAL A 129      42.985   4.106  54.342  1.00 29.63           C  
ANISOU  631  C   VAL A 129     3441   3987   3832   -293    -29    106       C  
ATOM    632  O   VAL A 129      43.471   3.825  53.247  1.00 36.01           O  
ANISOU  632  O   VAL A 129     4207   4770   4705   -220    -78    117       O  
ATOM    633  CB  VAL A 129      40.689   3.519  55.088  1.00 33.73           C  
ANISOU  633  CB  VAL A 129     3983   4468   4366   -278     37    171       C  
ATOM    634  CG1 VAL A 129      40.283   3.967  53.690  1.00 16.39           C  
ANISOU  634  CG1 VAL A 129     1752   2214   2261   -170     74    163       C  
ATOM    635  CG2 VAL A 129      39.788   2.394  55.584  1.00 17.23           C  
ANISOU  635  CG2 VAL A 129     1886   2391   2270   -297      5    235       C  
ATOM    636  N   ILE A 130      43.122   5.300  54.905  1.00 27.79           N  
ANISOU  636  N   ILE A 130     3267   3756   3537   -386     84     23       N  
ATOM    637  CA  ILE A 130      43.768   6.403  54.198  1.00 30.78           C  
ANISOU  637  CA  ILE A 130     3682   4085   3930   -410    174    -57       C  
ATOM    638  C   ILE A 130      45.236   6.123  53.813  1.00 29.36           C  
ANISOU  638  C   ILE A 130     3424   4002   3729   -448     78    -81       C  
ATOM    639  O   ILE A 130      45.636   6.414  52.680  1.00 35.10           O  
ANISOU  639  O   ILE A 130     4144   4674   4518   -399    100    -98       O  
ATOM    640  CB  ILE A 130      43.665   7.705  55.024  1.00 25.35           C  
ANISOU  640  CB  ILE A 130     3109   3359   3162   -538    346   -159       C  
ATOM    641  CG1 ILE A 130      42.205   8.168  55.068  1.00 23.92           C  
ANISOU  641  CG1 ILE A 130     2999   3062   3026   -443    478   -132       C  
ATOM    642  CG2 ILE A 130      44.561   8.790  54.448  1.00 19.19           C  
ANISOU  642  CG2 ILE A 130     2393   2527   2371   -617    455   -258       C  
ATOM    643  CD1 ILE A 130      41.967   9.393  55.921  1.00 25.11           C  
ANISOU  643  CD1 ILE A 130     3293   3143   3105   -546    679   -229       C  
ATOM    644  N   PRO A 131      46.042   5.549  54.731  1.00 27.60           N  
ANISOU  644  N   PRO A 131     3133   3944   3410   -522    -27    -75       N  
ATOM    645  CA  PRO A 131      47.387   5.172  54.273  1.00 27.16           C  
ANISOU  645  CA  PRO A 131     2966   4013   3341   -515   -125    -81       C  
ATOM    646  C   PRO A 131      47.348   4.090  53.196  1.00 29.03           C  
ANISOU  646  C   PRO A 131     3153   4185   3691   -337   -215     13       C  
ATOM    647  O   PRO A 131      48.150   4.117  52.255  1.00 34.78           O  
ANISOU  647  O   PRO A 131     3825   4929   4462   -302   -229    -12       O  
ATOM    648  CB  PRO A 131      48.058   4.650  55.546  1.00 19.89           C  
ANISOU  648  CB  PRO A 131     1970   3309   2279   -581   -231    -58       C  
ATOM    649  CG  PRO A 131      47.328   5.330  56.655  1.00 20.46           C  
ANISOU  649  CG  PRO A 131     2141   3368   2263   -714   -137   -111       C  
ATOM    650  CD  PRO A 131      45.907   5.393  56.191  1.00 19.30           C  
ANISOU  650  CD  PRO A 131     2096   3002   2235   -620    -48    -72       C  
ATOM    651  N   TYR A 132      46.418   3.151  53.340  1.00 22.78           N  
ANISOU  651  N   TYR A 132     2393   3323   2941   -248   -259    106       N  
ATOM    652  CA  TYR A 132      46.227   2.102  52.349  1.00 16.54           C  
ANISOU  652  CA  TYR A 132     1587   2448   2248   -112   -317    176       C  
ATOM    653  C   TYR A 132      45.925   2.702  50.981  1.00 21.49           C  
ANISOU  653  C   TYR A 132     2230   2972   2963    -74   -249    130       C  
ATOM    654  O   TYR A 132      46.550   2.340  49.985  1.00 23.34           O  
ANISOU  654  O   TYR A 132     2425   3196   3247     -7   -282    130       O  
ATOM    655  CB  TYR A 132      45.103   1.156  52.774  1.00 16.44           C  
ANISOU  655  CB  TYR A 132     1630   2363   2252    -80   -334    255       C  
ATOM    656  CG  TYR A 132      44.778   0.099  51.743  1.00 16.01           C  
ANISOU  656  CG  TYR A 132     1587   2208   2287     14   -365    299       C  
ATOM    657  CD1 TYR A 132      45.598  -1.005  51.574  1.00 21.79           C  
ANISOU  657  CD1 TYR A 132     2313   2938   3029    103   -434    359       C  
ATOM    658  CD2 TYR A 132      43.649   0.206  50.941  1.00 20.44           C  
ANISOU  658  CD2 TYR A 132     2165   2689   2911     16   -315    277       C  
ATOM    659  CE1 TYR A 132      45.308  -1.974  50.634  1.00 23.07           C  
ANISOU  659  CE1 TYR A 132     2514   2984   3265    168   -434    379       C  
ATOM    660  CE2 TYR A 132      43.350  -0.758  49.998  1.00 17.26           C  
ANISOU  660  CE2 TYR A 132     1774   2216   2568     62   -337    293       C  
ATOM    661  CZ  TYR A 132      44.184  -1.845  49.848  1.00 18.38           C  
ANISOU  661  CZ  TYR A 132     1939   2320   2723    126   -387    336       C  
ATOM    662  OH  TYR A 132      43.895  -2.808  48.913  1.00 24.91           O  
ANISOU  662  OH  TYR A 132     2808   3053   3603    151   -382    333       O  
ATOM    663  N   LEU A 133      44.972   3.628  50.941  1.00 27.40           N  
ANISOU  663  N   LEU A 133     3039   3651   3720   -102   -146     99       N  
ATOM    664  CA  LEU A 133      44.615   4.305  49.698  1.00 23.96           C  
ANISOU  664  CA  LEU A 133     2629   3131   3342    -41    -73     79       C  
ATOM    665  C   LEU A 133      45.806   5.065  49.127  1.00 24.31           C  
ANISOU  665  C   LEU A 133     2674   3185   3376    -81    -29     13       C  
ATOM    666  O   LEU A 133      46.001   5.109  47.911  1.00 26.44           O  
ANISOU  666  O   LEU A 133     2941   3413   3692    -16    -20     13       O  
ATOM    667  CB  LEU A 133      43.439   5.256  49.922  1.00 22.86           C  
ANISOU  667  CB  LEU A 133     2557   2932   3198    -31     47     74       C  
ATOM    668  CG  LEU A 133      42.092   4.582  50.187  1.00 26.67           C  
ANISOU  668  CG  LEU A 133     3011   3425   3697     14     21    132       C  
ATOM    669  CD1 LEU A 133      41.000   5.616  50.436  1.00 19.24           C  
ANISOU  669  CD1 LEU A 133     2115   2452   2745     52    155    130       C  
ATOM    670  CD2 LEU A 133      41.724   3.677  49.021  1.00 28.25           C  
ANISOU  670  CD2 LEU A 133     3153   3630   3952     92    -56    170       C  
ATOM    671  N   GLN A 134      46.599   5.661  50.013  1.00 20.45           N  
ANISOU  671  N   GLN A 134     2189   2770   2812   -210      5    -53       N  
ATOM    672  CA  GLN A 134      47.816   6.358  49.605  1.00 22.43           C  
ANISOU  672  CA  GLN A 134     2424   3063   3034   -298     56   -138       C  
ATOM    673  C   GLN A 134      48.758   5.422  48.847  1.00 21.27           C  
ANISOU  673  C   GLN A 134     2161   2997   2924   -226    -55   -114       C  
ATOM    674  O   GLN A 134      49.105   5.673  47.685  1.00 23.12           O  
ANISOU  674  O   GLN A 134     2403   3181   3201   -192    -13   -134       O  
ATOM    675  CB  GLN A 134      48.527   6.950  50.826  1.00 23.30           C  
ANISOU  675  CB  GLN A 134     2525   3299   3031   -484     88   -226       C  
ATOM    676  CG  GLN A 134      49.884   7.560  50.523  1.00 38.78           C  
ANISOU  676  CG  GLN A 134     4434   5361   4940   -622    133   -334       C  
ATOM    677  CD  GLN A 134      49.783   8.846  49.727  1.00 51.36           C  
ANISOU  677  CD  GLN A 134     6178   6781   6554   -684    329   -406       C  
ATOM    678  OE1 GLN A 134      48.931   9.693  49.997  1.00 51.67           O  
ANISOU  678  OE1 GLN A 134     6378   6667   6589   -703    471   -420       O  
ATOM    679  NE2 GLN A 134      50.655   8.999  48.736  1.00 59.07           N  
ANISOU  679  NE2 GLN A 134     7117   7775   7551   -702    355   -444       N  
ATOM    680  N   THR A 135      49.152   4.334  49.506  1.00 27.55           N  
ANISOU  680  N   THR A 135     2861   3912   3695   -187   -184    -61       N  
ATOM    681  CA  THR A 135      50.086   3.376  48.919  1.00 29.14           C  
ANISOU  681  CA  THR A 135     2955   4190   3926    -88   -275    -28       C  
ATOM    682  C   THR A 135      49.542   2.735  47.644  1.00 31.03           C  
ANISOU  682  C   THR A 135     3237   4285   4268     42   -279     15       C  
ATOM    683  O   THR A 135      50.280   2.545  46.678  1.00 38.03           O  
ANISOU  683  O   THR A 135     4076   5183   5189     91   -278     -6       O  
ATOM    684  CB  THR A 135      50.446   2.259  49.913  1.00 30.00           C  
ANISOU  684  CB  THR A 135     2988   4424   3986    -22   -397     55       C  
ATOM    685  OG1 THR A 135      49.249   1.624  50.377  1.00 33.34           O  
ANISOU  685  OG1 THR A 135     3505   4732   4431     26   -416    134       O  
ATOM    686  CG2 THR A 135      51.201   2.825  51.095  1.00 28.85           C  
ANISOU  686  CG2 THR A 135     2762   4494   3708   -155   -416      6       C  
ATOM    687  N   VAL A 136      48.256   2.399  47.649  1.00 28.00           N  
ANISOU  687  N   VAL A 136     2932   3787   3919     83   -279     66       N  
ATOM    688  CA  VAL A 136      47.608   1.820  46.478  1.00 26.56           C  
ANISOU  688  CA  VAL A 136     2784   3500   3806    170   -281     90       C  
ATOM    689  C   VAL A 136      47.672   2.786  45.300  1.00 27.45           C  
ANISOU  689  C   VAL A 136     2925   3572   3934    167   -200     40       C  
ATOM    690  O   VAL A 136      47.980   2.390  44.176  1.00 31.15           O  
ANISOU  690  O   VAL A 136     3383   4017   4435    224   -207     32       O  
ATOM    691  CB  VAL A 136      46.136   1.453  46.767  1.00 31.34           C  
ANISOU  691  CB  VAL A 136     3444   4041   4423    175   -285    134       C  
ATOM    692  CG1 VAL A 136      45.366   1.231  45.471  1.00 20.85           C  
ANISOU  692  CG1 VAL A 136     2134   2654   3133    223   -273    131       C  
ATOM    693  CG2 VAL A 136      46.064   0.220  47.657  1.00 35.52           C  
ANISOU  693  CG2 VAL A 136     3980   4573   4944    189   -353    195       C  
ATOM    694  N   SER A 137      47.390   4.058  45.571  1.00 18.50           N  
ANISOU  694  N   SER A 137     1845   2417   2766    102   -106     10       N  
ATOM    695  CA  SER A 137      47.474   5.097  44.554  1.00 24.25           C  
ANISOU  695  CA  SER A 137     2637   3084   3493    106      0    -21       C  
ATOM    696  C   SER A 137      48.887   5.182  43.982  1.00 29.18           C  
ANISOU  696  C   SER A 137     3215   3760   4113     62     15    -81       C  
ATOM    697  O   SER A 137      49.071   5.224  42.762  1.00 40.79           O  
ANISOU  697  O   SER A 137     4704   5194   5601    111     44    -85       O  
ATOM    698  CB  SER A 137      47.053   6.450  45.131  1.00 35.87           C  
ANISOU  698  CB  SER A 137     4211   4495   4924     44    133    -44       C  
ATOM    699  OG  SER A 137      46.999   7.442  44.121  1.00 50.71           O  
ANISOU  699  OG  SER A 137     6190   6281   6796     77    257    -47       O  
ATOM    700  N   VAL A 138      49.880   5.194  44.868  1.00 15.62           N  
ANISOU  700  N   VAL A 138     1421   2156   2357    -34     -6   -129       N  
ATOM    701  CA  VAL A 138      51.280   5.223  44.445  1.00 24.48           C  
ANISOU  701  CA  VAL A 138     2451   3384   3465    -84      3   -194       C  
ATOM    702  C   VAL A 138      51.626   4.039  43.532  1.00 35.52           C  
ANISOU  702  C   VAL A 138     3780   4795   4922     52    -75   -157       C  
ATOM    703  O   VAL A 138      52.205   4.218  42.455  1.00 27.12           O  
ANISOU  703  O   VAL A 138     2710   3723   3871     58    -22   -195       O  
ATOM    704  CB  VAL A 138      52.226   5.222  45.661  1.00 17.39           C  
ANISOU  704  CB  VAL A 138     1433   2677   2496   -194    -41   -241       C  
ATOM    705  CG1 VAL A 138      53.671   5.071  45.212  1.00 25.74           C  
ANISOU  705  CG1 VAL A 138     2344   3901   3536   -222    -50   -300       C  
ATOM    706  CG2 VAL A 138      52.042   6.496  46.473  1.00 17.98           C  
ANISOU  706  CG2 VAL A 138     1596   2737   2497   -374     70   -315       C  
ATOM    707  N   SER A 139      51.253   2.836  43.966  1.00 32.41           N  
ANISOU  707  N   SER A 139     3355   4403   4556    154   -181    -86       N  
ATOM    708  CA  SER A 139      51.491   1.615  43.198  1.00 25.46           C  
ANISOU  708  CA  SER A 139     2447   3497   3730    283   -231    -54       C  
ATOM    709  C   SER A 139      50.838   1.666  41.817  1.00 26.22           C  
ANISOU  709  C   SER A 139     2632   3473   3859    316   -184    -65       C  
ATOM    710  O   SER A 139      51.466   1.329  40.809  1.00 17.42           O  
ANISOU  710  O   SER A 139     1497   2358   2765    362   -161    -95       O  
ATOM    711  CB  SER A 139      50.978   0.396  43.969  1.00 31.18           C  
ANISOU  711  CB  SER A 139     3185   4190   4470    367   -316     28       C  
ATOM    712  OG  SER A 139      51.074  -0.785  43.189  1.00 35.55           O  
ANISOU  712  OG  SER A 139     3763   4669   5077    481   -328     50       O  
ATOM    713  N   VAL A 140      49.576   2.084  41.780  1.00 26.52           N  
ANISOU  713  N   VAL A 140     2756   3433   3888    298   -168    -38       N  
ATOM    714  CA  VAL A 140      48.857   2.224  40.521  1.00 24.65           C  
ANISOU  714  CA  VAL A 140     2584   3132   3650    333   -135    -37       C  
ATOM    715  C   VAL A 140      49.599   3.180  39.597  1.00 22.77           C  
ANISOU  715  C   VAL A 140     2368   2897   3387    308    -42    -81       C  
ATOM    716  O   VAL A 140      49.794   2.885  38.419  1.00 28.89           O  
ANISOU  716  O   VAL A 140     3157   3659   4160    346    -27    -98       O  
ATOM    717  CB  VAL A 140      47.418   2.733  40.732  1.00 23.76           C  
ANISOU  717  CB  VAL A 140     2526   2989   3513    335   -126      8       C  
ATOM    718  CG1 VAL A 140      46.794   3.133  39.402  1.00 14.02           C  
ANISOU  718  CG1 VAL A 140     1339   1745   2245    385    -90     21       C  
ATOM    719  CG2 VAL A 140      46.575   1.674  41.420  1.00 20.42           C  
ANISOU  719  CG2 VAL A 140     2086   2564   3109    339   -204     41       C  
ATOM    720  N   SER A 141      50.027   4.315  40.145  1.00 19.29           N  
ANISOU  720  N   SER A 141     1945   2467   2917    224     35   -108       N  
ATOM    721  CA  SER A 141      50.753   5.315  39.364  1.00 19.52           C  
ANISOU  721  CA  SER A 141     2023   2479   2914    167    156   -155       C  
ATOM    722  C   SER A 141      52.017   4.728  38.746  1.00 26.12           C  
ANISOU  722  C   SER A 141     2764   3395   3767    162    148   -213       C  
ATOM    723  O   SER A 141      52.227   4.798  37.530  1.00 40.44           O  
ANISOU  723  O   SER A 141     4617   5179   5568    188    202   -226       O  
ATOM    724  CB  SER A 141      51.110   6.520  40.237  1.00 21.04           C  
ANISOU  724  CB  SER A 141     2260   2668   3068     33    259   -201       C  
ATOM    725  OG  SER A 141      49.944   7.195  40.679  1.00 28.02           O  
ANISOU  725  OG  SER A 141     3256   3456   3935     58    305   -149       O  
ATOM    726  N   VAL A 142      52.847   4.137  39.595  1.00 26.15           N  
ANISOU  726  N   VAL A 142     2635   3514   3786    144     84   -238       N  
ATOM    727  CA  VAL A 142      54.108   3.551  39.159  1.00 27.85           C  
ANISOU  727  CA  VAL A 142     2726   3839   4017    168     80   -286       C  
ATOM    728  C   VAL A 142      53.935   2.471  38.090  1.00 30.09           C  
ANISOU  728  C   VAL A 142     3031   4059   4343    300     51   -265       C  
ATOM    729  O   VAL A 142      54.631   2.474  37.072  1.00 26.11           O  
ANISOU  729  O   VAL A 142     2510   3573   3836    306    116   -313       O  
ATOM    730  CB  VAL A 142      54.858   2.942  40.346  1.00 31.33           C  
ANISOU  730  CB  VAL A 142     3008   4442   4455    183     -7   -281       C  
ATOM    731  CG1 VAL A 142      56.129   2.304  39.874  1.00 32.30           C  
ANISOU  731  CG1 VAL A 142     2982   4699   4592    252     -6   -316       C  
ATOM    732  CG2 VAL A 142      55.152   4.008  41.376  1.00 47.41           C  
ANISOU  732  CG2 VAL A 142     5012   6577   6423     14     28   -331       C  
ATOM    733  N   LEU A 143      53.011   1.545  38.327  1.00 28.80           N  
ANISOU  733  N   LEU A 143     2911   3820   4210    385    -30   -205       N  
ATOM    734  CA  LEU A 143      52.785   0.449  37.392  1.00 23.03           C  
ANISOU  734  CA  LEU A 143     2223   3017   3509    478    -42   -204       C  
ATOM    735  C   LEU A 143      52.162   0.948  36.089  1.00 38.20           C  
ANISOU  735  C   LEU A 143     4246   4880   5389    450     12   -224       C  
ATOM    736  O   LEU A 143      52.372   0.359  35.027  1.00 23.00           O  
ANISOU  736  O   LEU A 143     2346   2931   3461    486     40   -261       O  
ATOM    737  CB  LEU A 143      51.899  -0.620  38.028  1.00 25.75           C  
ANISOU  737  CB  LEU A 143     2610   3289   3882    531   -120   -149       C  
ATOM    738  CG  LEU A 143      52.487  -1.288  39.274  1.00 34.17           C  
ANISOU  738  CG  LEU A 143     3601   4408   4975    596   -174   -103       C  
ATOM    739  CD1 LEU A 143      51.523  -2.324  39.835  1.00 29.86           C  
ANISOU  739  CD1 LEU A 143     3140   3755   4449    631   -222    -45       C  
ATOM    740  CD2 LEU A 143      53.843  -1.913  38.966  1.00 17.94           C  
ANISOU  740  CD2 LEU A 143     1452   2420   2945    704   -147   -122       C  
ATOM    741  N   THR A 144      51.398   2.034  36.174  1.00 24.92           N  
ANISOU  741  N   THR A 144     2627   3179   3663    397     35   -193       N  
ATOM    742  CA  THR A 144      50.817   2.648  34.987  1.00 22.56           C  
ANISOU  742  CA  THR A 144     2422   2850   3301    399     88   -182       C  
ATOM    743  C   THR A 144      51.919   3.256  34.130  1.00 22.25           C  
ANISOU  743  C   THR A 144     2392   2827   3234    362    195   -234       C  
ATOM    744  O   THR A 144      51.953   3.055  32.915  1.00 20.95           O  
ANISOU  744  O   THR A 144     2273   2659   3028    386    228   -253       O  
ATOM    745  CB  THR A 144      49.783   3.731  35.346  1.00 23.87           C  
ANISOU  745  CB  THR A 144     2658   2988   3423    395    109   -115       C  
ATOM    746  OG1 THR A 144      48.679   3.127  36.030  1.00 17.39           O  
ANISOU  746  OG1 THR A 144     1815   2173   2619    423     16    -74       O  
ATOM    747  CG2 THR A 144      49.267   4.407  34.091  1.00 21.43           C  
ANISOU  747  CG2 THR A 144     2445   2670   3029    437    168    -78       C  
ATOM    748  N   LEU A 145      52.824   3.992  34.770  1.00 20.06           N  
ANISOU  748  N   LEU A 145     2072   2583   2966    283    258   -268       N  
ATOM    749  CA  LEU A 145      53.982   4.541  34.070  1.00 22.03           C  
ANISOU  749  CA  LEU A 145     2311   2869   3189    213    375   -335       C  
ATOM    750  C   LEU A 145      54.821   3.427  33.448  1.00 27.90           C  
ANISOU  750  C   LEU A 145     2958   3677   3968    271    357   -389       C  
ATOM    751  O   LEU A 145      55.317   3.555  32.323  1.00 34.82           O  
ANISOU  751  O   LEU A 145     3866   4555   4809    258    443   -430       O  
ATOM    752  CB  LEU A 145      54.838   5.380  35.020  1.00 18.72           C  
ANISOU  752  CB  LEU A 145     1830   2516   2766     79    439   -387       C  
ATOM    753  CG  LEU A 145      54.209   6.690  35.496  1.00 22.96           C  
ANISOU  753  CG  LEU A 145     2509   2956   3259     -4    524   -359       C  
ATOM    754  CD1 LEU A 145      55.218   7.529  36.260  1.00 27.29           C  
ANISOU  754  CD1 LEU A 145     3010   3577   3782   -192    622   -451       C  
ATOM    755  CD2 LEU A 145      53.651   7.470  34.315  1.00 20.14           C  
ANISOU  755  CD2 LEU A 145     2338   2476   2840     30    635   -308       C  
ATOM    756  N   SER A 146      54.965   2.330  34.188  1.00 24.92           N  
ANISOU  756  N   SER A 146     2477   3338   3653    348    260   -382       N  
ATOM    757  CA  SER A 146      55.734   1.180  33.724  1.00 23.16           C  
ANISOU  757  CA  SER A 146     2176   3151   3472    443    259   -421       C  
ATOM    758  C   SER A 146      55.101   0.535  32.498  1.00 22.99           C  
ANISOU  758  C   SER A 146     2274   3032   3431    491    273   -431       C  
ATOM    759  O   SER A 146      55.803   0.128  31.573  1.00 19.52           O  
ANISOU  759  O   SER A 146     1824   2606   2988    521    344   -491       O  
ATOM    760  CB  SER A 146      55.872   0.146  34.841  1.00 18.91           C  
ANISOU  760  CB  SER A 146     1546   2643   2995    544    165   -381       C  
ATOM    761  OG  SER A 146      56.638   0.661  35.912  1.00 31.05           O  
ANISOU  761  OG  SER A 146     2943   4328   4526    497    147   -383       O  
ATOM    762  N   CYS A 147      53.775   0.440  32.497  1.00 18.23           N  
ANISOU  762  N   CYS A 147     1771   2353   2802    488    209   -383       N  
ATOM    763  CA  CYS A 147      53.052  -0.135  31.369  1.00 23.71           C  
ANISOU  763  CA  CYS A 147     2565   2997   3446    499    211   -404       C  
ATOM    764  C   CYS A 147      53.096   0.786  30.160  1.00 27.12           C  
ANISOU  764  C   CYS A 147     3067   3455   3783    453    290   -417       C  
ATOM    765  O   CYS A 147      53.127   0.324  29.021  1.00 33.11           O  
ANISOU  765  O   CYS A 147     3880   4213   4488    455    329   -467       O  
ATOM    766  CB  CYS A 147      51.603  -0.428  31.752  1.00 31.95           C  
ANISOU  766  CB  CYS A 147     3661   4008   4470    488    118   -354       C  
ATOM    767  SG  CYS A 147      51.427  -1.834  32.858  1.00 52.95           S  
ANISOU  767  SG  CYS A 147     6301   6597   7221    533     52   -346       S  
ATOM    768  N   ILE A 148      53.090   2.090  30.415  1.00 22.21           N  
ANISOU  768  N   ILE A 148     2464   2846   3127    408    330   -371       N  
ATOM    769  CA  ILE A 148      53.254   3.068  29.350  1.00 22.17           C  
ANISOU  769  CA  ILE A 148     2553   2844   3027    373    435   -364       C  
ATOM    770  C   ILE A 148      54.604   2.880  28.676  1.00 28.40           C  
ANISOU  770  C   ILE A 148     3298   3668   3825    341    539   -455       C  
ATOM    771  O   ILE A 148      54.685   2.721  27.454  1.00 42.75           O  
ANISOU  771  O   ILE A 148     5182   5492   5568    343    594   -485       O  
ATOM    772  CB  ILE A 148      53.143   4.509  29.875  1.00 20.35           C  
ANISOU  772  CB  ILE A 148     2383   2579   2771    327    502   -304       C  
ATOM    773  CG1 ILE A 148      51.700   4.812  30.274  1.00 23.57           C  
ANISOU  773  CG1 ILE A 148     2848   2961   3146    388    426   -203       C  
ATOM    774  CG2 ILE A 148      53.613   5.494  28.818  1.00 19.74           C  
ANISOU  774  CG2 ILE A 148     2422   2479   2600    282    652   -302       C  
ATOM    775  CD1 ILE A 148      51.499   6.172  30.908  1.00 18.26           C  
ANISOU  775  CD1 ILE A 148     2261   2221   2458    366    511   -142       C  
ATOM    776  N   ALA A 149      55.659   2.887  29.487  1.00 24.75           N  
ANISOU  776  N   ALA A 149     2709   3254   3441    311    564   -500       N  
ATOM    777  CA  ALA A 149      57.020   2.712  28.984  1.00 33.40           C  
ANISOU  777  CA  ALA A 149     3716   4426   4551    287    666   -590       C  
ATOM    778  C   ALA A 149      57.174   1.387  28.241  1.00 34.89           C  
ANISOU  778  C   ALA A 149     3892   4604   4760    385    657   -640       C  
ATOM    779  O   ALA A 149      57.827   1.319  27.201  1.00 29.63           O  
ANISOU  779  O   ALA A 149     3240   3963   4054    372    762   -705       O  
ATOM    780  CB  ALA A 149      58.019   2.796  30.128  1.00 30.80           C  
ANISOU  780  CB  ALA A 149     3205   4209   4290    255    661   -624       C  
ATOM    781  N   LEU A 150      56.563   0.340  28.783  1.00 38.61           N  
ANISOU  781  N   LEU A 150     4357   5025   5288    474    551   -615       N  
ATOM    782  CA  LEU A 150      56.617  -0.986  28.183  1.00 25.78           C  
ANISOU  782  CA  LEU A 150     2762   3347   3685    558    565   -669       C  
ATOM    783  C   LEU A 150      55.949  -0.976  26.814  1.00 30.15           C  
ANISOU  783  C   LEU A 150     3464   3866   4126    505    602   -702       C  
ATOM    784  O   LEU A 150      56.469  -1.535  25.848  1.00 33.18           O  
ANISOU  784  O   LEU A 150     3879   4242   4484    519    693   -784       O  
ATOM    785  CB  LEU A 150      55.939  -2.011  29.092  1.00 27.66           C  
ANISOU  785  CB  LEU A 150     3011   3508   3991    632    464   -629       C  
ATOM    786  CG  LEU A 150      56.390  -3.462  28.956  1.00 35.25           C  
ANISOU  786  CG  LEU A 150     3985   4393   5016    750    512   -677       C  
ATOM    787  CD1 LEU A 150      57.809  -3.612  29.478  1.00 39.64           C  
ANISOU  787  CD1 LEU A 150     4371   5043   5647    868    561   -678       C  
ATOM    788  CD2 LEU A 150      55.436  -4.384  29.700  1.00 43.01           C  
ANISOU  788  CD2 LEU A 150     5048   5259   6037    780    433   -634       C  
ATOM    789  N   ASP A 151      54.790  -0.331  26.746  1.00 25.04           N  
ANISOU  789  N   ASP A 151     2900   3215   3400    451    533   -634       N  
ATOM    790  CA  ASP A 151      54.024  -0.236  25.512  1.00 30.91           C  
ANISOU  790  CA  ASP A 151     3763   3978   4002    408    541   -643       C  
ATOM    791  C   ASP A 151      54.811   0.505  24.437  1.00 29.56           C  
ANISOU  791  C   ASP A 151     3636   3849   3747    370    669   -671       C  
ATOM    792  O   ASP A 151      54.913   0.046  23.294  1.00 34.95           O  
ANISOU  792  O   ASP A 151     4386   4549   4344    350    728   -741       O  
ATOM    793  CB  ASP A 151      52.688   0.464  25.773  1.00 42.49           C  
ANISOU  793  CB  ASP A 151     5272   5476   5396    396    442   -539       C  
ATOM    794  CG  ASP A 151      51.859   0.629  24.516  1.00 58.03           C  
ANISOU  794  CG  ASP A 151     7335   7525   7190    370    431   -527       C  
ATOM    795  OD1 ASP A 151      51.163  -0.336  24.145  1.00 59.95           O  
ANISOU  795  OD1 ASP A 151     7596   7800   7384    336    373   -584       O  
ATOM    796  OD2 ASP A 151      51.895   1.721  23.907  1.00 57.55           O  
ANISOU  796  OD2 ASP A 151     7339   7502   7027    377    488   -461       O  
ATOM    797  N   ARG A 152      55.371   1.652  24.812  1.00 28.39           N  
ANISOU  797  N   ARG A 152     3462   3713   3613    341    729   -627       N  
ATOM    798  CA  ARG A 152      56.162   2.446  23.879  1.00 31.23           C  
ANISOU  798  CA  ARG A 152     3877   4100   3891    281    877   -652       C  
ATOM    799  C   ARG A 152      57.390   1.680  23.415  1.00 24.43           C  
ANISOU  799  C   ARG A 152     2933   3270   3078    283    976   -775       C  
ATOM    800  O   ARG A 152      57.762   1.742  22.246  1.00 33.88           O  
ANISOU  800  O   ARG A 152     4201   4490   4181    248   1083   -825       O  
ATOM    801  CB  ARG A 152      56.578   3.779  24.511  1.00 29.02           C  
ANISOU  801  CB  ARG A 152     3595   3806   3625    214    949   -602       C  
ATOM    802  CG  ARG A 152      55.434   4.764  24.739  1.00 22.80           C  
ANISOU  802  CG  ARG A 152     2933   2964   2765    230    909   -471       C  
ATOM    803  CD  ARG A 152      54.764   5.176  23.432  1.00 23.64           C  
ANISOU  803  CD  ARG A 152     3205   3079   2699    261    945   -403       C  
ATOM    804  NE  ARG A 152      53.755   4.215  22.997  1.00 36.08           N  
ANISOU  804  NE  ARG A 152     4772   4718   4218    327    808   -397       N  
ATOM    805  CZ  ARG A 152      53.462   3.963  21.726  1.00 42.61           C  
ANISOU  805  CZ  ARG A 152     5678   5614   4895    331    818   -406       C  
ATOM    806  NH1 ARG A 152      54.101   4.604  20.756  1.00 54.03           N  
ANISOU  806  NH1 ARG A 152     7229   7061   6237    295    961   -404       N  
ATOM    807  NH2 ARG A 152      52.530   3.068  21.425  1.00 39.15           N  
ANISOU  807  NH2 ARG A 152     5220   5257   4399    351    694   -425       N  
ATOM    808  N   TRP A 153      58.014   0.949  24.332  1.00 27.53           N  
ANISOU  808  N   TRP A 153     3175   3676   3609    342    946   -815       N  
ATOM    809  CA  TRP A 153      59.207   0.180  24.001  1.00 32.13           C  
ANISOU  809  CA  TRP A 153     3655   4304   4248    392   1046   -917       C  
ATOM    810  C   TRP A 153      58.874  -0.941  23.024  1.00 30.02           C  
ANISOU  810  C   TRP A 153     3493   3973   3939    441   1071   -985       C  
ATOM    811  O   TRP A 153      59.639  -1.225  22.103  1.00 27.55           O  
ANISOU  811  O   TRP A 153     3186   3686   3595    441   1202  -1075       O  
ATOM    812  CB  TRP A 153      59.846  -0.390  25.267  1.00 38.70           C  
ANISOU  812  CB  TRP A 153     4300   5182   5221    488    995   -914       C  
ATOM    813  CG  TRP A 153      61.120  -1.129  25.009  1.00 45.66           C  
ANISOU  813  CG  TRP A 153     5046   6141   6162    582   1103  -1000       C  
ATOM    814  CD1 TRP A 153      62.357  -0.586  24.813  1.00 42.21           C  
ANISOU  814  CD1 TRP A 153     4461   5856   5721    534   1222  -1060       C  
ATOM    815  CD2 TRP A 153      61.287  -2.549  24.920  1.00 48.15           C  
ANISOU  815  CD2 TRP A 153     5362   6389   6545    748   1122  -1035       C  
ATOM    816  NE1 TRP A 153      63.282  -1.579  24.607  1.00 46.08           N  
ANISOU  816  NE1 TRP A 153     4832   6403   6274    683   1302  -1124       N  
ATOM    817  CE2 TRP A 153      62.651  -2.794  24.667  1.00 48.66           C  
ANISOU  817  CE2 TRP A 153     5264   6577   6648    828   1251  -1105       C  
ATOM    818  CE3 TRP A 153      60.415  -3.636  25.028  1.00 55.80           C  
ANISOU  818  CE3 TRP A 153     6463   7198   7541    829   1063  -1020       C  
ATOM    819  CZ2 TRP A 153      63.164  -4.081  24.522  1.00 55.70           C  
ANISOU  819  CZ2 TRP A 153     6132   7422   7610   1025   1326  -1144       C  
ATOM    820  CZ3 TRP A 153      60.926  -4.914  24.883  1.00 62.47           C  
ANISOU  820  CZ3 TRP A 153     7313   7971   8454    993   1149  -1069       C  
ATOM    821  CH2 TRP A 153      62.287  -5.125  24.633  1.00 57.91           C  
ANISOU  821  CH2 TRP A 153     6583   7503   7919   1109   1281  -1122       C  
ATOM    822  N   TYR A 154      57.722  -1.569  23.231  1.00 28.69           N  
ANISOU  822  N   TYR A 154     3411   3728   3763    461    957   -954       N  
ATOM    823  CA  TYR A 154      57.276  -2.655  22.370  1.00 34.46           C  
ANISOU  823  CA  TYR A 154     4262   4395   4438    463    983  -1037       C  
ATOM    824  C   TYR A 154      56.891  -2.148  20.985  1.00 44.30           C  
ANISOU  824  C   TYR A 154     5636   5697   5499    360   1030  -1064       C  
ATOM    825  O   TYR A 154      57.119  -2.826  19.988  1.00 41.85           O  
ANISOU  825  O   TYR A 154     5404   5373   5123    339   1126  -1172       O  
ATOM    826  CB  TYR A 154      56.095  -3.392  23.007  1.00 37.23           C  
ANISOU  826  CB  TYR A 154     4665   4668   4812    466    855  -1008       C  
ATOM    827  CG  TYR A 154      56.492  -4.534  23.919  1.00 40.00           C  
ANISOU  827  CG  TYR A 154     4971   4913   5314    584    864  -1025       C  
ATOM    828  CD1 TYR A 154      57.430  -5.476  23.517  1.00 49.80           C  
ANISOU  828  CD1 TYR A 154     6223   6089   6610    679   1004  -1116       C  
ATOM    829  CD2 TYR A 154      55.928  -4.669  25.182  1.00 40.91           C  
ANISOU  829  CD2 TYR A 154     5046   4990   5509    618    746   -939       C  
ATOM    830  CE1 TYR A 154      57.795  -6.523  24.346  1.00 47.27           C  
ANISOU  830  CE1 TYR A 154     5883   5660   6418    829   1028  -1105       C  
ATOM    831  CE2 TYR A 154      56.287  -5.712  26.018  1.00 56.25           C  
ANISOU  831  CE2 TYR A 154     6970   6830   7573    745    762   -931       C  
ATOM    832  CZ  TYR A 154      57.222  -6.636  25.595  1.00 61.93           C  
ANISOU  832  CZ  TYR A 154     7709   7479   8343    861    904  -1006       C  
ATOM    833  OH  TYR A 154      57.583  -7.678  26.423  1.00 71.82           O  
ANISOU  833  OH  TYR A 154     8963   8619   9708   1028    936   -973       O  
ATOM    834  N   ALA A 155      56.312  -0.953  20.922  1.00 48.66           N  
ANISOU  834  N   ALA A 155     6221   6310   5957    307    975   -961       N  
ATOM    835  CA  ALA A 155      55.834  -0.418  19.648  1.00 46.99           C  
ANISOU  835  CA  ALA A 155     6139   6172   5545    238   1005   -950       C  
ATOM    836  C   ALA A 155      56.945   0.243  18.829  1.00 51.98           C  
ANISOU  836  C   ALA A 155     6793   6834   6121    201   1174   -984       C  
ATOM    837  O   ALA A 155      56.900   0.245  17.597  1.00 48.24           O  
ANISOU  837  O   ALA A 155     6430   6411   5487    151   1244  -1024       O  
ATOM    838  CB  ALA A 155      54.702   0.570  19.887  1.00 38.77           C  
ANISOU  838  CB  ALA A 155     5139   5180   4413    238    891   -802       C  
ATOM    839  N   ILE A 156      57.938   0.797  19.517  1.00 49.79           N  
ANISOU  839  N   ILE A 156     6410   6547   5963    208   1244   -975       N  
ATOM    840  CA  ILE A 156      58.993   1.574  18.870  1.00 35.15           C  
ANISOU  840  CA  ILE A 156     4565   4733   4058    140   1418  -1006       C  
ATOM    841  C   ILE A 156      60.243   0.748  18.578  1.00 46.22           C  
ANISOU  841  C   ILE A 156     5859   6164   5539    162   1548  -1149       C  
ATOM    842  O   ILE A 156      60.768   0.772  17.462  1.00 47.54           O  
ANISOU  842  O   ILE A 156     6090   6366   5606    112   1689  -1221       O  
ATOM    843  CB  ILE A 156      59.391   2.786  19.737  1.00 31.68           C  
ANISOU  843  CB  ILE A 156     4071   4291   3675     88   1448   -934       C  
ATOM    844  CG1 ILE A 156      58.252   3.807  19.769  1.00 31.90           C  
ANISOU  844  CG1 ILE A 156     4252   4274   3596     81   1383   -785       C  
ATOM    845  CG2 ILE A 156      60.678   3.418  19.227  1.00 32.57           C  
ANISOU  845  CG2 ILE A 156     4157   4456   3763    -15   1649  -1004       C  
ATOM    846  CD1 ILE A 156      58.397   4.849  20.852  1.00 35.75           C  
ANISOU  846  CD1 ILE A 156     4711   4718   4156     37   1398   -719       C  
ATOM    847  N   CYS A 157      60.719   0.022  19.583  1.00 62.51           N  
ANISOU  847  N   CYS A 157     7288   9814   6650    318    365  -1966       N  
ATOM    848  CA  CYS A 157      61.949  -0.747  19.441  1.00 71.06           C  
ANISOU  848  CA  CYS A 157     8259  10945   7796    441    668  -1972       C  
ATOM    849  C   CYS A 157      61.710  -2.098  18.771  1.00 79.76           C  
ANISOU  849  C   CYS A 157     9499  11607   9201    445    859  -1893       C  
ATOM    850  O   CYS A 157      62.641  -2.708  18.247  1.00 79.56           O  
ANISOU  850  O   CYS A 157     9492  11477   9261    442   1116  -1988       O  
ATOM    851  CB  CYS A 157      62.609  -0.946  20.806  1.00 65.31           C  
ANISOU  851  CB  CYS A 157     7045  10707   7062    797    775  -1739       C  
ATOM    852  SG  CYS A 157      63.130   0.592  21.601  1.00 52.62           S  
ANISOU  852  SG  CYS A 157     5233   9669   5092    780    619  -1892       S  
ATOM    853  N   HIS A 158      60.466  -2.567  18.792  1.00 81.86           N  
ANISOU  853  N   HIS A 158     9849  11612   9643    447    746  -1736       N  
ATOM    854  CA  HIS A 158      60.126  -3.841  18.161  1.00 81.92           C  
ANISOU  854  CA  HIS A 158     9987  11182   9959    432    925  -1679       C  
ATOM    855  C   HIS A 158      58.741  -3.821  17.514  1.00 82.23           C  
ANISOU  855  C   HIS A 158    10346  10859  10040    193    721  -1707       C  
ATOM    856  O   HIS A 158      57.824  -4.488  17.990  1.00 88.59           O  
ANISOU  856  O   HIS A 158    11059  11538  11062    345    683  -1460       O  
ATOM    857  CB  HIS A 158      60.196  -4.975  19.186  1.00 87.68           C  
ANISOU  857  CB  HIS A 158    10323  11996  10994    827   1103  -1314       C  
ATOM    858  CG  HIS A 158      61.486  -5.022  19.942  1.00 98.04           C  
ANISOU  858  CG  HIS A 158    11267  13709  12274   1081   1284  -1215       C  
ATOM    859  ND1 HIS A 158      62.633  -5.582  19.425  1.00111.73           N  
ANISOU  859  ND1 HIS A 158    12981  15347  14125   1092   1579  -1327       N  
ATOM    860  CD2 HIS A 158      61.812  -4.566  21.175  1.00100.63           C  
ANISOU  860  CD2 HIS A 158    11219  14556  12459   1317   1215  -1020       C  
ATOM    861  CE1 HIS A 158      63.610  -5.475  20.308  1.00114.51           C  
ANISOU  861  CE1 HIS A 158    12960  16133  14414   1336   1674  -1178       C  
ATOM    862  NE2 HIS A 158      63.138  -4.862  21.378  1.00110.26           N  
ANISOU  862  NE2 HIS A 158    12200  15989  13704   1467   1456   -992       N  
ATOM    863  N   PRO A 159      58.589  -3.067  16.414  1.00 80.34           N  
ANISOU  863  N   PRO A 159    10472  10460   9595   -193    588  -1988       N  
ATOM    864  CA  PRO A 159      57.284  -2.928  15.757  1.00 80.06           C  
ANISOU  864  CA  PRO A 159    10736  10117   9566   -456    368  -2004       C  
ATOM    865  C   PRO A 159      56.856  -4.189  15.005  1.00 82.32           C  
ANISOU  865  C   PRO A 159    11189   9982  10107   -550    545  -2011       C  
ATOM    866  O   PRO A 159      57.080  -5.306  15.475  1.00 77.59           O  
ANISOU  866  O   PRO A 159    10375   9311   9793   -280    781  -1852       O  
ATOM    867  CB  PRO A 159      57.503  -1.765  14.775  1.00 80.54           C  
ANISOU  867  CB  PRO A 159    11090  10184   9325   -847    208  -2286       C  
ATOM    868  CG  PRO A 159      58.822  -1.144  15.161  1.00 75.21           C  
ANISOU  868  CG  PRO A 159    10234   9867   8475   -740    304  -2400       C  
ATOM    869  CD  PRO A 159      59.621  -2.258  15.745  1.00 77.67           C  
ANISOU  869  CD  PRO A 159    10268  10249   8995   -411    619  -2282       C  
ATOM    870  N   SER A 164      49.740  -3.851  20.207  1.00 69.13           N  
ANISOU  870  N   SER A 164     8701   8603   8961    399   -702   -455       N  
ATOM    871  CA  SER A 164      49.134  -3.369  21.444  1.00 70.00           C  
ANISOU  871  CA  SER A 164     8519   9033   9044    604   -871   -277       C  
ATOM    872  C   SER A 164      47.728  -2.830  21.207  1.00 60.00           C  
ANISOU  872  C   SER A 164     7443   7560   7795    422  -1156   -264       C  
ATOM    873  O   SER A 164      47.551  -1.763  20.621  1.00 60.20           O  
ANISOU  873  O   SER A 164     7670   7522   7680    161  -1335   -461       O  
ATOM    874  CB  SER A 164      50.004  -2.288  22.082  1.00 75.87           C  
ANISOU  874  CB  SER A 164     9044  10234   9550    663   -894   -414       C  
ATOM    875  OG  SER A 164      51.171  -2.842  22.667  1.00 82.44           O  
ANISOU  875  OG  SER A 164     9589  11356  10380    907   -649   -332       O  
ATOM    876  N   THR A 165      46.732  -3.573  21.675  1.00 55.54           N  
ANISOU  876  N   THR A 165     6795   6887   7421    563  -1199    -11       N  
ATOM    877  CA  THR A 165      45.339  -3.198  21.479  1.00 58.32           C  
ANISOU  877  CA  THR A 165     7311   7025   7823    410  -1459     36       C  
ATOM    878  C   THR A 165      44.748  -2.557  22.731  1.00 65.82           C  
ANISOU  878  C   THR A 165     7950   8316   8742    592  -1622    151       C  
ATOM    879  O   THR A 165      45.353  -2.593  23.803  1.00 67.03           O  
ANISOU  879  O   THR A 165     7743   8886   8840    850  -1521    232       O  
ATOM    880  CB  THR A 165      44.486  -4.416  21.092  1.00 53.83           C  
ANISOU  880  CB  THR A 165     6883   6081   7490    407  -1415    220       C  
ATOM    881  OG1 THR A 165      44.538  -5.387  22.144  1.00 47.92           O  
ANISOU  881  OG1 THR A 165     5798   5503   6907    758  -1268    498       O  
ATOM    882  CG2 THR A 165      45.007  -5.041  19.807  1.00 52.70           C  
ANISOU  882  CG2 THR A 165     7046   5596   7381    185  -1239     57       C  
ATOM    883  N   ALA A 166      43.562  -1.973  22.586  1.00 60.35           N  
ANISOU  883  N   ALA A 166     7382   7460   8087    444  -1870    157       N  
ATOM    884  CA  ALA A 166      42.876  -1.336  23.704  1.00 46.67           C  
ANISOU  884  CA  ALA A 166     5368   6012   6351    582  -2027    231       C  
ATOM    885  C   ALA A 166      42.367  -2.376  24.700  1.00 48.51           C  
ANISOU  885  C   ALA A 166     5330   6382   6722    875  -1962    540       C  
ATOM    886  O   ALA A 166      42.229  -2.090  25.890  1.00 54.61           O  
ANISOU  886  O   ALA A 166     5749   7552   7447   1066  -1995    618       O  
ATOM    887  CB  ALA A 166      41.729  -0.475  23.201  1.00 44.15           C  
ANISOU  887  CB  ALA A 166     5258   5433   6084    336  -2300    165       C  
ATOM    888  N   LYS A 167      42.085  -3.578  24.206  1.00 43.53           N  
ANISOU  888  N   LYS A 167     4850   5427   6262    894  -1865    709       N  
ATOM    889  CA  LYS A 167      41.690  -4.691  25.066  1.00 44.41           C  
ANISOU  889  CA  LYS A 167     4705   5630   6540   1172  -1779   1034       C  
ATOM    890  C   LYS A 167      42.846  -5.108  25.959  1.00 47.84           C  
ANISOU  890  C   LYS A 167     4765   6487   6924   1448  -1561   1145       C  
ATOM    891  O   LYS A 167      42.681  -5.301  27.168  1.00 55.04           O  
ANISOU  891  O   LYS A 167     5298   7780   7835   1687  -1561   1365       O  
ATOM    892  CB  LYS A 167      41.218  -5.881  24.230  1.00 48.28           C  
ANISOU  892  CB  LYS A 167     5451   5637   7256   1106  -1696   1156       C  
ATOM    893  CG  LYS A 167      39.760  -5.796  23.801  1.00 63.41           C  
ANISOU  893  CG  LYS A 167     7600   7227   9267    933  -1921   1203       C  
ATOM    894  CD  LYS A 167      38.854  -6.472  24.821  1.00 68.70           C  
ANISOU  894  CD  LYS A 167     8009   7998  10095   1177  -1964   1525       C  
ATOM    895  CE  LYS A 167      37.395  -6.052  24.651  1.00 64.73           C  
ANISOU  895  CE  LYS A 167     7665   7290   9641   1026  -2231   1556       C  
ATOM    896  NZ  LYS A 167      37.173  -4.582  24.879  1.00 55.89           N  
ANISOU  896  NZ  LYS A 167     6510   6368   8357    912  -2441   1368       N  
ATOM    897  N   ARG A 168      44.016  -5.248  25.345  1.00 47.66           N  
ANISOU  897  N   ARG A 168     4840   6413   6855   1399  -1375   1000       N  
ATOM    898  CA  ARG A 168      45.240  -5.569  26.063  1.00 51.97           C  
ANISOU  898  CA  ARG A 168     5048   7351   7348   1632  -1164   1090       C  
ATOM    899  C   ARG A 168      45.512  -4.513  27.125  1.00 52.74           C  
ANISOU  899  C   ARG A 168     4824   8016   7198   1713  -1258   1022       C  
ATOM    900  O   ARG A 168      45.936  -4.826  28.239  1.00 63.52           O  
ANISOU  900  O   ARG A 168     5773   9837   8525   1959  -1167   1233       O  
ATOM    901  CB  ARG A 168      46.419  -5.667  25.092  1.00 60.63           C  
ANISOU  901  CB  ARG A 168     6350   8273   8414   1512   -974    875       C  
ATOM    902  CG  ARG A 168      47.754  -5.939  25.759  1.00 80.66           C  
ANISOU  902  CG  ARG A 168     8544  11205  10898   1738   -754    959       C  
ATOM    903  CD  ARG A 168      48.914  -5.494  24.880  1.00 89.75           C  
ANISOU  903  CD  ARG A 168     9897  12290  11914   1569   -635    648       C  
ATOM    904  NE  ARG A 168      50.164  -5.411  25.631  1.00 91.09           N  
ANISOU  904  NE  ARG A 168     9717  12931  11964   1763   -477    694       N  
ATOM    905  CZ  ARG A 168      51.058  -6.391  25.710  1.00 97.05           C  
ANISOU  905  CZ  ARG A 168    10297  13695  12881   1943   -218    860       C  
ATOM    906  NH1 ARG A 168      50.846  -7.538  25.077  1.00 93.81           N  
ANISOU  906  NH1 ARG A 168    10032  12828  12785   1953    -70    968       N  
ATOM    907  NH2 ARG A 168      52.167  -6.225  26.419  1.00102.18           N  
ANISOU  907  NH2 ARG A 168    10613  14811  13400   2105    -98    916       N  
ATOM    908  N   ALA A 169      45.248  -3.259  26.772  1.00 36.20           N  
ANISOU  908  N   ALA A 169     5086   4431   4238    933  -1601   -742       N  
ATOM    909  CA  ALA A 169      45.454  -2.144  27.685  1.00 31.06           C  
ANISOU  909  CA  ALA A 169     4297   3833   3673    883  -1544   -611       C  
ATOM    910  C   ALA A 169      44.474  -2.203  28.851  1.00 42.15           C  
ANISOU  910  C   ALA A 169     5499   5191   5325    747  -1555   -707       C  
ATOM    911  O   ALA A 169      44.838  -1.910  29.987  1.00 42.81           O  
ANISOU  911  O   ALA A 169     5478   5288   5499    677  -1425   -611       O  
ATOM    912  CB  ALA A 169      45.324  -0.822  26.947  1.00 28.69           C  
ANISOU  912  CB  ALA A 169     4048   3582   3271    962  -1677   -554       C  
ATOM    913  N   ARG A 170      43.234  -2.587  28.563  1.00 42.40           N  
ANISOU  913  N   ARG A 170     5472   5180   5460    705  -1707   -905       N  
ATOM    914  CA  ARG A 170      42.209  -2.722  29.593  1.00 41.56           C  
ANISOU  914  CA  ARG A 170     5160   5042   5588    561  -1708  -1021       C  
ATOM    915  C   ARG A 170      42.618  -3.801  30.593  1.00 33.25           C  
ANISOU  915  C   ARG A 170     4110   3914   4611    450  -1499   -997       C  
ATOM    916  O   ARG A 170      42.550  -3.603  31.815  1.00 44.02           O  
ANISOU  916  O   ARG A 170     5347   5272   6106    357  -1386   -950       O  
ATOM    917  CB  ARG A 170      40.858  -3.053  28.955  1.00 49.66           C  
ANISOU  917  CB  ARG A 170     6113   6061   6695    530  -1910  -1260       C  
ATOM    918  CG  ARG A 170      39.650  -2.664  29.790  1.00 61.68           C  
ANISOU  918  CG  ARG A 170     7378   7612   8447    421  -1965  -1386       C  
ATOM    919  CD  ARG A 170      38.502  -2.197  28.900  1.00 81.62           C  
ANISOU  919  CD  ARG A 170     9826  10204  10984    492  -2188  -1536       C  
ATOM    920  NE  ARG A 170      38.845  -0.986  28.153  1.00 87.14           N  
ANISOU  920  NE  ARG A 170    10639  10947  11522    678  -2277  -1406       N  
ATOM    921  CZ  ARG A 170      38.685  -0.839  26.840  1.00 80.74           C  
ANISOU  921  CZ  ARG A 170     9968  10154  10557    809  -2413  -1434       C  
ATOM    922  NH1 ARG A 170      38.181  -1.827  26.113  1.00 76.06           N  
ANISOU  922  NH1 ARG A 170     9400   9551   9948    781  -2492  -1592       N  
ATOM    923  NH2 ARG A 170      39.028   0.300  26.254  1.00 73.22           N  
ANISOU  923  NH2 ARG A 170     9144   9217   9460    958  -2459  -1302       N  
ATOM    924  N   ASN A 171      43.055  -4.938  30.058  1.00 28.91           N  
ANISOU  924  N   ASN A 171     3730   3296   3959    477  -1448  -1027       N  
ATOM    925  CA  ASN A 171      43.598  -6.014  30.877  1.00 37.60           C  
ANISOU  925  CA  ASN A 171     4900   4304   5082    419  -1251   -984       C  
ATOM    926  C   ASN A 171      44.744  -5.518  31.750  1.00 31.58           C  
ANISOU  926  C   ASN A 171     4117   3606   4276    469  -1091   -771       C  
ATOM    927  O   ASN A 171      44.803  -5.818  32.944  1.00 41.62           O  
ANISOU  927  O   ASN A 171     5333   4836   5646    385   -957   -732       O  
ATOM    928  CB  ASN A 171      44.074  -7.172  29.997  1.00 46.48           C  
ANISOU  928  CB  ASN A 171     6254   5349   6057    496  -1230  -1030       C  
ATOM    929  CG  ASN A 171      42.927  -7.961  29.399  1.00 58.54           C  
ANISOU  929  CG  ASN A 171     7810   6780   7651    395  -1357  -1265       C  
ATOM    930  OD1 ASN A 171      41.914  -8.202  30.057  1.00 61.10           O  
ANISOU  930  OD1 ASN A 171     7999   7051   8164    218  -1362  -1391       O  
ATOM    931  ND2 ASN A 171      43.079  -8.367  28.143  1.00 66.84           N  
ANISOU  931  ND2 ASN A 171     9035   7819   8544    497  -1455  -1335       N  
ATOM    932  N   SER A 172      45.645  -4.750  31.143  1.00 26.70           N  
ANISOU  932  N   SER A 172     3547   3095   3501    597  -1105   -640       N  
ATOM    933  CA  SER A 172      46.770  -4.162  31.860  1.00 30.60           C  
ANISOU  933  CA  SER A 172     3999   3682   3945    633   -972   -451       C  
ATOM    934  C   SER A 172      46.291  -3.320  33.039  1.00 34.47           C  
ANISOU  934  C   SER A 172     4310   4190   4599    520   -960   -426       C  
ATOM    935  O   SER A 172      46.785  -3.478  34.154  1.00 25.09           O  
ANISOU  935  O   SER A 172     3074   3009   3451    483   -825   -344       O  
ATOM    936  CB  SER A 172      47.625  -3.310  30.918  1.00 33.78           C  
ANISOU  936  CB  SER A 172     4467   4201   4168    746  -1001   -338       C  
ATOM    937  OG  SER A 172      48.215  -4.106  29.904  1.00 34.51           O  
ANISOU  937  OG  SER A 172     4728   4293   4090    865   -980   -348       O  
ATOM    938  N   ILE A 173      45.327  -2.438  32.784  1.00 42.38           N  
ANISOU  938  N   ILE A 173     5220   5200   5681    485  -1107   -503       N  
ATOM    939  CA  ILE A 173      44.736  -1.597  33.825  1.00 40.42           C  
ANISOU  939  CA  ILE A 173     4806   4965   5588    394  -1108   -504       C  
ATOM    940  C   ILE A 173      44.215  -2.432  34.989  1.00 43.15           C  
ANISOU  940  C   ILE A 173     5072   5235   6086    270   -998   -573       C  
ATOM    941  O   ILE A 173      44.604  -2.227  36.150  1.00 46.20           O  
ANISOU  941  O   ILE A 173     5401   5637   6517    221   -875   -483       O  
ATOM    942  CB  ILE A 173      43.566  -0.749  33.279  1.00 33.22           C  
ANISOU  942  CB  ILE A 173     3813   4061   4748    405  -1303   -621       C  
ATOM    943  CG1 ILE A 173      44.021   0.142  32.123  1.00 24.38           C  
ANISOU  943  CG1 ILE A 173     2813   2992   3459    532  -1414   -544       C  
ATOM    944  CG2 ILE A 173      42.950   0.083  34.391  1.00 23.43           C  
ANISOU  944  CG2 ILE A 173     2403   2833   3666    330  -1291   -633       C  
ATOM    945  CD1 ILE A 173      45.044   1.163  32.509  1.00 35.74           C  
ANISOU  945  CD1 ILE A 173     4276   4485   4818    543  -1326   -358       C  
ATOM    946  N   VAL A 174      43.333  -3.375  34.664  1.00 24.41           N  
ANISOU  946  N   VAL A 174     2709   2780   3785    208  -1040   -736       N  
ATOM    947  CA  VAL A 174      42.719  -4.228  35.676  1.00 28.75           C  
ANISOU  947  CA  VAL A 174     3206   3239   4477     60   -925   -816       C  
ATOM    948  C   VAL A 174      43.774  -4.928  36.529  1.00 26.10           C  
ANISOU  948  C   VAL A 174     2986   2858   4072     74   -730   -677       C  
ATOM    949  O   VAL A 174      43.715  -4.898  37.765  1.00 35.05           O  
ANISOU  949  O   VAL A 174     4057   3975   5285     -6   -611   -635       O  
ATOM    950  CB  VAL A 174      41.803  -5.281  35.035  1.00 32.66           C  
ANISOU  950  CB  VAL A 174     3738   3643   5030    -23   -986  -1011       C  
ATOM    951  CG1 VAL A 174      41.263  -6.228  36.095  1.00 37.76           C  
ANISOU  951  CG1 VAL A 174     4368   4174   5807   -201   -831  -1080       C  
ATOM    952  CG2 VAL A 174      40.667  -4.603  34.285  1.00 27.63           C  
ANISOU  952  CG2 VAL A 174     2952   3074   4470    -29  -1197  -1170       C  
ATOM    953  N   ILE A 175      44.745  -5.542  35.859  1.00 25.22           N  
ANISOU  953  N   ILE A 175     3047   2737   3799    196   -703   -609       N  
ATOM    954  CA  ILE A 175      45.853  -6.201  36.541  1.00 33.77           C  
ANISOU  954  CA  ILE A 175     4244   3800   4788    263   -540   -476       C  
ATOM    955  C   ILE A 175      46.584  -5.242  37.482  1.00 28.63           C  
ANISOU  955  C   ILE A 175     3484   3270   4123    286   -480   -324       C  
ATOM    956  O   ILE A 175      46.864  -5.587  38.633  1.00 28.48           O  
ANISOU  956  O   ILE A 175     3475   3223   4125    259   -355   -262       O  
ATOM    957  CB  ILE A 175      46.854  -6.792  35.533  1.00 26.65           C  
ANISOU  957  CB  ILE A 175     3514   2914   3698    431   -537   -427       C  
ATOM    958  CG1 ILE A 175      46.223  -7.978  34.799  1.00 32.46           C  
ANISOU  958  CG1 ILE A 175     4405   3495   4435    403   -568   -580       C  
ATOM    959  CG2 ILE A 175      48.128  -7.228  36.236  1.00 27.14           C  
ANISOU  959  CG2 ILE A 175     3651   3012   3650    547   -389   -277       C  
ATOM    960  CD1 ILE A 175      47.094  -8.554  33.704  1.00 35.61           C  
ANISOU  960  CD1 ILE A 175     4986   3901   4642    579   -573   -557       C  
ATOM    961  N   ILE A 176      46.872  -4.039  36.987  1.00 26.53           N  
ANISOU  961  N   ILE A 176     3136   3129   3816    330   -570   -269       N  
ATOM    962  CA  ILE A 176      47.537  -3.002  37.774  1.00 35.25           C  
ANISOU  962  CA  ILE A 176     4140   4347   4908    327   -530   -142       C  
ATOM    963  C   ILE A 176      46.791  -2.730  39.078  1.00 30.69           C  
ANISOU  963  C   ILE A 176     3452   3727   4481    202   -483   -174       C  
ATOM    964  O   ILE A 176      47.387  -2.742  40.162  1.00 26.17           O  
ANISOU  964  O   ILE A 176     2866   3187   3892    196   -377    -85       O  
ATOM    965  CB  ILE A 176      47.664  -1.679  36.978  1.00 37.87           C  
ANISOU  965  CB  ILE A 176     4425   4772   5191    354   -644   -105       C  
ATOM    966  CG1 ILE A 176      48.719  -1.806  35.877  1.00 34.98           C  
ANISOU  966  CG1 ILE A 176     4165   4484   4641    475   -643    -29       C  
ATOM    967  CG2 ILE A 176      48.022  -0.524  37.903  1.00 19.20           C  
ANISOU  967  CG2 ILE A 176     1955   2486   2855    300   -615    -13       C  
ATOM    968  CD1 ILE A 176      48.808  -0.587  34.977  1.00 20.66           C  
ANISOU  968  CD1 ILE A 176     2356   2735   2759    493   -743      9       C  
ATOM    969  N   TRP A 177      45.484  -2.505  38.974  1.00 32.06           N  
ANISOU  969  N   TRP A 177     3543   3842   4795    111   -562   -311       N  
ATOM    970  CA  TRP A 177      44.684  -2.200  40.160  1.00 26.06           C  
ANISOU  970  CA  TRP A 177     2664   3055   4181     -6   -509   -359       C  
ATOM    971  C   TRP A 177      44.590  -3.376  41.138  1.00 32.32           C  
ANISOU  971  C   TRP A 177     3523   3748   5007    -80   -350   -368       C  
ATOM    972  O   TRP A 177      44.677  -3.182  42.357  1.00 27.48           O  
ANISOU  972  O   TRP A 177     2875   3142   4424   -129   -248   -315       O  
ATOM    973  CB  TRP A 177      43.283  -1.749  39.753  1.00 28.41           C  
ANISOU  973  CB  TRP A 177     2836   3338   4622    -69   -631   -523       C  
ATOM    974  CG  TRP A 177      43.209  -0.295  39.384  1.00 27.29           C  
ANISOU  974  CG  TRP A 177     2618   3276   4474     -8   -760   -500       C  
ATOM    975  CD1 TRP A 177      43.274   0.237  38.131  1.00 30.06           C  
ANISOU  975  CD1 TRP A 177     3014   3660   4746     89   -910   -503       C  
ATOM    976  CD2 TRP A 177      43.056   0.813  40.282  1.00 28.99           C  
ANISOU  976  CD2 TRP A 177     2735   3531   4750    -33   -746   -468       C  
ATOM    977  NE1 TRP A 177      43.168   1.606  38.190  1.00 33.89           N  
ANISOU  977  NE1 TRP A 177     3450   4189   5239    125   -989   -469       N  
ATOM    978  CE2 TRP A 177      43.034   1.984  39.500  1.00 27.81           C  
ANISOU  978  CE2 TRP A 177     2589   3421   4558     51   -892   -452       C  
ATOM    979  CE3 TRP A 177      42.936   0.926  41.672  1.00 30.34           C  
ANISOU  979  CE3 TRP A 177     2838   3696   4993   -115   -622   -452       C  
ATOM    980  CZ2 TRP A 177      42.894   3.254  40.059  1.00 19.73           C  
ANISOU  980  CZ2 TRP A 177     1509   2417   3568     57   -918   -425       C  
ATOM    981  CZ3 TRP A 177      42.798   2.188  42.226  1.00 23.43           C  
ANISOU  981  CZ3 TRP A 177     1892   2859   4152   -109   -650   -432       C  
ATOM    982  CH2 TRP A 177      42.778   3.335  41.421  1.00 20.57           C  
ANISOU  982  CH2 TRP A 177     1540   2522   3753    -24   -797   -421       C  
ATOM    983  N   ILE A 178      44.415  -4.588  40.613  1.00 28.80           N  
ANISOU  983  N   ILE A 178     3200   3198   4544    -88   -326   -434       N  
ATOM    984  CA  ILE A 178      44.352  -5.777  41.466  1.00 32.12           C  
ANISOU  984  CA  ILE A 178     3741   3488   4976   -156   -167   -435       C  
ATOM    985  C   ILE A 178      45.656  -5.987  42.240  1.00 41.25           C  
ANISOU  985  C   ILE A 178     5006   4677   5992    -39    -59   -261       C  
ATOM    986  O   ILE A 178      45.650  -6.114  43.473  1.00 42.60           O  
ANISOU  986  O   ILE A 178     5190   4816   6180    -90     59   -214       O  
ATOM    987  CB  ILE A 178      44.050  -7.049  40.654  1.00 30.54           C  
ANISOU  987  CB  ILE A 178     3697   3148   4759   -176   -165   -535       C  
ATOM    988  CG1 ILE A 178      42.659  -6.969  40.026  1.00 25.11           C  
ANISOU  988  CG1 ILE A 178     2883   2436   4221   -318   -271   -734       C  
ATOM    989  CG2 ILE A 178      44.150  -8.280  41.540  1.00 28.23           C  
ANISOU  989  CG2 ILE A 178     3589   2691   4445   -229     14   -508       C  
ATOM    990  CD1 ILE A 178      42.271  -8.214  39.257  1.00 28.86           C  
ANISOU  990  CD1 ILE A 178     3510   2767   4689   -374   -276   -859       C  
ATOM    991  N   VAL A 179      46.768  -6.022  41.509  1.00 30.86           N  
ANISOU  991  N   VAL A 179     3759   3437   4528    124   -100   -173       N  
ATOM    992  CA  VAL A 179      48.088  -6.163  42.115  1.00 31.70           C  
ANISOU  992  CA  VAL A 179     3929   3622   4492    262    -23    -20       C  
ATOM    993  C   VAL A 179      48.324  -5.089  43.171  1.00 36.37           C  
ANISOU  993  C   VAL A 179     4379   4332   5108    222    -10     55       C  
ATOM    994  O   VAL A 179      48.734  -5.392  44.297  1.00 32.62           O  
ANISOU  994  O   VAL A 179     3951   3853   4588    243     87    128       O  
ATOM    995  CB  VAL A 179      49.207  -6.089  41.055  1.00 34.56           C  
ANISOU  995  CB  VAL A 179     4321   4104   4705    432    -80     47       C  
ATOM    996  CG1 VAL A 179      50.562  -5.861  41.715  1.00 37.08           C  
ANISOU  996  CG1 VAL A 179     4611   4579   4897    558    -26    192       C  
ATOM    997  CG2 VAL A 179      49.223  -7.354  40.211  1.00 33.40           C  
ANISOU  997  CG2 VAL A 179     4366   3833   4493    514    -64    -10       C  
ATOM    998  N   SER A 180      48.049  -3.839  42.805  1.00 32.11           N  
ANISOU  998  N   SER A 180     3687   3887   4627    170   -111     34       N  
ATOM    999  CA  SER A 180      48.239  -2.717  43.719  1.00 32.04           C  
ANISOU  999  CA  SER A 180     3557   3976   4640    123   -110     90       C  
ATOM   1000  C   SER A 180      47.431  -2.885  45.007  1.00 34.10           C  
ANISOU 1000  C   SER A 180     3805   4151   5000     12    -17     48       C  
ATOM   1001  O   SER A 180      47.948  -2.671  46.102  1.00 30.64           O  
ANISOU 1001  O   SER A 180     3364   3765   4513     20     48    126       O  
ATOM   1002  CB  SER A 180      47.865  -1.403  43.034  1.00 25.81           C  
ANISOU 1002  CB  SER A 180     2651   3249   3906     82   -235     55       C  
ATOM   1003  OG  SER A 180      48.716  -1.150  41.929  1.00 29.26           O  
ANISOU 1003  OG  SER A 180     3115   3775   4229    174   -299    113       O  
ATOM   1004  N   CYS A 181      46.168  -3.278  44.876  1.00 28.34           N  
ANISOU 1004  N   CYS A 181     3065   3302   4402    -97     -6    -80       N  
ATOM   1005  CA  CYS A 181      45.320  -3.460  46.049  1.00 28.57           C  
ANISOU 1005  CA  CYS A 181     3074   3254   4528   -222    106   -131       C  
ATOM   1006  C   CYS A 181      45.791  -4.617  46.926  1.00 38.49           C  
ANISOU 1006  C   CYS A 181     4512   4419   5693   -198    257    -57       C  
ATOM   1007  O   CYS A 181      45.667  -4.565  48.152  1.00 26.54           O  
ANISOU 1007  O   CYS A 181     3015   2890   4180   -250    361    -26       O  
ATOM   1008  CB  CYS A 181      43.866  -3.683  45.635  1.00 20.74           C  
ANISOU 1008  CB  CYS A 181     2005   2176   3701   -356     89   -303       C  
ATOM   1009  SG  CYS A 181      43.032  -2.193  45.050  1.00 40.52           S  
ANISOU 1009  SG  CYS A 181     4285   4782   6328   -374    -75   -405       S  
ATOM   1010  N   ILE A 182      46.329  -5.661  46.304  1.00 39.03           N  
ANISOU 1010  N   ILE A 182     4740   4420   5669   -106    269    -28       N  
ATOM   1011  CA  ILE A 182      46.764  -6.827  47.066  1.00 32.88           C  
ANISOU 1011  CA  ILE A 182     4178   3527   4789    -54    406     44       C  
ATOM   1012  C   ILE A 182      48.077  -6.585  47.813  1.00 32.31           C  
ANISOU 1012  C   ILE A 182     4135   3583   4557    108    417    196       C  
ATOM   1013  O   ILE A 182      48.175  -6.877  49.004  1.00 44.40           O  
ANISOU 1013  O   ILE A 182     5762   5073   6036    108    520    254       O  
ATOM   1014  CB  ILE A 182      46.918  -8.062  46.160  1.00 38.13           C  
ANISOU 1014  CB  ILE A 182     5032   4059   5396     13    416     17       C  
ATOM   1015  CG1 ILE A 182      45.545  -8.519  45.666  1.00 24.20           C  
ANISOU 1015  CG1 ILE A 182     3264   2146   3786   -182    430   -149       C  
ATOM   1016  CG2 ILE A 182      47.609  -9.197  46.909  1.00 29.57           C  
ANISOU 1016  CG2 ILE A 182     4207   2861   4167    129    542    118       C  
ATOM   1017  CD1 ILE A 182      45.596  -9.712  44.751  1.00 31.48           C  
ANISOU 1017  CD1 ILE A 182     4386   2917   4658   -143    433   -199       C  
ATOM   1018  N   ILE A 183      49.079  -6.041  47.129  1.00 28.40           N  
ANISOU 1018  N   ILE A 183     3557   3255   3980    240    311    256       N  
ATOM   1019  CA  ILE A 183      50.398  -5.890  47.743  1.00 30.05           C  
ANISOU 1019  CA  ILE A 183     3768   3615   4034    397    311    383       C  
ATOM   1020  C   ILE A 183      50.434  -4.829  48.843  1.00 33.04           C  
ANISOU 1020  C   ILE A 183     4020   4103   4429    324    306    413       C  
ATOM   1021  O   ILE A 183      51.372  -4.791  49.637  1.00 35.79           O  
ANISOU 1021  O   ILE A 183     4381   4564   4653    429    316    503       O  
ATOM   1022  CB  ILE A 183      51.481  -5.541  46.695  1.00 37.06           C  
ANISOU 1022  CB  ILE A 183     4571   4679   4832    533    215    428       C  
ATOM   1023  CG1 ILE A 183      51.259  -4.137  46.126  1.00 35.92           C  
ANISOU 1023  CG1 ILE A 183     4228   4647   4772    422    113    393       C  
ATOM   1024  CG2 ILE A 183      51.520  -6.589  45.588  1.00 21.14           C  
ANISOU 1024  CG2 ILE A 183     2696   2561   2776    629    219    395       C  
ATOM   1025  CD1 ILE A 183      52.340  -3.700  45.159  1.00 32.24           C  
ANISOU 1025  CD1 ILE A 183     3683   4359   4209    523     44    445       C  
ATOM   1026  N   MET A 184      49.418  -3.975  48.901  1.00 19.34           N  
ANISOU 1026  N   MET A 184     2164   2341   2841    156    285    329       N  
ATOM   1027  CA  MET A 184      49.396  -2.916  49.904  1.00 23.35           C  
ANISOU 1027  CA  MET A 184     2567   2938   3365     87    281    344       C  
ATOM   1028  C   MET A 184      48.559  -3.284  51.127  1.00 37.58           C  
ANISOU 1028  C   MET A 184     4452   4619   5209     -6    410    315       C  
ATOM   1029  O   MET A 184      48.324  -2.448  52.000  1.00 36.05           O  
ANISOU 1029  O   MET A 184     4185   4474   5038    -76    422    304       O  
ATOM   1030  CB  MET A 184      48.887  -1.613  49.289  1.00 21.45           C  
ANISOU 1030  CB  MET A 184     2156   2753   3241    -10    178    275       C  
ATOM   1031  CG  MET A 184      49.812  -1.054  48.226  1.00 22.20           C  
ANISOU 1031  CG  MET A 184     2182   2981   3271     63     68    322       C  
ATOM   1032  SD  MET A 184      51.517  -1.004  48.809  1.00 42.48           S  
ANISOU 1032  SD  MET A 184     4740   5747   5653    186     66    452       S  
ATOM   1033  CE  MET A 184      52.394  -0.626  47.295  1.00 36.18           C  
ANISOU 1033  CE  MET A 184     3869   5080   4797    247    -22    483       C  
ATOM   1034  N   ILE A 185      48.121  -4.538  51.191  1.00 31.48           N  
ANISOU 1034  N   ILE A 185     3848   3679   4433    -14    516    301       N  
ATOM   1035  CA  ILE A 185      47.411  -5.044  52.366  1.00 34.23           C  
ANISOU 1035  CA  ILE A 185     4315   3898   4791   -107    672    289       C  
ATOM   1036  C   ILE A 185      48.258  -4.991  53.655  1.00 33.93           C  
ANISOU 1036  C   ILE A 185     4370   3933   4588     -6    713    402       C  
ATOM   1037  O   ILE A 185      47.732  -4.622  54.715  1.00 30.79           O  
ANISOU 1037  O   ILE A 185     3974   3519   4207    -99    795    385       O  
ATOM   1038  CB  ILE A 185      46.906  -6.490  52.130  1.00 30.17           C  
ANISOU 1038  CB  ILE A 185     4010   3170   4284   -142    788    262       C  
ATOM   1039  CG1 ILE A 185      45.744  -6.488  51.135  1.00 23.02           C  
ANISOU 1039  CG1 ILE A 185     2992   2191   3565   -300    763    113       C  
ATOM   1040  CG2 ILE A 185      46.468  -7.137  53.436  1.00 24.32           C  
ANISOU 1040  CG2 ILE A 185     3455   2291   3495   -214    973    290       C  
ATOM   1041  CD1 ILE A 185      45.247  -7.871  50.772  1.00 24.60           C  
ANISOU 1041  CD1 ILE A 185     3389   2178   3779   -365    864     65       C  
ATOM   1042  N   PRO A 186      49.561  -5.352  53.582  1.00 27.42           N  
ANISOU 1042  N   PRO A 186     3619   3203   3598    193    654    508       N  
ATOM   1043  CA  PRO A 186      50.391  -5.194  54.785  1.00 33.89           C  
ANISOU 1043  CA  PRO A 186     4494   4127   4254    301    658    601       C  
ATOM   1044  C   PRO A 186      50.355  -3.787  55.384  1.00 38.15           C  
ANISOU 1044  C   PRO A 186     4849   4816   4831    208    598    572       C  
ATOM   1045  O   PRO A 186      50.343  -3.645  56.611  1.00 43.92           O  
ANISOU 1045  O   PRO A 186     5650   5554   5482    202    655    599       O  
ATOM   1046  CB  PRO A 186      51.795  -5.522  54.279  1.00 35.10           C  
ANISOU 1046  CB  PRO A 186     4649   4426   4261    527    559    685       C  
ATOM   1047  CG  PRO A 186      51.562  -6.510  53.206  1.00 34.64           C  
ANISOU 1047  CG  PRO A 186     4700   4223   4240    565    587    662       C  
ATOM   1048  CD  PRO A 186      50.297  -6.070  52.521  1.00 28.03           C  
ANISOU 1048  CD  PRO A 186     3753   3287   3611    345    596    542       C  
ATOM   1049  N   GLN A 187      50.330  -2.770  54.527  1.00 31.33           N  
ANISOU 1049  N   GLN A 187     3778   4050   4073    142    487    518       N  
ATOM   1050  CA  GLN A 187      50.253  -1.389  54.984  1.00 25.00           C  
ANISOU 1050  CA  GLN A 187     2827   3359   3315     47    427    482       C  
ATOM   1051  C   GLN A 187      49.030  -1.183  55.869  1.00 31.95           C  
ANISOU 1051  C   GLN A 187     3737   4119   4282    -89    541    410       C  
ATOM   1052  O   GLN A 187      49.133  -0.634  56.964  1.00 41.54           O  
ANISOU 1052  O   GLN A 187     4963   5388   5432   -108    561    418       O  
ATOM   1053  CB  GLN A 187      50.208  -0.427  53.797  1.00 25.46           C  
ANISOU 1053  CB  GLN A 187     2709   3481   3482    -11    310    432       C  
ATOM   1054  CG  GLN A 187      50.366   1.027  54.193  1.00 25.15           C  
ANISOU 1054  CG  GLN A 187     2548   3550   3459    -90    236    408       C  
ATOM   1055  CD  GLN A 187      51.747   1.322  54.743  1.00 42.26           C  
ANISOU 1055  CD  GLN A 187     4689   5904   5463    -15    172    486       C  
ATOM   1056  OE1 GLN A 187      52.753   1.130  54.058  1.00 43.61           O  
ANISOU 1056  OE1 GLN A 187     4812   6197   5561     71    108    540       O  
ATOM   1057  NE2 GLN A 187      51.806   1.782  55.990  1.00 35.98           N  
ANISOU 1057  NE2 GLN A 187     3918   5147   4605    -46    190    481       N  
ATOM   1058  N   ALA A 188      47.877  -1.642  55.391  1.00 30.78           N  
ANISOU 1058  N   ALA A 188     3597   3822   4276   -186    618    329       N  
ATOM   1059  CA  ALA A 188      46.631  -1.539  56.142  1.00 29.47           C  
ANISOU 1059  CA  ALA A 188     3433   3556   4208   -326    747    244       C  
ATOM   1060  C   ALA A 188      46.695  -2.337  57.443  1.00 28.39           C  
ANISOU 1060  C   ALA A 188     3504   3346   3937   -309    903    309       C  
ATOM   1061  O   ALA A 188      46.159  -1.914  58.467  1.00 28.74           O  
ANISOU 1061  O   ALA A 188     3557   3383   3980   -384    994    276       O  
ATOM   1062  CB  ALA A 188      45.460  -2.009  55.292  1.00 20.98           C  
ANISOU 1062  CB  ALA A 188     2307   2359   3307   -435    793    136       C  
ATOM   1063  N   ILE A 189      47.351  -3.492  57.401  1.00 24.89           N  
ANISOU 1063  N   ILE A 189     3249   2841   3366   -196    935    402       N  
ATOM   1064  CA  ILE A 189      47.489  -4.318  58.595  1.00 35.57           C  
ANISOU 1064  CA  ILE A 189     4849   4106   4559   -151   1076    482       C  
ATOM   1065  C   ILE A 189      48.294  -3.617  59.693  1.00 38.11           C  
ANISOU 1065  C   ILE A 189     5180   4579   4721    -59   1021    544       C  
ATOM   1066  O   ILE A 189      47.888  -3.597  60.854  1.00 41.91           O  
ANISOU 1066  O   ILE A 189     5772   5015   5135   -107   1141    548       O  
ATOM   1067  CB  ILE A 189      48.158  -5.665  58.269  1.00 33.35           C  
ANISOU 1067  CB  ILE A 189     4793   3727   4153     -2   1096    576       C  
ATOM   1068  CG1 ILE A 189      47.268  -6.488  57.339  1.00 35.68           C  
ANISOU 1068  CG1 ILE A 189     5129   3836   4590   -119   1175    503       C  
ATOM   1069  CG2 ILE A 189      48.440  -6.443  59.543  1.00 37.89           C  
ANISOU 1069  CG2 ILE A 189     5657   4213   4525     86   1220    678       C  
ATOM   1070  CD1 ILE A 189      47.873  -7.811  56.932  1.00 38.91           C  
ANISOU 1070  CD1 ILE A 189     5784   4119   4882     27   1197    582       C  
ATOM   1071  N   VAL A 190      49.423  -3.026  59.316  1.00 29.73           N  
ANISOU 1071  N   VAL A 190     3996   3704   3594     61    843    584       N  
ATOM   1072  CA  VAL A 190      50.360  -2.470  60.291  1.00 23.69           C  
ANISOU 1072  CA  VAL A 190     3238   3106   2659    159    766    639       C  
ATOM   1073  C   VAL A 190      49.882  -1.164  60.952  1.00 26.19           C  
ANISOU 1073  C   VAL A 190     3433   3486   3033     25    756    559       C  
ATOM   1074  O   VAL A 190      50.160  -0.925  62.130  1.00 24.05           O  
ANISOU 1074  O   VAL A 190     3248   3271   2619     58    771    583       O  
ATOM   1075  CB  VAL A 190      51.740  -2.238  59.633  1.00 35.50           C  
ANISOU 1075  CB  VAL A 190     4609   4804   4076    304    585    690       C  
ATOM   1076  CG1 VAL A 190      52.722  -1.652  60.623  1.00 54.39           C  
ANISOU 1076  CG1 VAL A 190     6977   7393   6296    388    489    726       C  
ATOM   1077  CG2 VAL A 190      52.283  -3.547  59.098  1.00 44.75           C  
ANISOU 1077  CG2 VAL A 190     5920   5920   5161    478    598    768       C  
ATOM   1078  N   MET A 191      49.156  -0.331  60.209  1.00 29.83           N  
ANISOU 1078  N   MET A 191     3711   3933   3689   -109    726    461       N  
ATOM   1079  CA  MET A 191      48.702   0.960  60.735  1.00 26.69           C  
ANISOU 1079  CA  MET A 191     3207   3582   3349   -213    708    377       C  
ATOM   1080  C   MET A 191      47.840   0.797  61.981  1.00 31.41           C  
ANISOU 1080  C   MET A 191     3935   4086   3912   -276    882    345       C  
ATOM   1081  O   MET A 191      46.885   0.024  61.987  1.00 34.08           O  
ANISOU 1081  O   MET A 191     4345   4279   4325   -344   1041    319       O  
ATOM   1082  CB  MET A 191      47.917   1.740  59.674  1.00 27.17           C  
ANISOU 1082  CB  MET A 191     3086   3612   3625   -317    658    276       C  
ATOM   1083  CG  MET A 191      48.716   2.096  58.432  1.00 30.72           C  
ANISOU 1083  CG  MET A 191     3415   4154   4102   -275    494    303       C  
ATOM   1084  SD  MET A 191      50.293   2.883  58.813  1.00 41.67           S  
ANISOU 1084  SD  MET A 191     4759   5752   5321   -214    345    368       S  
ATOM   1085  CE  MET A 191      49.729   4.350  59.669  1.00 40.84           C  
ANISOU 1085  CE  MET A 191     4616   5645   5255   -332    338    271       C  
ATOM   1086  N   GLU A 192      48.190   1.523  63.040  1.00 30.55           N  
ANISOU 1086  N   GLU A 192     3859   4065   3683   -264    858    341       N  
ATOM   1087  CA  GLU A 192      47.431   1.475  64.287  1.00 34.06           C  
ANISOU 1087  CA  GLU A 192     4436   4438   4069   -316   1027    309       C  
ATOM   1088  C   GLU A 192      47.333   2.846  64.952  1.00 29.87           C  
ANISOU 1088  C   GLU A 192     3832   3988   3530   -366    977    225       C  
ATOM   1089  O   GLU A 192      48.192   3.713  64.760  1.00 37.09           O  
ANISOU 1089  O   GLU A 192     4655   5028   4408   -341    800    222       O  
ATOM   1090  CB  GLU A 192      48.059   0.477  65.269  1.00 44.52           C  
ANISOU 1090  CB  GLU A 192     6012   5751   5153   -199   1093    425       C  
ATOM   1091  CG  GLU A 192      48.060  -0.977  64.808  1.00 42.16           C  
ANISOU 1091  CG  GLU A 192     5859   5325   4836   -143   1179    510       C  
ATOM   1092  CD  GLU A 192      46.677  -1.602  64.803  1.00 45.73           C  
ANISOU 1092  CD  GLU A 192     6373   5583   5418   -293   1407    456       C  
ATOM   1093  OE1 GLU A 192      45.743  -1.005  65.376  1.00 42.49           O  
ANISOU 1093  OE1 GLU A 192     5913   5153   5079   -417   1522    363       O  
ATOM   1094  OE2 GLU A 192      46.525  -2.699  64.225  1.00 62.88           O  
ANISOU 1094  OE2 GLU A 192     8643   7628   7621   -292   1476    496       O  
ATOM   1095  N   CYS A 193      46.273   3.032  65.732  1.00 29.25           N  
ANISOU 1095  N   CYS A 193     3799   3832   3483   -445   1144    149       N  
ATOM   1096  CA  CYS A 193      46.114   4.228  66.545  1.00 34.34           C  
ANISOU 1096  CA  CYS A 193     4425   4531   4090   -475   1127     64       C  
ATOM   1097  C   CYS A 193      46.701   3.998  67.928  1.00 32.77           C  
ANISOU 1097  C   CYS A 193     4439   4379   3631   -407   1166    124       C  
ATOM   1098  O   CYS A 193      46.471   2.956  68.541  1.00 35.20           O  
ANISOU 1098  O   CYS A 193     4931   4611   3832   -383   1327    190       O  
ATOM   1099  CB  CYS A 193      44.640   4.622  66.662  1.00 42.01           C  
ANISOU 1099  CB  CYS A 193     5317   5416   5228   -575   1288    -67       C  
ATOM   1100  SG  CYS A 193      43.984   5.542  65.255  1.00 47.12           S  
ANISOU 1100  SG  CYS A 193     5700   6052   6151   -621   1172   -182       S  
ATOM   1101  N   SER A 194      47.463   4.970  68.415  1.00 35.69           N  
ANISOU 1101  N   SER A 194     4802   4868   3890   -381   1018     99       N  
ATOM   1102  CA  SER A 194      48.046   4.878  69.747  1.00 33.73           C  
ANISOU 1102  CA  SER A 194     4749   4687   3381   -308   1024    138       C  
ATOM   1103  C   SER A 194      47.744   6.131  70.563  1.00 30.66           C  
ANISOU 1103  C   SER A 194     4367   4325   2956   -364   1018     18       C  
ATOM   1104  O   SER A 194      47.862   7.259  70.071  1.00 32.14           O  
ANISOU 1104  O   SER A 194     4410   4549   3252   -422    887    -65       O  
ATOM   1105  CB  SER A 194      49.556   4.645  69.660  1.00 40.87           C  
ANISOU 1105  CB  SER A 194     5660   5746   4123   -193    818    231       C  
ATOM   1106  OG  SER A 194      50.173   5.587  68.801  1.00 68.07           O  
ANISOU 1106  OG  SER A 194     8898   9293   7673   -243    623    186       O  
ATOM   1107  N   THR A 195      47.340   5.913  71.810  1.00 41.06           N  
ANISOU 1107  N   THR A 195     5879   5610   4111   -345   1173     10       N  
ATOM   1108  CA  THR A 195      46.982   6.993  72.717  1.00 47.05           C  
ANISOU 1108  CA  THR A 195     6686   6383   4808   -383   1198   -109       C  
ATOM   1109  C   THR A 195      48.186   7.416  73.549  1.00 48.26           C  
ANISOU 1109  C   THR A 195     6949   6679   4708   -316   1018    -95       C  
ATOM   1110  O   THR A 195      48.878   6.583  74.134  1.00 61.53           O  
ANISOU 1110  O   THR A 195     8786   8419   6173   -211    999      9       O  
ATOM   1111  CB  THR A 195      45.826   6.581  73.651  1.00 54.04           C  
ANISOU 1111  CB  THR A 195     7723   7165   5645   -407   1485   -140       C  
ATOM   1112  OG1 THR A 195      44.685   6.210  72.865  1.00 66.45           O  
ANISOU 1112  OG1 THR A 195     9155   8629   7464   -489   1646   -176       O  
ATOM   1113  CG2 THR A 195      45.445   7.726  74.573  1.00 47.98           C  
ANISOU 1113  CG2 THR A 195     7008   6415   4808   -429   1517   -275       C  
ATOM   1114  N   VAL A 196      48.429   8.721  73.589  1.00 45.73           N  
ANISOU 1114  N   VAL A 196     6553   6411   4413   -375    880   -207       N  
ATOM   1115  CA  VAL A 196      49.571   9.291  74.287  1.00 55.71           C  
ANISOU 1115  CA  VAL A 196     7882   7823   5462   -350    684   -227       C  
ATOM   1116  C   VAL A 196      49.115  10.341  75.299  1.00 53.29           C  
ANISOU 1116  C   VAL A 196     7693   7488   5068   -393    727   -367       C  
ATOM   1117  O   VAL A 196      48.184  11.113  75.039  1.00 55.82           O  
ANISOU 1117  O   VAL A 196     7953   7697   5559   -461    813   -474       O  
ATOM   1118  CB  VAL A 196      50.570   9.933  73.301  1.00 58.17           C  
ANISOU 1118  CB  VAL A 196     7993   8241   5869   -409    441   -236       C  
ATOM   1119  CG1 VAL A 196      51.922  10.136  73.967  1.00 66.19           C  
ANISOU 1119  CG1 VAL A 196     9047   9455   6647   -375    233   -234       C  
ATOM   1120  CG2 VAL A 196      50.718   9.076  72.053  1.00 51.60           C  
ANISOU 1120  CG2 VAL A 196     7016   7400   5190   -382    432   -127       C  
ATOM   1121  N   PHE A 197      49.784  10.361  76.449  1.00 54.34           N  
ANISOU 1121  N   PHE A 197     7999   7725   4923   -334    658   -371       N  
ATOM   1122  CA  PHE A 197      49.439  11.259  77.547  1.00 47.66           C  
ANISOU 1122  CA  PHE A 197     7307   6859   3941   -357    698   -503       C  
ATOM   1123  C   PHE A 197      50.548  12.273  77.810  1.00 54.87           C  
ANISOU 1123  C   PHE A 197     8205   7907   4737   -412    433   -590       C  
ATOM   1124  O   PHE A 197      50.412  13.455  77.494  1.00 60.56           O  
ANISOU 1124  O   PHE A 197     8858   8574   5579   -522    366   -713       O  
ATOM   1125  CB  PHE A 197      49.155  10.455  78.817  1.00 44.61           C  
ANISOU 1125  CB  PHE A 197     7185   6469   3297   -251    866   -452       C  
ATOM   1126  CG  PHE A 197      47.944   9.572  78.717  1.00 57.04           C  
ANISOU 1126  CG  PHE A 197     8801   7897   4977   -242   1166   -394       C  
ATOM   1127  CD1 PHE A 197      47.999   8.370  78.026  1.00 51.09           C  
ANISOU 1127  CD1 PHE A 197     8001   7113   4298   -205   1218   -249       C  
ATOM   1128  CD2 PHE A 197      46.752   9.941  79.317  1.00 60.72           C  
ANISOU 1128  CD2 PHE A 197     9348   8259   5464   -277   1403   -494       C  
ATOM   1129  CE1 PHE A 197      46.885   7.559  77.931  1.00 52.44           C  
ANISOU 1129  CE1 PHE A 197     8209   7145   4569   -231   1497   -208       C  
ATOM   1130  CE2 PHE A 197      45.637   9.133  79.228  1.00 61.52           C  
ANISOU 1130  CE2 PHE A 197     9459   8246   5669   -297   1688   -455       C  
ATOM   1131  CZ  PHE A 197      45.703   7.940  78.532  1.00 57.80           C  
ANISOU 1131  CZ  PHE A 197     8945   7739   5278   -288   1734   -313       C  
ATOM   1132  N   LYS A 203      46.628  12.730  84.692  1.00 67.84           N  
ANISOU 1132  N   LYS A 203    11193   9271   5311   -140   1506   -953       N  
ATOM   1133  CA  LYS A 203      46.518  13.196  83.314  1.00 70.25           C  
ANISOU 1133  CA  LYS A 203    11192   9528   5970   -231   1409   -980       C  
ATOM   1134  C   LYS A 203      45.210  13.948  83.090  1.00 74.39           C  
ANISOU 1134  C   LYS A 203    11629   9923   6713   -272   1610  -1121       C  
ATOM   1135  O   LYS A 203      44.153  13.528  83.560  1.00 75.42           O  
ANISOU 1135  O   LYS A 203    11828   9995   6835   -245   1908  -1131       O  
ATOM   1136  CB  LYS A 203      46.624  12.022  82.336  1.00 65.98           C  
ANISOU 1136  CB  LYS A 203    10497   8984   5589   -229   1431   -805       C  
ATOM   1137  N   THR A 204      45.288  15.063  82.370  1.00 79.98           N  
ANISOU 1137  N   THR A 204    12188  10590   7612   -332   1450  -1233       N  
ATOM   1138  CA  THR A 204      44.108  15.864  82.069  1.00 85.26           C  
ANISOU 1138  CA  THR A 204    12765  11139   8492   -335   1599  -1375       C  
ATOM   1139  C   THR A 204      43.634  15.616  80.642  1.00 83.74           C  
ANISOU 1139  C   THR A 204    12288  10890   8640   -371   1609  -1323       C  
ATOM   1140  O   THR A 204      42.434  15.544  80.378  1.00 89.26           O  
ANISOU 1140  O   THR A 204    12875  11525   9516   -347   1823  -1375       O  
ATOM   1141  CB  THR A 204      44.378  17.370  82.257  1.00 87.20           C  
ANISOU 1141  CB  THR A 204    13086  11336   8709   -358   1430  -1550       C  
ATOM   1142  OG1 THR A 204      45.475  17.769  81.425  1.00 80.46           O  
ANISOU 1142  OG1 THR A 204    12128  10512   7930   -448   1131  -1516       O  
ATOM   1143  CG2 THR A 204      44.711  17.677  83.709  1.00 90.34           C  
ANISOU 1143  CG2 THR A 204    13777  11784   8766   -320   1433  -1632       C  
ATOM   1144  N   THR A 205      44.585  15.488  79.722  1.00 79.70           N  
ANISOU 1144  N   THR A 205    11652  10419   8211   -425   1375  -1229       N  
ATOM   1145  CA  THR A 205      44.263  15.265  78.318  1.00 82.75           C  
ANISOU 1145  CA  THR A 205    11786  10757   8897   -457   1353  -1176       C  
ATOM   1146  C   THR A 205      45.017  14.072  77.739  1.00 74.02           C  
ANISOU 1146  C   THR A 205    10601   9729   7792   -473   1279   -991       C  
ATOM   1147  O   THR A 205      45.889  13.493  78.386  1.00 77.25           O  
ANISOU 1147  O   THR A 205    11143  10236   7972   -448   1212   -905       O  
ATOM   1148  CB  THR A 205      44.579  16.508  77.458  1.00 82.08           C  
ANISOU 1148  CB  THR A 205    11610  10612   8967   -508   1139  -1261       C  
ATOM   1149  OG1 THR A 205      45.974  16.821  77.557  1.00 75.19           O  
ANISOU 1149  OG1 THR A 205    10800   9822   7945   -577    888  -1230       O  
ATOM   1150  CG2 THR A 205      43.760  17.705  77.919  1.00 88.43           C  
ANISOU 1150  CG2 THR A 205    12502  11309   9788   -465   1213  -1448       C  
ATOM   1151  N   LEU A 206      44.661  13.713  76.511  1.00 65.84           N  
ANISOU 1151  N   LEU A 206     9356   8652   7010   -496   1285   -939       N  
ATOM   1152  CA  LEU A 206      45.354  12.670  75.768  1.00 70.34           C  
ANISOU 1152  CA  LEU A 206     9836   9279   7612   -504   1202   -778       C  
ATOM   1153  C   LEU A 206      45.153  12.908  74.281  1.00 60.46           C  
ANISOU 1153  C   LEU A 206     8355   7976   6642   -545   1115   -776       C  
ATOM   1154  O   LEU A 206      44.104  13.403  73.867  1.00 55.61           O  
ANISOU 1154  O   LEU A 206     7642   7272   6215   -543   1207   -873       O  
ATOM   1155  CB  LEU A 206      44.852  11.277  76.170  1.00 75.95           C  
ANISOU 1155  CB  LEU A 206    10619   9978   8260   -468   1430   -676       C  
ATOM   1156  CG  LEU A 206      43.354  10.952  76.091  1.00 80.10           C  
ANISOU 1156  CG  LEU A 206    11071  10411   8952   -488   1711   -733       C  
ATOM   1157  CD1 LEU A 206      42.920  10.536  74.695  1.00 74.28           C  
ANISOU 1157  CD1 LEU A 206    10098   9630   8497   -527   1703   -701       C  
ATOM   1158  CD2 LEU A 206      43.002   9.862  77.086  1.00 89.88           C  
ANISOU 1158  CD2 LEU A 206    12501  11640  10010   -473   1956   -660       C  
ATOM   1159  N   PHE A 207      46.153  12.569  73.476  1.00 75.47           N  
ANISOU 1159  N   PHE A 207    10387  11666   6621   1673   -106   -904       N  
ATOM   1160  CA  PHE A 207      45.993  12.677  72.030  1.00 70.68           C  
ANISOU 1160  CA  PHE A 207     9712  10672   6471   1330    202   -597       C  
ATOM   1161  C   PHE A 207      46.273  11.334  71.375  1.00 60.86           C  
ANISOU 1161  C   PHE A 207     8463   9462   5200   1236     94   -217       C  
ATOM   1162  O   PHE A 207      46.985  10.511  71.930  1.00 56.81           O  
ANISOU 1162  O   PHE A 207     7919   9160   4506   1361   -214   -320       O  
ATOM   1163  CB  PHE A 207      46.901  13.771  71.448  1.00 77.99           C  
ANISOU 1163  CB  PHE A 207    10391  11186   8054   1112    327  -1083       C  
ATOM   1164  CG  PHE A 207      48.374  13.513  71.622  1.00 84.61           C  
ANISOU 1164  CG  PHE A 207    10983  11996   9168   1066      1  -1580       C  
ATOM   1165  CD1 PHE A 207      49.093  12.833  70.650  1.00 91.68           C  
ANISOU 1165  CD1 PHE A 207    11769  12720  10347    879      9  -1400       C  
ATOM   1166  CD2 PHE A 207      49.046  13.976  72.742  1.00 88.97           C  
ANISOU 1166  CD2 PHE A 207    11391  12706   9707   1238   -326  -2271       C  
ATOM   1167  CE1 PHE A 207      50.450  12.603  70.802  1.00101.18           C  
ANISOU 1167  CE1 PHE A 207    12717  13886  11843    839   -275  -1846       C  
ATOM   1168  CE2 PHE A 207      50.403  13.750  72.899  1.00101.50           C  
ANISOU 1168  CE2 PHE A 207    12695  14284  11587   1210   -659  -2773       C  
ATOM   1169  CZ  PHE A 207      51.106  13.065  71.927  1.00106.00           C  
ANISOU 1169  CZ  PHE A 207    13149  14654  12471    997   -616  -2535       C  
ATOM   1170  N   THR A 208      45.699  11.106  70.202  1.00 55.84           N  
ANISOU 1170  N   THR A 208     7849   8639   4727   1056    338    202       N  
ATOM   1171  CA  THR A 208      45.922   9.853  69.496  1.00 48.33           C  
ANISOU 1171  CA  THR A 208     6877   7691   3797    964    240    501       C  
ATOM   1172  C   THR A 208      46.682  10.098  68.201  1.00 43.19           C  
ANISOU 1172  C   THR A 208     6089   6733   3589    757    363    414       C  
ATOM   1173  O   THR A 208      46.353  11.011  67.445  1.00 39.36           O  
ANISOU 1173  O   THR A 208     5594   6038   3324    696    671    459       O  
ATOM   1174  CB  THR A 208      44.592   9.133  69.188  1.00 49.28           C  
ANISOU 1174  CB  THR A 208     7071   7821   3833    933    348    986       C  
ATOM   1175  OG1 THR A 208      43.947   8.776  70.417  1.00 64.37           O  
ANISOU 1175  OG1 THR A 208     9016   9812   5630   1038    271   1037       O  
ATOM   1176  CG2 THR A 208      44.837   7.872  68.372  1.00 40.61           C  
ANISOU 1176  CG2 THR A 208     5885   6595   2949    776    232   1134       C  
ATOM   1177  N   VAL A 209      47.711   9.293  67.952  1.00 46.45           N  
ANISOU 1177  N   VAL A 209     6402   7121   4125    697    164    325       N  
ATOM   1178  CA  VAL A 209      48.426   9.382  66.684  1.00 33.65           C  
ANISOU 1178  CA  VAL A 209     4670   5225   2892    552    317    313       C  
ATOM   1179  C   VAL A 209      48.254   8.099  65.880  1.00 31.36           C  
ANISOU 1179  C   VAL A 209     4428   4991   2498    525    240    643       C  
ATOM   1180  O   VAL A 209      48.048   7.022  66.443  1.00 45.16           O  
ANISOU 1180  O   VAL A 209     6220   6926   4012    576     17    782       O  
ATOM   1181  CB  VAL A 209      49.924   9.667  66.892  1.00 37.32           C  
ANISOU 1181  CB  VAL A 209     4916   5533   3732    489    198   -140       C  
ATOM   1182  CG1 VAL A 209      50.107  10.955  67.681  1.00 39.00           C  
ANISOU 1182  CG1 VAL A 209     5016   5652   4148    508    247   -585       C  
ATOM   1183  CG2 VAL A 209      50.602   8.504  67.596  1.00 43.95           C  
ANISOU 1183  CG2 VAL A 209     5720   6606   4371    559   -201   -221       C  
ATOM   1184  N   CYS A 210      48.319   8.225  64.559  1.00 37.23           N  
ANISOU 1184  N   CYS A 210     5156   5565   3425    486    454    769       N  
ATOM   1185  CA  CYS A 210      48.180   7.081  63.666  1.00 34.03           C  
ANISOU 1185  CA  CYS A 210     4777   5207   2946    487    369    985       C  
ATOM   1186  C   CYS A 210      49.535   6.730  63.070  1.00 39.57           C  
ANISOU 1186  C   CYS A 210     5374   5748   3914    442    344    841       C  
ATOM   1187  O   CYS A 210      50.133   7.539  62.360  1.00 48.67           O  
ANISOU 1187  O   CYS A 210     6466   6689   5338    458    615    775       O  
ATOM   1188  CB  CYS A 210      47.161   7.381  62.560  1.00 35.84           C  
ANISOU 1188  CB  CYS A 210     5079   5459   3078    579    586   1219       C  
ATOM   1189  SG  CYS A 210      46.989   6.103  61.281  1.00 46.85           S  
ANISOU 1189  SG  CYS A 210     6462   6910   4430    623    442   1316       S  
ATOM   1190  N   ASP A 211      50.028   5.530  63.362  1.00 32.18           N  
ANISOU 1190  N   ASP A 211     4405   4884   2939    410     71    827       N  
ATOM   1191  CA  ASP A 211      51.350   5.144  62.880  1.00 41.12           C  
ANISOU 1191  CA  ASP A 211     5425   5870   4330    375     37    691       C  
ATOM   1192  C   ASP A 211      51.516   3.632  62.762  1.00 43.60           C  
ANISOU 1192  C   ASP A 211     5746   6255   4564    372   -196    796       C  
ATOM   1193  O   ASP A 211      50.744   2.857  63.328  1.00 41.58           O  
ANISOU 1193  O   ASP A 211     5546   6139   4114    387   -343    948       O  
ATOM   1194  CB  ASP A 211      52.436   5.711  63.801  1.00 47.41           C  
ANISOU 1194  CB  ASP A 211     6056   6602   5354    334    -57    354       C  
ATOM   1195  CG  ASP A 211      53.783   5.851  63.106  1.00 62.64           C  
ANISOU 1195  CG  ASP A 211     7806   8279   7714    288     59    191       C  
ATOM   1196  OD1 ASP A 211      53.971   5.250  62.026  1.00 45.69           O  
ANISOU 1196  OD1 ASP A 211     5705   6057   5599    318    166    372       O  
ATOM   1197  OD2 ASP A 211      54.658   6.561  63.646  1.00 79.93           O  
ANISOU 1197  OD2 ASP A 211     9786  10342  10242    239     45   -147       O  
ATOM   1198  N   GLU A 212      52.537   3.228  62.015  1.00 39.83           N  
ANISOU 1198  N   GLU A 212     5196   5641   4297    365   -175    730       N  
ATOM   1199  CA  GLU A 212      52.880   1.824  61.858  1.00 35.93           C  
ANISOU 1199  CA  GLU A 212     4689   5159   3804    364   -367    790       C  
ATOM   1200  C   GLU A 212      53.252   1.196  63.193  1.00 37.18           C  
ANISOU 1200  C   GLU A 212     4791   5434   3903    373   -621    765       C  
ATOM   1201  O   GLU A 212      54.071   1.737  63.936  1.00 41.04           O  
ANISOU 1201  O   GLU A 212     5173   5951   4467    390   -703    555       O  
ATOM   1202  CB  GLU A 212      54.035   1.670  60.870  1.00 39.10           C  
ANISOU 1202  CB  GLU A 212     5019   5386   4451    385   -262    708       C  
ATOM   1203  CG  GLU A 212      53.725   2.187  59.480  1.00 50.57           C  
ANISOU 1203  CG  GLU A 212     6557   6773   5884    500     26    789       C  
ATOM   1204  CD  GLU A 212      54.946   2.214  58.585  1.00 56.71           C  
ANISOU 1204  CD  GLU A 212     7267   7364   6917    578    223    749       C  
ATOM   1205  OE1 GLU A 212      56.075   2.152  59.117  1.00 49.02           O  
ANISOU 1205  OE1 GLU A 212     6128   6269   6227    491    162    611       O  
ATOM   1206  OE2 GLU A 212      54.776   2.296  57.350  1.00 67.64           O  
ANISOU 1206  OE2 GLU A 212     8751   8745   8204    771    442    853       O  
ATOM   1207  N   ARG A 213      52.642   0.055  63.495  1.00 29.29           N  
ANISOU 1207  N   ARG A 213     3838   4500   2791    401   -730    968       N  
ATOM   1208  CA  ARG A 213      52.961  -0.677  64.712  1.00 30.81           C  
ANISOU 1208  CA  ARG A 213     4002   4817   2887    508   -904   1049       C  
ATOM   1209  C   ARG A 213      53.736  -1.935  64.354  1.00 37.77           C  
ANISOU 1209  C   ARG A 213     4816   5583   3950    519   -981   1104       C  
ATOM   1210  O   ARG A 213      53.193  -2.861  63.755  1.00 35.47           O  
ANISOU 1210  O   ARG A 213     4540   5165   3772    474   -932   1248       O  
ATOM   1211  CB  ARG A 213      51.692  -1.026  65.495  1.00 31.23           C  
ANISOU 1211  CB  ARG A 213     4142   4984   2742    585   -867   1325       C  
ATOM   1212  CG  ARG A 213      51.945  -1.408  66.945  1.00 33.63           C  
ANISOU 1212  CG  ARG A 213     4459   5499   2821    822   -977   1448       C  
ATOM   1213  CD  ARG A 213      50.656  -1.393  67.752  1.00 47.79           C  
ANISOU 1213  CD  ARG A 213     6357   7316   4484    885   -820   1641       C  
ATOM   1214  NE  ARG A 213      49.802  -2.538  67.450  1.00 62.30           N  
ANISOU 1214  NE  ARG A 213     8166   8954   6550    830   -665   1921       N  
ATOM   1215  CZ  ARG A 213      48.595  -2.730  67.975  1.00 69.36           C  
ANISOU 1215  CZ  ARG A 213     9081   9796   7477    855   -477   2105       C  
ATOM   1216  NH1 ARG A 213      48.092  -1.848  68.828  1.00 69.19           N  
ANISOU 1216  NH1 ARG A 213     9148   9903   7236    931   -421   2037       N  
ATOM   1217  NH2 ARG A 213      47.890  -3.804  67.644  1.00 70.86           N  
ANISOU 1217  NH2 ARG A 213     9163   9794   7968    812   -339   2371       N  
ATOM   1218  N   TRP A 214      55.013  -1.960  64.712  1.00 49.61           N  
ANISOU 1218  N   TRP A 214     6210   7116   5523    584  -1110    947       N  
ATOM   1219  CA  TRP A 214      55.861  -3.094  64.379  1.00 53.07           C  
ANISOU 1219  CA  TRP A 214     6576   7441   6147    613  -1168    997       C  
ATOM   1220  C   TRP A 214      56.212  -3.905  65.620  1.00 60.79           C  
ANISOU 1220  C   TRP A 214     7524   8592   6983    837  -1318   1159       C  
ATOM   1221  O   TRP A 214      56.412  -3.358  66.698  1.00 61.99           O  
ANISOU 1221  O   TRP A 214     7655   9001   6897   1007  -1457   1071       O  
ATOM   1222  CB  TRP A 214      57.133  -2.621  63.671  1.00 41.27           C  
ANISOU 1222  CB  TRP A 214     4951   5824   4904    551  -1158    734       C  
ATOM   1223  CG  TRP A 214      56.863  -2.006  62.339  1.00 42.87           C  
ANISOU 1223  CG  TRP A 214     5208   5854   5227    437   -932    674       C  
ATOM   1224  CD1 TRP A 214      56.859  -0.677  62.039  1.00 35.55           C  
ANISOU 1224  CD1 TRP A 214     4260   4884   4363    389   -770    532       C  
ATOM   1225  CD2 TRP A 214      56.540  -2.694  61.123  1.00 37.13           C  
ANISOU 1225  CD2 TRP A 214     4564   4991   4554    423   -823    756       C  
ATOM   1226  NE1 TRP A 214      56.561  -0.493  60.713  1.00 33.45           N  
ANISOU 1226  NE1 TRP A 214     4083   4492   4135    392   -537    591       N  
ATOM   1227  CE2 TRP A 214      56.359  -1.715  60.128  1.00 37.85           C  
ANISOU 1227  CE2 TRP A 214     4707   5024   4651    426   -602    691       C  
ATOM   1228  CE3 TRP A 214      56.386  -4.042  60.780  1.00 43.43           C  
ANISOU 1228  CE3 TRP A 214     5382   5706   5413    441   -883    854       C  
ATOM   1229  CZ2 TRP A 214      56.036  -2.039  58.812  1.00 36.17           C  
ANISOU 1229  CZ2 TRP A 214     4589   4756   4399    505   -482    709       C  
ATOM   1230  CZ3 TRP A 214      56.065  -4.360  59.471  1.00 39.41           C  
ANISOU 1230  CZ3 TRP A 214     4937   5101   4936    460   -793    795       C  
ATOM   1231  CH2 TRP A 214      55.892  -3.363  58.506  1.00 31.36           C  
ANISOU 1231  CH2 TRP A 214     3991   4107   3818    520   -616    719       C  
ATOM   1232  N   GLY A 215      56.281  -5.219  65.456  1.00 48.96           N  
ANISOU 1232  N   GLY A 215     6018   6959   5625    884  -1277   1389       N  
ATOM   1233  CA  GLY A 215      56.654  -6.105  66.542  1.00 56.11           C  
ANISOU 1233  CA  GLY A 215     6900   8005   6412   1165  -1345   1632       C  
ATOM   1234  C   GLY A 215      58.122  -6.484  66.498  1.00 61.53           C  
ANISOU 1234  C   GLY A 215     7446   8708   7224   1261  -1496   1494       C  
ATOM   1235  O   GLY A 215      58.476  -7.660  66.597  1.00 69.72           O  
ANISOU 1235  O   GLY A 215     8455   9654   8381   1394  -1453   1730       O  
ATOM   1236  N   GLY A 216      58.982  -5.485  66.336  1.00 56.90           N  
ANISOU 1236  N   GLY A 216     6740   8200   6678   1193  -1643   1112       N  
ATOM   1237  CA  GLY A 216      60.407  -5.723  66.206  1.00 61.50           C  
ANISOU 1237  CA  GLY A 216     7130   8771   7464   1255  -1781    930       C  
ATOM   1238  C   GLY A 216      61.092  -4.593  65.467  1.00 58.72           C  
ANISOU 1238  C   GLY A 216     6627   8292   7393   1044  -1773    533       C  
ATOM   1239  O   GLY A 216      60.439  -3.650  65.021  1.00 59.01           O  
ANISOU 1239  O   GLY A 216     6734   8245   7442    869  -1636    433       O  
ATOM   1240  N   GLU A 217      62.411  -4.688  65.338  1.00 55.95           N  
ANISOU 1240  N   GLU A 217     6046   7902   7310   1082  -1878    335       N  
ATOM   1241  CA  GLU A 217      63.194  -3.665  64.658  1.00 61.74           C  
ANISOU 1241  CA  GLU A 217     6569   8445   8446    905  -1797    -10       C  
ATOM   1242  C   GLU A 217      63.534  -4.078  63.231  1.00 60.99           C  
ANISOU 1242  C   GLU A 217     6508   8006   8658    770  -1510    109       C  
ATOM   1243  O   GLU A 217      63.930  -3.249  62.413  1.00 77.03           O  
ANISOU 1243  O   GLU A 217     8437   9815  11015    643  -1289    -44       O  
ATOM   1244  CB  GLU A 217      64.480  -3.375  65.432  1.00 70.85           C  
ANISOU 1244  CB  GLU A 217     7368   9760   9791   1042  -2091   -375       C  
ATOM   1245  CG  GLU A 217      64.292  -2.496  66.652  1.00 83.98           C  
ANISOU 1245  CG  GLU A 217     8930  11750  11230   1174  -2378   -702       C  
ATOM   1246  CD  GLU A 217      65.060  -1.196  66.538  1.00 95.28           C  
ANISOU 1246  CD  GLU A 217     9999  13025  13178   1016  -2400  -1242       C  
ATOM   1247  OE1 GLU A 217      65.176  -0.674  65.409  1.00 95.82           O  
ANISOU 1247  OE1 GLU A 217    10027  12688  13693    760  -2035  -1227       O  
ATOM   1248  OE2 GLU A 217      65.556  -0.703  67.574  1.00100.14           O  
ANISOU 1248  OE2 GLU A 217    10351  13917  13780   1184  -2766  -1692       O  
ATOM   1249  N   ILE A 218      63.373  -5.363  62.940  1.00 43.24           N  
ANISOU 1249  N   ILE A 218     4400   5705   6324    837  -1479    388       N  
ATOM   1250  CA  ILE A 218      63.760  -5.910  61.644  1.00 44.32           C  
ANISOU 1250  CA  ILE A 218     4576   5561   6703    780  -1252    459       C  
ATOM   1251  C   ILE A 218      62.650  -5.758  60.605  1.00 40.82           C  
ANISOU 1251  C   ILE A 218     4378   4995   6139    681  -1024    547       C  
ATOM   1252  O   ILE A 218      62.902  -5.393  59.449  1.00 48.20           O  
ANISOU 1252  O   ILE A 218     5338   5758   7219    663   -784    496       O  
ATOM   1253  CB  ILE A 218      64.137  -7.396  61.769  1.00 47.01           C  
ANISOU 1253  CB  ILE A 218     4926   5867   7067    912  -1323    658       C  
ATOM   1254  CG1 ILE A 218      65.077  -7.602  62.959  1.00 57.63           C  
ANISOU 1254  CG1 ILE A 218     6047   7438   8412   1104  -1592    612       C  
ATOM   1255  CG2 ILE A 218      64.767  -7.897  60.482  1.00 47.48           C  
ANISOU 1255  CG2 ILE A 218     4990   5653   7399    892  -1112    655       C  
ATOM   1256  CD1 ILE A 218      65.525  -9.031  63.146  1.00 67.59           C  
ANISOU 1256  CD1 ILE A 218     7304   8665   9713   1288  -1620    859       C  
ATOM   1257  N   TYR A 219      61.422  -6.039  61.030  1.00 40.30           N  
ANISOU 1257  N   TYR A 219     4476   5035   5801    665  -1090    686       N  
ATOM   1258  CA  TYR A 219      60.256  -5.963  60.155  1.00 39.45           C  
ANISOU 1258  CA  TYR A 219     4558   4864   5569    598   -948    726       C  
ATOM   1259  C   TYR A 219      60.083  -4.601  59.461  1.00 45.20           C  
ANISOU 1259  C   TYR A 219     5320   5582   6270    559   -756    609       C  
ATOM   1260  O   TYR A 219      59.882  -4.565  58.248  1.00 43.46           O  
ANISOU 1260  O   TYR A 219     5205   5275   6033    613   -574    597       O  
ATOM   1261  CB  TYR A 219      58.986  -6.318  60.937  1.00 44.66           C  
ANISOU 1261  CB  TYR A 219     5311   5634   6025    579  -1041    885       C  
ATOM   1262  CG  TYR A 219      58.979  -7.720  61.500  1.00 51.91           C  
ANISOU 1262  CG  TYR A 219     6204   6489   7032    656  -1109   1086       C  
ATOM   1263  CD1 TYR A 219      59.549  -7.996  62.736  1.00 68.89           C  
ANISOU 1263  CD1 TYR A 219     8271   8788   9116    807  -1231   1221       C  
ATOM   1264  CD2 TYR A 219      58.397  -8.769  60.798  1.00 52.44           C  
ANISOU 1264  CD2 TYR A 219     6309   6345   7271    619  -1039   1125       C  
ATOM   1265  CE1 TYR A 219      59.543  -9.277  63.256  1.00 80.56           C  
ANISOU 1265  CE1 TYR A 219     9732  10190  10688    941  -1212   1487       C  
ATOM   1266  CE2 TYR A 219      58.386 -10.054  61.310  1.00 64.02           C  
ANISOU 1266  CE2 TYR A 219     7721   7671   8933    689  -1022   1333       C  
ATOM   1267  CZ  TYR A 219      58.961 -10.301  62.540  1.00 81.45           C  
ANISOU 1267  CZ  TYR A 219     9872  10012  11062    860  -1075   1563       C  
ATOM   1268  OH  TYR A 219      58.955 -11.577  63.056  1.00 89.91           O  
ANISOU 1268  OH  TYR A 219    10896  10928  12337    993   -982   1850       O  
ATOM   1269  N   PRO A 220      60.160  -3.479  60.212  1.00 48.61           N  
ANISOU 1269  N   PRO A 220     5663   6107   6699    511   -777    516       N  
ATOM   1270  CA  PRO A 220      60.001  -2.201  59.503  1.00 40.71           C  
ANISOU 1270  CA  PRO A 220     4682   5027   5759    492   -508    451       C  
ATOM   1271  C   PRO A 220      61.105  -1.946  58.476  1.00 42.40           C  
ANISOU 1271  C   PRO A 220     4796   5019   6297    558   -231    414       C  
ATOM   1272  O   PRO A 220      60.828  -1.417  57.395  1.00 52.06           O  
ANISOU 1272  O   PRO A 220     6133   6162   7487    659     79    494       O  
ATOM   1273  CB  PRO A 220      60.056  -1.162  60.631  1.00 42.06           C  
ANISOU 1273  CB  PRO A 220     4716   5288   5977    422   -604    293       C  
ATOM   1274  CG  PRO A 220      60.756  -1.842  61.750  1.00 39.86           C  
ANISOU 1274  CG  PRO A 220     4288   5144   5713    464   -923    210       C  
ATOM   1275  CD  PRO A 220      60.331  -3.272  61.663  1.00 36.82           C  
ANISOU 1275  CD  PRO A 220     4053   4800   5135    524  -1018    449       C  
ATOM   1276  N   LYS A 221      62.334  -2.327  58.812  1.00 34.91           N  
ANISOU 1276  N   LYS A 221     5550   3933   3782    676   -461    789       N  
ATOM   1277  CA  LYS A 221      63.457  -2.178  57.893  1.00 38.26           C  
ANISOU 1277  CA  LYS A 221     5773   4474   4290    832   -537    762       C  
ATOM   1278  C   LYS A 221      63.205  -2.949  56.599  1.00 36.69           C  
ANISOU 1278  C   LYS A 221     5537   4262   4141    904   -499    726       C  
ATOM   1279  O   LYS A 221      63.339  -2.400  55.498  1.00 27.77           O  
ANISOU 1279  O   LYS A 221     4200   3254   3098    934   -446    692       O  
ATOM   1280  CB  LYS A 221      64.758  -2.652  58.547  1.00 34.37           C  
ANISOU 1280  CB  LYS A 221     5329   3982   3748    982   -715    787       C  
ATOM   1281  CG  LYS A 221      65.153  -1.870  59.793  1.00 31.80           C  
ANISOU 1281  CG  LYS A 221     5046   3678   3358    897   -784    826       C  
ATOM   1282  CD  LYS A 221      66.499  -2.337  60.331  1.00 34.31           C  
ANISOU 1282  CD  LYS A 221     5360   4047   3630   1056   -985    857       C  
ATOM   1283  CE  LYS A 221      66.791  -1.762  61.713  1.00 43.06           C  
ANISOU 1283  CE  LYS A 221     6587   5135   4640    945  -1080    903       C  
ATOM   1284  NZ  LYS A 221      66.927  -0.280  61.703  1.00 44.30           N  
ANISOU 1284  NZ  LYS A 221     6594   5420   4818    783  -1038    899       N  
ATOM   1285  N   MET A 222      62.826  -4.217  56.740  1.00 29.64           N  
ANISOU 1285  N   MET A 222     4886   3202   3172    914   -529    734       N  
ATOM   1286  CA  MET A 222      62.545  -5.056  55.579  1.00 29.83           C  
ANISOU 1286  CA  MET A 222     4958   3170   3205    960   -507    701       C  
ATOM   1287  C   MET A 222      61.397  -4.496  54.743  1.00 35.55           C  
ANISOU 1287  C   MET A 222     5542   3975   3992    791   -369    683       C  
ATOM   1288  O   MET A 222      61.503  -4.381  53.515  1.00 42.19           O  
ANISOU 1288  O   MET A 222     6247   4885   4898    850   -340    645       O  
ATOM   1289  CB  MET A 222      62.224  -6.486  56.017  1.00 41.27           C  
ANISOU 1289  CB  MET A 222     6774   4386   4519    945   -570    721       C  
ATOM   1290  CG  MET A 222      63.406  -7.221  56.630  1.00 59.89           C  
ANISOU 1290  CG  MET A 222     9305   6650   6801   1185   -728    735       C  
ATOM   1291  SD  MET A 222      63.032  -8.932  57.058  1.00 77.28           S  
ANISOU 1291  SD  MET A 222    12034   8521   8806   1178   -811    757       S  
ATOM   1292  CE  MET A 222      61.796  -8.707  58.334  1.00 72.29           C  
ANISOU 1292  CE  MET A 222    11547   7826   8093    819   -736    814       C  
ATOM   1293  N   TYR A 223      60.307  -4.135  55.414  1.00 33.34           N  
ANISOU 1293  N   TYR A 223     5287   3700   3679    594   -284    713       N  
ATOM   1294  CA  TYR A 223      59.129  -3.637  54.717  1.00 33.35           C  
ANISOU 1294  CA  TYR A 223     5141   3809   3723    453   -161    708       C  
ATOM   1295  C   TYR A 223      59.419  -2.362  53.945  1.00 32.26           C  
ANISOU 1295  C   TYR A 223     4736   3829   3693    532   -114    678       C  
ATOM   1296  O   TYR A 223      58.910  -2.173  52.845  1.00 31.95           O  
ANISOU 1296  O   TYR A 223     4574   3862   3702    510    -65    657       O  
ATOM   1297  CB  TYR A 223      57.974  -3.377  55.686  1.00 29.76           C  
ANISOU 1297  CB  TYR A 223     4720   3385   3201    268    -63    750       C  
ATOM   1298  CG  TYR A 223      56.751  -2.815  54.988  1.00 36.14           C  
ANISOU 1298  CG  TYR A 223     5328   4357   4047    161     58    751       C  
ATOM   1299  CD1 TYR A 223      55.876  -3.650  54.304  1.00 47.14           C  
ANISOU 1299  CD1 TYR A 223     6746   5762   5405      9     70    761       C  
ATOM   1300  CD2 TYR A 223      56.481  -1.451  54.995  1.00 33.94           C  
ANISOU 1300  CD2 TYR A 223     4854   4221   3820    216    147    746       C  
ATOM   1301  CE1 TYR A 223      54.763  -3.147  53.654  1.00 49.28           C  
ANISOU 1301  CE1 TYR A 223     6800   6220   5704    -81    161    770       C  
ATOM   1302  CE2 TYR A 223      55.369  -0.937  54.345  1.00 40.13           C  
ANISOU 1302  CE2 TYR A 223     5451   5169   4629    166    246    751       C  
ATOM   1303  CZ  TYR A 223      54.514  -1.792  53.677  1.00 48.14           C  
ANISOU 1303  CZ  TYR A 223     6440   6230   5619     20    249    766       C  
ATOM   1304  OH  TYR A 223      53.405  -1.293  53.029  1.00 48.59           O  
ANISOU 1304  OH  TYR A 223     6279   6489   5695    -26    328    779       O  
ATOM   1305  N   HIS A 224      60.221  -1.476  54.522  1.00 25.76           N  
ANISOU 1305  N   HIS A 224     3848   3050   2888    603   -140    680       N  
ATOM   1306  CA  HIS A 224      60.458  -0.193  53.877  1.00 36.83           C  
ANISOU 1306  CA  HIS A 224     5054   4579   4361    637    -95    659       C  
ATOM   1307  C   HIS A 224      61.515  -0.293  52.785  1.00 37.33           C  
ANISOU 1307  C   HIS A 224     5001   4698   4484    756   -151    624       C  
ATOM   1308  O   HIS A 224      61.477   0.466  51.808  1.00 30.33           O  
ANISOU 1308  O   HIS A 224     3972   3902   3648    759   -100    601       O  
ATOM   1309  CB  HIS A 224      60.831   0.859  54.915  1.00 28.22           C  
ANISOU 1309  CB  HIS A 224     3983   3506   3235    616   -100    678       C  
ATOM   1310  CG  HIS A 224      59.644   1.425  55.629  1.00 35.71           C  
ANISOU 1310  CG  HIS A 224     4991   4449   4127    531     13    699       C  
ATOM   1311  ND1 HIS A 224      58.889   2.456  55.112  1.00 33.93           N  
ANISOU 1311  ND1 HIS A 224     4667   4306   3919    533    118    689       N  
ATOM   1312  CD2 HIS A 224      59.059   1.082  56.801  1.00 38.34           C  
ANISOU 1312  CD2 HIS A 224     5474   4718   4374    460     46    731       C  
ATOM   1313  CE1 HIS A 224      57.902   2.736  55.944  1.00 32.99           C  
ANISOU 1313  CE1 HIS A 224     4614   4191   3729    494    216    712       C  
ATOM   1314  NE2 HIS A 224      57.983   1.917  56.977  1.00 32.29           N  
ANISOU 1314  NE2 HIS A 224     4672   4020   3576    433    183    737       N  
ATOM   1315  N   ILE A 225      62.445  -1.233  52.938  1.00 31.09           N  
ANISOU 1315  N   ILE A 225     4280   3860   3672    871   -250    622       N  
ATOM   1316  CA  ILE A 225      63.326  -1.574  51.828  1.00 25.87           C  
ANISOU 1316  CA  ILE A 225     3517   3264   3049   1016   -278    587       C  
ATOM   1317  C   ILE A 225      62.484  -2.055  50.647  1.00 34.70           C  
ANISOU 1317  C   ILE A 225     4665   4339   4182    987   -214    556       C  
ATOM   1318  O   ILE A 225      62.614  -1.546  49.526  1.00 29.50           O  
ANISOU 1318  O   ILE A 225     3865   3773   3572   1007   -166    526       O  
ATOM   1319  CB  ILE A 225      64.347  -2.659  52.208  1.00 33.11           C  
ANISOU 1319  CB  ILE A 225     4532   4132   3917   1200   -391    590       C  
ATOM   1320  CG1 ILE A 225      65.427  -2.080  53.118  1.00 28.02           C  
ANISOU 1320  CG1 ILE A 225     3782   3600   3264   1242   -479    621       C  
ATOM   1321  CG2 ILE A 225      64.993  -3.242  50.964  1.00 28.08           C  
ANISOU 1321  CG2 ILE A 225     3835   3540   3293   1382   -389    547       C  
ATOM   1322  CD1 ILE A 225      66.430  -3.109  53.585  1.00 35.74           C  
ANISOU 1322  CD1 ILE A 225     4837   4559   4184   1460   -608    635       C  
ATOM   1323  N   CYS A 226      61.606  -3.022  50.910  1.00 35.20           N  
ANISOU 1323  N   CYS A 226     4928   4260   4185    910   -218    568       N  
ATOM   1324  CA  CYS A 226      60.741  -3.570  49.868  1.00 26.09           C  
ANISOU 1324  CA  CYS A 226     3833   3062   3019    834   -181    548       C  
ATOM   1325  C   CYS A 226      59.859  -2.500  49.230  1.00 37.74           C  
ANISOU 1325  C   CYS A 226     5117   4668   4554    719    -93    548       C  
ATOM   1326  O   CYS A 226      59.709  -2.462  48.012  1.00 33.92           O  
ANISOU 1326  O   CYS A 226     4576   4220   4094    728    -72    518       O  
ATOM   1327  CB  CYS A 226      59.866  -4.690  50.431  1.00 28.98           C  
ANISOU 1327  CB  CYS A 226     4457   3271   3285    695   -206    576       C  
ATOM   1328  SG  CYS A 226      60.768  -6.198  50.838  1.00 46.87           S  
ANISOU 1328  SG  CYS A 226     7056   5316   5437    859   -325    570       S  
ATOM   1329  N   PHE A 227      59.280  -1.632  50.055  1.00 32.94           N  
ANISOU 1329  N   PHE A 227     4435   4124   3956    633    -43    580       N  
ATOM   1330  CA  PHE A 227      58.406  -0.573  49.561  1.00 31.30           C  
ANISOU 1330  CA  PHE A 227     4068   4039   3785    573     38    585       C  
ATOM   1331  C   PHE A 227      59.180   0.377  48.660  1.00 30.83           C  
ANISOU 1331  C   PHE A 227     3879   4054   3782    669     46    553       C  
ATOM   1332  O   PHE A 227      58.689   0.782  47.602  1.00 26.16           O  
ANISOU 1332  O   PHE A 227     3204   3523   3212    658     78    539       O  
ATOM   1333  CB  PHE A 227      57.769   0.201  50.719  1.00 31.92           C  
ANISOU 1333  CB  PHE A 227     4129   4161   3837    519     99    621       C  
ATOM   1334  CG  PHE A 227      56.618   1.074  50.303  1.00 23.45           C  
ANISOU 1334  CG  PHE A 227     2921   3217   2773    490    186    633       C  
ATOM   1335  CD1 PHE A 227      56.834   2.369  49.862  1.00 22.81           C  
ANISOU 1335  CD1 PHE A 227     2755   3191   2720    579    216    619       C  
ATOM   1336  CD2 PHE A 227      55.320   0.596  50.350  1.00 24.27           C  
ANISOU 1336  CD2 PHE A 227     2986   3396   2839    374    230    665       C  
ATOM   1337  CE1 PHE A 227      55.773   3.171  49.475  1.00 22.96           C  
ANISOU 1337  CE1 PHE A 227     2672   3321   2730    603    286    632       C  
ATOM   1338  CE2 PHE A 227      54.257   1.392  49.966  1.00 27.44           C  
ANISOU 1338  CE2 PHE A 227     3227   3958   3242    386    302    682       C  
ATOM   1339  CZ  PHE A 227      54.483   2.681  49.528  1.00 29.49           C  
ANISOU 1339  CZ  PHE A 227     3420   4254   3530    527    328    664       C  
ATOM   1340  N   PHE A 228      60.394   0.725  49.081  1.00 22.90           N  
ANISOU 1340  N   PHE A 228     2858   3055   2786    746      8    547       N  
ATOM   1341  CA  PHE A 228      61.246   1.595  48.281  1.00 22.55           C  
ANISOU 1341  CA  PHE A 228     2695   3100   2773    794     16    524       C  
ATOM   1342  C   PHE A 228      61.607   0.962  46.938  1.00 22.77           C  
ANISOU 1342  C   PHE A 228     2691   3143   2817    863     14    485       C  
ATOM   1343  O   PHE A 228      61.593   1.632  45.908  1.00 33.14           O  
ANISOU 1343  O   PHE A 228     3927   4519   4145    854     55    466       O  
ATOM   1344  CB  PHE A 228      62.521   1.954  49.042  1.00 29.60           C  
ANISOU 1344  CB  PHE A 228     3556   4037   3654    826    -39    535       C  
ATOM   1345  CG  PHE A 228      63.509   2.730  48.222  1.00 35.60           C  
ANISOU 1345  CG  PHE A 228     4182   4919   4426    833    -33    518       C  
ATOM   1346  CD1 PHE A 228      63.229   4.027  47.825  1.00 38.98           C  
ANISOU 1346  CD1 PHE A 228     4593   5378   4841    746     18    521       C  
ATOM   1347  CD2 PHE A 228      64.715   2.164  47.842  1.00 39.05           C  
ANISOU 1347  CD2 PHE A 228     4521   5450   4868    934    -72    503       C  
ATOM   1348  CE1 PHE A 228      64.132   4.746  47.065  1.00 41.06           C  
ANISOU 1348  CE1 PHE A 228     4761   5751   5091    707     27    511       C  
ATOM   1349  CE2 PHE A 228      65.623   2.878  47.083  1.00 40.20           C  
ANISOU 1349  CE2 PHE A 228     4517   5748   5009    911    -50    494       C  
ATOM   1350  CZ  PHE A 228      65.331   4.171  46.694  1.00 44.25           C  
ANISOU 1350  CZ  PHE A 228     5031   6278   5503    772     -2    499       C  
ATOM   1351  N   LEU A 229      61.931  -0.327  46.951  1.00 30.83           N  
ANISOU 1351  N   LEU A 229     3811   4088   3815    942    -32    472       N  
ATOM   1352  CA  LEU A 229      62.317  -1.024  45.727  1.00 31.53           C  
ANISOU 1352  CA  LEU A 229     3922   4167   3891   1037    -28    429       C  
ATOM   1353  C   LEU A 229      61.152  -1.178  44.755  1.00 38.36           C  
ANISOU 1353  C   LEU A 229     4840   4990   4746    938      2    418       C  
ATOM   1354  O   LEU A 229      61.293  -0.942  43.553  1.00 31.93           O  
ANISOU 1354  O   LEU A 229     3979   4219   3933    963     34    387       O  
ATOM   1355  CB  LEU A 229      62.888  -2.404  46.058  1.00 32.18           C  
ANISOU 1355  CB  LEU A 229     4167   4142   3920   1177    -90    418       C  
ATOM   1356  CG  LEU A 229      64.195  -2.432  46.848  1.00 37.41           C  
ANISOU 1356  CG  LEU A 229     4757   4877   4579   1328   -143    429       C  
ATOM   1357  CD1 LEU A 229      64.573  -3.864  47.199  1.00 39.92           C  
ANISOU 1357  CD1 LEU A 229     5292   5054   4820   1500   -215    422       C  
ATOM   1358  CD2 LEU A 229      65.307  -1.755  46.061  1.00 40.80           C  
ANISOU 1358  CD2 LEU A 229     4960   5506   5037   1419   -103    407       C  
ATOM   1359  N   VAL A 230      60.001  -1.578  45.286  1.00 41.10           N  
ANISOU 1359  N   VAL A 230     5276   5270   5068    810    -12    448       N  
ATOM   1360  CA  VAL A 230      58.831  -1.876  44.470  1.00 39.76           C  
ANISOU 1360  CA  VAL A 230     5146   5089   4872    684     -8    450       C  
ATOM   1361  C   VAL A 230      58.161  -0.616  43.934  1.00 37.50           C  
ANISOU 1361  C   VAL A 230     4684   4935   4628    635     38    462       C  
ATOM   1362  O   VAL A 230      57.853  -0.530  42.745  1.00 35.31           O  
ANISOU 1362  O   VAL A 230     4391   4684   4342    617     37    444       O  
ATOM   1363  CB  VAL A 230      57.790  -2.700  45.266  1.00 41.51           C  
ANISOU 1363  CB  VAL A 230     5491   5245   5036    523    -36    490       C  
ATOM   1364  CG1 VAL A 230      56.482  -2.807  44.495  1.00 34.73           C  
ANISOU 1364  CG1 VAL A 230     4602   4449   4147    349    -40    508       C  
ATOM   1365  CG2 VAL A 230      58.340  -4.083  45.588  1.00 42.43           C  
ANISOU 1365  CG2 VAL A 230     5870   5180   5073    565    -99    476       C  
ATOM   1366  N   THR A 231      57.945   0.364  44.806  1.00 36.56           N  
ANISOU 1366  N   THR A 231     4468   4886   4538    630     74    492       N  
ATOM   1367  CA  THR A 231      57.190   1.551  44.417  1.00 28.08           C  
ANISOU 1367  CA  THR A 231     3275   3917   3478    620    115    509       C  
ATOM   1368  C   THR A 231      58.059   2.637  43.797  1.00 25.03           C  
ANISOU 1368  C   THR A 231     2846   3556   3109    701    137    485       C  
ATOM   1369  O   THR A 231      57.543   3.638  43.307  1.00 25.90           O  
ANISOU 1369  O   THR A 231     2910   3720   3209    715    160    494       O  
ATOM   1370  CB  THR A 231      56.443   2.165  45.615  1.00 31.47           C  
ANISOU 1370  CB  THR A 231     3661   4399   3897    601    159    551       C  
ATOM   1371  OG1 THR A 231      57.386   2.752  46.521  1.00 35.05           O  
ANISOU 1371  OG1 THR A 231     4153   4808   4354    658    170    549       O  
ATOM   1372  CG2 THR A 231      55.632   1.103  46.340  1.00 44.48           C  
ANISOU 1372  CG2 THR A 231     5349   6041   5509    484    152    582       C  
ATOM   1373  N   TYR A 232      59.374   2.454  43.815  1.00 26.50           N  
ANISOU 1373  N   TYR A 232     3050   3716   3304    753    127    459       N  
ATOM   1374  CA  TYR A 232      60.248   3.494  43.290  1.00 33.10           C  
ANISOU 1374  CA  TYR A 232     3838   4603   4135    777    152    445       C  
ATOM   1375  C   TYR A 232      61.405   2.948  42.461  1.00 38.63           C  
ANISOU 1375  C   TYR A 232     4515   5331   4832    834    154    406       C  
ATOM   1376  O   TYR A 232      61.384   3.032  41.236  1.00 47.58           O  
ANISOU 1376  O   TYR A 232     5650   6482   5947    837    178    382       O  
ATOM   1377  CB  TYR A 232      60.793   4.355  44.433  1.00 30.85           C  
ANISOU 1377  CB  TYR A 232     3551   4331   3841    757    153    469       C  
ATOM   1378  CG  TYR A 232      61.463   5.630  43.967  1.00 33.53           C  
ANISOU 1378  CG  TYR A 232     3882   4715   4144    716    175    467       C  
ATOM   1379  CD1 TYR A 232      60.721   6.780  43.736  1.00 33.53           C  
ANISOU 1379  CD1 TYR A 232     3953   4688   4101    699    201    482       C  
ATOM   1380  CD2 TYR A 232      62.835   5.681  43.757  1.00 31.57           C  
ANISOU 1380  CD2 TYR A 232     3564   4547   3884    694    168    456       C  
ATOM   1381  CE1 TYR A 232      61.326   7.947  43.308  1.00 35.81           C  
ANISOU 1381  CE1 TYR A 232     4300   4981   4324    636    214    484       C  
ATOM   1382  CE2 TYR A 232      63.449   6.843  43.330  1.00 33.39           C  
ANISOU 1382  CE2 TYR A 232     3802   4828   4057    599    188    462       C  
ATOM   1383  CZ  TYR A 232      62.690   7.974  43.107  1.00 40.85           C  
ANISOU 1383  CZ  TYR A 232     4875   5698   4948    557    208    475       C  
ATOM   1384  OH  TYR A 232      63.298   9.135  42.681  1.00 39.28           O  
ANISOU 1384  OH  TYR A 232     4748   5514   4661    438    221    484       O  
ATOM   1385  N   MET A 233      62.402   2.383  43.134  1.00 27.42           N  
ANISOU 1385  N   MET A 233     3073   3927   3417    895    131    403       N  
ATOM   1386  CA  MET A 233      63.692   2.102  42.510  1.00 30.61           C  
ANISOU 1386  CA  MET A 233     3402   4422   3808    984    149    373       C  
ATOM   1387  C   MET A 233      63.638   1.198  41.274  1.00 35.54           C  
ANISOU 1387  C   MET A 233     4092   5009   4404   1069    174    328       C  
ATOM   1388  O   MET A 233      64.042   1.618  40.190  1.00 47.83           O  
ANISOU 1388  O   MET A 233     5600   6639   5934   1070    230    305       O  
ATOM   1389  CB  MET A 233      64.643   1.488  43.536  1.00 30.12           C  
ANISOU 1389  CB  MET A 233     3300   4396   3747   1079     99    384       C  
ATOM   1390  CG  MET A 233      66.115   1.688  43.201  1.00 41.13           C  
ANISOU 1390  CG  MET A 233     4522   5982   5123   1149    119    375       C  
ATOM   1391  SD  MET A 233      66.620   3.425  43.240  1.00 61.33           S  
ANISOU 1391  SD  MET A 233     6953   8688   7663    944    143    408       S  
ATOM   1392  CE  MET A 233      66.555   3.885  41.507  1.00 63.38           C  
ANISOU 1392  CE  MET A 233     7202   8991   7887    904    242    373       C  
ATOM   1393  N   ALA A 234      63.154  -0.032  41.432  1.00 32.52           N  
ANISOU 1393  N   ALA A 234     3855   4497   4003   1124    134    317       N  
ATOM   1394  CA  ALA A 234      63.180  -1.007  40.336  1.00 36.16           C  
ANISOU 1394  CA  ALA A 234     4446   4886   4406   1211    149    271       C  
ATOM   1395  C   ALA A 234      62.405  -0.556  39.082  1.00 44.38           C  
ANISOU 1395  C   ALA A 234     5517   5918   5426   1108    176    257       C  
ATOM   1396  O   ALA A 234      62.967  -0.564  37.975  1.00 52.19           O  
ANISOU 1396  O   ALA A 234     6512   6946   6371   1175    231    218       O  
ATOM   1397  CB  ALA A 234      62.663  -2.367  40.825  1.00 26.49           C  
ANISOU 1397  CB  ALA A 234     3444   3484   3135   1237     83    270       C  
ATOM   1398  N   PRO A 235      61.127  -0.151  39.238  1.00 38.48           N  
ANISOU 1398  N   PRO A 235     4781   5139   4700    958    140    291       N  
ATOM   1399  CA  PRO A 235      60.412   0.297  38.037  1.00 38.93           C  
ANISOU 1399  CA  PRO A 235     4857   5206   4728    880    145    285       C  
ATOM   1400  C   PRO A 235      61.020   1.556  37.424  1.00 47.60           C  
ANISOU 1400  C   PRO A 235     5848   6408   5829    887    207    280       C  
ATOM   1401  O   PRO A 235      60.943   1.737  36.210  1.00 53.19           O  
ANISOU 1401  O   PRO A 235     6606   7117   6486    873    227    258       O  
ATOM   1402  CB  PRO A 235      59.001   0.575  38.555  1.00 29.84           C  
ANISOU 1402  CB  PRO A 235     3678   4059   3600    752     94    334       C  
ATOM   1403  CG  PRO A 235      59.195   0.869  40.001  1.00 22.79           C  
ANISOU 1403  CG  PRO A 235     2711   3189   2758    766    102    365       C  
ATOM   1404  CD  PRO A 235      60.278  -0.043  40.439  1.00 32.48           C  
ANISOU 1404  CD  PRO A 235     4003   4361   3976    867    100    339       C  
ATOM   1405  N   LEU A 236      61.619   2.408  38.252  1.00 44.46           N  
ANISOU 1405  N   LEU A 236     5338   6086   5469    885    230    304       N  
ATOM   1406  CA  LEU A 236      62.274   3.611  37.754  1.00 41.57           C  
ANISOU 1406  CA  LEU A 236     4908   5809   5078    845    283    306       C  
ATOM   1407  C   LEU A 236      63.476   3.242  36.895  1.00 45.30           C  
ANISOU 1407  C   LEU A 236     5346   6363   5505    913    352    264       C  
ATOM   1408  O   LEU A 236      63.656   3.780  35.803  1.00 45.80           O  
ANISOU 1408  O   LEU A 236     5431   6461   5510    871    403    250       O  
ATOM   1409  CB  LEU A 236      62.710   4.514  38.907  1.00 48.02           C  
ANISOU 1409  CB  LEU A 236     5650   6677   5918    796    280    342       C  
ATOM   1410  CG  LEU A 236      62.703   6.014  38.616  1.00 52.43           C  
ANISOU 1410  CG  LEU A 236     6240   7256   6427    693    301    365       C  
ATOM   1411  CD1 LEU A 236      61.281   6.492  38.367  1.00 55.63           C  
ANISOU 1411  CD1 LEU A 236     6741   7575   6822    694    269    384       C  
ATOM   1412  CD2 LEU A 236      63.341   6.786  39.758  1.00 49.93           C  
ANISOU 1412  CD2 LEU A 236     5891   6976   6102    622    291    396       C  
ATOM   1413  N   CYS A 237      64.294   2.321  37.394  1.00 30.48           N  
ANISOU 1413  N   CYS A 237     3419   4522   3639   1034    358    247       N  
ATOM   1414  CA  CYS A 237      65.450   1.833  36.650  1.00 35.44           C  
ANISOU 1414  CA  CYS A 237     3992   5260   4215   1159    436    206       C  
ATOM   1415  C   CYS A 237      65.031   1.233  35.315  1.00 33.41           C  
ANISOU 1415  C   CYS A 237     3899   4909   3888   1204    470    160       C  
ATOM   1416  O   CYS A 237      65.574   1.584  34.259  1.00 39.95           O  
ANISOU 1416  O   CYS A 237     4704   5824   4649   1203    557    135       O  
ATOM   1417  CB  CYS A 237      66.213   0.793  37.468  1.00 47.36           C  
ANISOU 1417  CB  CYS A 237     5457   6802   5737   1343    416    198       C  
ATOM   1418  SG  CYS A 237      66.972   1.441  38.964  1.00 64.52           S  
ANISOU 1418  SG  CYS A 237     7427   9122   7967   1295    368    252       S  
ATOM   1419  N   LEU A 238      64.055   0.332  35.372  1.00 26.64           N  
ANISOU 1419  N   LEU A 238     3220   3874   3028   1216    397    151       N  
ATOM   1420  CA  LEU A 238      63.562  -0.327  34.167  1.00 35.18           C  
ANISOU 1420  CA  LEU A 238     4504   4841   4023   1228    401    110       C  
ATOM   1421  C   LEU A 238      63.030   0.679  33.147  1.00 32.23           C  
ANISOU 1421  C   LEU A 238     4137   4489   3620   1088    414    119       C  
ATOM   1422  O   LEU A 238      63.344   0.595  31.958  1.00 36.58           O  
ANISOU 1422  O   LEU A 238     4775   5041   4081   1117    477     80       O  
ATOM   1423  CB  LEU A 238      62.480  -1.345  34.527  1.00 33.71           C  
ANISOU 1423  CB  LEU A 238     4511   4471   3826   1184    296    116       C  
ATOM   1424  CG  LEU A 238      63.021  -2.539  35.318  1.00 45.37           C  
ANISOU 1424  CG  LEU A 238     6086   5868   5283   1344    278     99       C  
ATOM   1425  CD1 LEU A 238      61.908  -3.499  35.713  1.00 52.02           C  
ANISOU 1425  CD1 LEU A 238     7153   6520   6090   1235    171    115       C  
ATOM   1426  CD2 LEU A 238      64.096  -3.254  34.508  1.00 35.81           C  
ANISOU 1426  CD2 LEU A 238     4975   4660   3973   1574    365     36       C  
ATOM   1427  N   MET A 239      62.241   1.637  33.620  1.00 31.09           N  
ANISOU 1427  N   MET A 239     3921   4357   3535    956    358    170       N  
ATOM   1428  CA  MET A 239      61.678   2.662  32.748  1.00 28.09           C  
ANISOU 1428  CA  MET A 239     3571   3985   3116    852    350    187       C  
ATOM   1429  C   MET A 239      62.756   3.559  32.152  1.00 35.44           C  
ANISOU 1429  C   MET A 239     4444   5025   3995    836    455    177       C  
ATOM   1430  O   MET A 239      62.626   4.021  31.021  1.00 47.64           O  
ANISOU 1430  O   MET A 239     6085   6558   5458    783    477    167       O  
ATOM   1431  CB  MET A 239      60.659   3.512  33.504  1.00 29.82           C  
ANISOU 1431  CB  MET A 239     3733   4201   3394    773    275    245       C  
ATOM   1432  CG  MET A 239      59.293   2.871  33.629  1.00 24.04           C  
ANISOU 1432  CG  MET A 239     3051   3408   2676    730    173    266       C  
ATOM   1433  SD  MET A 239      58.101   4.006  34.354  1.00 47.94           S  
ANISOU 1433  SD  MET A 239     5979   6487   5747    693    114    334       S  
ATOM   1434  CE  MET A 239      58.559   3.917  36.086  1.00 44.86           C  
ANISOU 1434  CE  MET A 239     5489   6114   5441    724    145    350       C  
ATOM   1435  N   VAL A 240      63.814   3.809  32.916  1.00 37.12           N  
ANISOU 1435  N   VAL A 240     4504   5358   4241    859    511    184       N  
ATOM   1436  CA  VAL A 240      64.920   4.623  32.427  1.00 31.17           C  
ANISOU 1436  CA  VAL A 240     3667   4753   3423    798    614    183       C  
ATOM   1437  C   VAL A 240      65.647   3.894  31.304  1.00 34.97           C  
ANISOU 1437  C   VAL A 240     4175   5295   3816    898    720    128       C  
ATOM   1438  O   VAL A 240      65.908   4.475  30.248  1.00 39.26           O  
ANISOU 1438  O   VAL A 240     4773   5881   4263    818    794    119       O  
ATOM   1439  CB  VAL A 240      65.911   4.980  33.555  1.00 33.30           C  
ANISOU 1439  CB  VAL A 240     3740   5176   3738    775    632    211       C  
ATOM   1440  CG1 VAL A 240      67.250   5.410  32.979  1.00 32.72           C  
ANISOU 1440  CG1 VAL A 240     3532   5320   3580    719    753    205       C  
ATOM   1441  CG2 VAL A 240      65.330   6.078  34.436  1.00 28.66           C  
ANISOU 1441  CG2 VAL A 240     3180   4527   3184    640    557    264       C  
ATOM   1442  N   LEU A 241      65.956   2.619  31.528  1.00 40.63           N  
ANISOU 1442  N   LEU A 241     4890   6000   4547   1084    730     90       N  
ATOM   1443  CA  LEU A 241      66.580   1.795  30.491  1.00 41.52           C  
ANISOU 1443  CA  LEU A 241     5076   6143   4555   1236    836     29       C  
ATOM   1444  C   LEU A 241      65.728   1.762  29.220  1.00 41.61           C  
ANISOU 1444  C   LEU A 241     5336   5997   4477   1168    822      4       C  
ATOM   1445  O   LEU A 241      66.223   1.992  28.105  1.00 45.56           O  
ANISOU 1445  O   LEU A 241     5884   6563   4865   1161    933    -24       O  
ATOM   1446  CB  LEU A 241      66.807   0.373  31.003  1.00 45.83           C  
ANISOU 1446  CB  LEU A 241     5677   6627   5112   1472    818     -6       C  
ATOM   1447  CG  LEU A 241      67.734   0.220  32.210  1.00 52.74           C  
ANISOU 1447  CG  LEU A 241     6320   7664   6056   1589    821     16       C  
ATOM   1448  CD1 LEU A 241      67.833  -1.239  32.624  1.00 56.39           C  
ANISOU 1448  CD1 LEU A 241     6919   8007   6498   1846    786    -19       C  
ATOM   1449  CD2 LEU A 241      69.110   0.788  31.903  1.00 54.64           C  
ANISOU 1449  CD2 LEU A 241     6296   8215   6249   1617    960     18       C  
ATOM   1450  N   ALA A 242      64.441   1.484  29.406  1.00 40.55           N  
ANISOU 1450  N   ALA A 242     5349   5676   4381   1103    683     20       N  
ATOM   1451  CA  ALA A 242      63.493   1.407  28.301  1.00 32.97           C  
ANISOU 1451  CA  ALA A 242     4615   4576   3337   1020    626      8       C  
ATOM   1452  C   ALA A 242      63.445   2.711  27.517  1.00 36.99           C  
ANISOU 1452  C   ALA A 242     5121   5140   3792    881    655     33       C  
ATOM   1453  O   ALA A 242      63.477   2.704  26.288  1.00 39.96           O  
ANISOU 1453  O   ALA A 242     5657   5481   4046    862    700      3       O  
ATOM   1454  CB  ALA A 242      62.106   1.054  28.819  1.00 28.55           C  
ANISOU 1454  CB  ALA A 242     4130   3881   2836    937    460     42       C  
ATOM   1455  N   TYR A 243      63.383   3.829  28.232  1.00 29.35           N  
ANISOU 1455  N   TYR A 243     4014   4241   2897    785    629     87       N  
ATOM   1456  CA  TYR A 243      63.239   5.130  27.593  1.00 28.47           C  
ANISOU 1456  CA  TYR A 243     3962   4139   2716    650    634    119       C  
ATOM   1457  C   TYR A 243      64.526   5.637  26.955  1.00 40.47           C  
ANISOU 1457  C   TYR A 243     5442   5800   4134    600    795    102       C  
ATOM   1458  O   TYR A 243      64.474   6.453  26.038  1.00 42.95           O  
ANISOU 1458  O   TYR A 243     5890   6094   4337    487    819    113       O  
ATOM   1459  CB  TYR A 243      62.721   6.159  28.598  1.00 30.32           C  
ANISOU 1459  CB  TYR A 243     4123   4367   3029    578    552    181       C  
ATOM   1460  CG  TYR A 243      61.215   6.214  28.673  1.00 30.77           C  
ANISOU 1460  CG  TYR A 243     4260   4313   3120    583    401    213       C  
ATOM   1461  CD1 TYR A 243      60.443   6.180  27.518  1.00 36.55           C  
ANISOU 1461  CD1 TYR A 243     5156   4969   3763    562    335    211       C  
ATOM   1462  CD2 TYR A 243      60.563   6.289  29.895  1.00 29.96           C  
ANISOU 1462  CD2 TYR A 243     4053   4206   3124    610    326    250       C  
ATOM   1463  CE1 TYR A 243      59.065   6.227  27.578  1.00 26.87           C  
ANISOU 1463  CE1 TYR A 243     3952   3699   2559    567    188    250       C  
ATOM   1464  CE2 TYR A 243      59.183   6.335  29.966  1.00 35.94           C  
ANISOU 1464  CE2 TYR A 243     4833   4921   3902    622    202    286       C  
ATOM   1465  CZ  TYR A 243      58.441   6.303  28.803  1.00 32.95           C  
ANISOU 1465  CZ  TYR A 243     4581   4500   3439    601    129    288       C  
ATOM   1466  OH  TYR A 243      57.069   6.348  28.868  1.00 40.45           O  
ANISOU 1466  OH  TYR A 243     5505   5463   4403    614     -3    332       O  
ATOM   1467  N   LEU A 244      65.680   5.175  27.429  1.00 39.31           N  
ANISOU 1467  N   LEU A 244     5107   5816   4012    680    904     80       N  
ATOM   1468  CA  LEU A 244      66.928   5.579  26.789  1.00 43.63           C  
ANISOU 1468  CA  LEU A 244     5567   6561   4448    625   1072     68       C  
ATOM   1469  C   LEU A 244      67.143   4.748  25.524  1.00 44.44           C  
ANISOU 1469  C   LEU A 244     5810   6646   4428    742   1176      3       C  
ATOM   1470  O   LEU A 244      67.647   5.257  24.514  1.00 44.08           O  
ANISOU 1470  O   LEU A 244     5823   6680   4244    648   1294     -5       O  
ATOM   1471  CB  LEU A 244      68.121   5.465  27.750  1.00 44.16           C  
ANISOU 1471  CB  LEU A 244     5337   6870   4574    670   1147     79       C  
ATOM   1472  CG  LEU A 244      68.503   4.166  28.462  1.00 54.77           C  
ANISOU 1472  CG  LEU A 244     6550   8263   5997    924   1148     45       C  
ATOM   1473  CD1 LEU A 244      69.328   3.242  27.575  1.00 73.31           C  
ANISOU 1473  CD1 LEU A 244     8889  10726   8238   1130   1304    -19       C  
ATOM   1474  CD2 LEU A 244      69.252   4.480  29.749  1.00 49.61           C  
ANISOU 1474  CD2 LEU A 244     5623   7797   5429    896   1130     89       C  
ATOM   1475  N   GLN A 245      66.741   3.479  25.567  1.00 39.70           N  
ANISOU 1475  N   GLN A 245     5305   5923   3856    933   1131    -42       N  
ATOM   1476  CA  GLN A 245      66.750   2.666  24.352  1.00 35.11           C  
ANISOU 1476  CA  GLN A 245     4946   5258   3134   1041   1203   -106       C  
ATOM   1477  C   GLN A 245      65.784   3.251  23.321  1.00 34.77           C  
ANISOU 1477  C   GLN A 245     5158   5051   3002    873   1123    -93       C  
ATOM   1478  O   GLN A 245      66.098   3.330  22.128  1.00 46.85           O  
ANISOU 1478  O   GLN A 245     6839   6587   4373    853   1228   -125       O  
ATOM   1479  CB  GLN A 245      66.386   1.216  24.664  1.00 36.51           C  
ANISOU 1479  CB  GLN A 245     5254   5283   3336   1243   1138   -151       C  
ATOM   1480  CG  GLN A 245      67.389   0.512  25.559  1.00 52.65           C  
ANISOU 1480  CG  GLN A 245     7097   7474   5435   1467   1216   -169       C  
ATOM   1481  CD  GLN A 245      66.915  -0.856  25.999  1.00 65.63           C  
ANISOU 1481  CD  GLN A 245     8933   8914   7091   1643   1122   -203       C  
ATOM   1482  OE1 GLN A 245      66.421  -1.644  25.193  1.00 68.05           O  
ANISOU 1482  OE1 GLN A 245     9555   9021   7280   1690   1100   -250       O  
ATOM   1483  NE2 GLN A 245      67.054  -1.143  27.288  1.00 73.38           N  
ANISOU 1483  NE2 GLN A 245     9760   9928   8195   1719   1057   -176       N  
ATOM   1484  N   ILE A 246      64.612   3.667  23.797  1.00 33.06           N  
ANISOU 1484  N   ILE A 246     4983   4704   2876    768    938    -43       N  
ATOM   1485  CA  ILE A 246      63.614   4.325  22.961  1.00 32.84           C  
ANISOU 1485  CA  ILE A 246     5159   4546   2773    631    827    -15       C  
ATOM   1486  C   ILE A 246      64.168   5.617  22.365  1.00 41.00           C  
ANISOU 1486  C   ILE A 246     6212   5662   3705    489    919     12       C  
ATOM   1487  O   ILE A 246      63.975   5.891  21.184  1.00 44.79           O  
ANISOU 1487  O   ILE A 246     6911   6071   4037    420    929      3       O  
ATOM   1488  CB  ILE A 246      62.323   4.637  23.755  1.00 36.81           C  
ANISOU 1488  CB  ILE A 246     5628   4961   3398    581    625     44       C  
ATOM   1489  CG1 ILE A 246      61.508   3.363  23.981  1.00 40.89           C  
ANISOU 1489  CG1 ILE A 246     6213   5367   3955    644    510     25       C  
ATOM   1490  CG2 ILE A 246      61.464   5.660  23.024  1.00 34.35           C  
ANISOU 1490  CG2 ILE A 246     5469   4575   3008    468    518     90       C  
ATOM   1491  CD1 ILE A 246      60.282   3.572  24.850  1.00 34.41           C  
ANISOU 1491  CD1 ILE A 246     5301   4521   3251    594    335     86       C  
ATOM   1492  N   PHE A 247      64.857   6.403  23.185  1.00 36.40           N  
ANISOU 1492  N   PHE A 247     5428   5218   3182    421    977     48       N  
ATOM   1493  CA  PHE A 247      65.480   7.638  22.720  1.00 37.57           C  
ANISOU 1493  CA  PHE A 247     5614   5448   3213    238   1067     80       C  
ATOM   1494  C   PHE A 247      66.460   7.355  21.591  1.00 41.80           C  
ANISOU 1494  C   PHE A 247     6195   6103   3584    228   1264     32       C  
ATOM   1495  O   PHE A 247      66.422   8.008  20.545  1.00 51.21           O  
ANISOU 1495  O   PHE A 247     7598   7244   4614     95   1299     41       O  
ATOM   1496  CB  PHE A 247      66.197   8.356  23.870  1.00 40.20           C  
ANISOU 1496  CB  PHE A 247     5722   5932   3622    144   1100    123       C  
ATOM   1497  CG  PHE A 247      67.089   9.483  23.419  1.00 51.88           C  
ANISOU 1497  CG  PHE A 247     7229   7533   4951    -89   1219    154       C  
ATOM   1498  CD1 PHE A 247      66.569  10.745  23.182  1.00 56.47           C  
ANISOU 1498  CD1 PHE A 247     8051   7969   5438   -264   1135    207       C  
ATOM   1499  CD2 PHE A 247      68.450   9.282  23.235  1.00 58.18           C  
ANISOU 1499  CD2 PHE A 247     7821   8603   5682   -134   1413    135       C  
ATOM   1500  CE1 PHE A 247      67.386  11.783  22.766  1.00 63.15           C  
ANISOU 1500  CE1 PHE A 247     8977   8903   6115   -521   1238    240       C  
ATOM   1501  CE2 PHE A 247      69.270  10.315  22.818  1.00 64.11           C  
ANISOU 1501  CE2 PHE A 247     8591   9495   6275   -403   1526    172       C  
ATOM   1502  CZ  PHE A 247      68.737  11.567  22.585  1.00 61.08           C  
ANISOU 1502  CZ  PHE A 247     8492   8929   5788   -618   1435    225       C  
ATOM   1503  N   ARG A 248      67.336   6.378  21.808  1.00 41.08           N  
ANISOU 1503  N   ARG A 248     5916   6173   3521    388   1397    -17       N  
ATOM   1504  CA  ARG A 248      68.337   6.028  20.808  1.00 46.53           C  
ANISOU 1504  CA  ARG A 248     6610   7020   4049    431   1615    -66       C  
ATOM   1505  C   ARG A 248      67.673   5.551  19.518  1.00 53.61           C  
ANISOU 1505  C   ARG A 248     7852   7711   4805    476   1597   -112       C  
ATOM   1506  O   ARG A 248      68.165   5.817  18.421  1.00 53.83           O  
ANISOU 1506  O   ARG A 248     8007   7797   4649    402   1744   -132       O  
ATOM   1507  CB  ARG A 248      69.284   4.952  21.343  1.00 55.89           C  
ANISOU 1507  CB  ARG A 248     7541   8405   5289    678   1740   -112       C  
ATOM   1508  CG  ARG A 248      70.687   5.038  20.765  1.00 80.03           C  
ANISOU 1508  CG  ARG A 248    10417  11787   8203    684   2000   -132       C  
ATOM   1509  CD  ARG A 248      71.544   3.850  21.174  1.00 96.51           C  
ANISOU 1509  CD  ARG A 248    12282  14066  10321   1013   2117   -183       C  
ATOM   1510  NE  ARG A 248      72.955   4.071  20.863  1.00105.45           N  
ANISOU 1510  NE  ARG A 248    13122  15606  11339   1015   2363   -183       N  
ATOM   1511  CZ  ARG A 248      73.882   3.118  20.863  1.00103.45           C  
ANISOU 1511  CZ  ARG A 248    12686  15541  11080   1305   2490   -235       C  
ATOM   1512  NH1 ARG A 248      73.552   1.866  21.149  1.00 99.21           N  
ANISOU 1512  NH1 ARG A 248    12279  14814  10604   1635   2415   -291       N  
ATOM   1513  NH2 ARG A 248      75.141   3.416  20.570  1.00105.01           N  
ANISOU 1513  NH2 ARG A 248    12608  16044  11248   1224   2639   -229       N  
ATOM   1514  N   LYS A 249      66.546   4.858  19.658  1.00 46.15           N  
ANISOU 1514  N   LYS A 249     7066   6535   3934    570   1414   -125       N  
ATOM   1515  CA  LYS A 249      65.817   4.332  18.506  1.00 48.23           C  
ANISOU 1515  CA  LYS A 249     7671   6594   4061    589   1355   -163       C  
ATOM   1516  C   LYS A 249      65.132   5.437  17.695  1.00 48.68           C  
ANISOU 1516  C   LYS A 249     7945   6538   4013    381   1258   -115       C  
ATOM   1517  O   LYS A 249      65.251   5.488  16.472  1.00 45.10           O  
ANISOU 1517  O   LYS A 249     7734   6035   3367    332   1332   -141       O  
ATOM   1518  CB  LYS A 249      64.780   3.307  18.972  1.00 54.11           C  
ANISOU 1518  CB  LYS A 249     8505   7150   4904    692   1165   -176       C  
ATOM   1519  CG  LYS A 249      64.032   2.599  17.855  1.00 61.77           C  
ANISOU 1519  CG  LYS A 249     9838   7910   5722    692   1082   -215       C  
ATOM   1520  CD  LYS A 249      64.749   1.334  17.419  1.00 66.60           C  
ANISOU 1520  CD  LYS A 249    10590   8500   6215    898   1236   -305       C  
ATOM   1521  CE  LYS A 249      63.861   0.484  16.522  1.00 64.79           C  
ANISOU 1521  CE  LYS A 249    10762   8016   5838    877   1107   -342       C  
ATOM   1522  NZ  LYS A 249      64.584  -0.694  15.970  1.00 65.05           N  
ANISOU 1522  NZ  LYS A 249    11022   7990   5706   1096   1272   -437       N  
ATOM   1523  N   LEU A 250      64.421   6.322  18.387  1.00 47.47           N  
ANISOU 1523  N   LEU A 250     7727   6338   3970    279   1095    -44       N  
ATOM   1524  CA  LEU A 250      63.603   7.347  17.743  1.00 44.85           C  
ANISOU 1524  CA  LEU A 250     7622   5874   3544    137    959     10       C  
ATOM   1525  C   LEU A 250      64.391   8.553  17.245  1.00 45.36           C  
ANISOU 1525  C   LEU A 250     7760   6014   3462    -41   1092     39       C  
ATOM   1526  O   LEU A 250      64.077   9.113  16.192  1.00 51.72           O  
ANISOU 1526  O   LEU A 250     8850   6707   4093   -142   1059     54       O  
ATOM   1527  CB  LEU A 250      62.517   7.834  18.705  1.00 36.01           C  
ANISOU 1527  CB  LEU A 250     6419   4684   2580    145    741     74       C  
ATOM   1528  CG  LEU A 250      61.152   7.149  18.656  1.00 35.40           C  
ANISOU 1528  CG  LEU A 250     6414   4481   2555    216    522     82       C  
ATOM   1529  CD1 LEU A 250      60.222   7.778  19.678  1.00 33.99           C  
ANISOU 1529  CD1 LEU A 250     6098   4298   2519    238    353    151       C  
ATOM   1530  CD2 LEU A 250      60.556   7.242  17.263  1.00 36.76           C  
ANISOU 1530  CD2 LEU A 250     6899   4528   2539    156    433     83       C  
ATOM   1531  N   TRP A 251      65.404   8.963  17.998  1.00 39.12           N  
ANISOU 1531  N   TRP A 251     6728   5412   2724   -103   1231     52       N  
ATOM   1532  CA  TRP A 251      66.100  10.204  17.691  1.00 42.64           C  
ANISOU 1532  CA  TRP A 251     7246   5931   3025   -336   1333     96       C  
ATOM   1533  C   TRP A 251      67.402   9.994  16.911  1.00 47.54           C  
ANISOU 1533  C   TRP A 251     7812   6766   3483   -411   1604     55       C  
ATOM   1534  O   TRP A 251      67.748  10.790  16.033  1.00 62.03           O  
ANISOU 1534  O   TRP A 251     9852   8603   5112   -615   1692     77       O  
ATOM   1535  CB  TRP A 251      66.380  10.956  18.984  1.00 45.09           C  
ANISOU 1535  CB  TRP A 251     7353   6325   3455   -424   1300    149       C  
ATOM   1536  CG  TRP A 251      65.156  11.335  19.714  1.00 54.90           C  
ANISOU 1536  CG  TRP A 251     8664   7377   4819   -350   1066    192       C  
ATOM   1537  CD1 TRP A 251      64.450  10.572  20.626  1.00 55.41           C  
ANISOU 1537  CD1 TRP A 251     8556   7410   5086   -161    945    182       C  
ATOM   1538  CD2 TRP A 251      64.452  12.588  19.615  1.00 60.08           C  
ANISOU 1538  CD2 TRP A 251     9589   7852   5385   -446    927    256       C  
ATOM   1539  NE1 TRP A 251      63.359  11.292  21.092  1.00 49.56           N  
ANISOU 1539  NE1 TRP A 251     7924   6516   4391   -135    755    236       N  
ATOM   1540  CE2 TRP A 251      63.342  12.522  20.490  1.00 60.15           C  
ANISOU 1540  CE2 TRP A 251     9540   7758   5556   -281    738    280       C  
ATOM   1541  CE3 TRP A 251      64.655  13.753  18.877  1.00 58.67           C  
ANISOU 1541  CE3 TRP A 251     9717   7587   4988   -648    948    297       C  
ATOM   1542  CZ2 TRP A 251      62.437  13.585  20.644  1.00 63.38           C  
ANISOU 1542  CZ2 TRP A 251    10168   7997   5918   -265    574    340       C  
ATOM   1543  CZ3 TRP A 251      63.751  14.800  19.036  1.00 67.09           C  
ANISOU 1543  CZ3 TRP A 251    11046   8444   6003   -639    769    357       C  
ATOM   1544  CH2 TRP A 251      62.656  14.706  19.912  1.00 68.16           C  
ANISOU 1544  CH2 TRP A 251    11097   8496   6306   -426    587    376       C  
ATOM   1545  N   CYS A 252      68.110   8.912  17.215  1.00 56.51           N  
ANISOU 1545  N   CYS A 252     8689   8088   4696   -233   1741     -2       N  
ATOM   1546  CA  CYS A 252      69.429   8.697  16.635  1.00 57.38           C  
ANISOU 1546  CA  CYS A 252     8665   8475   4662   -258   2020    -36       C  
ATOM   1547  C   CYS A 252      69.400   7.790  15.409  1.00 64.27           C  
ANISOU 1547  C   CYS A 252     9758   9279   5382   -104   2126   -113       C  
ATOM   1548  O   CYS A 252      70.115   8.032  14.436  1.00 71.43           O  
ANISOU 1548  O   CYS A 252    10748  10313   6080   -207   2329   -128       O  
ATOM   1549  CB  CYS A 252      70.372   8.120  17.689  1.00 62.38           C  
ANISOU 1549  CB  CYS A 252     8867   9397   5438   -121   2125    -49       C  
ATOM   1550  SG  CYS A 252      70.534   9.150  19.166  1.00 69.39           S  
ANISOU 1550  SG  CYS A 252     9506  10380   6478   -322   2010     38       S  
ATOM   1551  N   ARG A 253      68.572   6.752  15.451  1.00 68.21           N  
ANISOU 1551  N   ARG A 253    11016  10248   4654     39   1485     93       N  
ATOM   1552  CA  ARG A 253      68.552   5.762  14.379  1.00 50.82           C  
ANISOU 1552  CA  ARG A 253     8762   7909   2637     -7   1396    260       C  
ATOM   1553  C   ARG A 253      67.383   5.946  13.409  1.00 58.40           C  
ANISOU 1553  C   ARG A 253     9642   8771   3776    -11   1584    267       C  
ATOM   1554  O   ARG A 253      67.478   5.572  12.240  1.00 57.77           O  
ANISOU 1554  O   ARG A 253     9552   8536   3863    -41   1455    315       O  
ATOM   1555  CB  ARG A 253      68.532   4.355  14.976  1.00 51.91           C  
ANISOU 1555  CB  ARG A 253     8968   8085   2670    -86   1416    524       C  
ATOM   1556  CG  ARG A 253      69.877   3.928  15.548  1.00 62.94           C  
ANISOU 1556  CG  ARG A 253    10430   9530   3954    -82   1170    579       C  
ATOM   1557  CD  ARG A 253      69.789   2.599  16.278  1.00 77.99           C  
ANISOU 1557  CD  ARG A 253    12410  11483   5741   -146   1214    846       C  
ATOM   1558  NE  ARG A 253      68.992   2.698  17.497  1.00 92.93           N  
ANISOU 1558  NE  ARG A 253    14353  13551   7406   -174   1457    884       N  
ATOM   1559  CZ  ARG A 253      68.836   1.708  18.371  1.00 99.22           C  
ANISOU 1559  CZ  ARG A 253    15217  14432   8049   -233   1529   1114       C  
ATOM   1560  NH1 ARG A 253      69.427   0.539  18.162  1.00 97.02           N  
ANISOU 1560  NH1 ARG A 253    14966  14062   7836   -265   1368   1323       N  
ATOM   1561  NH2 ARG A 253      68.092   1.888  19.454  1.00106.35           N  
ANISOU 1561  NH2 ARG A 253    16168  15502   8738   -253   1776   1140       N  
ATOM   1562  N   GLN A 254      66.285   6.519  13.889  1.00 64.18           N  
ANISOU 1562  N   GLN A 254    10322   9587   4474     20   1905    236       N  
ATOM   1563  CA  GLN A 254      65.165   6.842  13.012  1.00 61.17           C  
ANISOU 1563  CA  GLN A 254     9820   9131   4290     28   2128    269       C  
ATOM   1564  C   GLN A 254      65.226   8.302  12.587  1.00 65.96           C  
ANISOU 1564  C   GLN A 254    10369   9699   4995    163   2126     -3       C  
ATOM   1565  O   GLN A 254      65.953   9.102  13.179  1.00 67.48           O  
ANISOU 1565  O   GLN A 254    10625   9933   5082    229   2006   -207       O  
ATOM   1566  CB  GLN A 254      63.827   6.555  13.694  1.00 73.19           C  
ANISOU 1566  CB  GLN A 254    11232  10761   5815      2   2549    468       C  
ATOM   1567  CG  GLN A 254      63.486   5.084  13.819  1.00 76.37           C  
ANISOU 1567  CG  GLN A 254    11650  11157   6212   -175   2581    801       C  
ATOM   1568  CD  GLN A 254      62.135   4.856  14.464  1.00 95.74           C  
ANISOU 1568  CD  GLN A 254    13910  13725   8740   -211   3011   1043       C  
ATOM   1569  OE1 GLN A 254      61.260   5.721  14.420  1.00109.64           O  
ANISOU 1569  OE1 GLN A 254    15458  15533  10666    -99   3310   1013       O  
ATOM   1570  NE2 GLN A 254      61.958   3.689  15.073  1.00104.38           N  
ANISOU 1570  NE2 GLN A 254    15037  14865   9756   -353   3044   1307       N  
ATOM   1571  N   GLY A1001      64.457   8.644  11.559  1.00 57.08           N  
ANISOU 1571  N   GLY A1001     9125   8481   4081    187   2260     21       N  
ATOM   1572  CA  GLY A1001      64.394  10.012  11.088  1.00 60.12           C  
ANISOU 1572  CA  GLY A1001     9418   8810   4616    328   2268   -211       C  
ATOM   1573  C   GLY A1001      65.007  10.186   9.716  1.00 68.62           C  
ANISOU 1573  C   GLY A1001    10431   9732   5910    292   1893   -282       C  
ATOM   1574  O   GLY A1001      65.615   9.265   9.170  1.00 69.77           O  
ANISOU 1574  O   GLY A1001    10655   9809   6046    182   1638   -181       O  
ATOM   1575  N   ILE A1002      64.848  11.382   9.161  1.00 61.17           N  
ANISOU 1575  N   ILE A1002     9367   8721   5156    402   1885   -450       N  
ATOM   1576  CA  ILE A1002      65.346  11.692   7.830  1.00 57.85           C  
ANISOU 1576  CA  ILE A1002     8880   8158   4943    383   1565   -511       C  
ATOM   1577  C   ILE A1002      65.423  13.205   7.667  1.00 51.31           C  
ANISOU 1577  C   ILE A1002     8021   7276   4198    535   1603   -741       C  
ATOM   1578  O   ILE A1002      64.545  13.928   8.137  1.00 68.82           O  
ANISOU 1578  O   ILE A1002    10120   9520   6508    650   1888   -783       O  
ATOM   1579  CB  ILE A1002      64.443  11.074   6.733  1.00 60.85           C  
ANISOU 1579  CB  ILE A1002     8992   8451   5678    255   1448   -301       C  
ATOM   1580  CG1 ILE A1002      64.929  11.460   5.337  1.00 49.07           C  
ANISOU 1580  CG1 ILE A1002     7481   6808   4356    244   1135   -371       C  
ATOM   1581  CG2 ILE A1002      62.991  11.490   6.929  1.00 71.74           C  
ANISOU 1581  CG2 ILE A1002    10044   9881   7335    291   1717   -188       C  
ATOM   1582  CD1 ILE A1002      63.999  11.016   4.230  1.00 53.66           C  
ANISOU 1582  CD1 ILE A1002     7840   7289   5259    102    980   -184       C  
ATOM   1583  N   ASP A1003      66.483  13.686   7.027  1.00 44.52           N  
ANISOU 1583  N   ASP A1003     7273   6330   3313    549   1337   -873       N  
ATOM   1584  CA  ASP A1003      66.622  15.114   6.773  1.00 55.17           C  
ANISOU 1584  CA  ASP A1003     8605   7595   4763    669   1330  -1076       C  
ATOM   1585  C   ASP A1003      65.603  15.555   5.722  1.00 54.39           C  
ANISOU 1585  C   ASP A1003     8188   7403   5073    698   1330   -999       C  
ATOM   1586  O   ASP A1003      65.918  15.634   4.533  1.00 58.35           O  
ANISOU 1586  O   ASP A1003     8621   7806   5743    652   1071   -969       O  
ATOM   1587  CB  ASP A1003      68.046  15.448   6.320  1.00 67.53           C  
ANISOU 1587  CB  ASP A1003    10265   9102   6293    620   1003  -1159       C  
ATOM   1588  CG  ASP A1003      68.387  16.919   6.493  1.00 76.41           C  
ANISOU 1588  CG  ASP A1003    11375  10153   7502    672    971  -1350       C  
ATOM   1589  OD1 ASP A1003      67.470  17.764   6.401  1.00 78.72           O  
ANISOU 1589  OD1 ASP A1003    11621  10375   7915    812   1175  -1449       O  
ATOM   1590  OD2 ASP A1003      69.575  17.230   6.723  1.00 78.82           O  
ANISOU 1590  OD2 ASP A1003    11717  10462   7768    580    763  -1383       O  
ATOM   1591  N   CYS A1004      64.384  15.837   6.172  1.00 48.36           N  
ANISOU 1591  N   CYS A1004     7230   6677   4467    780   1628   -942       N  
ATOM   1592  CA  CYS A1004      63.292  16.214   5.279  1.00 50.70           C  
ANISOU 1592  CA  CYS A1004     7169   6906   5189    804   1633   -808       C  
ATOM   1593  C   CYS A1004      63.549  17.538   4.567  1.00 52.19           C  
ANISOU 1593  C   CYS A1004     7326   6953   5551    921   1522   -964       C  
ATOM   1594  O   CYS A1004      63.047  17.764   3.465  1.00 53.28           O  
ANISOU 1594  O   CYS A1004     7222   7010   6010    894   1359   -844       O  
ATOM   1595  CB  CYS A1004      61.974  16.297   6.053  1.00 52.73           C  
ANISOU 1595  CB  CYS A1004     7193   7246   5595    905   2034   -683       C  
ATOM   1596  SG  CYS A1004      61.306  14.702   6.566  1.00 66.19           S  
ANISOU 1596  SG  CYS A1004     8793   9100   7258    725   2141   -384       S  
ATOM   1597  N   SER A1005      64.330  18.410   5.197  1.00 42.57           N  
ANISOU 1597  N   SER A1005     6369   5694   4113   1030   1584  -1216       N  
ATOM   1598  CA  SER A1005      64.639  19.712   4.614  1.00 50.41           C  
ANISOU 1598  CA  SER A1005     7366   6528   5259   1132   1483  -1369       C  
ATOM   1599  C   SER A1005      65.600  19.580   3.436  1.00 55.04           C  
ANISOU 1599  C   SER A1005     7988   7050   5875   1009   1090  -1344       C  
ATOM   1600  O   SER A1005      65.718  20.492   2.617  1.00 60.48           O  
ANISOU 1600  O   SER A1005     8605   7608   6765   1058    958  -1385       O  
ATOM   1601  CB  SER A1005      65.228  20.650   5.671  1.00 55.34           C  
ANISOU 1601  CB  SER A1005     8309   7098   5618   1246   1633  -1648       C  
ATOM   1602  OG  SER A1005      66.471  20.167   6.152  1.00 55.47           O  
ANISOU 1602  OG  SER A1005     8578   7189   5308   1090   1422  -1709       O  
ATOM   1603  N   PHE A1006      66.283  18.440   3.352  1.00 46.16           N  
ANISOU 1603  N   PHE A1006     6982   6007   4550    867    928  -1261       N  
ATOM   1604  CA  PHE A1006      67.242  18.198   2.279  1.00 39.13           C  
ANISOU 1604  CA  PHE A1006     6155   5058   3655    780    617  -1219       C  
ATOM   1605  C   PHE A1006      66.682  17.271   1.205  1.00 51.16           C  
ANISOU 1605  C   PHE A1006     7541   6562   5336    669    471  -1007       C  
ATOM   1606  O   PHE A1006      66.881  17.497   0.011  1.00 48.62           O  
ANISOU 1606  O   PHE A1006     7187   6142   5146    642    264   -960       O  
ATOM   1607  CB  PHE A1006      68.538  17.609   2.841  1.00 32.06           C  
ANISOU 1607  CB  PHE A1006     5513   4233   2434    725    529  -1260       C  
ATOM   1608  CG  PHE A1006      69.533  17.222   1.784  1.00 29.67           C  
ANISOU 1608  CG  PHE A1006     5266   3880   2129    670    277  -1178       C  
ATOM   1609  CD1 PHE A1006      70.378  18.168   1.231  1.00 28.75           C  
ANISOU 1609  CD1 PHE A1006     5146   3682   2095    692    136  -1234       C  
ATOM   1610  CD2 PHE A1006      69.625  15.912   1.346  1.00 39.43           C  
ANISOU 1610  CD2 PHE A1006     6549   5134   3301    592    205  -1019       C  
ATOM   1611  CE1 PHE A1006      71.294  17.817   0.256  1.00 35.71           C  
ANISOU 1611  CE1 PHE A1006     6026   4527   3015    647    -34  -1105       C  
ATOM   1612  CE2 PHE A1006      70.539  15.554   0.372  1.00 39.53           C  
ANISOU 1612  CE2 PHE A1006     6624   5081   3314    573     33   -934       C  
ATOM   1613  CZ  PHE A1006      71.374  16.509  -0.173  1.00 37.21           C  
ANISOU 1613  CZ  PHE A1006     6269   4732   3136    601    -66   -958       C  
ATOM   1614  N   TRP A1007      65.988  16.221   1.633  1.00 50.44           N  
ANISOU 1614  N   TRP A1007     7399   6553   5215    587    569   -872       N  
ATOM   1615  CA  TRP A1007      65.484  15.220   0.702  1.00 37.84           C  
ANISOU 1615  CA  TRP A1007     5735   4913   3731    435    394   -672       C  
ATOM   1616  C   TRP A1007      64.084  15.554   0.197  1.00 42.57           C  
ANISOU 1616  C   TRP A1007     6010   5482   4682    406    398   -525       C  
ATOM   1617  O   TRP A1007      63.116  14.883   0.548  1.00 52.13           O  
ANISOU 1617  O   TRP A1007     7056   6753   5997    318    491   -357       O  
ATOM   1618  CB  TRP A1007      65.482  13.835   1.357  1.00 33.49           C  
ANISOU 1618  CB  TRP A1007     5300   4436   2990    325    453   -566       C  
ATOM   1619  CG  TRP A1007      66.841  13.366   1.789  1.00 45.05           C  
ANISOU 1619  CG  TRP A1007     7051   5927   4138    350    419   -648       C  
ATOM   1620  CD1 TRP A1007      67.322  13.311   3.065  1.00 40.88           C  
ANISOU 1620  CD1 TRP A1007     6645   5515   3371    403    581   -723       C  
ATOM   1621  CD2 TRP A1007      67.895  12.887   0.944  1.00 29.96           C  
ANISOU 1621  CD2 TRP A1007     5336   3925   2122    331    214   -634       C  
ATOM   1622  NE1 TRP A1007      68.607  12.827   3.067  1.00 32.52           N  
ANISOU 1622  NE1 TRP A1007     5803   4452   2100    406    456   -733       N  
ATOM   1623  CE2 TRP A1007      68.983  12.560   1.777  1.00 29.51           C  
ANISOU 1623  CE2 TRP A1007     5459   3944   1809    381    259   -676       C  
ATOM   1624  CE3 TRP A1007      68.024  12.703  -0.435  1.00 37.33           C  
ANISOU 1624  CE3 TRP A1007     6325   4717   3141    286      9   -577       C  
ATOM   1625  CZ2 TRP A1007      70.182  12.060   1.278  1.00 28.09           C  
ANISOU 1625  CZ2 TRP A1007     5409   3709   1556    398    129   -625       C  
ATOM   1626  CZ3 TRP A1007      69.217  12.207  -0.930  1.00 36.60           C  
ANISOU 1626  CZ3 TRP A1007     6463   4560   2884    325    -85   -570       C  
ATOM   1627  CH2 TRP A1007      70.279  11.891  -0.076  1.00 33.89           C  
ANISOU 1627  CH2 TRP A1007     6202   4300   2376    389    -10   -578       C  
ATOM   1628  N   ASN A1008      63.977  16.594  -0.624  1.00 40.18           N  
ANISOU 1628  N   ASN A1008     5594   5087   4584    474    289   -556       N  
ATOM   1629  CA  ASN A1008      62.715  16.899  -1.288  1.00 57.68           C  
ANISOU 1629  CA  ASN A1008     7485   7265   7165    435    221   -369       C  
ATOM   1630  C   ASN A1008      62.944  17.436  -2.700  1.00 54.60           C  
ANISOU 1630  C   ASN A1008     7113   6743   6891    403    -83   -343       C  
ATOM   1631  O   ASN A1008      64.032  17.908  -3.029  1.00 37.62           O  
ANISOU 1631  O   ASN A1008     5176   4534   4582    470   -155   -496       O  
ATOM   1632  CB  ASN A1008      61.887  17.888  -0.461  1.00 66.38           C  
ANISOU 1632  CB  ASN A1008     8323   8411   8486    626    540   -389       C  
ATOM   1633  CG  ASN A1008      62.584  19.213  -0.261  1.00 70.31           C  
ANISOU 1633  CG  ASN A1008     8940   8834   8942    825    630   -630       C  
ATOM   1634  OD1 ASN A1008      62.407  20.143  -1.046  1.00 75.41           O  
ANISOU 1634  OD1 ASN A1008     9463   9370   9820    892    518   -615       O  
ATOM   1635  ND2 ASN A1008      63.377  19.312   0.799  1.00 74.29           N  
ANISOU 1635  ND2 ASN A1008     9698   9384   9146    903    810   -841       N  
ATOM   1636  N   GLU A1009      61.906  17.353  -3.527  1.00 65.02           N  
ANISOU 1636  N   GLU A1009     8196   8020   8487    287   -269   -121       N  
ATOM   1637  CA  GLU A1009      62.015  17.625  -4.958  1.00 65.13           C  
ANISOU 1637  CA  GLU A1009     8269   7910   8567    203   -607    -49       C  
ATOM   1638  C   GLU A1009      62.348  19.083  -5.281  1.00 54.04           C  
ANISOU 1638  C   GLU A1009     6805   6436   7290    390   -584   -154       C  
ATOM   1639  O   GLU A1009      62.893  19.376  -6.347  1.00 41.67           O  
ANISOU 1639  O   GLU A1009     5395   4772   5665    358   -814   -157       O  
ATOM   1640  CB  GLU A1009      60.710  17.218  -5.657  1.00 81.08           C  
ANISOU 1640  CB  GLU A1009    10027   9909  10872      6   -845    247       C  
ATOM   1641  CG  GLU A1009      60.792  17.121  -7.179  1.00 94.14           C  
ANISOU 1641  CG  GLU A1009    11845  11429  12494   -160  -1261    347       C  
ATOM   1642  CD  GLU A1009      60.506  18.440  -7.877  1.00100.52           C  
ANISOU 1642  CD  GLU A1009    12450  12178  13564    -49  -1361    406       C  
ATOM   1643  OE1 GLU A1009      59.931  19.345  -7.235  1.00104.43           O  
ANISOU 1643  OE1 GLU A1009    12601  12722  14355    134  -1132    429       O  
ATOM   1644  OE2 GLU A1009      60.860  18.571  -9.068  1.00 95.04           O  
ANISOU 1644  OE2 GLU A1009    11963  11377  12769   -131  -1653    435       O  
ATOM   1645  N   SER A1010      62.034  19.989  -4.358  1.00 50.54           N  
ANISOU 1645  N   SER A1010     6171   6025   7006    589   -293   -238       N  
ATOM   1646  CA  SER A1010      62.171  21.426  -4.600  1.00 47.95           C  
ANISOU 1646  CA  SER A1010     5770   5595   6855    770   -258   -320       C  
ATOM   1647  C   SER A1010      63.575  21.844  -5.037  1.00 41.77           C  
ANISOU 1647  C   SER A1010     5302   4735   5833    791   -372   -499       C  
ATOM   1648  O   SER A1010      63.742  22.843  -5.736  1.00 55.54           O  
ANISOU 1648  O   SER A1010     7017   6365   7720    858   -479   -496       O  
ATOM   1649  CB  SER A1010      61.776  22.213  -3.347  1.00 57.04           C  
ANISOU 1649  CB  SER A1010     6786   6763   8122    996    129   -440       C  
ATOM   1650  OG  SER A1010      60.417  21.993  -3.010  1.00 60.29           O  
ANISOU 1650  OG  SER A1010     6840   7243   8825   1020    281   -227       O  
ATOM   1651  N   TYR A1011      64.581  21.075  -4.635  1.00 38.48           N  
ANISOU 1651  N   TYR A1011     5164   4381   5078    733   -348   -621       N  
ATOM   1652  CA  TYR A1011      65.964  21.416  -4.949  1.00 47.66           C  
ANISOU 1652  CA  TYR A1011     6578   5492   6039    757   -427   -749       C  
ATOM   1653  C   TYR A1011      66.366  21.009  -6.365  1.00 50.16           C  
ANISOU 1653  C   TYR A1011     7034   5745   6280    647   -697   -624       C  
ATOM   1654  O   TYR A1011      67.317  21.552  -6.929  1.00 48.66           O  
ANISOU 1654  O   TYR A1011     6975   5491   6022    685   -770   -663       O  
ATOM   1655  CB  TYR A1011      66.904  20.776  -3.929  1.00 40.95           C  
ANISOU 1655  CB  TYR A1011     5938   4739   4883    755   -294   -888       C  
ATOM   1656  CG  TYR A1011      66.797  21.407  -2.564  1.00 47.65           C  
ANISOU 1656  CG  TYR A1011     6758   5621   5724    872    -42  -1055       C  
ATOM   1657  CD1 TYR A1011      67.569  22.510  -2.227  1.00 51.90           C  
ANISOU 1657  CD1 TYR A1011     7396   6082   6240    959    -15  -1222       C  
ATOM   1658  CD2 TYR A1011      65.910  20.914  -1.617  1.00 59.76           C  
ANISOU 1658  CD2 TYR A1011     8195   7250   7263    887    169  -1039       C  
ATOM   1659  CE1 TYR A1011      67.469  23.099  -0.980  1.00 63.82           C  
ANISOU 1659  CE1 TYR A1011     8964   7589   7695   1056    204  -1399       C  
ATOM   1660  CE2 TYR A1011      65.802  21.496  -0.368  1.00 63.80           C  
ANISOU 1660  CE2 TYR A1011     8744   7780   7716   1010    432  -1202       C  
ATOM   1661  CZ  TYR A1011      66.584  22.588  -0.055  1.00 60.40           C  
ANISOU 1661  CZ  TYR A1011     8469   7252   7226   1094    441  -1397       C  
ATOM   1662  OH  TYR A1011      66.482  23.170   1.185  1.00 66.67           O  
ANISOU 1662  OH  TYR A1011     9385   8032   7916   1206    690  -1583       O  
ATOM   1663  N   LEU A1012      65.642  20.056  -6.939  1.00 43.78           N  
ANISOU 1663  N   LEU A1012     6218   4943   5473    502   -844   -466       N  
ATOM   1664  CA  LEU A1012      65.912  19.630  -8.305  1.00 49.99           C  
ANISOU 1664  CA  LEU A1012     7209   5643   6143    389  -1101   -356       C  
ATOM   1665  C   LEU A1012      65.215  20.557  -9.291  1.00 56.82           C  
ANISOU 1665  C   LEU A1012     7908   6419   7262    379  -1295   -220       C  
ATOM   1666  O   LEU A1012      64.168  21.126  -8.986  1.00 62.07           O  
ANISOU 1666  O   LEU A1012     8253   7096   8236    413  -1267   -142       O  
ATOM   1667  CB  LEU A1012      65.461  18.185  -8.521  1.00 44.37           C  
ANISOU 1667  CB  LEU A1012     6634   4933   5289    205  -1219   -253       C  
ATOM   1668  CG  LEU A1012      66.024  17.160  -7.535  1.00 37.67           C  
ANISOU 1668  CG  LEU A1012     5939   4163   4212    209  -1037   -347       C  
ATOM   1669  CD1 LEU A1012      65.581  15.763  -7.920  1.00 35.42           C  
ANISOU 1669  CD1 LEU A1012     5835   3826   3799     12  -1187   -234       C  
ATOM   1670  CD2 LEU A1012      67.540  17.247  -7.469  1.00 34.73           C  
ANISOU 1670  CD2 LEU A1012     5801   3791   3604    334   -933   -474       C  
ATOM   1671  N   THR A1013      65.800  20.709 -10.473  1.00 52.73           N  
ANISOU 1671  N   THR A1013     6634   5210   8190   -415   -569   -657       N  
ATOM   1672  CA  THR A1013      65.227  21.576 -11.493  1.00 53.49           C  
ANISOU 1672  CA  THR A1013     6776   5090   8456   -434   -587   -424       C  
ATOM   1673  C   THR A1013      64.846  20.785 -12.738  1.00 52.33           C  
ANISOU 1673  C   THR A1013     6684   5105   8095   -433   -578   -168       C  
ATOM   1674  O   THR A1013      65.462  19.766 -13.052  1.00 54.46           O  
ANISOU 1674  O   THR A1013     6962   5582   8149   -495   -527   -148       O  
ATOM   1675  CB  THR A1013      66.199  22.701 -11.889  1.00 55.21           C  
ANISOU 1675  CB  THR A1013     6984   5057   8938   -588   -548   -359       C  
ATOM   1676  OG1 THR A1013      67.419  22.129 -12.378  1.00 52.28           O  
ANISOU 1676  OG1 THR A1013     6578   4838   8446   -735   -479   -296       O  
ATOM   1677  CG2 THR A1013      66.504  23.587 -10.689  1.00 59.14           C  
ANISOU 1677  CG2 THR A1013     7411   5397   9661   -598   -569   -670       C  
ATOM   1678  N   GLY A1014      63.826  21.261 -13.442  1.00 54.04           N  
ANISOU 1678  N   GLY A1014     6931   5240   8363   -341   -637      6       N  
ATOM   1679  CA  GLY A1014      63.361  20.607 -14.649  1.00 27.35           C  
ANISOU 1679  CA  GLY A1014     3584   2047   4760   -318   -671    205       C  
ATOM   1680  C   GLY A1014      62.515  19.389 -14.344  1.00 36.69           C  
ANISOU 1680  C   GLY A1014     4710   3455   5774   -266   -692     55       C  
ATOM   1681  O   GLY A1014      62.483  18.912 -13.208  1.00 40.78           O  
ANISOU 1681  O   GLY A1014     5190   3999   6306   -251   -638   -156       O  
ATOM   1682  N   SER A1015      61.825  18.886 -15.362  1.00 34.08           N  
ANISOU 1682  N   SER A1015     4371   3293   5284   -234   -762    158       N  
ATOM   1683  CA  SER A1015      61.002  17.692 -15.218  1.00 31.39           C  
ANISOU 1683  CA  SER A1015     3953   3142   4833   -229   -763     -3       C  
ATOM   1684  C   SER A1015      61.864  16.468 -14.942  1.00 42.41           C  
ANISOU 1684  C   SER A1015     5397   4640   6076   -341   -624   -112       C  
ATOM   1685  O   SER A1015      63.080  16.492 -15.140  1.00 38.33           O  
ANISOU 1685  O   SER A1015     4958   4117   5490   -413   -562    -42       O  
ATOM   1686  CB  SER A1015      60.167  17.461 -16.476  1.00 33.19           C  
ANISOU 1686  CB  SER A1015     4136   3554   4920   -185   -899     85       C  
ATOM   1687  OG  SER A1015      61.000  17.125 -17.572  1.00 35.72           O  
ANISOU 1687  OG  SER A1015     4562   3999   5009   -256   -888    215       O  
ATOM   1688  N   ARG A1016      61.228  15.392 -14.493  1.00 40.37           N  
ANISOU 1688  N   ARG A1016     5085   4465   5789   -349   -553   -274       N  
ATOM   1689  CA  ARG A1016      61.948  14.158 -14.223  1.00 34.16           C  
ANISOU 1689  CA  ARG A1016     4363   3744   4875   -417   -393   -356       C  
ATOM   1690  C   ARG A1016      62.501  13.554 -15.514  1.00 31.28           C  
ANISOU 1690  C   ARG A1016     4063   3509   4312   -503   -401   -290       C  
ATOM   1691  O   ARG A1016      63.570  12.945 -15.508  1.00 31.36           O  
ANISOU 1691  O   ARG A1016     4153   3550   4212   -541   -283   -285       O  
ATOM   1692  CB  ARG A1016      61.044  13.151 -13.509  1.00 26.93           C  
ANISOU 1692  CB  ARG A1016     3386   2833   4014   -408   -267   -514       C  
ATOM   1693  CG  ARG A1016      61.775  11.906 -13.049  1.00 25.60           C  
ANISOU 1693  CG  ARG A1016     3311   2674   3742   -429    -57   -566       C  
ATOM   1694  CD  ARG A1016      60.877  10.974 -12.254  1.00 33.77           C  
ANISOU 1694  CD  ARG A1016     4304   3656   4872   -415    132   -680       C  
ATOM   1695  NE  ARG A1016      61.677  10.074 -11.429  1.00 30.17           N  
ANISOU 1695  NE  ARG A1016     3971   3167   4325   -346    356   -668       N  
ATOM   1696  CZ  ARG A1016      62.046  10.343 -10.182  1.00 19.70           C  
ANISOU 1696  CZ  ARG A1016     2690   1828   2967   -192    431   -647       C  
ATOM   1697  NH1 ARG A1016      61.671  11.479  -9.609  1.00 22.81           N  
ANISOU 1697  NH1 ARG A1016     3017   2211   3437   -119    312   -672       N  
ATOM   1698  NH2 ARG A1016      62.782   9.475  -9.504  1.00 19.09           N  
ANISOU 1698  NH2 ARG A1016     2728   1760   2766    -84    622   -610       N  
ATOM   1699  N   ASP A1017      61.777  13.729 -16.616  1.00 29.25           N  
ANISOU 1699  N   ASP A1017     3766   3357   3991   -506   -543   -248       N  
ATOM   1700  CA  ASP A1017      62.216  13.213 -17.913  1.00 37.15           C  
ANISOU 1700  CA  ASP A1017     4837   4524   4756   -560   -564   -205       C  
ATOM   1701  C   ASP A1017      63.549  13.818 -18.326  1.00 42.38           C  
ANISOU 1701  C   ASP A1017     5609   5166   5326   -569   -516     -3       C  
ATOM   1702  O   ASP A1017      64.453  13.117 -18.793  1.00 46.55           O  
ANISOU 1702  O   ASP A1017     6215   5781   5692   -623   -406     -4       O  
ATOM   1703  CB  ASP A1017      61.176  13.498 -18.996  1.00 42.70           C  
ANISOU 1703  CB  ASP A1017     5466   5393   5365   -509   -770   -188       C  
ATOM   1704  CG  ASP A1017      59.829  12.895 -18.681  1.00 55.90           C  
ANISOU 1704  CG  ASP A1017     6966   7110   7163   -527   -823   -422       C  
ATOM   1705  OD1 ASP A1017      59.642  11.687 -18.941  1.00 46.23           O  
ANISOU 1705  OD1 ASP A1017     5716   5968   5883   -634   -757   -634       O  
ATOM   1706  OD2 ASP A1017      58.956  13.632 -18.179  1.00 72.77           O  
ANISOU 1706  OD2 ASP A1017     8982   9185   9481   -439   -912   -407       O  
ATOM   1707  N   GLU A1018      63.657  15.130 -18.151  1.00 31.40           N  
ANISOU 1707  N   GLU A1018     4214   3643   4072   -519   -575    163       N  
ATOM   1708  CA  GLU A1018      64.861  15.858 -18.512  1.00 31.49           C  
ANISOU 1708  CA  GLU A1018     4298   3590   4078   -557   -503    359       C  
ATOM   1709  C   GLU A1018      66.034  15.436 -17.633  1.00 33.19           C  
ANISOU 1709  C   GLU A1018     4502   3757   4350   -629   -356    256       C  
ATOM   1710  O   GLU A1018      67.156  15.260 -18.117  1.00 44.88           O  
ANISOU 1710  O   GLU A1018     6016   5300   5734   -689   -248    335       O  
ATOM   1711  CB  GLU A1018      64.614  17.363 -18.405  1.00 38.05           C  
ANISOU 1711  CB  GLU A1018     5121   4217   5120   -498   -572    530       C  
ATOM   1712  CG  GLU A1018      63.548  17.868 -19.368  1.00 59.75           C  
ANISOU 1712  CG  GLU A1018     7883   7037   7781   -366   -724    691       C  
ATOM   1713  CD  GLU A1018      63.074  19.272 -19.044  1.00 79.03           C  
ANISOU 1713  CD  GLU A1018    10313   9229  10484   -262   -781    831       C  
ATOM   1714  OE1 GLU A1018      63.534  19.838 -18.030  1.00 83.80           O  
ANISOU 1714  OE1 GLU A1018    10895   9596  11351   -320   -706    753       O  
ATOM   1715  OE2 GLU A1018      62.238  19.808 -19.802  1.00 83.10           O  
ANISOU 1715  OE2 GLU A1018    10841   9795  10939   -104   -906   1005       O  
ATOM   1716  N   ARG A1019      65.766  15.258 -16.343  1.00 29.70           N  
ANISOU 1716  N   ARG A1019     4003   3237   4046   -598   -348     81       N  
ATOM   1717  CA  ARG A1019      66.797  14.830 -15.405  1.00 21.84           C  
ANISOU 1717  CA  ARG A1019     2986   2248   3066   -607   -241    -28       C  
ATOM   1718  C   ARG A1019      67.283  13.424 -15.726  1.00 25.48           C  
ANISOU 1718  C   ARG A1019     3497   2859   3325   -611   -116    -77       C  
ATOM   1719  O   ARG A1019      68.470  13.136 -15.621  1.00 20.01           O  
ANISOU 1719  O   ARG A1019     2794   2227   2580   -620    -24    -73       O  
ATOM   1720  CB  ARG A1019      66.281  14.888 -13.967  1.00 20.95           C  
ANISOU 1720  CB  ARG A1019     2826   2060   3075   -520   -255   -194       C  
ATOM   1721  CG  ARG A1019      66.048  16.294 -13.448  1.00 26.39           C  
ANISOU 1721  CG  ARG A1019     3464   2578   3986   -505   -353   -204       C  
ATOM   1722  CD  ARG A1019      65.665  16.281 -11.976  1.00 37.33           C  
ANISOU 1722  CD  ARG A1019     4813   3935   5434   -395   -348   -398       C  
ATOM   1723  NE  ARG A1019      64.332  16.833 -11.755  1.00 43.79           N  
ANISOU 1723  NE  ARG A1019     5607   4647   6383   -324   -412   -422       N  
ATOM   1724  CZ  ARG A1019      63.294  16.127 -11.324  1.00 33.69           C  
ANISOU 1724  CZ  ARG A1019     4313   3419   5068   -247   -361   -493       C  
ATOM   1725  NH1 ARG A1019      63.435  14.840 -11.052  1.00 25.43           N  
ANISOU 1725  NH1 ARG A1019     3302   2489   3871   -235   -229   -535       N  
ATOM   1726  NH2 ARG A1019      62.116  16.710 -11.154  1.00 52.36           N  
ANISOU 1726  NH2 ARG A1019     6618   5700   7575   -176   -418   -518       N  
ATOM   1727  N   LYS A1020      66.359  12.550 -16.112  1.00 26.66           N  
ANISOU 1727  N   LYS A1020     3684   3060   3387   -604   -109   -144       N  
ATOM   1728  CA  LYS A1020      66.707  11.179 -16.467  1.00 29.01           C  
ANISOU 1728  CA  LYS A1020     4046   3447   3529   -613     30   -219       C  
ATOM   1729  C   LYS A1020      67.531  11.153 -17.748  1.00 29.05           C  
ANISOU 1729  C   LYS A1020     4103   3575   3359   -663     56   -114       C  
ATOM   1730  O   LYS A1020      68.474  10.367 -17.881  1.00 34.39           O  
ANISOU 1730  O   LYS A1020     4820   4317   3932   -650    199   -135       O  
ATOM   1731  CB  LYS A1020      65.451  10.328 -16.635  1.00 26.60           C  
ANISOU 1731  CB  LYS A1020     3742   3136   3229   -635     35   -362       C  
ATOM   1732  CG  LYS A1020      65.744   8.876 -16.959  1.00 28.69           C  
ANISOU 1732  CG  LYS A1020     4086   3427   3390   -657    208   -477       C  
ATOM   1733  CD  LYS A1020      64.515   8.180 -17.501  1.00 21.50           C  
ANISOU 1733  CD  LYS A1020     3144   2522   2504   -740    183   -653       C  
ATOM   1734  CE  LYS A1020      64.818   6.736 -17.820  1.00 32.82           C  
ANISOU 1734  CE  LYS A1020     4667   3922   3880   -777    381   -803       C  
ATOM   1735  NZ  LYS A1020      63.658   6.047 -18.448  1.00 38.22           N  
ANISOU 1735  NZ  LYS A1020     5291   4614   4616   -900    349  -1042       N  
ATOM   1736  N   LYS A1021      67.168  12.022 -18.688  1.00 30.33           N  
ANISOU 1736  N   LYS A1021     4270   3778   3475   -691    -67     17       N  
ATOM   1737  CA  LYS A1021      67.907  12.133 -19.937  1.00 37.51           C  
ANISOU 1737  CA  LYS A1021     5243   4820   4187   -715    -21    161       C  
ATOM   1738  C   LYS A1021      69.335  12.594 -19.657  1.00 41.63           C  
ANISOU 1738  C   LYS A1021     5727   5307   4784   -746    105    274       C  
ATOM   1739  O   LYS A1021      70.297  12.025 -20.180  1.00 55.84           O  
ANISOU 1739  O   LYS A1021     7552   7221   6444   -754    248    293       O  
ATOM   1740  CB  LYS A1021      67.207  13.095 -20.897  1.00 42.88           C  
ANISOU 1740  CB  LYS A1021     5950   5549   4794   -687   -167    334       C  
ATOM   1741  CG  LYS A1021      67.602  12.911 -22.352  1.00 46.88           C  
ANISOU 1741  CG  LYS A1021     6556   6266   4990   -669   -125    451       C  
ATOM   1742  CD  LYS A1021      66.929  13.938 -23.248  1.00 54.08           C  
ANISOU 1742  CD  LYS A1021     7510   7242   5795   -581   -268    678       C  
ATOM   1743  CE  LYS A1021      67.300  13.715 -24.707  1.00 57.25           C  
ANISOU 1743  CE  LYS A1021     8032   7904   5814   -522   -218    801       C  
ATOM   1744  NZ  LYS A1021      66.757  14.782 -25.592  1.00 68.94           N  
ANISOU 1744  NZ  LYS A1021     9580   9464   7150   -382   -333   1093       N  
ATOM   1745  N   SER A1022      69.466  13.620 -18.817  1.00 29.72           N  
ANISOU 1745  N   SER A1022     4135   3644   3514   -765     54    316       N  
ATOM   1746  CA  SER A1022      70.779  14.103 -18.394  1.00 33.16           C  
ANISOU 1746  CA  SER A1022     4474   4044   4082   -821    148    353       C  
ATOM   1747  C   SER A1022      71.576  13.003 -17.701  1.00 33.94           C  
ANISOU 1747  C   SER A1022     4525   4248   4123   -765    247    195       C  
ATOM   1748  O   SER A1022      72.769  12.848 -17.937  1.00 40.47           O  
ANISOU 1748  O   SER A1022     5284   5170   4924   -787    367    229       O  
ATOM   1749  CB  SER A1022      70.638  15.306 -17.460  1.00 31.18           C  
ANISOU 1749  CB  SER A1022     4133   3596   4119   -853     54    330       C  
ATOM   1750  OG  SER A1022      70.022  16.394 -18.122  1.00 57.76           O  
ANISOU 1750  OG  SER A1022     7551   6827   7569   -877     -5    517       O  
ATOM   1751  N   LEU A1023      70.899  12.245 -16.848  1.00 26.89           N  
ANISOU 1751  N   LEU A1023     3663   3337   3218   -673    215     40       N  
ATOM   1752  CA  LEU A1023      71.512  11.157 -16.101  1.00 34.39           C  
ANISOU 1752  CA  LEU A1023     4601   4363   4102   -561    322    -73       C  
ATOM   1753  C   LEU A1023      72.127  10.123 -17.031  1.00 33.77           C  
ANISOU 1753  C   LEU A1023     4590   4403   3839   -542    478    -51       C  
ATOM   1754  O   LEU A1023      73.322   9.815 -16.947  1.00 27.83           O  
ANISOU 1754  O   LEU A1023     3763   3755   3055   -489    582    -45       O  
ATOM   1755  CB  LEU A1023      70.476  10.487 -15.198  1.00 31.07           C  
ANISOU 1755  CB  LEU A1023     4246   3868   3692   -464    316   -188       C  
ATOM   1756  CG  LEU A1023      70.915   9.202 -14.493  1.00 34.47           C  
ANISOU 1756  CG  LEU A1023     4723   4341   4034   -305    471   -255       C  
ATOM   1757  CD1 LEU A1023      71.940   9.505 -13.414  1.00 27.20           C  
ANISOU 1757  CD1 LEU A1023     3685   3517   3133   -180    445   -282       C  
ATOM   1758  CD2 LEU A1023      69.717   8.464 -13.913  1.00 27.73           C  
ANISOU 1758  CD2 LEU A1023     3963   3367   3206   -248    535   -325       C  
ATOM   1759  N   LEU A1024      71.299   9.593 -17.923  1.00 30.72           N  
ANISOU 1759  N   LEU A1024     4325   4015   3332   -576    488    -69       N  
ATOM   1760  CA  LEU A1024      71.745   8.563 -18.847  1.00 35.65           C  
ANISOU 1760  CA  LEU A1024     5035   4740   3769   -554    637   -102       C  
ATOM   1761  C   LEU A1024      72.817   9.095 -19.790  1.00 25.94           C  
ANISOU 1761  C   LEU A1024     3763   3645   2447   -600    706     44       C  
ATOM   1762  O   LEU A1024      73.740   8.371 -20.158  1.00 31.34           O  
ANISOU 1762  O   LEU A1024     4453   4431   3023   -541    872     27       O  
ATOM   1763  CB  LEU A1024      70.557   8.007 -19.629  1.00 29.12           C  
ANISOU 1763  CB  LEU A1024     4320   3906   2839   -603    594   -210       C  
ATOM   1764  CG  LEU A1024      69.585   7.274 -18.704  1.00 29.06           C  
ANISOU 1764  CG  LEU A1024     4334   3746   2963   -576    606   -364       C  
ATOM   1765  CD1 LEU A1024      68.409   6.705 -19.470  1.00 36.58           C  
ANISOU 1765  CD1 LEU A1024     5337   4696   3865   -659    558   -529       C  
ATOM   1766  CD2 LEU A1024      70.327   6.180 -17.948  1.00 25.73           C  
ANISOU 1766  CD2 LEU A1024     3954   3261   2560   -449    816   -413       C  
ATOM   1767  N   SER A1025      72.702  10.364 -20.168  1.00 25.62           N  
ANISOU 1767  N   SER A1025     3681   3587   2466   -692    610    200       N  
ATOM   1768  CA  SER A1025      73.722  10.985 -21.006  1.00 26.82           C  
ANISOU 1768  CA  SER A1025     3785   3832   2574   -749    724    381       C  
ATOM   1769  C   SER A1025      75.063  11.049 -20.278  1.00 27.44           C  
ANISOU 1769  C   SER A1025     3679   3939   2809   -746    828    363       C  
ATOM   1770  O   SER A1025      76.112  10.807 -20.873  1.00 45.90           O  
ANISOU 1770  O   SER A1025     5961   6409   5070   -742   1003    421       O  
ATOM   1771  CB  SER A1025      73.291  12.386 -21.435  1.00 32.31           C  
ANISOU 1771  CB  SER A1025     4485   4438   3355   -836    634    585       C  
ATOM   1772  OG  SER A1025      74.285  12.988 -22.245  1.00 37.41           O  
ANISOU 1772  OG  SER A1025     5092   5142   3981   -900    801    794       O  
ATOM   1773  N   LYS A1026      75.019  11.374 -18.989  1.00 26.50           N  
ANISOU 1773  N   LYS A1026     3449   3725   2895   -731    715    262       N  
ATOM   1774  CA  LYS A1026      76.222  11.475 -18.169  1.00 33.02           C  
ANISOU 1774  CA  LYS A1026     4059   4623   3864   -707    751    192       C  
ATOM   1775  C   LYS A1026      76.859  10.112 -17.942  1.00 29.75           C  
ANISOU 1775  C   LYS A1026     3645   4358   3303   -526    871     97       C  
ATOM   1776  O   LYS A1026      78.081   9.992 -17.886  1.00 37.12           O  
ANISOU 1776  O   LYS A1026     4399   5436   4268   -487    968     88       O  
ATOM   1777  CB  LYS A1026      75.903  12.125 -16.818  1.00 43.28           C  
ANISOU 1777  CB  LYS A1026     5260   5822   5362   -700    572     67       C  
ATOM   1778  CG  LYS A1026      75.571  13.608 -16.884  1.00 52.81           C  
ANISOU 1778  CG  LYS A1026     6420   6850   6797   -873    479    136       C  
ATOM   1779  CD  LYS A1026      74.972  14.090 -15.566  1.00 50.60           C  
ANISOU 1779  CD  LYS A1026     6099   6463   6662   -831    299    -32       C  
ATOM   1780  CE  LYS A1026      74.414  15.499 -15.686  1.00 51.45           C  
ANISOU 1780  CE  LYS A1026     6210   6336   7004   -975    220     33       C  
ATOM   1781  NZ  LYS A1026      73.747  15.941 -14.429  1.00 56.65           N  
ANISOU 1781  NZ  LYS A1026     6847   6894   7784   -913     57   -156       N  
ATOM   1782  N   PHE A1027      76.026   9.085 -17.805  1.00 32.89           N  
ANISOU 1782  N   PHE A1027     4227   4704   3567   -411    880     24       N  
ATOM   1783  CA  PHE A1027      76.527   7.739 -17.538  1.00 34.30           C  
ANISOU 1783  CA  PHE A1027     4445   4954   3633   -211   1024    -50       C  
ATOM   1784  C   PHE A1027      76.882   6.974 -18.810  1.00 30.78           C  
ANISOU 1784  C   PHE A1027     4101   4581   3014   -202   1214    -29       C  
ATOM   1785  O   PHE A1027      77.400   5.860 -18.742  1.00 42.94           O  
ANISOU 1785  O   PHE A1027     5679   6161   4476    -29   1370    -86       O  
ATOM   1786  CB  PHE A1027      75.504   6.946 -16.723  1.00 32.68           C  
ANISOU 1786  CB  PHE A1027     4394   4606   3415    -95   1004   -137       C  
ATOM   1787  CG  PHE A1027      75.679   7.085 -15.242  1.00 34.19           C  
ANISOU 1787  CG  PHE A1027     4490   4818   3683     54    918   -176       C  
ATOM   1788  CD1 PHE A1027      75.128   8.159 -14.562  1.00 32.73           C  
ANISOU 1788  CD1 PHE A1027     4237   4580   3619    -32    731   -201       C  
ATOM   1789  CD2 PHE A1027      76.405   6.147 -14.529  1.00 46.82           C  
ANISOU 1789  CD2 PHE A1027     6073   6506   5212    314   1026   -190       C  
ATOM   1790  CE1 PHE A1027      75.294   8.291 -13.196  1.00 34.15           C  
ANISOU 1790  CE1 PHE A1027     4335   4820   3821    128    644   -270       C  
ATOM   1791  CE2 PHE A1027      76.574   6.273 -13.164  1.00 48.03           C  
ANISOU 1791  CE2 PHE A1027     6145   6735   5369    498    931   -222       C  
ATOM   1792  CZ  PHE A1027      76.018   7.346 -12.496  1.00 39.00           C  
ANISOU 1792  CZ  PHE A1027     4935   5564   4319    399    735   -277       C  
ATOM   1793  N   GLY A1028      76.609   7.574 -19.964  1.00 32.26           N  
ANISOU 1793  N   GLY A1028     4342   4791   3124   -359   1210     58       N  
ATOM   1794  CA  GLY A1028      76.904   6.943 -21.238  1.00 28.14           C  
ANISOU 1794  CA  GLY A1028     3928   4377   2385   -343   1383     61       C  
ATOM   1795  C   GLY A1028      76.011   5.747 -21.506  1.00 41.38           C  
ANISOU 1795  C   GLY A1028     5820   5970   3934   -281   1416   -111       C  
ATOM   1796  O   GLY A1028      76.477   4.683 -21.917  1.00 39.08           O  
ANISOU 1796  O   GLY A1028     5603   5716   3529   -168   1601   -208       O  
ATOM   1797  N   MET A1029      74.717   5.924 -21.266  1.00 39.42           N  
ANISOU 1797  N   MET A1029     5652   5593   3733   -359   1249   -170       N  
ATOM   1798  CA  MET A1029      73.739   4.867 -21.487  1.00 37.29           C  
ANISOU 1798  CA  MET A1029     5542   5218   3406   -354   1272   -371       C  
ATOM   1799  C   MET A1029      72.638   5.329 -22.431  1.00 35.53           C  
ANISOU 1799  C   MET A1029     5385   5054   3060   -484   1105   -411       C  
ATOM   1800  O   MET A1029      72.346   6.522 -22.519  1.00 28.16           O  
ANISOU 1800  O   MET A1029     4388   4163   2147   -555    944   -252       O  
ATOM   1801  CB  MET A1029      73.125   4.418 -20.161  1.00 41.23           C  
ANISOU 1801  CB  MET A1029     6046   5512   4108   -299   1256   -441       C  
ATOM   1802  CG  MET A1029      74.018   3.536 -19.308  1.00 53.44           C  
ANISOU 1802  CG  MET A1029     7589   7002   5713    -98   1446   -437       C  
ATOM   1803  SD  MET A1029      73.271   3.217 -17.697  1.00 69.70           S  
ANISOU 1803  SD  MET A1029     9671   8852   7959      0   1440   -442       S  
ATOM   1804  CE  MET A1029      74.179   1.767 -17.178  1.00 67.47           C  
ANISOU 1804  CE  MET A1029     9418   8497   7721    268   1624   -414       C  
ATOM   1805  N   ASP A1030      72.032   4.381 -23.140  1.00 37.87           N  
ANISOU 1805  N   ASP A1030     5802   5354   3234   -502   1141   -638       N  
ATOM   1806  CA  ASP A1030      70.859   4.679 -23.951  1.00 41.57           C  
ANISOU 1806  CA  ASP A1030     6304   5916   3577   -600    942   -738       C  
ATOM   1807  C   ASP A1030      69.662   4.862 -23.028  1.00 48.35           C  
ANISOU 1807  C   ASP A1030     7092   6600   4679   -669    791   -798       C  
ATOM   1808  O   ASP A1030      69.719   4.494 -21.854  1.00 47.20           O  
ANISOU 1808  O   ASP A1030     6920   6254   4760   -637    886   -801       O  
ATOM   1809  CB  ASP A1030      70.582   3.564 -24.964  1.00 41.30           C  
ANISOU 1809  CB  ASP A1030     6387   5958   3347   -610   1011  -1041       C  
ATOM   1810  CG  ASP A1030      71.772   3.272 -25.860  1.00 53.57           C  
ANISOU 1810  CG  ASP A1030     8013   7685   4656   -509   1194  -1002       C  
ATOM   1811  OD1 ASP A1030      72.648   4.149 -26.003  1.00 65.55           O  
ANISOU 1811  OD1 ASP A1030     9487   9331   6089   -470   1239   -721       O  
ATOM   1812  OD2 ASP A1030      71.826   2.161 -26.428  1.00 58.67           O  
ANISOU 1812  OD2 ASP A1030     8711   8304   5278   -445   1267  -1224       O  
ATOM   1813  N   GLU A1031      68.580   5.429 -23.551  1.00 58.04           N  
ANISOU 1813  N   GLU A1031     8283   7926   5843   -736    564   -835       N  
ATOM   1814  CA  GLU A1031      67.363   5.578 -22.766  1.00 58.32           C  
ANISOU 1814  CA  GLU A1031     8225   7821   6114   -800    431   -917       C  
ATOM   1815  C   GLU A1031      66.804   4.202 -22.421  1.00 53.19           C  
ANISOU 1815  C   GLU A1031     7596   6992   5621   -865    570  -1223       C  
ATOM   1816  O   GLU A1031      67.065   3.222 -23.120  1.00 44.57           O  
ANISOU 1816  O   GLU A1031     6595   5925   4416   -881    692  -1432       O  
ATOM   1817  CB  GLU A1031      66.316   6.407 -23.515  1.00 72.67           C  
ANISOU 1817  CB  GLU A1031     9974   9820   7816   -825    151   -910       C  
ATOM   1818  CG  GLU A1031      65.751   5.737 -24.759  1.00 81.26           C  
ANISOU 1818  CG  GLU A1031    11092  11123   8661   -859     59  -1186       C  
ATOM   1819  CD  GLU A1031      64.467   6.389 -25.237  1.00 93.33           C  
ANISOU 1819  CD  GLU A1031    12501  12833  10129   -859   -249  -1237       C  
ATOM   1820  OE1 GLU A1031      63.710   6.910 -24.389  1.00 95.04           O  
ANISOU 1820  OE1 GLU A1031    12590  12915  10604   -879   -341  -1180       O  
ATOM   1821  OE2 GLU A1031      64.214   6.383 -26.461  1.00 98.02           O  
ANISOU 1821  OE2 GLU A1031    13121  13726  10395   -812   -400  -1336       O  
ATOM   1822  N   GLY A1032      66.039   4.136 -21.337  1.00 43.08           N  
ANISOU 1822  N   GLY A1032     6948   4607   4813   -786    302   -399       N  
ATOM   1823  CA  GLY A1032      65.472   2.884 -20.873  1.00 38.33           C  
ANISOU 1823  CA  GLY A1032     6438   4015   4109   -765    322   -405       C  
ATOM   1824  C   GLY A1032      65.185   2.961 -19.389  1.00 28.76           C  
ANISOU 1824  C   GLY A1032     5102   2847   2979   -753    214   -399       C  
ATOM   1825  O   GLY A1032      65.651   3.877 -18.717  1.00 25.47           O  
ANISOU 1825  O   GLY A1032     4554   2439   2682   -738    120   -403       O  
ATOM   1826  N   VAL A1033      64.415   2.008 -18.875  1.00 27.19           N  
ANISOU 1826  N   VAL A1033     4955   2656   2719   -766    227   -389       N  
ATOM   1827  CA  VAL A1033      64.075   1.996 -17.457  1.00 31.90           C  
ANISOU 1827  CA  VAL A1033     5487   3281   3355   -748    158   -384       C  
ATOM   1828  C   VAL A1033      65.344   1.824 -16.620  1.00 36.78           C  
ANISOU 1828  C   VAL A1033     6182   3801   3994   -663    146   -396       C  
ATOM   1829  O   VAL A1033      66.162   0.948 -16.891  1.00 41.24           O  
ANISOU 1829  O   VAL A1033     6922   4239   4506   -602    247   -386       O  
ATOM   1830  CB  VAL A1033      63.052   0.884 -17.133  1.00 17.56           C  
ANISOU 1830  CB  VAL A1033     3757   1448   1466   -791    202   -363       C  
ATOM   1831  CG1 VAL A1033      63.557  -0.475 -17.603  1.00 36.02           C  
ANISOU 1831  CG1 VAL A1033     6308   3657   3721   -770    311   -367       C  
ATOM   1832  CG2 VAL A1033      62.734   0.865 -15.650  1.00 17.32           C  
ANISOU 1832  CG2 VAL A1033     3707   1428   1446   -771    157   -355       C  
ATOM   1833  N   THR A1034      65.522   2.677 -15.617  1.00 27.73           N  
ANISOU 1833  N   THR A1034     4917   2694   2924   -644     24   -415       N  
ATOM   1834  CA  THR A1034      66.760   2.662 -14.844  1.00 33.40           C  
ANISOU 1834  CA  THR A1034     5712   3307   3672   -573    -37   -426       C  
ATOM   1835  C   THR A1034      66.554   2.235 -13.395  1.00 30.61           C  
ANISOU 1835  C   THR A1034     5424   2960   3247   -534    -94   -438       C  
ATOM   1836  O   THR A1034      65.690   2.757 -12.691  1.00 29.93           O  
ANISOU 1836  O   THR A1034     5230   2982   3161   -556   -157   -459       O  
ATOM   1837  CB  THR A1034      67.447   4.040 -14.861  1.00 32.30           C  
ANISOU 1837  CB  THR A1034     5411   3168   3695   -589   -187   -444       C  
ATOM   1838  OG1 THR A1034      66.629   4.997 -14.180  1.00 44.73           O  
ANISOU 1838  OG1 THR A1034     6796   4885   5315   -611   -290   -485       O  
ATOM   1839  CG2 THR A1034      67.667   4.497 -16.287  1.00 17.54           C  
ANISOU 1839  CG2 THR A1034     3497   1267   1900   -632   -115   -411       C  
ATOM   1840  N   PHE A1035      67.368   1.279 -12.964  1.00 35.57           N  
ANISOU 1840  N   PHE A1035     6256   3449   3811   -450    -47   -415       N  
ATOM   1841  CA  PHE A1035      67.334   0.771 -11.604  1.00 34.35           C  
ANISOU 1841  CA  PHE A1035     6206   3289   3556   -383    -93   -412       C  
ATOM   1842  C   PHE A1035      68.592   1.191 -10.861  1.00 35.41           C  
ANISOU 1842  C   PHE A1035     6185   3490   3781   -247   -244   -335       C  
ATOM   1843  O   PHE A1035      69.646   1.384 -11.470  1.00 32.82           O  
ANISOU 1843  O   PHE A1035     5726   3146   3597   -184   -244   -243       O  
ATOM   1844  CB  PHE A1035      67.196  -0.749 -11.605  1.00 27.71           C  
ANISOU 1844  CB  PHE A1035     5572   2333   2624   -337     96   -352       C  
ATOM   1845  CG  PHE A1035      66.018  -1.243 -12.386  1.00 33.57           C  
ANISOU 1845  CG  PHE A1035     6290   3112   3352   -451    209   -342       C  
ATOM   1846  CD1 PHE A1035      64.773  -1.353 -11.789  1.00 39.58           C  
ANISOU 1846  CD1 PHE A1035     7028   3938   4073   -522    199   -334       C  
ATOM   1847  CD2 PHE A1035      66.151  -1.592 -13.721  1.00 39.17           C  
ANISOU 1847  CD2 PHE A1035     7008   3788   4088   -474    312   -332       C  
ATOM   1848  CE1 PHE A1035      63.683  -1.805 -12.506  1.00 48.74           C  
ANISOU 1848  CE1 PHE A1035     8166   5118   5237   -626    270   -314       C  
ATOM   1849  CE2 PHE A1035      65.065  -2.044 -14.445  1.00 45.09           C  
ANISOU 1849  CE2 PHE A1035     7740   4578   4813   -574    366   -329       C  
ATOM   1850  CZ  PHE A1035      63.828  -2.151 -13.836  1.00 50.41           C  
ANISOU 1850  CZ  PHE A1035     8381   5307   5467   -654    336   -318       C  
ATOM   1851  N   MET A1036      68.484   1.329  -9.545  1.00 33.86           N  
ANISOU 1851  N   MET A1036     5998   3371   3496   -196   -375   -358       N  
ATOM   1852  CA  MET A1036      69.596   1.830  -8.752  1.00 26.22           C  
ANISOU 1852  CA  MET A1036     4884   2481   2599    -90   -576   -308       C  
ATOM   1853  C   MET A1036      69.758   1.096  -7.424  1.00 33.25           C  
ANISOU 1853  C   MET A1036     5869   3430   3333     41   -612   -249       C  
ATOM   1854  O   MET A1036      68.790   0.887  -6.693  1.00 31.72           O  
ANISOU 1854  O   MET A1036     5814   3273   2965     35   -585   -312       O  
ATOM   1855  CB  MET A1036      69.416   3.327  -8.499  1.00 22.41           C  
ANISOU 1855  CB  MET A1036     4266   2062   2187   -171   -802   -442       C  
ATOM   1856  CG  MET A1036      70.458   3.937  -7.580  1.00 29.91           C  
ANISOU 1856  CG  MET A1036     5077   3082   3205    -91  -1068   -429       C  
ATOM   1857  SD  MET A1036      70.109   5.670  -7.233  1.00 44.15           S  
ANISOU 1857  SD  MET A1036     6772   4916   5089   -194  -1330   -627       S  
ATOM   1858  CE  MET A1036      71.326   6.014  -5.965  1.00 48.04           C  
ANISOU 1858  CE  MET A1036     7168   5483   5602    -91  -1662   -619       C  
ATOM   1859  N   PHE A1037      70.994   0.699  -7.133  1.00 25.48           N  
ANISOU 1859  N   PHE A1037     4797   2466   2419    172   -660   -100       N  
ATOM   1860  CA  PHE A1037      71.365   0.180  -5.822  1.00 28.87           C  
ANISOU 1860  CA  PHE A1037     5268   2988   2712    313   -746    -21       C  
ATOM   1861  C   PHE A1037      72.416   1.103  -5.220  1.00 28.52           C  
ANISOU 1861  C   PHE A1037     5029   3046   2761    352  -1057    -15       C  
ATOM   1862  O   PHE A1037      73.272   1.617  -5.938  1.00 33.60           O  
ANISOU 1862  O   PHE A1037     5480   3652   3634    322  -1125     45       O  
ATOM   1863  CB  PHE A1037      71.893  -1.252  -5.925  1.00 29.90           C  
ANISOU 1863  CB  PHE A1037     5469   3050   2843    442   -527    182       C  
ATOM   1864  CG  PHE A1037      72.354  -1.829  -4.614  1.00 36.04           C  
ANISOU 1864  CG  PHE A1037     6266   3937   3490    605   -604    306       C  
ATOM   1865  CD1 PHE A1037      71.459  -2.462  -3.766  1.00 41.94           C  
ANISOU 1865  CD1 PHE A1037     7190   4719   4025    653   -515    300       C  
ATOM   1866  CD2 PHE A1037      73.685  -1.745  -4.231  1.00 31.74           C  
ANISOU 1866  CD2 PHE A1037     5547   3470   3043    715   -765    456       C  
ATOM   1867  CE1 PHE A1037      71.882  -2.996  -2.560  1.00 45.61           C  
ANISOU 1867  CE1 PHE A1037     7672   5306   4352    822   -576    435       C  
ATOM   1868  CE2 PHE A1037      74.113  -2.276  -3.028  1.00 45.17           C  
ANISOU 1868  CE2 PHE A1037     7261   5295   4609    869   -849    585       C  
ATOM   1869  CZ  PHE A1037      73.210  -2.903  -2.192  1.00 46.47           C  
ANISOU 1869  CZ  PHE A1037     7617   5504   4536    930   -749    571       C  
ATOM   1870  N   ILE A1038      72.358   1.312  -3.909  1.00 36.56           N  
ANISOU 1870  N   ILE A1038     6097   4192   3605    421  -1251    -69       N  
ATOM   1871  CA  ILE A1038      73.220   2.301  -3.263  1.00 42.04           C  
ANISOU 1871  CA  ILE A1038     6631   4976   4367    430  -1602   -115       C  
ATOM   1872  C   ILE A1038      73.916   1.741  -2.013  1.00 60.81           C  
ANISOU 1872  C   ILE A1038     9022   7491   6590    593  -1749      3       C  
ATOM   1873  O   ILE A1038      74.944   2.263  -1.578  1.00 79.74           O  
ANISOU 1873  O   ILE A1038    11255   9958   9085    613  -2039     40       O  
ATOM   1874  CB  ILE A1038      72.404   3.570  -2.896  1.00 43.51           C  
ANISOU 1874  CB  ILE A1038     6866   5186   4479    328  -1785   -380       C  
ATOM   1875  CG1 ILE A1038      73.300   4.679  -2.331  1.00 49.27           C  
ANISOU 1875  CG1 ILE A1038     7438   5966   5318    307  -2175   -462       C  
ATOM   1876  CG2 ILE A1038      71.290   3.225  -1.928  1.00 56.16           C  
ANISOU 1876  CG2 ILE A1038     8712   6868   5757    401  -1709   -470       C  
ATOM   1877  CD1 ILE A1038      74.319   5.212  -3.311  1.00 49.73           C  
ANISOU 1877  CD1 ILE A1038     7218   5934   5745    222  -2257   -359       C  
ATOM   1878  N   GLY A1039      73.373   0.664  -1.455  1.00 34.15           N  
ANISOU 1878  N   GLY A1039     5829   4156   2991    708  -1553     84       N  
ATOM   1879  CA  GLY A1039      73.908   0.082  -0.231  1.00 58.27           C  
ANISOU 1879  CA  GLY A1039     8912   7364   5863    882  -1665    213       C  
ATOM   1880  C   GLY A1039      75.335  -0.451  -0.277  1.00 55.78           C  
ANISOU 1880  C   GLY A1039     8405   7074   5714    977  -1723    471       C  
ATOM   1881  O   GLY A1039      76.018  -0.367  -1.298  1.00 62.26           O  
ANISOU 1881  O   GLY A1039     9057   7785   6816    919  -1669    565       O  
ATOM   1882  N   ARG A1040      75.782  -1.003   0.849  1.00 58.87           N  
ANISOU 1882  N   ARG A1040     8818   7623   5928   1140  -1825    607       N  
ATOM   1883  CA  ARG A1040      77.121  -1.579   0.976  1.00 54.77           C  
ANISOU 1883  CA  ARG A1040     8109   7156   5545   1255  -1885    891       C  
ATOM   1884  C   ARG A1040      77.172  -2.980   0.363  1.00 56.81           C  
ANISOU 1884  C   ARG A1040     8410   7291   5886   1356  -1475   1137       C  
ATOM   1885  O   ARG A1040      76.140  -3.636   0.225  1.00 59.93           O  
ANISOU 1885  O   ARG A1040     9010   7602   6158   1361  -1193   1092       O  
ATOM   1886  CB  ARG A1040      77.535  -1.631   2.451  1.00 61.45           C  
ANISOU 1886  CB  ARG A1040     8968   8237   6143   1398  -2164    948       C  
ATOM   1887  CG  ARG A1040      79.002  -1.952   2.696  1.00 79.78           C  
ANISOU 1887  CG  ARG A1040    11044  10650   8618   1495  -2331   1235       C  
ATOM   1888  CD  ARG A1040      79.229  -2.451   4.116  1.00 92.55           C  
ANISOU 1888  CD  ARG A1040    12723  12506   9934   1681  -2486   1356       C  
ATOM   1889  NE  ARG A1040      80.646  -2.656   4.408  1.00105.37           N  
ANISOU 1889  NE  ARG A1040    14086  14241  11708   1762  -2698   1638       N  
ATOM   1890  CZ  ARG A1040      81.315  -3.775   4.144  1.00108.61           C  
ANISOU 1890  CZ  ARG A1040    14382  14623  12261   1900  -2448   1994       C  
ATOM   1891  NH1 ARG A1040      80.700  -4.802   3.575  1.00114.43           N  
ANISOU 1891  NH1 ARG A1040    15264  15204  13009   1967  -1985   2084       N  
ATOM   1892  NH2 ARG A1040      82.604  -3.866   4.447  1.00103.33           N  
ANISOU 1892  NH2 ARG A1040    13448  14063  11750   1954  -2657   2257       N  
ATOM   1893  N   PHE A1041      78.367  -3.440  -0.001  1.00 57.80           N  
ANISOU 1893  N   PHE A1041     8339   7391   6230   1437  -1440   1403       N  
ATOM   1894  CA  PHE A1041      78.521  -4.763  -0.605  1.00 52.46           C  
ANISOU 1894  CA  PHE A1041     7712   6573   5648   1552  -1044   1637       C  
ATOM   1895  C   PHE A1041      78.736  -5.839   0.455  1.00 58.87           C  
ANISOU 1895  C   PHE A1041     8575   7500   6293   1757   -972   1871       C  
ATOM   1896  O   PHE A1041      79.866  -6.109   0.864  1.00 56.13           O  
ANISOU 1896  O   PHE A1041     8041   7257   6028   1886  -1080   2130       O  
ATOM   1897  CB  PHE A1041      79.683  -4.781  -1.602  1.00 56.11           C  
ANISOU 1897  CB  PHE A1041     7947   6934   6439   1572   -976   1838       C  
ATOM   1898  CG  PHE A1041      79.405  -4.039  -2.885  1.00 50.28           C  
ANISOU 1898  CG  PHE A1041     7185   6045   5876   1408   -912   1666       C  
ATOM   1899  CD1 PHE A1041      78.238  -3.309  -3.054  1.00 49.46           C  
ANISOU 1899  CD1 PHE A1041     7227   5912   5651   1239   -962   1350       C  
ATOM   1900  CD2 PHE A1041      80.313  -4.086  -3.928  1.00 41.83           C  
ANISOU 1900  CD2 PHE A1041     5939   4867   5087   1444   -783   1848       C  
ATOM   1901  CE1 PHE A1041      77.991  -2.632  -4.234  1.00 43.78           C  
ANISOU 1901  CE1 PHE A1041     6474   5072   5089   1098   -902   1218       C  
ATOM   1902  CE2 PHE A1041      80.073  -3.414  -5.109  1.00 40.95           C  
ANISOU 1902  CE2 PHE A1041     5804   4636   5118   1316   -713   1715       C  
ATOM   1903  CZ  PHE A1041      78.910  -2.686  -5.263  1.00 43.91           C  
ANISOU 1903  CZ  PHE A1041     6320   4993   5369   1138   -780   1398       C  
ATOM   1904  N   ASP A1042      77.642  -6.451   0.893  1.00 65.00           N  
ANISOU 1904  N   ASP A1042     9587   8261   6850   1791   -785   1806       N  
ATOM   1905  CA  ASP A1042      77.697  -7.489   1.915  1.00 56.93           C  
ANISOU 1905  CA  ASP A1042     8627   7346   5659   1995   -685   2037       C  
ATOM   1906  C   ASP A1042      77.098  -8.796   1.414  1.00 66.08           C  
ANISOU 1906  C   ASP A1042     9951   8284   6871   2050   -238   2151       C  
ATOM   1907  O   ASP A1042      76.361  -8.813   0.428  1.00 75.99           O  
ANISOU 1907  O   ASP A1042    11327   9331   8216   1908    -47   1984       O  
ATOM   1908  CB  ASP A1042      76.950  -7.046   3.176  1.00 50.34           C  
ANISOU 1908  CB  ASP A1042     7916   6727   4484   2026   -891   1895       C  
ATOM   1909  CG  ASP A1042      77.432  -5.714   3.708  1.00 78.31           C  
ANISOU 1909  CG  ASP A1042    11343  10460   7950   1959  -1354   1725       C  
ATOM   1910  OD1 ASP A1042      78.415  -5.700   4.478  1.00 91.87           O  
ANISOU 1910  OD1 ASP A1042    12917  12367   9623   2073  -1601   1891       O  
ATOM   1911  OD2 ASP A1042      76.817  -4.681   3.366  1.00 84.99           O  
ANISOU 1911  OD2 ASP A1042    12242  11262   8789   1789  -1479   1427       O  
ATOM   1912  N   ARG A1043      77.413  -9.889   2.099  1.00 64.10           N  
ANISOU 1912  N   ARG A1043     9689   8077   6590   2224    -85   2409       N  
ATOM   1913  CA  ARG A1043      76.702 -11.141   1.885  1.00 61.52           C  
ANISOU 1913  CA  ARG A1043     9496   7554   6324   2227    304   2447       C  
ATOM   1914  C   ARG A1043      75.791 -11.404   3.074  1.00 54.88           C  
ANISOU 1914  C   ARG A1043     8750   6857   5245   2273    302   2424       C  
ATOM   1915  O   ARG A1043      76.252 -11.791   4.145  1.00 66.17           O  
ANISOU 1915  O   ARG A1043    10082   8475   6584   2405    236   2584       O  
ATOM   1916  CB  ARG A1043      77.669 -12.312   1.685  1.00 66.04           C  
ANISOU 1916  CB  ARG A1043     9938   8033   7121   2332    534   2684       C  
ATOM   1917  CG  ARG A1043      78.241 -12.436   0.278  1.00 64.23           C  
ANISOU 1917  CG  ARG A1043     9673   7577   7156   2278    701   2674       C  
ATOM   1918  CD  ARG A1043      78.875 -13.801   0.073  1.00 62.15           C  
ANISOU 1918  CD  ARG A1043     9347   7189   7077   2382   1008   2851       C  
ATOM   1919  NE  ARG A1043      79.661 -13.875  -1.157  1.00 61.90           N  
ANISOU 1919  NE  ARG A1043     9246   7001   7272   2368   1146   2859       N  
ATOM   1920  CZ  ARG A1043      79.203 -14.345  -2.314  1.00 66.21           C  
ANISOU 1920  CZ  ARG A1043     9945   7295   7916   2292   1406   2704       C  
ATOM   1921  NH1 ARG A1043      77.957 -14.789  -2.403  1.00 64.79           N  
ANISOU 1921  NH1 ARG A1043     9983   6975   7661   2201   1540   2536       N  
ATOM   1922  NH2 ARG A1043      79.991 -14.370  -3.380  1.00 71.10           N  
ANISOU 1922  NH2 ARG A1043    10495   7815   8707   2307   1525   2716       N  
ATOM   1923  N   GLY A1044      74.497 -11.174   2.886  1.00 54.01           N  
ANISOU 1923  N   GLY A1044     8817   6662   5041   2161    378   2230       N  
ATOM   1924  CA  GLY A1044      73.520 -11.448   3.922  1.00 63.02           C  
ANISOU 1924  CA  GLY A1044    10033   7915   5996   2201    425   2215       C  
ATOM   1925  C   GLY A1044      73.094 -10.230   4.719  1.00 70.34           C  
ANISOU 1925  C   GLY A1044    10994   9085   6648   2186    124   2031       C  
ATOM   1926  O   GLY A1044      72.613 -10.361   5.844  1.00 78.14           O  
ANISOU 1926  O   GLY A1044    11996  10238   7455   2271    111   2051       O  
ATOM   1927  N   GLN A1045      73.264  -9.042   4.144  1.00 72.44           N  
ANISOU 1927  N   GLN A1045    11269   9362   6892   2081   -112   1839       N  
ATOM   1928  CA  GLN A1045      72.906  -7.804   4.835  1.00 62.20           C  
ANISOU 1928  CA  GLN A1045     9997   8268   5367   2042   -415   1608       C  
ATOM   1929  C   GLN A1045      72.179  -6.819   3.917  1.00 51.85           C  
ANISOU 1929  C   GLN A1045     8786   6836   4080   1859   -471   1341       C  
ATOM   1930  O   GLN A1045      70.973  -6.614   4.052  1.00 47.62           O  
ANISOU 1930  O   GLN A1045     8355   6279   3462   1785   -374   1199       O  
ATOM   1931  CB  GLN A1045      74.156  -7.149   5.430  1.00 69.76           C  
ANISOU 1931  CB  GLN A1045    10798   9437   6271   2103   -779   1625       C  
ATOM   1932  CG  GLN A1045      74.851  -8.001   6.487  1.00 78.68           C  
ANISOU 1932  CG  GLN A1045    11826  10728   7342   2271   -767   1875       C  
ATOM   1933  CD  GLN A1045      76.304  -7.623   6.688  1.00 84.53           C  
ANISOU 1933  CD  GLN A1045    12367  11602   8147   2303  -1079   1975       C  
ATOM   1934  OE1 GLN A1045      76.660  -6.445   6.680  1.00 88.76           O  
ANISOU 1934  OE1 GLN A1045    12846  12218   8661   2206  -1421   1787       O  
ATOM   1935  NE2 GLN A1045      77.156  -8.628   6.863  1.00 87.61           N  
ANISOU 1935  NE2 GLN A1045    12631  12001   8654   2422   -961   2273       N  
ATOM   1936  N   LYS A1046      72.912  -6.209   2.990  1.00 49.51           N  
ANISOU 1936  N   LYS A1046     8356   6451   4003   1724   -601   1245       N  
ATOM   1937  CA  LYS A1046      72.313  -5.272   2.042  1.00 43.67           C  
ANISOU 1937  CA  LYS A1046     7628   5588   3376   1502   -638    977       C  
ATOM   1938  C   LYS A1046      71.847  -5.988   0.776  1.00 42.96           C  
ANISOU 1938  C   LYS A1046     7589   5234   3500   1384   -316    998       C  
ATOM   1939  O   LYS A1046      71.034  -5.462   0.016  1.00 45.24           O  
ANISOU 1939  O   LYS A1046     7927   5416   3847   1209   -275    806       O  
ATOM   1940  CB  LYS A1046      73.298  -4.158   1.689  1.00 42.47           C  
ANISOU 1940  CB  LYS A1046     7294   5480   3361   1415   -949    864       C  
ATOM   1941  CG  LYS A1046      73.627  -3.245   2.856  1.00 47.40           C  
ANISOU 1941  CG  LYS A1046     7895   6338   3777   1481  -1324    761       C  
ATOM   1942  CD  LYS A1046      72.363  -2.645   3.445  1.00 46.66           C  
ANISOU 1942  CD  LYS A1046     7988   6309   3430   1464  -1347    542       C  
ATOM   1943  CE  LYS A1046      72.664  -1.839   4.692  1.00 62.52           C  
ANISOU 1943  CE  LYS A1046     9944   8525   5285   1500  -1639    412       C  
ATOM   1944  NZ  LYS A1046      71.421  -1.327   5.332  1.00 71.28           N  
ANISOU 1944  NZ  LYS A1046    11159   9670   6256   1466  -1548    219       N  
ATOM   1945  N   GLY A1047      72.377  -7.186   0.555  1.00 44.61           N  
ANISOU 1945  N   GLY A1047     7791   5335   3822   1487    -95   1232       N  
ATOM   1946  CA  GLY A1047      71.896  -8.055  -0.503  1.00 48.37           C  
ANISOU 1946  CA  GLY A1047     8367   5547   4465   1403    221   1254       C  
ATOM   1947  C   GLY A1047      72.257  -7.650  -1.919  1.00 45.81           C  
ANISOU 1947  C   GLY A1047     7986   5064   4353   1257    241   1138       C  
ATOM   1948  O   GLY A1047      71.446  -7.798  -2.834  1.00 44.91           O  
ANISOU 1948  O   GLY A1047     7983   4774   4306   1110    398   1014       O  
ATOM   1949  N   VAL A1048      73.473  -7.151  -2.114  1.00 36.74           N  
ANISOU 1949  N   VAL A1048     6660   3985   3316   1302     81   1195       N  
ATOM   1950  CA  VAL A1048      73.928  -6.822  -3.459  1.00 36.24           C  
ANISOU 1950  CA  VAL A1048     6527   3783   3461   1206    132   1138       C  
ATOM   1951  C   VAL A1048      74.193  -8.114  -4.233  1.00 38.89           C  
ANISOU 1951  C   VAL A1048     6961   3894   3922   1285    470   1291       C  
ATOM   1952  O   VAL A1048      74.162  -8.128  -5.463  1.00 41.85           O  
ANISOU 1952  O   VAL A1048     7381   4104   4415   1204    607   1212       O  
ATOM   1953  CB  VAL A1048      75.195  -5.934  -3.446  1.00 36.36           C  
ANISOU 1953  CB  VAL A1048     6292   3925   3600   1241   -125   1199       C  
ATOM   1954  CG1 VAL A1048      76.422  -6.742  -3.041  1.00 47.41           C  
ANISOU 1954  CG1 VAL A1048     7576   5359   5079   1448    -75   1508       C  
ATOM   1955  CG2 VAL A1048      75.406  -5.285  -4.808  1.00 34.92           C  
ANISOU 1955  CG2 VAL A1048     6030   3628   3608   1119    -99   1104       C  
ATOM   1956  N   ASP A1049      74.433  -9.202  -3.503  1.00 42.50           N  
ANISOU 1956  N   ASP A1049     7464   4341   4342   1453    610   1507       N  
ATOM   1957  CA  ASP A1049      74.633 -10.513  -4.113  1.00 44.36           C  
ANISOU 1957  CA  ASP A1049     7821   4337   4697   1545    948   1653       C  
ATOM   1958  C   ASP A1049      73.357 -10.983  -4.806  1.00 40.37           C  
ANISOU 1958  C   ASP A1049     7540   3616   4181   1381   1137   1464       C  
ATOM   1959  O   ASP A1049      73.400 -11.563  -5.897  1.00 50.89           O  
ANISOU 1959  O   ASP A1049     8927   4769   5642   1327   1328   1380       O  
ATOM   1960  CB  ASP A1049      75.079 -11.536  -3.063  1.00 55.84           C  
ANISOU 1960  CB  ASP A1049     9214   5866   6138   1727   1034   1891       C  
ATOM   1961  CG  ASP A1049      74.282 -11.440  -1.772  1.00 67.06           C  
ANISOU 1961  CG  ASP A1049    10686   7452   7341   1750    917   1900       C  
ATOM   1962  OD1 ASP A1049      73.228 -10.771  -1.764  1.00 77.71           O  
ANISOU 1962  OD1 ASP A1049    12140   8820   8566   1608    825   1701       O  
ATOM   1963  OD2 ASP A1049      74.709 -12.040  -0.763  1.00 67.79           O  
ANISOU 1963  OD2 ASP A1049    10684   7678   7394   1898    920   2087       O  
ATOM   1964  N   VAL A1050      72.224 -10.715  -4.164  1.00 36.98           N  
ANISOU 1964  N   VAL A1050     7186   3259   3607   1283   1054   1357       N  
ATOM   1965  CA  VAL A1050      70.918 -11.027  -4.729  1.00 42.13           C  
ANISOU 1965  CA  VAL A1050     8013   3736   4260   1101   1181   1190       C  
ATOM   1966  C   VAL A1050      70.706 -10.270  -6.034  1.00 37.09           C  
ANISOU 1966  C   VAL A1050     7398   3019   3676    920   1134    967       C  
ATOM   1967  O   VAL A1050      70.219 -10.832  -7.018  1.00 48.33           O  
ANISOU 1967  O   VAL A1050     8933   4256   5176    806   1285    847       O  
ATOM   1968  CB  VAL A1050      69.781 -10.680  -3.748  1.00 39.68           C  
ANISOU 1968  CB  VAL A1050     7729   3559   3787   1043   1081   1144       C  
ATOM   1969  CG1 VAL A1050      68.430 -11.018  -4.358  1.00 44.62           C  
ANISOU 1969  CG1 VAL A1050     8485   4009   4458    839   1199    998       C  
ATOM   1970  CG2 VAL A1050      69.972 -11.418  -2.436  1.00 37.54           C  
ANISOU 1970  CG2 VAL A1050     7412   3403   3447   1236   1128   1366       C  
ATOM   1971  N   LEU A1051      71.087  -8.996  -6.039  1.00 32.98           N  
ANISOU 1971  N   LEU A1051     6713   2688   3131    883    895    878       N  
ATOM   1972  CA  LEU A1051      70.936  -8.161  -7.225  1.00 34.16           C  
ANISOU 1972  CA  LEU A1051     6841   2800   3338    727    839    691       C  
ATOM   1973  C   LEU A1051      71.847  -8.611  -8.360  1.00 39.46           C  
ANISOU 1973  C   LEU A1051     7533   3316   4143    800   1007    753       C  
ATOM   1974  O   LEU A1051      71.424  -8.651  -9.511  1.00 46.36           O  
ANISOU 1974  O   LEU A1051     8523   4050   5041    688   1107    617       O  
ATOM   1975  CB  LEU A1051      71.210  -6.692  -6.898  1.00 30.85           C  
ANISOU 1975  CB  LEU A1051     6223   2602   2897    685    548    609       C  
ATOM   1976  CG  LEU A1051      71.178  -5.762  -8.116  1.00 36.98           C  
ANISOU 1976  CG  LEU A1051     6939   3354   3760    546    494    457       C  
ATOM   1977  CD1 LEU A1051      69.837  -5.853  -8.835  1.00 27.54           C  
ANISOU 1977  CD1 LEU A1051     5905   2046   2513    356    586    283       C  
ATOM   1978  CD2 LEU A1051      71.480  -4.328  -7.717  1.00 28.16           C  
ANISOU 1978  CD2 LEU A1051     5616   2426   2657    507    205    388       C  
ATOM   1979  N   LEU A1052      73.096  -8.938  -8.044  1.00 35.48           N  
ANISOU 1979  N   LEU A1052     6916   2846   3717   1000   1041    968       N  
ATOM   1980  CA  LEU A1052      74.033  -9.381  -9.072  1.00 43.58           C  
ANISOU 1980  CA  LEU A1052     7955   3730   4874   1113   1234   1066       C  
ATOM   1981  C   LEU A1052      73.563 -10.699  -9.685  1.00 47.45           C  
ANISOU 1981  C   LEU A1052     8602   4057   5369   1081   1488    968       C  
ATOM   1982  O   LEU A1052      73.546 -10.863 -10.913  1.00 52.46           O  
ANISOU 1982  O   LEU A1052     9311   4598   6022   1034   1608    846       O  
ATOM   1983  CB  LEU A1052      75.443  -9.524  -8.493  1.00 42.92           C  
ANISOU 1983  CB  LEU A1052     7662   3753   4893   1331   1211   1339       C  
ATOM   1984  CG  LEU A1052      76.074  -8.236  -7.953  1.00 40.47           C  
ANISOU 1984  CG  LEU A1052     7074   3685   4618   1321    890   1379       C  
ATOM   1985  CD1 LEU A1052      77.456  -8.505  -7.378  1.00 44.27           C  
ANISOU 1985  CD1 LEU A1052     7351   4256   5215   1533    863   1685       C  
ATOM   1986  CD2 LEU A1052      76.139  -7.163  -9.029  1.00 38.12           C  
ANISOU 1986  CD2 LEU A1052     6682   3396   4405   1204    810   1245       C  
ATOM   1987  N   LYS A1053      73.158 -11.626  -8.822  1.00 51.85           N  
ANISOU 1987  N   LYS A1053     9215   4589   5898   1112   1558   1027       N  
ATOM   1988  CA  LYS A1053      72.647 -12.915  -9.273  1.00 60.34           C  
ANISOU 1988  CA  LYS A1053    10436   5496   6992   1076   1772    945       C  
ATOM   1989  C   LYS A1053      71.403 -12.747 -10.151  1.00 59.15           C  
ANISOU 1989  C   LYS A1053    10435   5264   6774    840   1749    687       C  
ATOM   1990  O   LYS A1053      71.279 -13.387 -11.201  1.00 65.35           O  
ANISOU 1990  O   LYS A1053    11337   5933   7562    792   1882    576       O  
ATOM   1991  CB  LYS A1053      72.332 -13.808  -8.072  1.00 58.27           C  
ANISOU 1991  CB  LYS A1053    10175   5233   6731   1142   1825   1075       C  
ATOM   1992  CG  LYS A1053      72.060 -15.259  -8.423  1.00 60.73           C  
ANISOU 1992  CG  LYS A1053    10607   5358   7109   1144   2054   1049       C  
ATOM   1993  CD  LYS A1053      73.236 -15.877  -9.161  1.00 66.50           C  
ANISOU 1993  CD  LYS A1053    11331   6016   7921   1299   2240   1121       C  
ATOM   1994  CE  LYS A1053      73.256 -17.391  -8.999  1.00 69.35           C  
ANISOU 1994  CE  LYS A1053    11770   6222   8358   1378   2465   1193       C  
ATOM   1995  NZ  LYS A1053      71.947 -18.013  -9.342  1.00 67.50           N  
ANISOU 1995  NZ  LYS A1053    11710   5828   8108   1184   2496   1016       N  
ATOM   1996  N   ALA A1054      70.491 -11.876  -9.723  1.00 39.75           N  
ANISOU 1996  N   ALA A1054     7615   2800   4690    261   1949    -50       N  
ATOM   1997  CA  ALA A1054      69.266 -11.615 -10.477  1.00 46.76           C  
ANISOU 1997  CA  ALA A1054     8403   3704   5662     87   1924   -174       C  
ATOM   1998  C   ALA A1054      69.567 -10.948 -11.819  1.00 40.54           C  
ANISOU 1998  C   ALA A1054     7486   2990   4927     94   1767   -203       C  
ATOM   1999  O   ALA A1054      68.873 -11.178 -12.811  1.00 44.35           O  
ANISOU 1999  O   ALA A1054     7964   3440   5447    -17   1765   -323       O  
ATOM   2000  CB  ALA A1054      68.314 -10.755  -9.661  1.00 46.97           C  
ANISOU 2000  CB  ALA A1054     8315   3783   5749     -2   1856   -199       C  
ATOM   2001  N   ILE A1055      70.603 -10.117 -11.840  1.00 31.65           N  
ANISOU 2001  N   ILE A1055     6263   1955   3809    225   1629   -101       N  
ATOM   2002  CA  ILE A1055      71.049  -9.475 -13.067  1.00 37.50           C  
ANISOU 2002  CA  ILE A1055     6902   2756   4589    258   1513   -101       C  
ATOM   2003  C   ILE A1055      71.551 -10.539 -14.029  1.00 46.87           C  
ANISOU 2003  C   ILE A1055     8256   3853   5701    301   1682   -132       C  
ATOM   2004  O   ILE A1055      71.281 -10.481 -15.231  1.00 54.88           O  
ANISOU 2004  O   ILE A1055     9288   4860   6705    244   1659   -222       O  
ATOM   2005  CB  ILE A1055      72.152  -8.430 -12.797  1.00 34.96           C  
ANISOU 2005  CB  ILE A1055     6425   2532   4327    399   1356     32       C  
ATOM   2006  CG1 ILE A1055      71.526  -7.119 -12.318  1.00 33.76           C  
ANISOU 2006  CG1 ILE A1055     6080   2468   4281    324   1146     34       C  
ATOM   2007  CG2 ILE A1055      72.986  -8.182 -14.044  1.00 29.84           C  
ANISOU 2007  CG2 ILE A1055     5737   1908   3694    488   1345     74       C  
ATOM   2008  CD1 ILE A1055      72.534  -6.026 -12.030  1.00 28.01           C  
ANISOU 2008  CD1 ILE A1055     5173   1821   3650    432    961    162       C  
ATOM   2009  N   GLU A1056      72.266 -11.524 -13.493  1.00 47.17           N  
ANISOU 2009  N   GLU A1056     8429   3806   5687    403   1849    -67       N  
ATOM   2010  CA  GLU A1056      72.714 -12.645 -14.311  1.00 50.96           C  
ANISOU 2010  CA  GLU A1056     9077   4170   6115    444   2042    -98       C  
ATOM   2011  C   GLU A1056      71.529 -13.449 -14.845  1.00 51.65           C  
ANISOU 2011  C   GLU A1056     9286   4160   6179    264   2128   -270       C  
ATOM   2012  O   GLU A1056      71.539 -13.880 -15.997  1.00 60.43           O  
ANISOU 2012  O   GLU A1056    10493   5216   7253    237   2186   -370       O  
ATOM   2013  CB  GLU A1056      73.658 -13.550 -13.519  1.00 49.41           C  
ANISOU 2013  CB  GLU A1056     8984   3882   5907    591   2194      7       C  
ATOM   2014  CG  GLU A1056      75.045 -12.959 -13.339  1.00 60.66           C  
ANISOU 2014  CG  GLU A1056    10280   5370   7397    789   2117    152       C  
ATOM   2015  CD  GLU A1056      75.988 -13.889 -12.609  1.00 79.51           C  
ANISOU 2015  CD  GLU A1056    12752   7646   9811    942   2238    245       C  
ATOM   2016  OE1 GLU A1056      77.217 -13.699 -12.728  1.00 87.87           O  
ANISOU 2016  OE1 GLU A1056    13707   8710  10969   1110   2219    355       O  
ATOM   2017  OE2 GLU A1056      75.503 -14.807 -11.914  1.00 88.40           O  
ANISOU 2017  OE2 GLU A1056    14036   8667  10884    896   2351    213       O  
ATOM   2018  N   ILE A1057      70.509 -13.642 -14.013  1.00 46.21           N  
ANISOU 2018  N   ILE A1057     8592   3446   5520    144   2137   -316       N  
ATOM   2019  CA  ILE A1057      69.301 -14.338 -14.452  1.00 45.56           C  
ANISOU 2019  CA  ILE A1057     8573   3270   5466    -34   2196   -491       C  
ATOM   2020  C   ILE A1057      68.621 -13.584 -15.596  1.00 56.83           C  
ANISOU 2020  C   ILE A1057     9898   4765   6929   -142   2002   -632       C  
ATOM   2021  O   ILE A1057      68.136 -14.189 -16.553  1.00 71.24           O  
ANISOU 2021  O   ILE A1057    11815   6515   8737   -235   2018   -800       O  
ATOM   2022  CB  ILE A1057      68.295 -14.522 -13.294  1.00 47.06           C  
ANISOU 2022  CB  ILE A1057     8739   3427   5714   -135   2254   -505       C  
ATOM   2023  CG1 ILE A1057      68.895 -15.401 -12.195  1.00 49.61           C  
ANISOU 2023  CG1 ILE A1057     9216   3660   5974    -34   2454   -388       C  
ATOM   2024  CG2 ILE A1057      66.993 -15.132 -13.800  1.00 40.62           C  
ANISOU 2024  CG2 ILE A1057     7937   2516   4982   -320   2290   -701       C  
ATOM   2025  CD1 ILE A1057      67.948 -15.674 -11.042  1.00 40.67           C  
ANISOU 2025  CD1 ILE A1057     8109   2475   4869   -123   2566   -399       C  
ATOM   2026  N   LEU A1058      68.607 -12.258 -15.498  1.00 49.45           N  
ANISOU 2026  N   LEU A1058     8780   3967   6042   -126   1803   -573       N  
ATOM   2027  CA  LEU A1058      67.928 -11.417 -16.480  1.00 35.09           C  
ANISOU 2027  CA  LEU A1058     6850   2210   4272   -226   1588   -692       C  
ATOM   2028  C   LEU A1058      68.720 -11.237 -17.772  1.00 44.10           C  
ANISOU 2028  C   LEU A1058     8134   3347   5274   -167   1613   -709       C  
ATOM   2029  O   LEU A1058      68.140 -10.981 -18.826  1.00 52.66           O  
ANISOU 2029  O   LEU A1058     9296   4414   6298   -287   1534   -857       O  
ATOM   2030  CB  LEU A1058      67.631 -10.044 -15.878  1.00 31.75           C  
ANISOU 2030  CB  LEU A1058     6198   1901   3964   -233   1395   -611       C  
ATOM   2031  CG  LEU A1058      66.554  -9.966 -14.799  1.00 31.80           C  
ANISOU 2031  CG  LEU A1058     6102   1892   4087   -331   1404   -631       C  
ATOM   2032  CD1 LEU A1058      66.575  -8.602 -14.139  1.00 33.14           C  
ANISOU 2032  CD1 LEU A1058     6072   2172   4348   -296   1244   -528       C  
ATOM   2033  CD2 LEU A1058      65.189 -10.246 -15.397  1.00 39.56           C  
ANISOU 2033  CD2 LEU A1058     7048   2803   5181   -508   1332   -819       C  
ATOM   2034  N   SER A1059      70.040 -11.377 -17.689  1.00 43.99           N  
ANISOU 2034  N   SER A1059     8206   3327   5182     10   1760   -559       N  
ATOM   2035  CA  SER A1059      70.922 -11.094 -18.822  1.00 45.24           C  
ANISOU 2035  CA  SER A1059     8541   3459   5189    104   1870   -528       C  
ATOM   2036  C   SER A1059      70.655 -11.980 -20.043  1.00 46.85           C  
ANISOU 2036  C   SER A1059     9006   3560   5235     18   1993   -721       C  
ATOM   2037  O   SER A1059      71.051 -11.643 -21.158  1.00 41.62           O  
ANISOU 2037  O   SER A1059     8523   2893   4399     47   2053   -755       O  
ATOM   2038  CB  SER A1059      72.386 -11.237 -18.396  1.00 49.49           C  
ANISOU 2038  CB  SER A1059     9075   3994   5734    334   2021   -323       C  
ATOM   2039  OG  SER A1059      72.668 -12.558 -17.969  1.00 66.04           O  
ANISOU 2039  OG  SER A1059    11256   5994   7843    369   2179   -329       O  
ATOM   2040  N   SER A1060      69.984 -13.107 -19.830  1.00 56.58           N  
ANISOU 2040  N   SER A1060    10270   4714   6513    -82   2030   -855       N  
ATOM   2041  CA  SER A1060      69.664 -14.020 -20.923  1.00 57.40           C  
ANISOU 2041  CA  SER A1060    10605   4723   6481   -174   2118  -1070       C  
ATOM   2042  C   SER A1060      68.348 -13.643 -21.597  1.00 57.50           C  
ANISOU 2042  C   SER A1060    10610   4772   6467   -392   1890  -1293       C  
ATOM   2043  O   SER A1060      68.070 -14.069 -22.716  1.00 67.72           O  
ANISOU 2043  O   SER A1060    12115   6028   7588   -487   1890  -1494       O  
ATOM   2044  CB  SER A1060      69.599 -15.460 -20.414  1.00 57.70           C  
ANISOU 2044  CB  SER A1060    10689   4636   6598   -169   2269  -1115       C  
ATOM   2045  OG  SER A1060      68.575 -15.608 -19.447  1.00 54.29           O  
ANISOU 2045  OG  SER A1060    10073   4212   6342   -271   2147  -1142       O  
ATOM   2046  N   LYS A1061      67.543 -12.840 -20.908  1.00 48.80           N  
ANISOU 2046  N   LYS A1061     9260   3741   5541   -471   1680  -1261       N  
ATOM   2047  CA  LYS A1061      66.238 -12.432 -21.419  1.00 51.14           C  
ANISOU 2047  CA  LYS A1061     9485   4055   5890   -679   1425  -1451       C  
ATOM   2048  C   LYS A1061      66.333 -11.233 -22.359  1.00 54.45           C  
ANISOU 2048  C   LYS A1061     9981   4564   6141   -741   1264  -1462       C  
ATOM   2049  O   LYS A1061      67.214 -10.384 -22.214  1.00 66.16           O  
ANISOU 2049  O   LYS A1061    11462   6107   7568   -612   1314  -1277       O  
ATOM   2050  CB  LYS A1061      65.296 -12.106 -20.258  1.00 50.52           C  
ANISOU 2050  CB  LYS A1061     9087   3996   6113   -726   1279  -1401       C  
ATOM   2051  CG  LYS A1061      64.997 -13.284 -19.344  1.00 54.52           C  
ANISOU 2051  CG  LYS A1061     9557   4413   6747   -700   1416  -1404       C  
ATOM   2052  CD  LYS A1061      64.073 -12.872 -18.206  1.00 63.31           C  
ANISOU 2052  CD  LYS A1061    10449   5528   8079   -763   1358  -1344       C  
ATOM   2053  CE  LYS A1061      63.611 -14.072 -17.394  1.00 69.36           C  
ANISOU 2053  CE  LYS A1061    11293   6153   8907   -810   1594  -1374       C  
ATOM   2054  NZ  LYS A1061      64.768 -14.829 -16.853  1.00 75.16           N  
ANISOU 2054  NZ  LYS A1061    12195   6856   9506   -669   1864  -1233       N  
ATOM   2055  N   LYS A1062      65.408 -11.162 -23.312  1.00 53.80           N  
ANISOU 2055  N   LYS A1062     9974   4490   5980   -945   1046  -1674       N  
ATOM   2056  CA  LYS A1062      65.385 -10.077 -24.289  1.00 59.08           C  
ANISOU 2056  CA  LYS A1062    10757   5262   6428  -1052    836  -1693       C  
ATOM   2057  C   LYS A1062      65.054  -8.734 -23.634  1.00 59.30           C  
ANISOU 2057  C   LYS A1062    10486   5353   6694  -1090    623  -1537       C  
ATOM   2058  O   LYS A1062      65.404  -7.676 -24.160  1.00 54.13           O  
ANISOU 2058  O   LYS A1062     9916   4781   5869  -1126    489  -1451       O  
ATOM   2059  CB  LYS A1062      64.379 -10.380 -25.405  1.00 66.97           C  
ANISOU 2059  CB  LYS A1062    11878   6275   7292  -1289    577  -1951       C  
ATOM   2060  CG  LYS A1062      62.939 -10.483 -24.930  1.00 76.32           C  
ANISOU 2060  CG  LYS A1062    12733   7395   8871  -1447    328  -2064       C  
ATOM   2061  CD  LYS A1062      61.979 -10.655 -26.095  1.00 84.48           C  
ANISOU 2061  CD  LYS A1062    13859   8445   9793  -1681     11  -2306       C  
ATOM   2062  CE  LYS A1062      60.540 -10.714 -25.611  1.00 89.48           C  
ANISOU 2062  CE  LYS A1062    14110   8982  10908  -1809   -236  -2406       C  
ATOM   2063  NZ  LYS A1062      59.571 -10.847 -26.733  1.00 99.64           N  
ANISOU 2063  NZ  LYS A1062    15434  10282  12142  -2039   -586  -2640       N  
ATOM   2064  N   GLU A1063      64.388  -8.779 -22.483  1.00 53.34           N  
ANISOU 2064  N   GLU A1063     9387   4560   6321  -1076    589  -1491       N  
ATOM   2065  CA  GLU A1063      64.010  -7.559 -21.773  1.00 47.29           C  
ANISOU 2065  CA  GLU A1063     8284   3849   5834  -1091    403  -1342       C  
ATOM   2066  C   GLU A1063      65.214  -6.855 -21.151  1.00 35.18           C  
ANISOU 2066  C   GLU A1063     6742   2359   4264   -895    546  -1101       C  
ATOM   2067  O   GLU A1063      65.159  -5.660 -20.854  1.00 37.87           O  
ANISOU 2067  O   GLU A1063     6872   2753   4763   -910    381   -963       O  
ATOM   2068  CB  GLU A1063      62.979  -7.865 -20.684  1.00 42.27           C  
ANISOU 2068  CB  GLU A1063     7323   3162   5574  -1087    350  -1351       C  
ATOM   2069  CG  GLU A1063      61.548  -8.007 -21.183  1.00 58.53           C  
ANISOU 2069  CG  GLU A1063     9243   5156   7839  -1283     86  -1533       C  
ATOM   2070  CD  GLU A1063      61.198  -9.427 -21.583  1.00 78.63           C  
ANISOU 2070  CD  GLU A1063    11988   7589  10300  -1334    173  -1738       C  
ATOM   2071  OE1 GLU A1063      62.107 -10.284 -21.616  1.00 80.74           O  
ANISOU 2071  OE1 GLU A1063    12514   7842  10321  -1228    448  -1743       O  
ATOM   2072  OE2 GLU A1063      60.007  -9.686 -21.859  1.00 88.26           O  
ANISOU 2072  OE2 GLU A1063    13087   8715  11733  -1476    -48  -1884       O  
ATOM   2073  N   PHE A1064      66.298  -7.602 -20.961  1.00 35.25           N  
ANISOU 2073  N   PHE A1064     6948   2338   4107   -707    833  -1038       N  
ATOM   2074  CA  PHE A1064      67.503  -7.078 -20.327  1.00 44.21           C  
ANISOU 2074  CA  PHE A1064     8047   3503   5247   -487    961   -804       C  
ATOM   2075  C   PHE A1064      68.079  -5.892 -21.090  1.00 45.83           C  
ANISOU 2075  C   PHE A1064     8374   3713   5328   -471    876   -697       C  
ATOM   2076  O   PHE A1064      68.653  -4.981 -20.492  1.00 45.48           O  
ANISOU 2076  O   PHE A1064     8146   3698   5435   -343    831   -475       O  
ATOM   2077  CB  PHE A1064      68.558  -8.179 -20.203  1.00 45.77           C  
ANISOU 2077  CB  PHE A1064     8429   3659   5304   -302   1260   -755       C  
ATOM   2078  CG  PHE A1064      69.769  -7.772 -19.412  1.00 44.70           C  
ANISOU 2078  CG  PHE A1064     8188   3566   5231    -70   1352   -511       C  
ATOM   2079  CD1 PHE A1064      69.680  -7.557 -18.046  1.00 34.86           C  
ANISOU 2079  CD1 PHE A1064     6663   2397   4185    -32   1255   -411       C  
ATOM   2080  CD2 PHE A1064      70.999  -7.616 -20.032  1.00 43.47           C  
ANISOU 2080  CD2 PHE A1064     8202   3385   4930    118   1526   -389       C  
ATOM   2081  CE1 PHE A1064      70.793  -7.186 -17.314  1.00 29.72           C  
ANISOU 2081  CE1 PHE A1064     5894   1813   3584    155   1271   -219       C  
ATOM   2082  CE2 PHE A1064      72.116  -7.246 -19.305  1.00 31.07           C  
ANISOU 2082  CE2 PHE A1064     6461   1875   3471    335   1567   -162       C  
ATOM   2083  CZ  PHE A1064      72.013  -7.030 -17.944  1.00 28.90           C  
ANISOU 2083  CZ  PHE A1064     5896   1694   3389    333   1407    -93       C  
ATOM   2084  N   GLN A1065      67.911  -5.906 -22.410  1.00 49.83           N  
ANISOU 2084  N   GLN A1065     9190   4206   5536   -604    818   -845       N  
ATOM   2085  CA  GLN A1065      68.407  -4.832 -23.267  1.00 51.40           C  
ANISOU 2085  CA  GLN A1065     9276   4680   5575   -552    651   -613       C  
ATOM   2086  C   GLN A1065      67.671  -3.516 -23.025  1.00 43.07           C  
ANISOU 2086  C   GLN A1065     7815   3765   4787   -694    268   -458       C  
ATOM   2087  O   GLN A1065      68.179  -2.445 -23.359  1.00 36.17           O  
ANISOU 2087  O   GLN A1065     6720   3115   3907   -605    133   -179       O  
ATOM   2088  CB  GLN A1065      68.289  -5.230 -24.741  1.00 53.31           C  
ANISOU 2088  CB  GLN A1065     9825   5047   5385   -653    620   -758       C  
ATOM   2089  CG  GLN A1065      69.092  -6.464 -25.108  1.00 67.57           C  
ANISOU 2089  CG  GLN A1065    12044   6716   6913   -498   1034   -910       C  
ATOM   2090  CD  GLN A1065      70.566  -6.311 -24.787  1.00 78.26           C  
ANISOU 2090  CD  GLN A1065    13332   8094   8310   -158   1345   -634       C  
ATOM   2091  OE1 GLN A1065      71.133  -7.097 -24.027  1.00 77.74           O  
ANISOU 2091  OE1 GLN A1065    13355   7803   8380     11   1642   -667       O  
ATOM   2092  NE2 GLN A1065      71.196  -5.296 -25.369  1.00 83.28           N  
ANISOU 2092  NE2 GLN A1065    13798   8987   8860    -57   1272   -347       N  
ATOM   2093  N   GLU A1066      66.475  -3.598 -22.449  1.00 44.61           N  
ANISOU 2093  N   GLU A1066     7899   3805   5247   -912    116   -635       N  
ATOM   2094  CA  GLU A1066      65.694  -2.402 -22.152  1.00 45.36           C  
ANISOU 2094  CA  GLU A1066     7593   3984   5659  -1050   -215   -511       C  
ATOM   2095  C   GLU A1066      66.069  -1.800 -20.801  1.00 41.52           C  
ANISOU 2095  C   GLU A1066     6866   3409   5500   -906   -125   -340       C  
ATOM   2096  O   GLU A1066      65.779  -0.633 -20.531  1.00 38.55           O  
ANISOU 2096  O   GLU A1066     6146   3125   5375   -946   -351   -172       O  
ATOM   2097  CB  GLU A1066      64.196  -2.716 -22.174  1.00 43.82           C  
ANISOU 2097  CB  GLU A1066     7291   3693   5665  -1317   -398   -757       C  
ATOM   2098  CG  GLU A1066      63.604  -2.854 -23.562  1.00 49.71           C  
ANISOU 2098  CG  GLU A1066     8221   4523   6144  -1554   -692   -896       C  
ATOM   2099  CD  GLU A1066      62.109  -3.110 -23.531  1.00 63.75           C  
ANISOU 2099  CD  GLU A1066     9666   6315   8240  -1677   -832  -1063       C  
ATOM   2100  OE1 GLU A1066      61.658  -3.905 -22.680  1.00 61.92           O  
ANISOU 2100  OE1 GLU A1066     9295   5958   8275  -1581   -598  -1195       O  
ATOM   2101  OE2 GLU A1066      61.384  -2.512 -24.354  1.00 77.06           O  
ANISOU 2101  OE2 GLU A1066    11213   8137   9930  -1843  -1190  -1040       O  
ATOM   2102  N   MET A1067      66.715  -2.600 -19.958  1.00 36.11           N  
ANISOU 2102  N   MET A1067     6270   2643   4807   -697    178   -363       N  
ATOM   2103  CA  MET A1067      67.014  -2.186 -18.591  1.00 36.27           C  
ANISOU 2103  CA  MET A1067     5961   2740   5080   -520    202   -222       C  
ATOM   2104  C   MET A1067      68.366  -1.486 -18.465  1.00 34.85           C  
ANISOU 2104  C   MET A1067     5757   2609   4875   -316    232     45       C  
ATOM   2105  O   MET A1067      69.264  -1.688 -19.281  1.00 35.14           O  
ANISOU 2105  O   MET A1067     6064   2601   4686   -210    362    143       O  
ATOM   2106  CB  MET A1067      66.975  -3.393 -17.653  1.00 36.81           C  
ANISOU 2106  CB  MET A1067     6058   2812   5115   -420    375   -331       C  
ATOM   2107  CG  MET A1067      65.674  -4.176 -17.693  1.00 35.38           C  
ANISOU 2107  CG  MET A1067     5862   2585   4997   -567    346   -534       C  
ATOM   2108  SD  MET A1067      65.843  -5.788 -16.903  1.00 44.18           S  
ANISOU 2108  SD  MET A1067     7128   3670   5987   -470    596   -604       S  
ATOM   2109  CE  MET A1067      64.207  -6.466 -17.157  1.00 48.88           C  
ANISOU 2109  CE  MET A1067     7677   4180   6715   -652    504   -805       C  
ATOM   2110  N   ARG A1068      68.483  -0.657 -17.433  1.00 32.39           N  
ANISOU 2110  N   ARG A1068     5091   2404   4811   -243    102    169       N  
ATOM   2111  CA  ARG A1068      69.718   0.035 -17.083  1.00 32.92           C  
ANISOU 2111  CA  ARG A1068     5016   2582   4911    -67     33    400       C  
ATOM   2112  C   ARG A1068      69.971  -0.181 -15.597  1.00 36.25           C  
ANISOU 2112  C   ARG A1068     5349   3093   5329     -6    -30    331       C  
ATOM   2113  O   ARG A1068      69.031  -0.178 -14.807  1.00 38.15           O  
ANISOU 2113  O   ARG A1068     5564   3339   5594    -88    -65    216       O  
ATOM   2114  CB  ARG A1068      69.623   1.532 -17.390  1.00 27.29           C  
ANISOU 2114  CB  ARG A1068     4202   2010   4156    -78    -14    529       C  
ATOM   2115  CG  ARG A1068      69.106   1.861 -18.778  1.00 28.12           C  
ANISOU 2115  CG  ARG A1068     4241   2105   4339   -241   -241    640       C  
ATOM   2116  CD  ARG A1068      70.131   1.516 -19.835  1.00 21.91           C  
ANISOU 2116  CD  ARG A1068     3627   1391   3306   -107   -148    801       C  
ATOM   2117  NE  ARG A1068      69.608   1.689 -21.185  1.00 23.96           N  
ANISOU 2117  NE  ARG A1068     3913   1841   3348   -254   -292    786       N  
ATOM   2118  CZ  ARG A1068      69.081   0.711 -21.915  1.00 26.19           C  
ANISOU 2118  CZ  ARG A1068     4501   2097   3354   -374   -224    549       C  
ATOM   2119  NH1 ARG A1068      69.000  -0.518 -21.423  1.00 26.51           N  
ANISOU 2119  NH1 ARG A1068     4821   1917   3334   -363     15    308       N  
ATOM   2120  NH2 ARG A1068      68.635   0.962 -23.140  1.00 28.39           N  
ANISOU 2120  NH2 ARG A1068     4820   2557   3408   -510   -408    554       N  
ATOM   2121  N   PHE A1069      71.227  -0.368 -15.208  1.00 33.00           N  
ANISOU 2121  N   PHE A1069     4956   2725   4857    140     15    414       N  
ATOM   2122  CA  PHE A1069      71.535  -0.625 -13.805  1.00 24.80           C  
ANISOU 2122  CA  PHE A1069     3934   1688   3803    198     73    378       C  
ATOM   2123  C   PHE A1069      72.658   0.268 -13.288  1.00 30.83           C  
ANISOU 2123  C   PHE A1069     4629   2530   4555    288    -69    492       C  
ATOM   2124  O   PHE A1069      73.704   0.397 -13.922  1.00 38.26           O  
ANISOU 2124  O   PHE A1069     5541   3527   5471    390    -49    593       O  
ATOM   2125  CB  PHE A1069      71.907  -2.097 -13.597  1.00 19.84           C  
ANISOU 2125  CB  PHE A1069     3509    999   3031    278    334    306       C  
ATOM   2126  CG  PHE A1069      70.784  -3.059 -13.881  1.00 30.75           C  
ANISOU 2126  CG  PHE A1069     5053   2302   4329    176    481    141       C  
ATOM   2127  CD1 PHE A1069      69.884  -3.410 -12.886  1.00 35.13           C  
ANISOU 2127  CD1 PHE A1069     5657   2823   4866    100    546     45       C  
ATOM   2128  CD2 PHE A1069      70.635  -3.623 -15.138  1.00 40.27           C  
ANISOU 2128  CD2 PHE A1069     6385   3456   5460    150    568     80       C  
ATOM   2129  CE1 PHE A1069      68.852  -4.300 -13.144  1.00 40.68           C  
ANISOU 2129  CE1 PHE A1069     6480   3457   5519     -7    674    -94       C  
ATOM   2130  CE2 PHE A1069      69.606  -4.515 -15.401  1.00 37.89           C  
ANISOU 2130  CE2 PHE A1069     6234   3074   5090     32    677    -91       C  
ATOM   2131  CZ  PHE A1069      68.715  -4.853 -14.404  1.00 33.95           C  
ANISOU 2131  CZ  PHE A1069     5718   2561   4622    -47    709   -169       C  
ATOM   2132  N   ILE A1070      72.425   0.885 -12.133  1.00 33.80           N  
ANISOU 2132  N   ILE A1070     4106   4130   4604    491    644   -582       N  
ATOM   2133  CA  ILE A1070      73.441   1.687 -11.461  1.00 31.73           C  
ANISOU 2133  CA  ILE A1070     3667   4029   4360    616    594   -543       C  
ATOM   2134  C   ILE A1070      73.743   1.114 -10.077  1.00 32.81           C  
ANISOU 2134  C   ILE A1070     3771   4171   4523    883    626   -500       C  
ATOM   2135  O   ILE A1070      73.008   1.366  -9.122  1.00 24.36           O  
ANISOU 2135  O   ILE A1070     2873   3004   3379    848    604   -545       O  
ATOM   2136  CB  ILE A1070      73.001   3.156 -11.305  1.00 32.98           C  
ANISOU 2136  CB  ILE A1070     3781   4250   4498    341    390   -712       C  
ATOM   2137  CG1 ILE A1070      72.408   3.690 -12.611  1.00 31.69           C  
ANISOU 2137  CG1 ILE A1070     3634   4056   4352     59    328   -745       C  
ATOM   2138  CG2 ILE A1070      74.173   4.014 -10.850  1.00 26.38           C  
ANISOU 2138  CG2 ILE A1070     2554   3715   3753    426    150   -777       C  
ATOM   2139  CD1 ILE A1070      73.435   3.982 -13.673  1.00 37.96           C  
ANISOU 2139  CD1 ILE A1070     4276   4929   5220     67    323   -747       C  
ATOM   2140  N   ILE A1071      74.819   0.340  -9.971  1.00 33.26           N  
ANISOU 2140  N   ILE A1071     3617   4254   4767   1060    671   -391       N  
ATOM   2141  CA  ILE A1071      75.192  -0.270  -8.695  1.00 40.45           C  
ANISOU 2141  CA  ILE A1071     4570   5140   5661   1322    681   -147       C  
ATOM   2142  C   ILE A1071      76.279   0.541  -7.995  1.00 36.65           C  
ANISOU 2142  C   ILE A1071     3839   4952   5136   1427    344     82       C  
ATOM   2143  O   ILE A1071      77.376   0.696  -8.520  1.00 35.87           O  
ANISOU 2143  O   ILE A1071     3425   5034   5170   1471    272    234       O  
ATOM   2144  CB  ILE A1071      75.684  -1.722  -8.874  1.00 42.38           C  
ANISOU 2144  CB  ILE A1071     4848   5275   5979   1444    851    -25       C  
ATOM   2145  CG1 ILE A1071      74.548  -2.626  -9.356  1.00 38.10           C  
ANISOU 2145  CG1 ILE A1071     4556   4521   5399   1278    973   -189       C  
ATOM   2146  CG2 ILE A1071      76.245  -2.256  -7.570  1.00 48.12           C  
ANISOU 2146  CG2 ILE A1071     5580   6035   6667   1721    824    249       C  
ATOM   2147  CD1 ILE A1071      74.460  -2.756 -10.857  1.00 43.40           C  
ANISOU 2147  CD1 ILE A1071     5210   5203   6077   1134    974   -329       C  
ATOM   2148  N   ILE A1072      75.972   1.044  -6.803  1.00 32.25           N  
ANISOU 2148  N   ILE A1072     3449   4431   4376   1389     76    107       N  
ATOM   2149  CA  ILE A1072      76.885   1.930  -6.088  1.00 33.57           C  
ANISOU 2149  CA  ILE A1072     3459   4837   4458   1348   -378    274       C  
ATOM   2150  C   ILE A1072      77.259   1.388  -4.714  1.00 37.64           C  
ANISOU 2150  C   ILE A1072     4084   5363   4853   1590   -505    504       C  
ATOM   2151  O   ILE A1072      76.390   0.960  -3.953  1.00 32.69           O  
ANISOU 2151  O   ILE A1072     3768   4578   4072   1686   -385    457       O  
ATOM   2152  CB  ILE A1072      76.271   3.334  -5.906  1.00 38.45           C  
ANISOU 2152  CB  ILE A1072     4205   5512   4892   1062   -698     73       C  
ATOM   2153  CG1 ILE A1072      75.705   3.852  -7.230  1.00 38.39           C  
ANISOU 2153  CG1 ILE A1072     4137   5471   4980    822   -543   -181       C  
ATOM   2154  CG2 ILE A1072      77.297   4.303  -5.331  1.00 30.98           C  
ANISOU 2154  CG2 ILE A1072     3084   4793   3895    987  -1214    239       C  
ATOM   2155  CD1 ILE A1072      74.843   5.085  -7.077  1.00 34.01           C  
ANISOU 2155  CD1 ILE A1072     3771   4920   4230    564   -771   -409       C  
ATOM   2156  N   GLY A1073      78.550   1.412  -4.395  1.00 39.38           N  
ANISOU 2156  N   GLY A1073     4039   5775   5149   1695   -748    775       N  
ATOM   2157  CA  GLY A1073      79.004   1.041  -3.067  1.00 44.14           C  
ANISOU 2157  CA  GLY A1073     4753   6385   5634   1859   -924    975       C  
ATOM   2158  C   GLY A1073      80.317   0.283  -3.028  1.00 55.56           C  
ANISOU 2158  C   GLY A1073     5960   7883   7265   1975   -884   1218       C  
ATOM   2159  O   GLY A1073      80.801  -0.205  -4.049  1.00 57.57           O  
ANISOU 2159  O   GLY A1073     5998   8155   7720   2008   -632   1254       O  
ATOM   2160  N   LYS A1074      80.894   0.191  -1.833  1.00 55.44           N  
ANISOU 2160  N   LYS A1074     6019   7882   7161   2033  -1130   1362       N  
ATOM   2161  CA  LYS A1074      82.122  -0.562  -1.617  1.00 50.17           C  
ANISOU 2161  CA  LYS A1074     5163   7274   6625   2174  -1111   1585       C  
ATOM   2162  C   LYS A1074      81.834  -1.776  -0.743  1.00 54.13           C  
ANISOU 2162  C   LYS A1074     5868   7665   7036   2445   -879   1687       C  
ATOM   2163  O   LYS A1074      80.690  -2.010  -0.354  1.00 47.15           O  
ANISOU 2163  O   LYS A1074     5270   6646   5998   2514   -719   1579       O  
ATOM   2164  CB  LYS A1074      83.189   0.311  -0.956  1.00 48.29           C  
ANISOU 2164  CB  LYS A1074     4840   7123   6384   2024  -1606   1647       C  
ATOM   2165  CG  LYS A1074      83.196   1.757  -1.411  1.00 57.37           C  
ANISOU 2165  CG  LYS A1074     5965   8306   7525   1735  -1910   1446       C  
ATOM   2166  CD  LYS A1074      84.113   2.590  -0.531  1.00 77.33           C  
ANISOU 2166  CD  LYS A1074     8547  10891   9944   1697  -2350   1407       C  
ATOM   2167  CE  LYS A1074      84.003   4.070  -0.851  1.00 85.12           C  
ANISOU 2167  CE  LYS A1074     9558  12011  10771   1506  -2483   1147       C  
ATOM   2168  NZ  LYS A1074      84.855   4.891   0.055  1.00 88.92           N  
ANISOU 2168  NZ  LYS A1074    10026  12692  11068   1501  -2722   1167       N  
ATOM   2169  N   GLY A1075      82.874  -2.540  -0.427  1.00 55.84           N  
ANISOU 2169  N   GLY A1075     5946   7932   7340   2591   -850   1890       N  
ATOM   2170  CA  GLY A1075      82.727  -3.669   0.473  1.00 62.19           C  
ANISOU 2170  CA  GLY A1075     6931   8638   8059   2828   -661   1994       C  
ATOM   2171  C   GLY A1075      83.573  -4.870   0.105  1.00 60.47           C  
ANISOU 2171  C   GLY A1075     6547   8436   7994   3013   -373   2166       C  
ATOM   2172  O   GLY A1075      84.778  -4.752  -0.117  1.00 64.52           O  
ANISOU 2172  O   GLY A1075     6790   9098   8628   2998   -510   2315       O  
ATOM   2173  N   ASP A1076      82.931  -6.033   0.051  1.00 60.99           N  
ANISOU 2173  N   ASP A1076     6795   8333   8045   3171     26   2140       N  
ATOM   2174  CA  ASP A1076      83.605  -7.286  -0.264  1.00 69.31           C  
ANISOU 2174  CA  ASP A1076     7766   9361   9206   3345    322   2281       C  
ATOM   2175  C   ASP A1076      84.264  -7.220  -1.639  1.00 68.43           C  
ANISOU 2175  C   ASP A1076     7409   9325   9265   3285    442   2288       C  
ATOM   2176  O   ASP A1076      83.580  -7.053  -2.649  1.00 66.02           O  
ANISOU 2176  O   ASP A1076     7159   8923   9002   3173    609   2100       O  
ATOM   2177  CB  ASP A1076      82.608  -8.447  -0.202  1.00 80.64           C  
ANISOU 2177  CB  ASP A1076     9489  10555  10595   3443    700   2196       C  
ATOM   2178  CG  ASP A1076      83.278  -9.804  -0.298  1.00 97.90           C  
ANISOU 2178  CG  ASP A1076    11650  12699  12849   3630    962   2349       C  
ATOM   2179  OD1 ASP A1076      84.458  -9.920   0.093  1.00104.60           O  
ANISOU 2179  OD1 ASP A1076    12301  13712  13729   3744    834   2560       O  
ATOM   2180  OD2 ASP A1076      82.616 -10.760  -0.756  1.00104.82           O  
ANISOU 2180  OD2 ASP A1076    12712  13369  13746   3646   1276   2259       O  
ATOM   2181  N   PRO A1077      85.603  -7.343  -1.679  1.00 73.46           N  
ANISOU 2181  N   PRO A1077     7785  10135   9992   3354    356   2505       N  
ATOM   2182  CA  PRO A1077      86.375  -7.285  -2.926  1.00 68.98           C  
ANISOU 2182  CA  PRO A1077     6978   9666   9566   3317    475   2557       C  
ATOM   2183  C   PRO A1077      85.929  -8.336  -3.938  1.00 74.84           C  
ANISOU 2183  C   PRO A1077     7878  10224  10333   3404    905   2456       C  
ATOM   2184  O   PRO A1077      86.053  -8.121  -5.145  1.00 78.71           O  
ANISOU 2184  O   PRO A1077     8286  10727  10894   3325   1016   2385       O  
ATOM   2185  CB  PRO A1077      87.814  -7.546  -2.464  1.00 66.12           C  
ANISOU 2185  CB  PRO A1077     6372   9488   9264   3433    355   2849       C  
ATOM   2186  CG  PRO A1077      87.680  -8.212  -1.132  1.00 65.95           C  
ANISOU 2186  CG  PRO A1077     6520   9402   9135   3591    312   2926       C  
ATOM   2187  CD  PRO A1077      86.469  -7.592  -0.514  1.00 72.00           C  
ANISOU 2187  CD  PRO A1077     7531  10055   9770   3477    153   2722       C  
ATOM   2188  N   GLU A1078      85.413  -9.457  -3.445  1.00 78.28           N  
ANISOU 2188  N   GLU A1078     8563  10478  10701   3547   1120   2443       N  
ATOM   2189  CA  GLU A1078      84.879 -10.497  -4.313  1.00 72.82           C  
ANISOU 2189  CA  GLU A1078     8084   9563  10020   3587   1466   2319       C  
ATOM   2190  C   GLU A1078      83.593 -10.015  -4.983  1.00 64.56           C  
ANISOU 2190  C   GLU A1078     7218   8350   8962   3373   1501   2018       C  
ATOM   2191  O   GLU A1078      83.404 -10.193  -6.189  1.00 65.84           O  
ANISOU 2191  O   GLU A1078     7429   8419   9169   3299   1649   1881       O  
ATOM   2192  CB  GLU A1078      84.628 -11.782  -3.521  1.00 69.19           C  
ANISOU 2192  CB  GLU A1078     7843   8948   9500   3757   1643   2389       C  
ATOM   2193  CG  GLU A1078      84.290 -12.990  -4.380  1.00 82.68           C  
ANISOU 2193  CG  GLU A1078     9759  10429  11227   3804   1953   2302       C  
ATOM   2194  CD  GLU A1078      84.280 -14.285  -3.588  1.00 97.93           C  
ANISOU 2194  CD  GLU A1078    11856  12238  13115   3985   2113   2422       C  
ATOM   2195  OE1 GLU A1078      84.460 -14.231  -2.353  1.00101.99           O  
ANISOU 2195  OE1 GLU A1078    12337  12841  13574   4072   1998   2558       O  
ATOM   2196  OE2 GLU A1078      84.096 -15.358  -4.203  1.00 97.60           O  
ANISOU 2196  OE2 GLU A1078    11985  12010  13089   4041   2337   2377       O  
ATOM   2197  N   LEU A1079      82.717  -9.395  -4.197  1.00 51.23           N  
ANISOU 2197  N   LEU A1079     5638   6627   7202   3275   1352   1919       N  
ATOM   2198  CA  LEU A1079      81.473  -8.840  -4.721  1.00 51.34           C  
ANISOU 2198  CA  LEU A1079     5808   6499   7199   3062   1367   1646       C  
ATOM   2199  C   LEU A1079      81.737  -7.619  -5.602  1.00 61.07           C  
ANISOU 2199  C   LEU A1079     6831   7883   8492   2905   1213   1559       C  
ATOM   2200  O   LEU A1079      81.030  -7.389  -6.587  1.00 61.75           O  
ANISOU 2200  O   LEU A1079     7001   7857   8603   2737   1297   1333       O  
ATOM   2201  CB  LEU A1079      80.523  -8.470  -3.580  1.00 49.25           C  
ANISOU 2201  CB  LEU A1079     5718   6178   6817   3027   1254   1598       C  
ATOM   2202  CG  LEU A1079      79.983  -9.640  -2.755  1.00 65.16           C  
ANISOU 2202  CG  LEU A1079     7974   8018   8767   3135   1429   1652       C  
ATOM   2203  CD1 LEU A1079      78.982  -9.151  -1.721  1.00 64.28           C  
ANISOU 2203  CD1 LEU A1079     8042   7865   8518   3088   1328   1600       C  
ATOM   2204  CD2 LEU A1079      79.357 -10.696  -3.656  1.00 67.02           C  
ANISOU 2204  CD2 LEU A1079     8380   8013   9072   3058   1698   1522       C  
ATOM   2205  N   GLU A1080      82.754  -6.839  -5.242  1.00 63.07           N  
ANISOU 2205  N   GLU A1080     6806   8388   8770   2931    961   1740       N  
ATOM   2206  CA  GLU A1080      83.166  -5.701  -6.058  1.00 58.94           C  
ANISOU 2206  CA  GLU A1080     6045   8032   8319   2768    797   1701       C  
ATOM   2207  C   GLU A1080      83.656  -6.183  -7.417  1.00 51.94           C  
ANISOU 2207  C   GLU A1080     5095   7124   7516   2781   1030   1684       C  
ATOM   2208  O   GLU A1080      83.320  -5.604  -8.449  1.00 48.95           O  
ANISOU 2208  O   GLU A1080     4701   6730   7168   2622   1052   1507       O  
ATOM   2209  CB  GLU A1080      84.261  -4.888  -5.361  1.00 61.85           C  
ANISOU 2209  CB  GLU A1080     6133   8658   8708   2749    438   1922       C  
ATOM   2210  CG  GLU A1080      83.763  -4.016  -4.218  1.00 72.04           C  
ANISOU 2210  CG  GLU A1080     7504   9983   9883   2660     91   1885       C  
ATOM   2211  CD  GLU A1080      84.853  -3.144  -3.625  1.00 80.02           C  
ANISOU 2211  CD  GLU A1080     8288  11203  10912   2560   -336   2048       C  
ATOM   2212  OE1 GLU A1080      84.720  -1.903  -3.684  1.00 78.93           O  
ANISOU 2212  OE1 GLU A1080     8103  11134  10753   2329   -643   1940       O  
ATOM   2213  OE2 GLU A1080      85.840  -3.697  -3.096  1.00 82.67           O  
ANISOU 2213  OE2 GLU A1080     8516  11614  11280   2694   -374   2265       O  
ATOM   2214  N   GLY A1081      84.446  -7.252  -7.405  1.00 49.29           N  
ANISOU 2214  N   GLY A1081     4743   6786   7197   2982   1198   1869       N  
ATOM   2215  CA  GLY A1081      84.963  -7.839  -8.627  1.00 50.55           C  
ANISOU 2215  CA  GLY A1081     4888   6918   7400   3046   1419   1883       C  
ATOM   2216  C   GLY A1081      83.865  -8.454  -9.473  1.00 53.03           C  
ANISOU 2216  C   GLY A1081     5510   6960   7678   2974   1623   1604       C  
ATOM   2217  O   GLY A1081      83.913  -8.397 -10.702  1.00 48.09           O  
ANISOU 2217  O   GLY A1081     4894   6308   7071   2918   1708   1496       O  
ATOM   2218  N   TRP A1082      82.880  -9.053  -8.811  1.00 47.53           N  
ANISOU 2218  N   TRP A1082     5068   6062   6929   2964   1680   1495       N  
ATOM   2219  CA  TRP A1082      81.715  -9.607  -9.494  1.00 47.78           C  
ANISOU 2219  CA  TRP A1082     5386   5830   6938   2837   1809   1231       C  
ATOM   2220  C   TRP A1082      80.958  -8.485 -10.206  1.00 48.31           C  
ANISOU 2220  C   TRP A1082     5443   5903   7010   2578   1691    980       C  
ATOM   2221  O   TRP A1082      80.578  -8.608 -11.380  1.00 47.09           O  
ANISOU 2221  O   TRP A1082     5381   5651   6859   2470   1751    796       O  
ATOM   2222  CB  TRP A1082      80.812 -10.333  -8.491  1.00 47.39           C  
ANISOU 2222  CB  TRP A1082     5569   5595   6843   2845   1860   1207       C  
ATOM   2223  CG  TRP A1082      79.671 -11.103  -9.095  1.00 44.34           C  
ANISOU 2223  CG  TRP A1082     5453   4941   6452   2713   1974    993       C  
ATOM   2224  CD1 TRP A1082      79.405 -11.278 -10.422  1.00 43.68           C  
ANISOU 2224  CD1 TRP A1082     5440   4768   6390   2612   2019    817       C  
ATOM   2225  CD2 TRP A1082      78.643 -11.805  -8.384  1.00 49.02           C  
ANISOU 2225  CD2 TRP A1082     6265   5339   7021   2665   2030    954       C  
ATOM   2226  NE1 TRP A1082      78.274 -12.042 -10.581  1.00 44.36           N  
ANISOU 2226  NE1 TRP A1082     5761   4619   6473   2497   2074    671       N  
ATOM   2227  CE2 TRP A1082      77.787 -12.378  -9.345  1.00 43.24           C  
ANISOU 2227  CE2 TRP A1082     5706   4409   6314   2521   2092    760       C  
ATOM   2228  CE3 TRP A1082      78.362 -12.002  -7.027  1.00 47.43           C  
ANISOU 2228  CE3 TRP A1082     6124   5122   6776   2736   2027   1079       C  
ATOM   2229  CZ2 TRP A1082      76.671 -13.136  -8.995  1.00 44.07           C  
ANISOU 2229  CZ2 TRP A1082     6013   4308   6425   2431   2149    704       C  
ATOM   2230  CZ3 TRP A1082      77.252 -12.754  -6.681  1.00 44.27           C  
ANISOU 2230  CZ3 TRP A1082     5940   4512   6371   2653   2111   1020       C  
ATOM   2231  CH2 TRP A1082      76.421 -13.312  -7.661  1.00 44.49           C  
ANISOU 2231  CH2 TRP A1082     6109   4349   6447   2496   2171    841       C  
ATOM   2232  N   ALA A1083      80.761  -7.382  -9.489  1.00 40.58           N  
ANISOU 2232  N   ALA A1083     4351   5048   6019   2488   1505    980       N  
ATOM   2233  CA  ALA A1083      80.099  -6.210 -10.045  1.00 42.08           C  
ANISOU 2233  CA  ALA A1083     4510   5270   6207   2251   1381    759       C  
ATOM   2234  C   ALA A1083      80.867  -5.651 -11.242  1.00 46.17           C  
ANISOU 2234  C   ALA A1083     4832   5931   6779   2207   1361    752       C  
ATOM   2235  O   ALA A1083      80.270  -5.297 -12.257  1.00 45.99           O  
ANISOU 2235  O   ALA A1083     4882   5849   6744   2032   1366    520       O  
ATOM   2236  CB  ALA A1083      79.932  -5.142  -8.979  1.00 36.26           C  
ANISOU 2236  CB  ALA A1083     3673   4664   5439   2213   1167    809       C  
ATOM   2237  N   ARG A1084      82.190  -5.578 -11.122  1.00 45.10           N  
ANISOU 2237  N   ARG A1084     4447   5995   6693   2358   1326   1021       N  
ATOM   2238  CA  ARG A1084      83.025  -5.054 -12.200  1.00 50.18           C  
ANISOU 2238  CA  ARG A1084     4891   6790   7387   2328   1315   1069       C  
ATOM   2239  C   ARG A1084      83.032  -5.980 -13.414  1.00 49.77           C  
ANISOU 2239  C   ARG A1084     5000   6595   7314   2400   1537    981       C  
ATOM   2240  O   ARG A1084      83.154  -5.522 -14.552  1.00 46.95           O  
ANISOU 2240  O   ARG A1084     4598   6280   6963   2318   1545    886       O  
ATOM   2241  CB  ARG A1084      84.458  -4.824 -11.711  1.00 56.60           C  
ANISOU 2241  CB  ARG A1084     5394   7853   8260   2456   1210   1415       C  
ATOM   2242  CG  ARG A1084      84.612  -3.649 -10.753  1.00 58.41           C  
ANISOU 2242  CG  ARG A1084     5418   8263   8514   2326    888   1498       C  
ATOM   2243  CD  ARG A1084      84.293  -2.327 -11.434  1.00 65.69           C  
ANISOU 2243  CD  ARG A1084     6250   9255   9456   2069    730   1327       C  
ATOM   2244  NE  ARG A1084      84.266  -1.214 -10.487  1.00 75.91           N  
ANISOU 2244  NE  ARG A1084     7418  10679  10747   1914    380   1362       N  
ATOM   2245  CZ  ARG A1084      83.958   0.038 -10.810  1.00 73.22           C  
ANISOU 2245  CZ  ARG A1084     7016  10397  10406   1666    178   1216       C  
ATOM   2246  NH1 ARG A1084      83.651   0.348 -12.063  1.00 63.87           N  
ANISOU 2246  NH1 ARG A1084     5866   9166   9234   1556    313   1031       N  
ATOM   2247  NH2 ARG A1084      83.956   0.984  -9.880  1.00 71.48           N  
ANISOU 2247  NH2 ARG A1084     6743  10265  10151   1519   -179   1235       N  
ATOM   2248  N   SER A1085      82.904  -7.281 -13.170  1.00 50.78           N  
ANISOU 2248  N   SER A1085     5325   6558   7412   2558   1700   1018       N  
ATOM   2249  CA  SER A1085      82.861  -8.253 -14.257  1.00 48.24           C  
ANISOU 2249  CA  SER A1085     5183   6085   7060   2639   1881    938       C  
ATOM   2250  C   SER A1085      81.547  -8.115 -15.009  1.00 41.84           C  
ANISOU 2250  C   SER A1085     4588   5098   6212   2418   1855    612       C  
ATOM   2251  O   SER A1085      81.516  -8.143 -16.241  1.00 58.90           O  
ANISOU 2251  O   SER A1085     6812   7218   8348   2419   1943    547       O  
ATOM   2252  CB  SER A1085      83.028  -9.678 -13.728  1.00 49.91           C  
ANISOU 2252  CB  SER A1085     5554   6161   7251   2855   2042   1069       C  
ATOM   2253  OG  SER A1085      81.914 -10.065 -12.946  1.00 63.46           O  
ANISOU 2253  OG  SER A1085     7473   7691   8946   2758   2020    937       O  
ATOM   2254  N   LEU A1086      80.460  -7.958 -14.261  1.00 39.39           N  
ANISOU 2254  N   LEU A1086     4397   4685   5885   2257   1762    465       N  
ATOM   2255  CA  LEU A1086      79.159  -7.728 -14.876  1.00 36.98           C  
ANISOU 2255  CA  LEU A1086     4278   4233   5539   2043   1743    229       C  
ATOM   2256  C   LEU A1086      79.133  -6.398 -15.627  1.00 40.13           C  
ANISOU 2256  C   LEU A1086     4537   4780   5931   1878   1626    115       C  
ATOM   2257  O   LEU A1086      78.466  -6.272 -16.653  1.00 48.58           O  
ANISOU 2257  O   LEU A1086     5727   5766   6967   1762   1648    -30       O  
ATOM   2258  CB  LEU A1086      78.053  -7.766 -13.822  1.00 35.06           C  
ANISOU 2258  CB  LEU A1086     4167   3879   5274   1911   1671    149       C  
ATOM   2259  CG  LEU A1086      77.674  -9.165 -13.336  1.00 55.36           C  
ANISOU 2259  CG  LEU A1086     6945   6240   7847   2016   1808    216       C  
ATOM   2260  CD1 LEU A1086      76.712  -9.091 -12.163  1.00 45.28           C  
ANISOU 2260  CD1 LEU A1086     5758   4895   6552   1904   1738    188       C  
ATOM   2261  CD2 LEU A1086      77.072  -9.974 -14.477  1.00 61.17           C  
ANISOU 2261  CD2 LEU A1086     7890   6773   8576   1986   1934    122       C  
ATOM   2262  N   GLU A1087      79.865  -5.413 -15.115  1.00 47.34           N  
ANISOU 2262  N   GLU A1087     5192   5914   6880   1865   1490    194       N  
ATOM   2263  CA  GLU A1087      79.944  -4.100 -15.751  1.00 45.21           C  
ANISOU 2263  CA  GLU A1087     4765   5802   6612   1708   1371    107       C  
ATOM   2264  C   GLU A1087      80.703  -4.177 -17.070  1.00 44.56           C  
ANISOU 2264  C   GLU A1087     4619   5770   6544   1802   1488    182       C  
ATOM   2265  O   GLU A1087      80.291  -3.593 -18.072  1.00 53.13           O  
ANISOU 2265  O   GLU A1087     5735   6857   7594   1679   1474     45       O  
ATOM   2266  CB  GLU A1087      80.618  -3.084 -14.826  1.00 45.43           C  
ANISOU 2266  CB  GLU A1087     4526   6039   6698   1686   1201    242       C  
ATOM   2267  CG  GLU A1087      80.724  -1.687 -15.426  1.00 55.15           C  
ANISOU 2267  CG  GLU A1087     5585   7430   7940   1497   1051    151       C  
ATOM   2268  CD  GLU A1087      81.539  -0.737 -14.569  1.00 68.25           C  
ANISOU 2268  CD  GLU A1087     6962   9294   9676   1484    860    377       C  
ATOM   2269  OE1 GLU A1087      82.561  -1.176 -14.002  1.00 82.54           O  
ANISOU 2269  OE1 GLU A1087     8626  11198  11538   1663    859    671       O  
ATOM   2270  OE2 GLU A1087      81.156   0.449 -14.462  1.00 60.54           O  
ANISOU 2270  OE2 GLU A1087     5916   8392   8695   1281    677    264       O  
ATOM   2271  N   GLU A1088      81.819  -4.897 -17.059  1.00 50.33           N  
ANISOU 2271  N   GLU A1088     5333   6801   6990    990   1302    -50       N  
ATOM   2272  CA  GLU A1088      82.616  -5.078 -18.264  1.00 61.67           C  
ANISOU 2272  CA  GLU A1088     6797   8233   8403    900   1649   -265       C  
ATOM   2273  C   GLU A1088      81.868  -5.936 -19.280  1.00 61.61           C  
ANISOU 2273  C   GLU A1088     7158   7989   8264   1018   1630   -189       C  
ATOM   2274  O   GLU A1088      82.083  -5.816 -20.487  1.00 56.16           O  
ANISOU 2274  O   GLU A1088     6711   7209   7420    882   1913   -296       O  
ATOM   2275  CB  GLU A1088      83.964  -5.718 -17.927  1.00 66.18           C  
ANISOU 2275  CB  GLU A1088     6855   9046   9246   1044   1730   -534       C  
ATOM   2276  CG  GLU A1088      84.959  -5.706 -19.076  1.00 81.04           C  
ANISOU 2276  CG  GLU A1088     8679  10976  11137    888   2164   -828       C  
ATOM   2277  CD  GLU A1088      85.962  -6.837 -18.987  1.00 94.29           C  
ANISOU 2277  CD  GLU A1088     9923  12812  13092   1160   2166  -1086       C  
ATOM   2278  OE1 GLU A1088      85.624  -7.884 -18.393  1.00 96.94           O  
ANISOU 2278  OE1 GLU A1088    10194  13104  13535   1505   1826   -969       O  
ATOM   2279  OE2 GLU A1088      87.086  -6.682 -19.509  1.00102.66           O  
ANISOU 2279  OE2 GLU A1088    10713  14024  14267   1027   2517  -1421       O  
ATOM   2280  N   LYS A1089      80.986  -6.799 -18.784  1.00 59.78           N  
ANISOU 2280  N   LYS A1089     6981   7649   8084   1256   1309    -16       N  
ATOM   2281  CA  LYS A1089      80.250  -7.716 -19.646  1.00 48.19           C  
ANISOU 2281  CA  LYS A1089     5814   5959   6535   1384   1255     29       C  
ATOM   2282  C   LYS A1089      79.064  -7.038 -20.333  1.00 43.99           C  
ANISOU 2282  C   LYS A1089     5753   5215   5744   1241   1202    158       C  
ATOM   2283  O   LYS A1089      78.785  -7.301 -21.502  1.00 38.75           O  
ANISOU 2283  O   LYS A1089     5407   4396   4921   1232   1296    105       O  
ATOM   2284  CB  LYS A1089      79.766  -8.921 -18.841  1.00 52.83           C  
ANISOU 2284  CB  LYS A1089     6290   6487   7297   1667    959    143       C  
ATOM   2285  CG  LYS A1089      79.504 -10.164 -19.671  1.00 57.45           C  
ANISOU 2285  CG  LYS A1089     7034   6891   7902   1840    957     92       C  
ATOM   2286  CD  LYS A1089      80.222 -11.366 -19.077  1.00 65.29           C  
ANISOU 2286  CD  LYS A1089     7730   7938   9138   2122    873     27       C  
ATOM   2287  CE  LYS A1089      79.841 -11.566 -17.617  1.00 66.27           C  
ANISOU 2287  CE  LYS A1089     7732   8080   9368   2247    588    219       C  
ATOM   2288  NZ  LYS A1089      80.597 -12.684 -16.986  1.00 67.72           N  
ANISOU 2288  NZ  LYS A1089     7681   8294   9757   2554    471    168       N  
ATOM   2289  N   HIS A1090      78.371  -6.165 -19.609  1.00 37.80           N  
ANISOU 2289  N   HIS A1090     5018   4426   4917   1149   1033    305       N  
ATOM   2290  CA  HIS A1090      77.171  -5.528 -20.143  1.00 39.65           C  
ANISOU 2290  CA  HIS A1090     5669   4458   4940   1067    909    408       C  
ATOM   2291  C   HIS A1090      77.266  -4.002 -20.138  1.00 42.00           C  
ANISOU 2291  C   HIS A1090     6111   4769   5077    825   1011    432       C  
ATOM   2292  O   HIS A1090      77.669  -3.396 -19.145  1.00 45.99           O  
ANISOU 2292  O   HIS A1090     6347   5435   5691    744   1008    450       O  
ATOM   2293  CB  HIS A1090      75.941  -5.978 -19.352  1.00 43.47           C  
ANISOU 2293  CB  HIS A1090     6131   4857   5528   1206    573    546       C  
ATOM   2294  CG  HIS A1090      75.827  -7.465 -19.209  1.00 48.19           C  
ANISOU 2294  CG  HIS A1090     6605   5408   6296   1421    482    539       C  
ATOM   2295  ND1 HIS A1090      75.930  -8.105 -17.994  1.00 45.86           N  
ANISOU 2295  ND1 HIS A1090     6025   5198   6201   1546    359    615       N  
ATOM   2296  CD2 HIS A1090      75.629  -8.437 -20.132  1.00 50.86           C  
ANISOU 2296  CD2 HIS A1090     7103   5601   6621   1535    498    463       C  
ATOM   2297  CE1 HIS A1090      75.794  -9.409 -18.172  1.00 49.79           C  
ANISOU 2297  CE1 HIS A1090     6528   5584   6807   1723    310    599       C  
ATOM   2298  NE2 HIS A1090      75.611  -9.635 -19.460  1.00 50.81           N  
ANISOU 2298  NE2 HIS A1090     6901   5579   6825   1716    393    496       N  
ATOM   2299  N   GLY A1091      76.885  -3.389 -21.255  1.00 47.60           N  
ANISOU 2299  N   GLY A1091     7279   5290   5515    718   1089    428       N  
ATOM   2300  CA  GLY A1091      76.954  -1.946 -21.403  1.00 53.03           C  
ANISOU 2300  CA  GLY A1091     8210   5923   6014    488   1201    458       C  
ATOM   2301  C   GLY A1091      75.857  -1.208 -20.660  1.00 49.91           C  
ANISOU 2301  C   GLY A1091     7882   5457   5625    509    886    588       C  
ATOM   2302  O   GLY A1091      75.953  -0.001 -20.435  1.00 45.27           O  
ANISOU 2302  O   GLY A1091     7399   4849   4951    335    943    618       O  
ATOM   2303  N   ASN A1092      74.810  -1.935 -20.280  1.00 46.49           N  
ANISOU 2303  N   ASN A1092     7382   4977   5307    711    572    644       N  
ATOM   2304  CA  ASN A1092      73.691  -1.350 -19.548  1.00 37.69           C  
ANISOU 2304  CA  ASN A1092     6279   3808   4234    744    278    725       C  
ATOM   2305  C   ASN A1092      73.848  -1.540 -18.043  1.00 32.84           C  
ANISOU 2305  C   ASN A1092     5204   3403   3870    761    209    771       C  
ATOM   2306  O   ASN A1092      72.872  -1.511 -17.293  1.00 29.52           O  
ANISOU 2306  O   ASN A1092     4706   2967   3545    825    -26    819       O  
ATOM   2307  CB  ASN A1092      72.365  -1.952 -20.021  1.00 35.09           C  
ANISOU 2307  CB  ASN A1092     6145   3297   3891    924    -10    712       C  
ATOM   2308  CG  ASN A1092      72.311  -3.461 -19.847  1.00 41.60           C  
ANISOU 2308  CG  ASN A1092     6730   4167   4909   1075    -43    687       C  
ATOM   2309  OD1 ASN A1092      73.306  -4.159 -20.048  1.00 40.38           O  
ANISOU 2309  OD1 ASN A1092     6446   4102   4796   1087    167    653       O  
ATOM   2310  ND2 ASN A1092      71.143  -3.971 -19.471  1.00 35.19           N  
ANISOU 2310  ND2 ASN A1092     5858   3282   4233   1187   -297    681       N  
ATOM   2311  N   VAL A1093      75.089  -1.738 -17.612  1.00 33.36           N  
ANISOU 2311  N   VAL A1093     4971   3670   4036    708    416    732       N  
ATOM   2312  CA  VAL A1093      75.404  -1.881 -16.197  1.00 27.07           C  
ANISOU 2312  CA  VAL A1093     3771   3081   3433    741    343    766       C  
ATOM   2313  C   VAL A1093      76.597  -1.004 -15.831  1.00 30.12           C  
ANISOU 2313  C   VAL A1093     3961   3650   3835    564    548    687       C  
ATOM   2314  O   VAL A1093      77.673  -1.132 -16.417  1.00 33.39           O  
ANISOU 2314  O   VAL A1093     4304   4133   4248    498    800    567       O  
ATOM   2315  CB  VAL A1093      75.714  -3.345 -15.828  1.00 28.83           C  
ANISOU 2315  CB  VAL A1093     3751   3380   3822    941    304    768       C  
ATOM   2316  CG1 VAL A1093      76.267  -3.428 -14.417  1.00 28.07           C  
ANISOU 2316  CG1 VAL A1093     3290   3503   3872    987    238    794       C  
ATOM   2317  CG2 VAL A1093      74.469  -4.206 -15.969  1.00 25.32           C  
ANISOU 2317  CG2 VAL A1093     3459   2756   3405   1082    105    834       C  
ATOM   2318  N   LYS A1094      76.398  -0.108 -14.870  1.00 32.38           N  
ANISOU 2318  N   LYS A1094     4142   4014   4147    475    453    722       N  
ATOM   2319  CA  LYS A1094      77.462   0.780 -14.416  1.00 33.29           C  
ANISOU 2319  CA  LYS A1094     4043   4304   4302    292    625    620       C  
ATOM   2320  C   LYS A1094      77.704   0.630 -12.920  1.00 33.36           C  
ANISOU 2320  C   LYS A1094     3663   4544   4469    375    464    626       C  
ATOM   2321  O   LYS A1094      76.762   0.636 -12.124  1.00 25.53           O  
ANISOU 2321  O   LYS A1094     2689   3530   3483    451    240    736       O  
ATOM   2322  CB  LYS A1094      77.130   2.234 -14.751  1.00 28.34           C  
ANISOU 2322  CB  LYS A1094     3716   3530   3522     70    690    628       C  
ATOM   2323  CG  LYS A1094      77.471   2.636 -16.175  1.00 36.68           C  
ANISOU 2323  CG  LYS A1094     5147   4401   4387    -84    958    578       C  
ATOM   2324  CD  LYS A1094      78.973   2.723 -16.384  1.00 51.89           C  
ANISOU 2324  CD  LYS A1094     6839   6492   6385   -264   1315    400       C  
ATOM   2325  CE  LYS A1094      79.303   3.168 -17.799  1.00 67.72           C  
ANISOU 2325  CE  LYS A1094     9273   8294   8163   -462   1641    350       C  
ATOM   2326  NZ  LYS A1094      78.837   2.175 -18.803  1.00 71.88           N  
ANISOU 2326  NZ  LYS A1094    10061   8681   8569   -283   1601    398       N  
ATOM   2327  N   VAL A1095      78.973   0.497 -12.547  1.00 45.23           N  
ANISOU 2327  N   VAL A1095     4818   6272   6096    363    581    483       N  
ATOM   2328  CA  VAL A1095      79.352   0.317 -11.150  1.00 40.78           C  
ANISOU 2328  CA  VAL A1095     3899   5940   5655    475    403    465       C  
ATOM   2329  C   VAL A1095      80.143   1.512 -10.630  1.00 42.22           C  
ANISOU 2329  C   VAL A1095     3866   6293   5883    262    502    307       C  
ATOM   2330  O   VAL A1095      81.143   1.912 -11.225  1.00 52.23           O  
ANISOU 2330  O   VAL A1095     5020   7623   7201     94    763    118       O  
ATOM   2331  CB  VAL A1095      80.187  -0.963 -10.953  1.00 41.00           C  
ANISOU 2331  CB  VAL A1095     3650   6108   5820    717    360    394       C  
ATOM   2332  CG1 VAL A1095      80.659  -1.078  -9.510  1.00 31.34           C  
ANISOU 2332  CG1 VAL A1095     2103   5119   4685    855    146    363       C  
ATOM   2333  CG2 VAL A1095      79.379  -2.186 -11.356  1.00 46.93           C  
ANISOU 2333  CG2 VAL A1095     4617   6672   6543    923    256    547       C  
ATOM   2334  N   ILE A1096      79.681   2.077  -9.520  1.00 34.54           N  
ANISOU 2334  N   ILE A1096     2837   5391   4895    251    315    365       N  
ATOM   2335  CA  ILE A1096      80.348   3.200  -8.876  1.00 41.26           C  
ANISOU 2335  CA  ILE A1096     3474   6407   5798     60    368    207       C  
ATOM   2336  C   ILE A1096      80.836   2.802  -7.486  1.00 48.83           C  
ANISOU 2336  C   ILE A1096     4072   7635   6845    241    135    150       C  
ATOM   2337  O   ILE A1096      80.037   2.611  -6.569  1.00 50.05           O  
ANISOU 2337  O   ILE A1096     4296   7793   6928    367    -96    300       O  
ATOM   2338  CB  ILE A1096      79.416   4.424  -8.752  1.00 36.98           C  
ANISOU 2338  CB  ILE A1096     3200   5707   5142   -125    344    287       C  
ATOM   2339  CG1 ILE A1096      78.672   4.674 -10.067  1.00 31.92           C  
ANISOU 2339  CG1 ILE A1096     3005   4755   4366   -213    470    387       C  
ATOM   2340  CG2 ILE A1096      80.201   5.655  -8.318  1.00 34.30           C  
ANISOU 2340  CG2 ILE A1096     2675   5492   4863   -372    463     94       C  
ATOM   2341  CD1 ILE A1096      79.582   4.922 -11.249  1.00 50.54           C  
ANISOU 2341  CD1 ILE A1096     5447   7049   6707   -402    803    259       C  
ATOM   2342  N   THR A1097      82.150   2.675  -7.334  1.00 47.91           N  
ANISOU 2342  N   THR A1097     3580   7746   6879    258    194    -86       N  
ATOM   2343  CA  THR A1097      82.733   2.327  -6.045  1.00 45.31           C  
ANISOU 2343  CA  THR A1097     2925   7671   6621    462    -68   -175       C  
ATOM   2344  C   THR A1097      83.245   3.567  -5.315  1.00 50.80           C  
ANISOU 2344  C   THR A1097     3495   8449   7357    246    -61   -348       C  
ATOM   2345  O   THR A1097      83.584   3.509  -4.133  1.00 55.35           O  
ANISOU 2345  O   THR A1097     4022   9075   7933    362   -289   -371       O  
ATOM   2346  CB  THR A1097      83.887   1.321  -6.206  1.00 43.60           C  
ANISOU 2346  CB  THR A1097     2518   7491   6556    649    -82   -321       C  
ATOM   2347  OG1 THR A1097      84.810   1.808  -7.187  1.00 47.35           O  
ANISOU 2347  OG1 THR A1097     2799   8032   7160    431    242   -575       O  
ATOM   2348  CG2 THR A1097      83.358  -0.034  -6.647  1.00 37.04           C  
ANISOU 2348  CG2 THR A1097     1857   6531   5685    910   -157   -139       C  
ATOM   2349  N   GLU A1098      83.294   4.688  -6.026  1.00 54.87           N  
ANISOU 2349  N   GLU A1098     4004   8954   7890    -85    218   -466       N  
ATOM   2350  CA  GLU A1098      83.800   5.934  -5.462  1.00 53.99           C  
ANISOU 2350  CA  GLU A1098     3813   8877   7826   -316    262   -637       C  
ATOM   2351  C   GLU A1098      82.763   6.577  -4.546  1.00 45.87           C  
ANISOU 2351  C   GLU A1098     2948   7815   6664   -330     67   -492       C  
ATOM   2352  O   GLU A1098      81.584   6.227  -4.588  1.00 54.55           O  
ANISOU 2352  O   GLU A1098     4285   8812   7628   -229    -37   -253       O  
ATOM   2353  CB  GLU A1098      84.199   6.895  -6.584  1.00 67.85           C  
ANISOU 2353  CB  GLU A1098     5620  10532   9630   -696    669   -796       C  
ATOM   2354  CG  GLU A1098      85.253   7.918  -6.194  1.00 90.28           C  
ANISOU 2354  CG  GLU A1098     8310  13419  12574   -903    762  -1048       C  
ATOM   2355  CD  GLU A1098      85.956   8.514  -7.399  1.00106.90           C  
ANISOU 2355  CD  GLU A1098    10488  15399  14732  -1230   1190  -1220       C  
ATOM   2356  OE1 GLU A1098      86.028   7.834  -8.445  1.00106.35           O  
ANISOU 2356  OE1 GLU A1098    10493  15262  14653  -1223   1389  -1194       O  
ATOM   2357  OE2 GLU A1098      86.436   9.663  -7.301  1.00114.06           O  
ANISOU 2357  OE2 GLU A1098    11411  16253  15673  -1495   1338  -1383       O  
ATOM   2358  N   MET A1099      83.207   7.513  -3.714  1.00 47.62           N  
ANISOU 2358  N   MET A1099     3090   8084   6917   -445     17   -634       N  
ATOM   2359  CA  MET A1099      82.318   8.187  -2.774  1.00 59.18           C  
ANISOU 2359  CA  MET A1099     4701   9516   8268   -461   -151   -541       C  
ATOM   2360  C   MET A1099      81.522   9.291  -3.466  1.00 59.83           C  
ANISOU 2360  C   MET A1099     4968   9462   8303   -760     37   -517       C  
ATOM   2361  O   MET A1099      82.077  10.078  -4.232  1.00 61.22           O  
ANISOU 2361  O   MET A1099     5148   9558   8555  -1046    315   -668       O  
ATOM   2362  CB  MET A1099      83.117   8.770  -1.607  1.00 71.71           C  
ANISOU 2362  CB  MET A1099     6135  11215   9895   -464   -274   -717       C  
ATOM   2363  CG  MET A1099      82.264   9.282  -0.458  1.00 82.74           C  
ANISOU 2363  CG  MET A1099     7679  12595  11165   -429   -463   -633       C  
ATOM   2364  SD  MET A1099      81.754   7.971   0.670  1.00 91.81           S  
ANISOU 2364  SD  MET A1099     8949  13767  12168    -78   -759   -437       S  
ATOM   2365  CE  MET A1099      83.316   7.577   1.453  1.00 87.30           C  
ANISOU 2365  CE  MET A1099     8109  13388  11674     63   -899   -634       C  
ATOM   2366  N   LEU A1100      80.223   9.346  -3.189  1.00 56.20           N  
ANISOU 2366  N   LEU A1100     4760   8887   7706   -688   -106   -312       N  
ATOM   2367  CA  LEU A1100      79.350  10.355  -3.783  1.00 47.52           C  
ANISOU 2367  CA  LEU A1100     4028   7487   6539   -875      3   -236       C  
ATOM   2368  C   LEU A1100      78.791  11.294  -2.720  1.00 55.48           C  
ANISOU 2368  C   LEU A1100     5037   8529   7513   -932   -142   -286       C  
ATOM   2369  O   LEU A1100      78.501  10.870  -1.600  1.00 60.45           O  
ANISOU 2369  O   LEU A1100     5526   9346   8094   -759   -362   -260       O  
ATOM   2370  CB  LEU A1100      78.202   9.690  -4.545  1.00 34.07           C  
ANISOU 2370  CB  LEU A1100     2673   5541   4731   -723    -38     11       C  
ATOM   2371  CG  LEU A1100      78.601   8.618  -5.562  1.00 37.74           C  
ANISOU 2371  CG  LEU A1100     3166   5966   5209   -626     76     76       C  
ATOM   2372  CD1 LEU A1100      77.367   7.919  -6.114  1.00 26.41           C  
ANISOU 2372  CD1 LEU A1100     2039   4317   3680   -455    -22    294       C  
ATOM   2373  CD2 LEU A1100      79.436   9.222  -6.684  1.00 38.30           C  
ANISOU 2373  CD2 LEU A1100     3322   5918   5311   -878    391    -46       C  
ATOM   2374  N   SER A1101      78.642  12.567  -3.073  1.00 56.96           N  
ANISOU 2374  N   SER A1101     5417   8516   7709  -1175    -10   -361       N  
ATOM   2375  CA  SER A1101      78.071  13.552  -2.160  1.00 47.49           C  
ANISOU 2375  CA  SER A1101     4246   7310   6489  -1237   -133   -430       C  
ATOM   2376  C   SER A1101      76.568  13.343  -2.019  1.00 54.33           C  
ANISOU 2376  C   SER A1101     5365   8025   7254  -1057   -307   -246       C  
ATOM   2377  O   SER A1101      75.946  12.690  -2.857  1.00 60.42           O  
ANISOU 2377  O   SER A1101     6353   8623   7979   -938   -305    -78       O  
ATOM   2378  CB  SER A1101      78.358  14.974  -2.647  1.00 41.80           C  
ANISOU 2378  CB  SER A1101     3697   6368   5815  -1548     68   -567       C  
ATOM   2379  OG  SER A1101      77.757  15.209  -3.909  1.00 40.52           O  
ANISOU 2379  OG  SER A1101     3982   5838   5576  -1590    188   -418       O  
ATOM   2380  N   ARG A1102      75.991  13.895  -0.956  1.00 54.51           N  
ANISOU 2380  N   ARG A1102     5338   8118   7254  -1042   -453   -312       N  
ATOM   2381  CA  ARG A1102      74.552  13.803  -0.737  1.00 39.74           C  
ANISOU 2381  CA  ARG A1102     3654   6121   5323   -898   -593   -206       C  
ATOM   2382  C   ARG A1102      73.780  14.459  -1.874  1.00 33.77           C  
ANISOU 2382  C   ARG A1102     3271   4989   4572   -940   -550   -155       C  
ATOM   2383  O   ARG A1102      72.709  13.994  -2.249  1.00 37.00           O  
ANISOU 2383  O   ARG A1102     3844   5257   4957   -783   -644    -47       O  
ATOM   2384  CB  ARG A1102      74.154  14.450   0.591  1.00 39.89           C  
ANISOU 2384  CB  ARG A1102     3553   6281   5322   -913   -714   -337       C  
ATOM   2385  CG  ARG A1102      74.354  13.570   1.810  1.00 50.02           C  
ANISOU 2385  CG  ARG A1102     4695   7776   6535   -726   -794   -304       C  
ATOM   2386  CD  ARG A1102      73.339  13.910   2.892  1.00 62.35           C  
ANISOU 2386  CD  ARG A1102     6334   9316   8041   -662   -869   -341       C  
ATOM   2387  NE  ARG A1102      73.329  15.335   3.213  1.00 71.51           N  
ANISOU 2387  NE  ARG A1102     7498  10426   9246   -815   -868   -516       N  
ATOM   2388  CZ  ARG A1102      72.472  15.906   4.055  1.00 69.41           C  
ANISOU 2388  CZ  ARG A1102     7287  10133   8954   -796   -915   -591       C  
ATOM   2389  NH1 ARG A1102      71.547  15.173   4.663  1.00 64.26           N  
ANISOU 2389  NH1 ARG A1102     6673   9516   8227   -664   -944   -519       N  
ATOM   2390  NH2 ARG A1102      72.538  17.211   4.288  1.00 59.90           N  
ANISOU 2390  NH2 ARG A1102     6095   8866   7799   -929   -913   -758       N  
ATOM   2391  N   GLU A1103      74.328  15.542  -2.413  1.00 34.60           N  
ANISOU 2391  N   GLU A1103     3522   4919   4704  -1151   -413   -246       N  
ATOM   2392  CA  GLU A1103      73.675  16.274  -3.492  1.00 42.85           C  
ANISOU 2392  CA  GLU A1103     5001   5568   5713  -1182   -390   -195       C  
ATOM   2393  C   GLU A1103      73.583  15.416  -4.750  1.00 44.07           C  
ANISOU 2393  C   GLU A1103     5369   5574   5799  -1084   -334    -27       C  
ATOM   2394  O   GLU A1103      72.540  15.371  -5.414  1.00 50.50           O  
ANISOU 2394  O   GLU A1103     6478   6146   6564   -936   -460     57       O  
ATOM   2395  CB  GLU A1103      74.423  17.578  -3.789  1.00 39.28           C  
ANISOU 2395  CB  GLU A1103     4706   4937   5280  -1463   -208   -318       C  
ATOM   2396  CG  GLU A1103      74.319  18.633  -2.688  1.00 42.80           C  
ANISOU 2396  CG  GLU A1103     5030   5440   5792  -1559   -282   -502       C  
ATOM   2397  CD  GLU A1103      75.144  18.295  -1.456  1.00 57.62           C  
ANISOU 2397  CD  GLU A1103     6422   7741   7732  -1603   -293   -641       C  
ATOM   2398  OE1 GLU A1103      76.066  17.457  -1.565  1.00 57.70           O  
ANISOU 2398  OE1 GLU A1103     6198   7967   7758  -1613   -201   -627       O  
ATOM   2399  OE2 GLU A1103      74.868  18.866  -0.378  1.00 58.31           O  
ANISOU 2399  OE2 GLU A1103     6369   7942   7845  -1609   -410   -779       O  
ATOM   2400  N   PHE A1104      74.673  14.724  -5.064  1.00 33.27           N  
ANISOU 2400  N   PHE A1104     3837   4364   4441  -1154   -161    -10       N  
ATOM   2401  CA  PHE A1104      74.701  13.841  -6.222  1.00 34.49           C  
ANISOU 2401  CA  PHE A1104     4166   4409   4530  -1068    -86    127       C  
ATOM   2402  C   PHE A1104      73.716  12.686  -6.059  1.00 32.46           C  
ANISOU 2402  C   PHE A1104     3852   4215   4266   -791   -292    246       C  
ATOM   2403  O   PHE A1104      72.965  12.369  -6.981  1.00 28.67           O  
ANISOU 2403  O   PHE A1104     3655   3514   3724   -672   -354    343       O  
ATOM   2404  CB  PHE A1104      76.109  13.297  -6.459  1.00 37.15           C  
ANISOU 2404  CB  PHE A1104     4262   4939   4912  -1188    144     71       C  
ATOM   2405  CG  PHE A1104      76.217  12.419  -7.671  1.00 53.17           C  
ANISOU 2405  CG  PHE A1104     6473   6857   6872  -1117    253    187       C  
ATOM   2406  CD1 PHE A1104      76.155  12.963  -8.943  1.00 59.35           C  
ANISOU 2406  CD1 PHE A1104     7711   7310   7529  -1235    414    235       C  
ATOM   2407  CD2 PHE A1104      76.371  11.050  -7.541  1.00 58.66           C  
ANISOU 2407  CD2 PHE A1104     6925   7757   7605   -924    192    247       C  
ATOM   2408  CE1 PHE A1104      76.247  12.159 -10.060  1.00 60.66           C  
ANISOU 2408  CE1 PHE A1104     8065   7379   7605  -1168    515    327       C  
ATOM   2409  CE2 PHE A1104      76.466  10.240  -8.656  1.00 51.49           C  
ANISOU 2409  CE2 PHE A1104     6182   6745   6639   -857    293    332       C  
ATOM   2410  CZ  PHE A1104      76.403  10.795  -9.915  1.00 52.76           C  
ANISOU 2410  CZ  PHE A1104     6775   6601   6670   -981    456    365       C  
ATOM   2411  N   VAL A1105      73.724  12.061  -4.885  1.00 24.15           N  
ANISOU 2411  N   VAL A1105     2454   3452   3269   -697   -394    228       N  
ATOM   2412  CA  VAL A1105      72.796  10.972  -4.594  1.00 28.84           C  
ANISOU 2412  CA  VAL A1105     2997   4099   3863   -478   -546    329       C  
ATOM   2413  C   VAL A1105      71.346  11.454  -4.681  1.00 27.81           C  
ANISOU 2413  C   VAL A1105     3073   3756   3738   -396   -703    313       C  
ATOM   2414  O   VAL A1105      70.471  10.740  -5.175  1.00 29.93           O  
ANISOU 2414  O   VAL A1105     3445   3914   4013   -248   -791    377       O  
ATOM   2415  CB  VAL A1105      73.061  10.364  -3.202  1.00 31.29           C  
ANISOU 2415  CB  VAL A1105     2976   4727   4187   -413   -614    313       C  
ATOM   2416  CG1 VAL A1105      71.981   9.355  -2.842  1.00 32.18           C  
ANISOU 2416  CG1 VAL A1105     3092   4845   4290   -236   -727    409       C  
ATOM   2417  CG2 VAL A1105      74.438   9.715  -3.162  1.00 23.19           C  
ANISOU 2417  CG2 VAL A1105     1725   3911   3175   -419   -522    306       C  
ATOM   2418  N   ARG A1106      71.106  12.676  -4.216  1.00 24.14           N  
ANISOU 2418  N   ARG A1106     2651   3230   3290   -489   -746    195       N  
ATOM   2419  CA  ARG A1106      69.784  13.283  -4.292  1.00 22.07           C  
ANISOU 2419  CA  ARG A1106     2565   2760   3061   -397   -913    127       C  
ATOM   2420  C   ARG A1106      69.364  13.448  -5.745  1.00 32.53           C  
ANISOU 2420  C   ARG A1106     4276   3751   4334   -325   -960    182       C  
ATOM   2421  O   ARG A1106      68.209  13.206  -6.098  1.00 29.47           O  
ANISOU 2421  O   ARG A1106     3991   3225   3982   -151  -1135    158       O  
ATOM   2422  CB  ARG A1106      69.762  14.635  -3.575  1.00 25.18           C  
ANISOU 2422  CB  ARG A1106     2952   3131   3484   -512   -939    -24       C  
ATOM   2423  CG  ARG A1106      68.409  15.331  -3.617  1.00 32.36           C  
ANISOU 2423  CG  ARG A1106     4020   3822   4452   -390  -1132   -137       C  
ATOM   2424  CD  ARG A1106      68.365  16.536  -2.701  1.00 35.74           C  
ANISOU 2424  CD  ARG A1106     4385   4268   4925   -488  -1159   -307       C  
ATOM   2425  NE  ARG A1106      69.298  17.580  -3.116  1.00 42.36           N  
ANISOU 2425  NE  ARG A1106     5428   4947   5719   -677  -1044   -319       N  
ATOM   2426  CZ  ARG A1106      69.443  18.743  -2.490  1.00 41.59           C  
ANISOU 2426  CZ  ARG A1106     5330   4811   5660   -799  -1041   -469       C  
ATOM   2427  NH1 ARG A1106      68.713  19.016  -1.419  1.00 45.34           N  
ANISOU 2427  NH1 ARG A1106     5608   5412   6207   -734  -1157   -622       N  
ATOM   2428  NH2 ARG A1106      70.316  19.634  -2.937  1.00 38.52           N  
ANISOU 2428  NH2 ARG A1106     5148   4249   5238  -1004   -898   -482       N  
ATOM   2429  N   GLU A1107      70.308  13.857  -6.587  1.00 27.67           N  
ANISOU 2429  N   GLU A1107     3878   3006   3628   -463   -800    235       N  
ATOM   2430  CA  GLU A1107      70.041  13.945  -8.019  1.00 27.16           C  
ANISOU 2430  CA  GLU A1107     4247   2620   3451   -401   -822    309       C  
ATOM   2431  C   GLU A1107      69.737  12.566  -8.604  1.00 30.67           C  
ANISOU 2431  C   GLU A1107     4656   3112   3886   -237   -861    403       C  
ATOM   2432  O   GLU A1107      68.885  12.429  -9.484  1.00 25.03           O  
ANISOU 2432  O   GLU A1107     4217   2170   3121    -74  -1022    417       O  
ATOM   2433  CB  GLU A1107      71.223  14.579  -8.753  1.00 39.86           C  
ANISOU 2433  CB  GLU A1107     6103   4097   4946   -633   -562    344       C  
ATOM   2434  CG  GLU A1107      71.427  16.051  -8.448  1.00 64.30           C  
ANISOU 2434  CG  GLU A1107     9359   7034   8038   -808   -518    249       C  
ATOM   2435  CD  GLU A1107      72.618  16.636  -9.179  1.00 88.10           C  
ANISOU 2435  CD  GLU A1107    12620   9904  10950  -1089   -199    265       C  
ATOM   2436  OE1 GLU A1107      73.336  15.869  -9.857  1.00 96.73           O  
ANISOU 2436  OE1 GLU A1107    13704  11063  11985  -1146     -3    333       O  
ATOM   2437  OE2 GLU A1107      72.836  17.862  -9.077  1.00 97.57           O  
ANISOU 2437  OE2 GLU A1107    14024  10913  12134  -1267   -122    194       O  
ATOM   2438  N   LEU A1108      70.437  11.547  -8.112  1.00 28.31           N  
ANISOU 2438  N   LEU A1108     2216   4437   4104   -236   -541    -65       N  
ATOM   2439  CA  LEU A1108      70.223  10.178  -8.572  1.00 21.03           C  
ANISOU 2439  CA  LEU A1108     1606   3488   2895   -174   -502     29       C  
ATOM   2440  C   LEU A1108      68.805   9.726  -8.275  1.00 21.73           C  
ANISOU 2440  C   LEU A1108     1827   3385   3046   -295   -527      7       C  
ATOM   2441  O   LEU A1108      68.088   9.291  -9.172  1.00 28.04           O  
ANISOU 2441  O   LEU A1108     2825   4000   3830   -393   -571    102       O  
ATOM   2442  CB  LEU A1108      71.223   9.225  -7.923  1.00 20.06           C  
ANISOU 2442  CB  LEU A1108     1609   3542   2469     77   -385      4       C  
ATOM   2443  CG  LEU A1108      72.637   9.285  -8.495  1.00 32.86           C  
ANISOU 2443  CG  LEU A1108     3194   5318   3971    217   -342     48       C  
ATOM   2444  CD1 LEU A1108      73.588   8.419  -7.687  1.00 39.05           C  
ANISOU 2444  CD1 LEU A1108     4061   6273   4502    472   -248      1       C  
ATOM   2445  CD2 LEU A1108      72.622   8.854  -9.947  1.00 22.10           C  
ANISOU 2445  CD2 LEU A1108     2055   3833   2510    162   -344    194       C  
ATOM   2446  N   TYR A1109      68.410   9.839  -7.010  1.00 21.86           N  
ANISOU 2446  N   TYR A1109     1728   3446   3132   -294   -495   -130       N  
ATOM   2447  CA  TYR A1109      67.059   9.489  -6.583  1.00 17.94           C  
ANISOU 2447  CA  TYR A1109     1321   2773   2723   -419   -498   -183       C  
ATOM   2448  C   TYR A1109      65.984  10.205  -7.398  1.00 27.18           C  
ANISOU 2448  C   TYR A1109     2435   3726   4164   -639   -603   -156       C  
ATOM   2449  O   TYR A1109      64.917   9.651  -7.653  1.00 21.83           O  
ANISOU 2449  O   TYR A1109     1922   2854   3518   -735   -623   -139       O  
ATOM   2450  CB  TYR A1109      66.868   9.819  -5.107  1.00 18.02           C  
ANISOU 2450  CB  TYR A1109     1151   2886   2812   -416   -446   -356       C  
ATOM   2451  CG  TYR A1109      67.568   8.885  -4.151  1.00 29.63           C  
ANISOU 2451  CG  TYR A1109     2774   4525   3959   -203   -326   -382       C  
ATOM   2452  CD1 TYR A1109      67.864   7.577  -4.512  1.00 18.81           C  
ANISOU 2452  CD1 TYR A1109     1739   3130   2279    -58   -261   -266       C  
ATOM   2453  CD2 TYR A1109      67.923   9.312  -2.876  1.00 27.84           C  
ANISOU 2453  CD2 TYR A1109     2358   4480   3742   -150   -286   -526       C  
ATOM   2454  CE1 TYR A1109      68.498   6.722  -3.630  1.00 32.04           C  
ANISOU 2454  CE1 TYR A1109     3556   4946   3672    141   -167   -280       C  
ATOM   2455  CE2 TYR A1109      68.557   8.465  -1.989  1.00 25.77           C  
ANISOU 2455  CE2 TYR A1109     2245   4370   3178     45   -197   -539       C  
ATOM   2456  CZ  TYR A1109      68.842   7.173  -2.369  1.00 28.14           C  
ANISOU 2456  CZ  TYR A1109     2878   4631   3183    193   -143   -410       C  
ATOM   2457  OH  TYR A1109      69.473   6.332  -1.483  1.00 36.89           O  
ANISOU 2457  OH  TYR A1109     4136   5878   4004    391    -70   -413       O  
ATOM   2458  N   GLY A1110      66.271  11.440  -7.798  1.00 25.41           N  
ANISOU 2458  N   GLY A1110     2158   3560   3934   -630   -550   -151       N  
ATOM   2459  CA  GLY A1110      65.319  12.239  -8.546  1.00 21.48           C  
ANISOU 2459  CA  GLY A1110     1757   2915   3488   -700   -534   -136       C  
ATOM   2460  C   GLY A1110      65.339  11.997 -10.044  1.00 29.88           C  
ANISOU 2460  C   GLY A1110     2919   3836   4596   -727   -627    -12       C  
ATOM   2461  O   GLY A1110      64.542  12.577 -10.778  1.00 31.78           O  
ANISOU 2461  O   GLY A1110     3230   3959   4887   -757   -638     17       O  
ATOM   2462  N   SER A1111      66.242  11.133 -10.501  1.00 35.20           N  
ANISOU 2462  N   SER A1111     3613   4551   5211   -724   -722    109       N  
ATOM   2463  CA  SER A1111      66.392  10.874 -11.930  1.00 28.22           C  
ANISOU 2463  CA  SER A1111     2865   3579   4279   -799   -832    291       C  
ATOM   2464  C   SER A1111      66.041   9.436 -12.309  1.00 32.28           C  
ANISOU 2464  C   SER A1111     3670   4005   4591   -825   -862    383       C  
ATOM   2465  O   SER A1111      65.377   9.200 -13.320  1.00 33.27           O  
ANISOU 2465  O   SER A1111     3963   3959   4719   -941   -952    477       O  
ATOM   2466  CB  SER A1111      67.820  11.190 -12.377  1.00 18.59           C  
ANISOU 2466  CB  SER A1111     1531   2543   2987   -759   -849    376       C  
ATOM   2467  OG  SER A1111      68.112  12.564 -12.199  1.00 62.29           O  
ANISOU 2467  OG  SER A1111     6923   8109   8634   -694   -749    255       O  
ATOM   2468  N   VAL A1112      66.494   8.481 -11.504  1.00 26.39           N  
ANISOU 2468  N   VAL A1112     3050   3370   3606   -643   -716    328       N  
ATOM   2469  CA  VAL A1112      66.247   7.071 -11.782  1.00 27.10           C  
ANISOU 2469  CA  VAL A1112     3486   3381   3432   -566   -640    378       C  
ATOM   2470  C   VAL A1112      64.764   6.730 -11.687  1.00 25.41           C  
ANISOU 2470  C   VAL A1112     3366   2938   3350   -710   -693    342       C  
ATOM   2471  O   VAL A1112      63.978   7.481 -11.112  1.00 30.95           O  
ANISOU 2471  O   VAL A1112     3858   3567   4333   -840   -760    250       O  
ATOM   2472  CB  VAL A1112      67.027   6.155 -10.820  1.00 21.37           C  
ANISOU 2472  CB  VAL A1112     2860   2813   2448   -336   -481    327       C  
ATOM   2473  CG1 VAL A1112      68.523   6.338 -11.012  1.00 19.03           C  
ANISOU 2473  CG1 VAL A1112     2492   2728   2009   -178   -426    358       C  
ATOM   2474  CG2 VAL A1112      66.622   6.434  -9.381  1.00 18.39           C  
ANISOU 2474  CG2 VAL A1112     2316   2480   2193   -334   -450    188       C  
ATOM   2475  N   ASP A1113      64.391   5.589 -12.254  1.00 25.07           N  
ANISOU 2475  N   ASP A1113     3630   2777   3117   -689   -657    402       N  
ATOM   2476  CA  ASP A1113      63.007   5.139 -12.227  1.00 18.55           C  
ANISOU 2476  CA  ASP A1113     2916   1727   2405   -817   -696    363       C  
ATOM   2477  C   ASP A1113      62.720   4.365 -10.950  1.00 25.12           C  
ANISOU 2477  C   ASP A1113     3819   2570   3157   -727   -554    260       C  
ATOM   2478  O   ASP A1113      61.772   4.669 -10.226  1.00 38.60           O  
ANISOU 2478  O   ASP A1113     5408   4179   5078   -840   -569    152       O  
ATOM   2479  CB  ASP A1113      62.705   4.281 -13.454  1.00 31.33           C  
ANISOU 2479  CB  ASP A1113     4830   3209   3866   -847   -725    467       C  
ATOM   2480  CG  ASP A1113      62.813   5.063 -14.748  1.00 42.41           C  
ANISOU 2480  CG  ASP A1113     6187   4578   5350   -972   -880    574       C  
ATOM   2481  OD1 ASP A1113      62.267   6.183 -14.811  1.00 52.50           O  
ANISOU 2481  OD1 ASP A1113     7197   5866   6886  -1036   -973    529       O  
ATOM   2482  OD2 ASP A1113      63.451   4.566 -15.698  1.00 48.40           O  
ANISOU 2482  OD2 ASP A1113     7137   5378   5875   -916   -854    673       O  
ATOM   2483  N   PHE A1114      63.552   3.367 -10.675  1.00 21.65           N  
ANISOU 2483  N   PHE A1114     3571   2246   2410   -525   -416    292       N  
ATOM   2484  CA  PHE A1114      63.380   2.539  -9.491  1.00 18.93           C  
ANISOU 2484  CA  PHE A1114     3332   1916   1944   -424   -278    221       C  
ATOM   2485  C   PHE A1114      64.661   2.446  -8.680  1.00 24.11           C  
ANISOU 2485  C   PHE A1114     3938   2815   2408   -211   -184    212       C  
ATOM   2486  O   PHE A1114      65.763   2.563  -9.218  1.00 25.21           O  
ANISOU 2486  O   PHE A1114     4059   3090   2429    -99   -190    278       O  
ATOM   2487  CB  PHE A1114      62.921   1.133  -9.876  1.00 19.35           C  
ANISOU 2487  CB  PHE A1114     3728   1816   1810   -384   -201    270       C  
ATOM   2488  CG  PHE A1114      61.641   1.103 -10.650  1.00 19.30           C  
ANISOU 2488  CG  PHE A1114     3787   1565   1980   -583   -294    268       C  
ATOM   2489  CD1 PHE A1114      61.653   1.172 -12.032  1.00 32.05           C  
ANISOU 2489  CD1 PHE A1114     5480   3109   3587   -650   -400    360       C  
ATOM   2490  CD2 PHE A1114      60.427   0.995  -9.998  1.00 25.97           C  
ANISOU 2490  CD2 PHE A1114     4620   2249   2998   -707   -276    166       C  
ATOM   2491  CE1 PHE A1114      60.473   1.142 -12.750  1.00 36.07           C  
ANISOU 2491  CE1 PHE A1114     6010   3439   4257   -804   -497    343       C  
ATOM   2492  CE2 PHE A1114      59.244   0.964 -10.707  1.00 33.58           C  
ANISOU 2492  CE2 PHE A1114     5544   3074   4142   -826   -351    141       C  
ATOM   2493  CZ  PHE A1114      59.266   1.037 -12.085  1.00 30.41           C  
ANISOU 2493  CZ  PHE A1114     5148   2684   3721   -833   -452    220       C  
ATOM   2494  N   VAL A1115      64.503   2.232  -7.379  1.00 24.70           N  
ANISOU 2494  N   VAL A1115     3992   2942   2452   -160    -99    125       N  
ATOM   2495  CA  VAL A1115      65.632   1.969  -6.500  1.00 28.24           C  
ANISOU 2495  CA  VAL A1115     4431   3607   2690     54    -16    116       C  
ATOM   2496  C   VAL A1115      65.467   0.585  -5.871  1.00 30.74           C  
ANISOU 2496  C   VAL A1115     5043   3870   2767    176    111    137       C  
ATOM   2497  O   VAL A1115      64.448   0.289  -5.245  1.00 28.26           O  
ANISOU 2497  O   VAL A1115     4799   3430   2509     76    162     78       O  
ATOM   2498  CB  VAL A1115      65.766   3.046  -5.405  1.00 29.14           C  
ANISOU 2498  CB  VAL A1115     4240   3873   2959     20    -36     -7       C  
ATOM   2499  CG1 VAL A1115      64.411   3.347  -4.778  1.00 35.65           C  
ANISOU 2499  CG1 VAL A1115     4995   4552   3998   -178    -32   -118       C  
ATOM   2500  CG2 VAL A1115      66.782   2.617  -4.353  1.00 25.55           C  
ANISOU 2500  CG2 VAL A1115     3814   3627   2266    241     46    -24       C  
ATOM   2501  N   ILE A1116      66.465  -0.269  -6.063  1.00 36.40           N  
ANISOU 2501  N   ILE A1116     5933   4670   3227    386    168    221       N  
ATOM   2502  CA  ILE A1116      66.400  -1.636  -5.563  1.00 31.89           C  
ANISOU 2502  CA  ILE A1116     5621   4034   2464    507    276    256       C  
ATOM   2503  C   ILE A1116      67.029  -1.744  -4.178  1.00 28.01           C  
ANISOU 2503  C   ILE A1116     5034   3706   1903    635    315    211       C  
ATOM   2504  O   ILE A1116      68.194  -1.391  -3.990  1.00 28.40           O  
ANISOU 2504  O   ILE A1116     4931   3939   1922    760    280    208       O  
ATOM   2505  CB  ILE A1116      67.099  -2.612  -6.526  1.00 36.75           C  
ANISOU 2505  CB  ILE A1116     6281   4605   3076    597    279    320       C  
ATOM   2506  CG1 ILE A1116      66.473  -2.508  -7.918  1.00 32.46           C  
ANISOU 2506  CG1 ILE A1116     5819   3912   2600    461    233    357       C  
ATOM   2507  CG2 ILE A1116      67.012  -4.036  -5.999  1.00 35.92           C  
ANISOU 2507  CG2 ILE A1116     6309   4402   2936    681    355    325       C  
ATOM   2508  CD1 ILE A1116      67.131  -3.384  -8.955  1.00 34.00           C  
ANISOU 2508  CD1 ILE A1116     6056   4082   2781    533    248    391       C  
ATOM   2509  N   ILE A1117      66.246  -2.221  -3.213  1.00 24.41           N  
ANISOU 2509  N   ILE A1117     4675   3173   1427    589    384    173       N  
ATOM   2510  CA  ILE A1117      66.715  -2.389  -1.840  1.00 27.35           C  
ANISOU 2510  CA  ILE A1117     4986   3681   1724    680    413    140       C  
ATOM   2511  C   ILE A1117      66.536  -3.837  -1.388  1.00 39.73           C  
ANISOU 2511  C   ILE A1117     6727   5121   3249    733    473    194       C  
ATOM   2512  O   ILE A1117      65.610  -4.151  -0.641  1.00 40.94           O  
ANISOU 2512  O   ILE A1117     6980   5186   3389    651    542    163       O  
ATOM   2513  CB  ILE A1117      65.966  -1.459  -0.869  1.00 28.93           C  
ANISOU 2513  CB  ILE A1117     5121   3945   1926    564    451     17       C  
ATOM   2514  CG1 ILE A1117      65.755  -0.084  -1.503  1.00 35.54           C  
ANISOU 2514  CG1 ILE A1117     5680   4804   3020    411    356    -59       C  
ATOM   2515  CG2 ILE A1117      66.723  -1.335   0.442  1.00 24.45           C  
ANISOU 2515  CG2 ILE A1117     4432   3582   1277    663    449    -23       C  
ATOM   2516  CD1 ILE A1117      64.863   0.823  -0.695  1.00 38.35           C  
ANISOU 2516  CD1 ILE A1117     5824   5151   3596    209    359   -210       C  
ATOM   2517  N   PRO A1118      67.435  -4.725  -1.835  1.00 41.14           N  
ANISOU 2517  N   PRO A1118     6947   5282   3401    874    456    263       N  
ATOM   2518  CA  PRO A1118      67.303  -6.168  -1.631  1.00 39.67           C  
ANISOU 2518  CA  PRO A1118     6943   4953   3178    943    510    311       C  
ATOM   2519  C   PRO A1118      67.927  -6.657  -0.328  1.00 38.87           C  
ANISOU 2519  C   PRO A1118     6857   4940   2970   1062    520    327       C  
ATOM   2520  O   PRO A1118      68.529  -7.731  -0.305  1.00 39.68           O  
ANISOU 2520  O   PRO A1118     7063   4990   3024   1200    532    378       O  
ATOM   2521  CB  PRO A1118      68.045  -6.749  -2.838  1.00 43.51           C  
ANISOU 2521  CB  PRO A1118     7456   5390   3686   1037    490    354       C  
ATOM   2522  CG  PRO A1118      69.027  -5.658  -3.266  1.00 33.38           C  
ANISOU 2522  CG  PRO A1118     5981   4286   2417   1073    420    340       C  
ATOM   2523  CD  PRO A1118      68.702  -4.394  -2.504  1.00 36.02           C  
ANISOU 2523  CD  PRO A1118     6177   4754   2755    987    394    283       C  
ATOM   2524  N   SER A1119      67.773  -5.880   0.739  1.00 36.69           N  
ANISOU 2524  N   SER A1119     6490   4796   2653   1008    517    276       N  
ATOM   2525  CA  SER A1119      68.377  -6.206   2.026  1.00 40.52           C  
ANISOU 2525  CA  SER A1119     6986   5386   3023   1107    513    287       C  
ATOM   2526  C   SER A1119      67.872  -7.528   2.596  1.00 45.55           C  
ANISOU 2526  C   SER A1119     7838   5874   3595   1128    582    341       C  
ATOM   2527  O   SER A1119      66.709  -7.883   2.419  1.00 48.42           O  
ANISOU 2527  O   SER A1119     8318   6076   4005   1010    653    333       O  
ATOM   2528  CB  SER A1119      68.107  -5.086   3.035  1.00 38.92           C  
ANISOU 2528  CB  SER A1119     6651   5347   2788   1008    510    199       C  
ATOM   2529  OG  SER A1119      68.566  -3.838   2.551  1.00 50.47           O  
ANISOU 2529  OG  SER A1119     7914   6948   4314    999    450    138       O  
ATOM   2530  N   TYR A1120      68.756  -8.255   3.275  1.00 45.77           N  
ANISOU 2530  N   TYR A1120     7927   5946   3518   1287    564    393       N  
ATOM   2531  CA  TYR A1120      68.345  -9.395   4.087  1.00 42.62           C  
ANISOU 2531  CA  TYR A1120     7727   5437   3029   1311    627    443       C  
ATOM   2532  C   TYR A1120      67.825  -8.872   5.416  1.00 45.95           C  
ANISOU 2532  C   TYR A1120     8127   5966   3366   1200    652    401       C  
ATOM   2533  O   TYR A1120      66.924  -9.450   6.024  1.00 48.35           O  
ANISOU 2533  O   TYR A1120     8576   6166   3628   1120    734    412       O  
ATOM   2534  CB  TYR A1120      69.504 -10.364   4.331  1.00 36.48           C  
ANISOU 2534  CB  TYR A1120     7037   4666   2157   1531    595    514       C  
ATOM   2535  CG  TYR A1120      69.982 -11.134   3.121  1.00 45.76           C  
ANISOU 2535  CG  TYR A1120     8274   5719   3394   1649    599    547       C  
ATOM   2536  CD1 TYR A1120      70.739 -10.517   2.133  1.00 53.04           C  
ANISOU 2536  CD1 TYR A1120     9049   6715   4388   1701    545    521       C  
ATOM   2537  CD2 TYR A1120      69.704 -12.487   2.983  1.00 42.01           C  
ANISOU 2537  CD2 TYR A1120     8009   5059   2893   1711    664    595       C  
ATOM   2538  CE1 TYR A1120      71.191 -11.223   1.035  1.00 60.51           C  
ANISOU 2538  CE1 TYR A1120    10057   7562   5374   1802    560    541       C  
ATOM   2539  CE2 TYR A1120      70.152 -13.201   1.888  1.00 48.58           C  
ANISOU 2539  CE2 TYR A1120     8901   5789   3770   1817    678    608       C  
ATOM   2540  CZ  TYR A1120      70.895 -12.564   0.917  1.00 55.09           C  
ANISOU 2540  CZ  TYR A1120     9577   6696   4659   1859    627    581       C  
ATOM   2541  OH  TYR A1120      71.343 -13.271  -0.175  1.00 62.37           O  
ANISOU 2541  OH  TYR A1120    10564   7523   5610   1958    651    587       O  
ATOM   2542  N   PHE A1121      68.417  -7.766   5.854  1.00 49.44           N  
ANISOU 2542  N   PHE A1121     8386   6617   3782   1198    589    344       N  
ATOM   2543  CA  PHE A1121      68.096  -7.152   7.135  1.00 55.24           C  
ANISOU 2543  CA  PHE A1121     9073   7493   4424   1097    608    280       C  
ATOM   2544  C   PHE A1121      68.125  -5.629   7.013  1.00 50.43           C  
ANISOU 2544  C   PHE A1121     8234   7045   3883   1003    574    163       C  
ATOM   2545  O   PHE A1121      69.111  -5.051   6.548  1.00 49.07           O  
ANISOU 2545  O   PHE A1121     7921   6975   3749   1108    490    153       O  
ATOM   2546  CB  PHE A1121      69.076  -7.631   8.208  1.00 57.18           C  
ANISOU 2546  CB  PHE A1121     9373   7845   4506   1243    558    333       C  
ATOM   2547  CG  PHE A1121      68.890  -6.971   9.543  1.00 67.19           C  
ANISOU 2547  CG  PHE A1121    10589   9283   5658   1143    569    261       C  
ATOM   2548  CD1 PHE A1121      67.830  -7.321  10.364  1.00 71.92           C  
ANISOU 2548  CD1 PHE A1121    11308   9836   6182   1000    669    249       C  
ATOM   2549  CD2 PHE A1121      69.785  -6.010   9.985  1.00 72.95           C  
ANISOU 2549  CD2 PHE A1121    11149  10216   6352   1196    485    196       C  
ATOM   2550  CE1 PHE A1121      67.660  -6.717  11.598  1.00 63.23           C  
ANISOU 2550  CE1 PHE A1121    10157   8904   4961    895    691    168       C  
ATOM   2551  CE2 PHE A1121      69.621  -5.404  11.219  1.00 73.46           C  
ANISOU 2551  CE2 PHE A1121    11171  10437   6305   1096    499    114       C  
ATOM   2552  CZ  PHE A1121      68.556  -5.757  12.025  1.00 59.47           C  
ANISOU 2552  CZ  PHE A1121     9520   8632   4446    935    605     97       C  
ATOM   2553  N   GLU A1122      67.039  -4.984   7.426  1.00 65.31           N  
ANISOU 2553  N   GLU A1122    10076   5896   8841  -1281  -1482    858       N  
ATOM   2554  CA  GLU A1122      66.909  -3.537   7.294  1.00 48.23           C  
ANISOU 2554  CA  GLU A1122     7647   3974   6706  -1103  -1232    696       C  
ATOM   2555  C   GLU A1122      65.938  -2.978   8.329  1.00 50.07           C  
ANISOU 2555  C   GLU A1122     7890   4456   6678  -1349   -938    673       C  
ATOM   2556  O   GLU A1122      64.752  -2.818   8.045  1.00 50.62           O  
ANISOU 2556  O   GLU A1122     7739   4765   6728  -1428   -697    580       O  
ATOM   2557  CB  GLU A1122      66.439  -3.172   5.883  1.00 50.70           C  
ANISOU 2557  CB  GLU A1122     7609   4397   7259   -862  -1121    552       C  
ATOM   2558  CG  GLU A1122      66.366  -1.677   5.600  1.00 65.41           C  
ANISOU 2558  CG  GLU A1122     9262   6436   9154   -625   -898    395       C  
ATOM   2559  CD  GLU A1122      67.645  -1.130   4.997  1.00 83.00           C  
ANISOU 2559  CD  GLU A1122    11464   8529  11541   -350  -1042    360       C  
ATOM   2560  OE1 GLU A1122      68.703  -1.779   5.146  1.00 81.59           O  
ANISOU 2560  OE1 GLU A1122    11431   8176  11393   -347  -1312    440       O  
ATOM   2561  OE2 GLU A1122      67.590  -0.051   4.367  1.00 94.30           O  
ANISOU 2561  OE2 GLU A1122    12737  10042  13050   -137   -887    244       O  
ATOM   2562  N   PRO A1123      66.442  -2.670   9.533  1.00 51.29           N  
ANISOU 2562  N   PRO A1123     8278   4596   6614  -1453   -963    731       N  
ATOM   2563  CA  PRO A1123      65.592  -2.167  10.618  1.00 55.18           C  
ANISOU 2563  CA  PRO A1123     8800   5346   6821  -1685   -696    700       C  
ATOM   2564  C   PRO A1123      65.090  -0.753  10.341  1.00 59.13           C  
ANISOU 2564  C   PRO A1123     9018   6094   7354  -1463   -423    474       C  
ATOM   2565  O   PRO A1123      64.022  -0.372  10.819  1.00 67.07           O  
ANISOU 2565  O   PRO A1123     9914   7396   8175  -1585   -158    380       O  
ATOM   2566  CB  PRO A1123      66.524  -2.193  11.831  1.00 54.76           C  
ANISOU 2566  CB  PRO A1123     9081   5171   6553  -1773   -860    810       C  
ATOM   2567  CG  PRO A1123      67.885  -2.013  11.253  1.00 56.54           C  
ANISOU 2567  CG  PRO A1123     9306   5181   6996  -1468  -1125    784       C  
ATOM   2568  CD  PRO A1123      67.865  -2.705   9.915  1.00 53.08           C  
ANISOU 2568  CD  PRO A1123     8716   4612   6840  -1327  -1244    793       C  
ATOM   2569  N   PHE A1124      65.856   0.010   9.570  1.00 49.62           N  
ANISOU 2569  N   PHE A1124     7713   4774   6365  -1136   -491    382       N  
ATOM   2570  CA  PHE A1124      65.472   1.370   9.214  1.00 52.47           C  
ANISOU 2570  CA  PHE A1124     7890   5282   6762   -890   -269    183       C  
ATOM   2571  C   PHE A1124      65.677   1.628   7.726  1.00 56.39           C  
ANISOU 2571  C   PHE A1124     8188   5688   7549   -585   -309    120       C  
ATOM   2572  O   PHE A1124      66.801   1.846   7.272  1.00 60.68           O  
ANISOU 2572  O   PHE A1124     8780   6034   8240   -444   -470    141       O  
ATOM   2573  CB  PHE A1124      66.267   2.381  10.038  1.00 59.58           C  
ANISOU 2573  CB  PHE A1124     8964   6123   7550   -844   -269    122       C  
ATOM   2574  CG  PHE A1124      66.252   2.101  11.509  1.00 85.92           C  
ANISOU 2574  CG  PHE A1124    12522   9538  10587  -1123   -270    193       C  
ATOM   2575  CD1 PHE A1124      65.099   2.297  12.250  1.00103.73           C  
ANISOU 2575  CD1 PHE A1124    14736  12082  12595  -1269    -22    121       C  
ATOM   2576  CD2 PHE A1124      67.387   1.636  12.153  1.00 85.83           C  
ANISOU 2576  CD2 PHE A1124    12750   9347  10514  -1225   -522    317       C  
ATOM   2577  CE1 PHE A1124      65.079   2.035  13.604  1.00107.17           C  
ANISOU 2577  CE1 PHE A1124    15385  12612  12722  -1540    -10    193       C  
ATOM   2578  CE2 PHE A1124      67.372   1.374  13.507  1.00 87.92           C  
ANISOU 2578  CE2 PHE A1124    13247   9686  10472  -1467   -533    393       C  
ATOM   2579  CZ  PHE A1124      66.218   1.575  14.233  1.00 99.05           C  
ANISOU 2579  CZ  PHE A1124    14633  11370  11631  -1638   -268    341       C  
ATOM   2580  N   GLY A1125      64.585   1.603   6.970  1.00 56.06           N  
ANISOU 2580  N   GLY A1125     7906   5830   7564   -490   -159     32       N  
ATOM   2581  CA  GLY A1125      64.649   1.830   5.538  1.00 58.50           C  
ANISOU 2581  CA  GLY A1125     8028   6087   8113   -190   -186    -28       C  
ATOM   2582  C   GLY A1125      64.794   3.299   5.195  1.00 43.47           C  
ANISOU 2582  C   GLY A1125     6123   4166   6229    111    -58   -162       C  
ATOM   2583  O   GLY A1125      63.939   3.876   4.523  1.00 43.62           O  
ANISOU 2583  O   GLY A1125     5976   4334   6263    353     93   -293       O  
ATOM   2584  N   LEU A1126      65.880   3.906   5.661  1.00 47.86           N  
ANISOU 2584  N   LEU A1126     6883   4533   6769     98   -128   -138       N  
ATOM   2585  CA  LEU A1126      66.124   5.322   5.424  1.00 45.70           C  
ANISOU 2585  CA  LEU A1126     6693   4174   6496    320    -15   -253       C  
ATOM   2586  C   LEU A1126      66.392   5.582   3.946  1.00 43.55           C  
ANISOU 2586  C   LEU A1126     6318   3799   6429    580    -45   -255       C  
ATOM   2587  O   LEU A1126      65.978   6.608   3.409  1.00 43.65           O  
ANISOU 2587  O   LEU A1126     6353   3799   6433    835     94   -356       O  
ATOM   2588  CB  LEU A1126      67.294   5.820   6.275  1.00 49.01           C  
ANISOU 2588  CB  LEU A1126     7347   4425   6849    175    -97   -236       C  
ATOM   2589  CG  LEU A1126      67.143   5.625   7.786  1.00 62.06           C  
ANISOU 2589  CG  LEU A1126     9135   6177   8267    -71    -82   -231       C  
ATOM   2590  CD1 LEU A1126      68.280   6.299   8.538  1.00 60.80           C  
ANISOU 2590  CD1 LEU A1126     9191   5872   8038   -171   -159   -262       C  
ATOM   2591  CD2 LEU A1126      65.792   6.138   8.271  1.00 68.03           C  
ANISOU 2591  CD2 LEU A1126     9844   7167   8837     -6    159   -367       C  
ATOM   2592  N   VAL A1127      67.083   4.647   3.299  1.00 43.16           N  
ANISOU 2592  N   VAL A1127     6181   3675   6542    533   -235   -147       N  
ATOM   2593  CA  VAL A1127      67.338   4.727   1.864  1.00 45.89           C  
ANISOU 2593  CA  VAL A1127     6402   3967   7065    761   -271   -145       C  
ATOM   2594  C   VAL A1127      66.017   4.796   1.109  1.00 44.06           C  
ANISOU 2594  C   VAL A1127     5991   3911   6840    992   -137   -227       C  
ATOM   2595  O   VAL A1127      65.840   5.614   0.200  1.00 44.88           O  
ANISOU 2595  O   VAL A1127     6087   3990   6976   1268    -50   -283       O  
ATOM   2596  CB  VAL A1127      68.156   3.517   1.365  1.00 44.44           C  
ANISOU 2596  CB  VAL A1127     6121   3731   7033    689   -512    -47       C  
ATOM   2597  CG1 VAL A1127      68.211   3.498  -0.153  1.00 35.88           C  
ANISOU 2597  CG1 VAL A1127     4869   2656   6107    936   -531    -61       C  
ATOM   2598  CG2 VAL A1127      69.557   3.543   1.956  1.00 47.25           C  
ANISOU 2598  CG2 VAL A1127     6611   3964   7378    535   -665     -4       C  
ATOM   2599  N   ALA A1128      65.089   3.935   1.514  1.00 25.65           N  
ANISOU 2599  N   ALA A1128     3322   3543   2881    491    384    191       N  
ATOM   2600  CA  ALA A1128      63.748   3.908   0.949  1.00 23.72           C  
ANISOU 2600  CA  ALA A1128     2985   3299   2729    355    472    146       C  
ATOM   2601  C   ALA A1128      63.069   5.263   1.085  1.00 35.42           C  
ANISOU 2601  C   ALA A1128     4277   4882   4299    382    412    -29       C  
ATOM   2602  O   ALA A1128      62.515   5.774   0.122  1.00 41.49           O  
ANISOU 2602  O   ALA A1128     4936   5609   5219    349    358    -99       O  
ATOM   2603  CB  ALA A1128      62.910   2.824   1.619  1.00 25.34           C  
ANISOU 2603  CB  ALA A1128     3291   3534   2803    239    663    214       C  
ATOM   2604  N   LEU A1129      63.122   5.845   2.281  1.00 30.75           N  
ANISOU 2604  N   LEU A1129     3662   4420   3603    466    406   -109       N  
ATOM   2605  CA  LEU A1129      62.467   7.124   2.545  1.00 25.79           C  
ANISOU 2605  CA  LEU A1129     2863   3891   3044    517    339   -297       C  
ATOM   2606  C   LEU A1129      63.066   8.257   1.717  1.00 27.47           C  
ANISOU 2606  C   LEU A1129     3003   4000   3436    585    149   -360       C  
ATOM   2607  O   LEU A1129      62.340   9.061   1.125  1.00 44.23           O  
ANISOU 2607  O   LEU A1129     5013   6105   5687    584     84   -471       O  
ATOM   2608  CB  LEU A1129      62.547   7.462   4.034  1.00 26.48           C  
ANISOU 2608  CB  LEU A1129     2961   4139   2961    616    360   -372       C  
ATOM   2609  CG  LEU A1129      61.633   6.626   4.932  1.00 44.20           C  
ANISOU 2609  CG  LEU A1129     5255   6519   5020    537    579   -342       C  
ATOM   2610  CD1 LEU A1129      61.914   6.893   6.403  1.00 55.36           C  
ANISOU 2610  CD1 LEU A1129     6726   8090   6218    666    593   -393       C  
ATOM   2611  CD2 LEU A1129      60.175   6.906   4.605  1.00 40.00           C  
ANISOU 2611  CD2 LEU A1129     4538   6074   4585    437    664   -475       C  
ATOM   2612  N   GLU A1130      64.393   8.311   1.679  1.00 29.69           N  
ANISOU 2612  N   GLU A1130     3352   4208   3720    644     62   -293       N  
ATOM   2613  CA  GLU A1130      65.110   9.314   0.902  1.00 31.72           C  
ANISOU 2613  CA  GLU A1130     3556   4351   4144    674    -87   -328       C  
ATOM   2614  C   GLU A1130      64.758   9.223  -0.576  1.00 33.77           C  
ANISOU 2614  C   GLU A1130     3817   4485   4529    596    -88   -265       C  
ATOM   2615  O   GLU A1130      64.512  10.237  -1.233  1.00 31.53           O  
ANISOU 2615  O   GLU A1130     3478   4126   4375    609   -184   -334       O  
ATOM   2616  CB  GLU A1130      66.618   9.152   1.093  1.00 22.18           C  
ANISOU 2616  CB  GLU A1130     2401   3109   2918    726   -146   -268       C  
ATOM   2617  CG  GLU A1130      67.088   9.445   2.508  1.00 35.26           C  
ANISOU 2617  CG  GLU A1130     4051   4884   4461    840   -198   -364       C  
ATOM   2618  CD  GLU A1130      68.513   8.999   2.752  1.00 44.83           C  
ANISOU 2618  CD  GLU A1130     5314   6089   5628    907   -253   -317       C  
ATOM   2619  OE1 GLU A1130      68.974   8.070   2.057  1.00 48.23           O  
ANISOU 2619  OE1 GLU A1130     5819   6456   6050    870   -203   -184       O  
ATOM   2620  OE2 GLU A1130      69.172   9.581   3.639  1.00 62.51           O  
ANISOU 2620  OE2 GLU A1130     7511   8395   7845   1012   -360   -434       O  
ATOM   2621  N   ALA A1131      64.728   7.999  -1.092  1.00 26.74           N  
ANISOU 2621  N   ALA A1131     3009   3562   3590    530     10   -138       N  
ATOM   2622  CA  ALA A1131      64.418   7.777  -2.496  1.00 25.40           C  
ANISOU 2622  CA  ALA A1131     2853   3285   3513    474      6    -84       C  
ATOM   2623  C   ALA A1131      62.959   8.110  -2.819  1.00 28.82           C  
ANISOU 2623  C   ALA A1131     3197   3748   4004    448      6   -197       C  
ATOM   2624  O   ALA A1131      62.665   8.711  -3.852  1.00 31.59           O  
ANISOU 2624  O   ALA A1131     3529   4016   4457    466    -79   -227       O  
ATOM   2625  CB  ALA A1131      64.730   6.345  -2.874  1.00 26.35           C  
ANISOU 2625  CB  ALA A1131     3083   3364   3564    423     96     53       C  
ATOM   2626  N   MET A1132      62.052   7.720  -1.929  1.00 23.20           N  
ANISOU 2626  N   MET A1132     2435   3163   3219    412    104   -264       N  
ATOM   2627  CA  MET A1132      60.624   7.941  -2.130  1.00 26.77           C  
ANISOU 2627  CA  MET A1132     2761   3682   3727    385    118   -405       C  
ATOM   2628  C   MET A1132      60.276   9.422  -2.060  1.00 35.88           C  
ANISOU 2628  C   MET A1132     3813   4857   4962    496    -25   -570       C  
ATOM   2629  O   MET A1132      59.377   9.887  -2.756  1.00 41.28           O  
ANISOU 2629  O   MET A1132     4417   5530   5737    526    -99   -684       O  
ATOM   2630  CB  MET A1132      59.809   7.159  -1.100  1.00 23.76           C  
ANISOU 2630  CB  MET A1132     2338   3449   3240    298    293   -438       C  
ATOM   2631  CG  MET A1132      59.800   5.658  -1.336  1.00 33.70           C  
ANISOU 2631  CG  MET A1132     3703   4652   4450    166    432   -295       C  
ATOM   2632  SD  MET A1132      59.178   4.718   0.071  1.00 34.45           S  
ANISOU 2632  SD  MET A1132     3825   4885   4380     47    669   -270       S  
ATOM   2633  CE  MET A1132      57.417   5.020  -0.056  1.00 31.83           C  
ANISOU 2633  CE  MET A1132     3241   4700   4153    -43    739   -493       C  
ATOM   2634  N   CYS A1133      60.997  10.162  -1.223  1.00 26.50           N  
ANISOU 2634  N   CYS A1133     2635   3691   3743    571    -83   -596       N  
ATOM   2635  CA  CYS A1133      60.792  11.603  -1.120  1.00 33.88           C  
ANISOU 2635  CA  CYS A1133     3501   4610   4764    683   -238   -753       C  
ATOM   2636  C   CYS A1133      61.149  12.312  -2.423  1.00 30.26           C  
ANISOU 2636  C   CYS A1133     3108   3955   4437    711   -378   -710       C  
ATOM   2637  O   CYS A1133      60.723  13.441  -2.665  1.00 42.30           O  
ANISOU 2637  O   CYS A1133     4603   5420   6046    801   -519   -833       O  
ATOM   2638  CB  CYS A1133      61.617  12.185   0.030  1.00 23.81           C  
ANISOU 2638  CB  CYS A1133     2232   3380   3435    752   -282   -794       C  
ATOM   2639  SG  CYS A1133      60.938  11.879   1.676  1.00 46.73           S  
ANISOU 2639  SG  CYS A1133     5055   6537   6162    784   -159   -912       S  
ATOM   2640  N   LEU A1134      61.930  11.640  -3.261  1.00 32.43           N  
ANISOU 2640  N   LEU A1134     3486   4124   4713    643   -337   -534       N  
ATOM   2641  CA  LEU A1134      62.395  12.225  -4.509  1.00 40.48           C  
ANISOU 2641  CA  LEU A1134     4594   4963   5823    656   -434   -460       C  
ATOM   2642  C   LEU A1134      61.770  11.547  -5.723  1.00 39.01           C  
ANISOU 2642  C   LEU A1134     4447   4736   5640    634   -413   -410       C  
ATOM   2643  O   LEU A1134      62.204  11.756  -6.855  1.00 45.51           O  
ANISOU 2643  O   LEU A1134     5373   5424   6496    641   -461   -315       O  
ATOM   2644  CB  LEU A1134      63.919  12.158  -4.576  1.00 36.42           C  
ANISOU 2644  CB  LEU A1134     4155   4371   5312    611   -411   -320       C  
ATOM   2645  CG  LEU A1134      64.571  13.096  -3.559  1.00 42.64           C  
ANISOU 2645  CG  LEU A1134     4899   5165   6136    648   -482   -403       C  
ATOM   2646  CD1 LEU A1134      66.019  12.732  -3.324  1.00 48.03           C  
ANISOU 2646  CD1 LEU A1134     5603   5841   6805    603   -440   -305       C  
ATOM   2647  CD2 LEU A1134      64.450  14.538  -4.027  1.00 43.53           C  
ANISOU 2647  CD2 LEU A1134     5040   5126   6375    693   -627   -473       C  
ATOM   2648  N   GLY A1135      60.747  10.736  -5.481  1.00 21.29           N  
ANISOU 2648  N   GLY A1135     2118   2613   3358    602   -338   -483       N  
ATOM   2649  CA  GLY A1135      59.954  10.175  -6.558  1.00 41.06           C  
ANISOU 2649  CA  GLY A1135     4623   5093   5885    594   -348   -497       C  
ATOM   2650  C   GLY A1135      60.407   8.820  -7.067  1.00 39.04           C  
ANISOU 2650  C   GLY A1135     4445   4809   5580    501   -240   -351       C  
ATOM   2651  O   GLY A1135      59.725   8.207  -7.888  1.00 37.66           O  
ANISOU 2651  O   GLY A1135     4262   4623   5424    486   -245   -380       O  
ATOM   2652  N   ALA A1136      61.556   8.351  -6.593  1.00 28.97           N  
ANISOU 2652  N   ALA A1136     3242   3521   4246    456   -161   -214       N  
ATOM   2653  CA  ALA A1136      62.041   7.032  -6.983  1.00 26.06           C  
ANISOU 2653  CA  ALA A1136     2958   3121   3823    391    -71    -86       C  
ATOM   2654  C   ALA A1136      61.170   5.945  -6.362  1.00 27.44           C  
ANISOU 2654  C   ALA A1136     3085   3378   3961    297     46   -126       C  
ATOM   2655  O   ALA A1136      60.827   6.011  -5.182  1.00 40.64           O  
ANISOU 2655  O   ALA A1136     4695   5155   5592    268    115   -181       O  
ATOM   2656  CB  ALA A1136      63.493   6.850  -6.575  1.00 29.47           C  
ANISOU 2656  CB  ALA A1136     3468   3531   4200    395    -36     40       C  
ATOM   2657  N   ILE A1137      60.810   4.949  -7.166  1.00 20.20           N  
ANISOU 2657  N   ILE A1137     2206   2411   3059    244     75   -102       N  
ATOM   2658  CA  ILE A1137      59.959   3.859  -6.706  1.00 26.55           C  
ANISOU 2658  CA  ILE A1137     2974   3259   3853    119    196   -136       C  
ATOM   2659  C   ILE A1137      60.803   2.691  -6.203  1.00 33.48           C  
ANISOU 2659  C   ILE A1137     4002   4085   4635     62    302     23       C  
ATOM   2660  O   ILE A1137      61.673   2.196  -6.915  1.00 20.39           O  
ANISOU 2660  O   ILE A1137     2461   2329   2958    103    265    125       O  
ATOM   2661  CB  ILE A1137      59.020   3.377  -7.825  1.00 22.95           C  
ANISOU 2661  CB  ILE A1137     2468   2765   3485     87    153   -229       C  
ATOM   2662  CG1 ILE A1137      58.083   4.509  -8.256  1.00 25.39           C  
ANISOU 2662  CG1 ILE A1137     2633   3134   3878    174     29   -411       C  
ATOM   2663  CG2 ILE A1137      58.229   2.163  -7.371  1.00 23.97           C  
ANISOU 2663  CG2 ILE A1137     2564   2914   3629    -81    296   -258       C  
ATOM   2664  CD1 ILE A1137      57.344   4.233  -9.548  1.00 28.27           C  
ANISOU 2664  CD1 ILE A1137     2968   3456   4318    205    -73   -514       C  
ATOM   2665  N   PRO A1138      60.554   2.254  -4.961  1.00 28.24           N  
ANISOU 2665  N   PRO A1138     3346   3489   3895    -18    431     39       N  
ATOM   2666  CA  PRO A1138      61.369   1.207  -4.337  1.00 22.32           C  
ANISOU 2666  CA  PRO A1138     2776   2680   3027    -43    515    194       C  
ATOM   2667  C   PRO A1138      60.960  -0.215  -4.711  1.00 28.64           C  
ANISOU 2667  C   PRO A1138     3674   3368   3838   -167    599    248       C  
ATOM   2668  O   PRO A1138      59.777  -0.551  -4.690  1.00 37.93           O  
ANISOU 2668  O   PRO A1138     4762   4569   5081   -307    684    162       O  
ATOM   2669  CB  PRO A1138      61.146   1.448  -2.844  1.00 23.36           C  
ANISOU 2669  CB  PRO A1138     2892   2934   3051    -65    618    183       C  
ATOM   2670  CG  PRO A1138      59.772   2.013  -2.770  1.00 24.24           C  
ANISOU 2670  CG  PRO A1138     2804   3160   3245   -139    658     15       C  
ATOM   2671  CD  PRO A1138      59.586   2.839  -4.017  1.00 24.58           C  
ANISOU 2671  CD  PRO A1138     2738   3173   3430    -60    497    -88       C  
ATOM   2672  N   ILE A1139      61.946  -1.033  -5.064  1.00 29.21           N  
ANISOU 2672  N   ILE A1139     3921   3318   3859   -115    568    372       N  
ATOM   2673  CA  ILE A1139      61.761  -2.474  -5.175  1.00 32.10           C  
ANISOU 2673  CA  ILE A1139     4440   3547   4212   -218    642    445       C  
ATOM   2674  C   ILE A1139      62.560  -3.109  -4.049  1.00 35.90           C  
ANISOU 2674  C   ILE A1139     5125   3989   4525   -184    708    591       C  
ATOM   2675  O   ILE A1139      63.764  -3.328  -4.182  1.00 52.90           O  
ANISOU 2675  O   ILE A1139     7399   6091   6610    -39    621    668       O  
ATOM   2676  CB  ILE A1139      62.230  -3.029  -6.537  1.00 30.47           C  
ANISOU 2676  CB  ILE A1139     4296   3215   4064   -153    533    456       C  
ATOM   2677  CG1 ILE A1139      61.576  -2.263  -7.688  1.00 30.94           C  
ANISOU 2677  CG1 ILE A1139     4181   3322   4253   -134    439    316       C  
ATOM   2678  CG2 ILE A1139      61.923  -4.516  -6.646  1.00 24.78           C  
ANISOU 2678  CG2 ILE A1139     3734   2329   3352   -268    597    506       C  
ATOM   2679  CD1 ILE A1139      62.057  -2.701  -9.054  1.00 25.24           C  
ANISOU 2679  CD1 ILE A1139     3526   2504   3561    -45    331    320       C  
ATOM   2680  N   ALA A1140      61.897  -3.388  -2.932  1.00 28.93           N  
ANISOU 2680  N   ALA A1140     4282   3143   3566   -305    860    618       N  
ATOM   2681  CA  ALA A1140      62.613  -3.764  -1.718  1.00 30.43           C  
ANISOU 2681  CA  ALA A1140     4675   3327   3560   -239    912    749       C  
ATOM   2682  C   ALA A1140      62.153  -5.085  -1.119  1.00 33.29           C  
ANISOU 2682  C   ALA A1140     5263   3550   3836   -393   1073    871       C  
ATOM   2683  O   ALA A1140      61.048  -5.556  -1.384  1.00 30.97           O  
ANISOU 2683  O   ALA A1140     4913   3209   3646   -603   1191    831       O  
ATOM   2684  CB  ALA A1140      62.483  -2.659  -0.683  1.00 29.23           C  
ANISOU 2684  CB  ALA A1140     4405   3371   3330   -191    943    689       C  
ATOM   2685  N   SER A1141      63.019  -5.673  -0.299  1.00 43.34           N  
ANISOU 2685  N   SER A1141     6798   4753   4918   -285   1073   1014       N  
ATOM   2686  CA  SER A1141      62.696  -6.901   0.413  1.00 43.76           C  
ANISOU 2686  CA  SER A1141     7132   4648   4847   -412   1227   1164       C  
ATOM   2687  C   SER A1141      61.615  -6.660   1.452  1.00 44.94           C  
ANISOU 2687  C   SER A1141     7230   4923   4923   -594   1452   1162       C  
ATOM   2688  O   SER A1141      61.501  -5.564   2.003  1.00 45.00           O  
ANISOU 2688  O   SER A1141     7060   5151   4888   -528   1455   1073       O  
ATOM   2689  CB  SER A1141      63.939  -7.473   1.088  1.00 33.92           C  
ANISOU 2689  CB  SER A1141     6195   3308   3384   -200   1142   1308       C  
ATOM   2690  OG  SER A1141      64.899  -7.874   0.130  1.00 45.90           O  
ANISOU 2690  OG  SER A1141     7751   4721   4966    -32    948   1295       O  
ATOM   2691  N   ALA A1142      60.824  -7.691   1.721  1.00 37.64           N  
ANISOU 2691  N   ALA A1142     6459   3857   3985   -829   1647   1255       N  
ATOM   2692  CA  ALA A1142      59.777  -7.597   2.726  1.00 41.03           C  
ANISOU 2692  CA  ALA A1142     6850   4408   4331  -1032   1905   1264       C  
ATOM   2693  C   ALA A1142      60.336  -7.889   4.113  1.00 46.66           C  
ANISOU 2693  C   ALA A1142     7848   5136   4745   -915   1957   1426       C  
ATOM   2694  O   ALA A1142      59.845  -8.772   4.814  1.00 45.67           O  
ANISOU 2694  O   ALA A1142     7858   4946   4548  -1051   2078   1519       O  
ATOM   2695  CB  ALA A1142      58.638  -8.547   2.399  1.00 42.31           C  
ANISOU 2695  CB  ALA A1142     6998   4435   4642  -1352   2080   1262       C  
ATOM   2696  N   VAL A1143      61.372  -7.150   4.499  1.00 49.21           N  
ANISOU 2696  N   VAL A1143     8217   5562   4919   -636   1812   1429       N  
ATOM   2697  CA  VAL A1143      61.941  -7.268   5.836  1.00 49.55           C  
ANISOU 2697  CA  VAL A1143     8476   5666   4686   -475   1801   1527       C  
ATOM   2698  C   VAL A1143      61.501  -6.083   6.690  1.00 56.69           C  
ANISOU 2698  C   VAL A1143     9223   6855   5463   -450   1923   1439       C  
ATOM   2699  O   VAL A1143      61.356  -4.968   6.185  1.00 53.41           O  
ANISOU 2699  O   VAL A1143     8470   6607   5218   -405   1820   1246       O  
ATOM   2700  CB  VAL A1143      63.481  -7.352   5.800  1.00 45.25           C  
ANISOU 2700  CB  VAL A1143     8095   5050   4047   -152   1533   1561       C  
ATOM   2701  CG1 VAL A1143      63.922  -8.634   5.116  1.00 41.80           C  
ANISOU 2701  CG1 VAL A1143     7825   4352   3706   -155   1419   1629       C  
ATOM   2702  CG2 VAL A1143      64.072  -6.144   5.096  1.00 47.15           C  
ANISOU 2702  CG2 VAL A1143     8080   5427   4409     13   1361   1411       C  
ATOM   2703  N   GLY A1144      61.279  -6.340   7.978  1.00 67.20           N  
ANISOU 2703  N   GLY A1144    10687   8269   6577   -453   2028   1510       N  
ATOM   2704  CA  GLY A1144      60.755  -5.346   8.901  1.00 64.98           C  
ANISOU 2704  CA  GLY A1144    10265   8271   6154   -435   2158   1418       C  
ATOM   2705  C   GLY A1144      61.499  -4.026   8.878  1.00 60.45           C  
ANISOU 2705  C   GLY A1144     9523   7873   5574   -165   1957   1261       C  
ATOM   2706  O   GLY A1144      62.670  -3.957   9.242  1.00 72.61           O  
ANISOU 2706  O   GLY A1144    11227   9391   6972    101   1764   1297       O  
ATOM   2707  N   GLY A1145      60.806  -2.975   8.457  1.00 43.70           N  
ANISOU 2707  N   GLY A1145     7021   5929   3653   -228   1947   1049       N  
ATOM   2708  CA  GLY A1145      61.425  -1.683   8.231  1.00 43.86           C  
ANISOU 2708  CA  GLY A1145     6807   6083   3776     -9   1699    863       C  
ATOM   2709  C   GLY A1145      61.046  -1.214   6.841  1.00 52.87           C  
ANISOU 2709  C   GLY A1145     7654   7183   5253   -104   1602    727       C  
ATOM   2710  O   GLY A1145      60.323  -0.231   6.681  1.00 57.40           O  
ANISOU 2710  O   GLY A1145     7939   7916   5954   -135   1600    541       O  
ATOM   2711  N   LEU A1146      61.537  -1.927   5.832  1.00 43.90           N  
ANISOU 2711  N   LEU A1146     6605   5831   4245   -130   1511    813       N  
ATOM   2712  CA  LEU A1146      61.059  -1.742   4.469  1.00 45.84           C  
ANISOU 2712  CA  LEU A1146     6627   6015   4776   -242   1451    713       C  
ATOM   2713  C   LEU A1146      59.621  -2.233   4.397  1.00 48.49           C  
ANISOU 2713  C   LEU A1146     6871   6369   5185   -519   1684    686       C  
ATOM   2714  O   LEU A1146      58.783  -1.670   3.691  1.00 53.46           O  
ANISOU 2714  O   LEU A1146     7222   7074   6016   -606   1673    519       O  
ATOM   2715  CB  LEU A1146      61.934  -2.500   3.471  1.00 47.72           C  
ANISOU 2715  CB  LEU A1146     7005   6029   5098   -194   1314    812       C  
ATOM   2716  CG  LEU A1146      63.430  -2.191   3.484  1.00 46.56           C  
ANISOU 2716  CG  LEU A1146     6941   5861   4890     63   1098    835       C  
ATOM   2717  CD1 LEU A1146      64.174  -3.137   2.554  1.00 41.70           C  
ANISOU 2717  CD1 LEU A1146     6473   5036   4334     97   1003    931       C  
ATOM   2718  CD2 LEU A1146      63.679  -0.744   3.094  1.00 47.79           C  
ANISOU 2718  CD2 LEU A1146     6823   6149   5185    170    942    662       C  
ATOM   2719  N   ARG A1147      59.354  -3.297   5.146  1.00 48.46           N  
ANISOU 2719  N   ARG A1147     7111   6290   5011   -654   1894    849       N  
ATOM   2720  CA  ARG A1147      58.027  -3.886   5.243  1.00 51.47           C  
ANISOU 2720  CA  ARG A1147     7427   6684   5446   -954   2160    840       C  
ATOM   2721  C   ARG A1147      57.044  -2.887   5.849  1.00 59.60           C  
ANISOU 2721  C   ARG A1147     8167   8010   6469   -998   2281    651       C  
ATOM   2722  O   ARG A1147      55.856  -2.891   5.525  1.00 67.51           O  
ANISOU 2722  O   ARG A1147     8931   9092   7629  -1211   2421    518       O  
ATOM   2723  CB  ARG A1147      58.090  -5.167   6.081  1.00 47.51           C  
ANISOU 2723  CB  ARG A1147     7302   6028   4721  -1077   2370   1084       C  
ATOM   2724  CG  ARG A1147      56.826  -6.004   6.091  1.00 60.27           C  
ANISOU 2724  CG  ARG A1147     8862   7600   6436  -1409   2610   1093       C  
ATOM   2725  CD  ARG A1147      57.003  -7.212   6.999  1.00 78.74           C  
ANISOU 2725  CD  ARG A1147    11531   9792   8593  -1441   2673   1315       C  
ATOM   2726  NE  ARG A1147      55.806  -8.046   7.056  1.00 99.10           N  
ANISOU 2726  NE  ARG A1147    14040  12325  11290  -1743   2869   1322       N  
ATOM   2727  CZ  ARG A1147      55.591  -9.097   6.271  1.00110.08           C  
ANISOU 2727  CZ  ARG A1147    15498  13466  12861  -1903   2848   1362       C  
ATOM   2728  NH1 ARG A1147      56.494  -9.444   5.363  1.00109.76           N  
ANISOU 2728  NH1 ARG A1147    15597  13211  12897  -1777   2638   1401       N  
ATOM   2729  NH2 ARG A1147      54.473  -9.800   6.393  1.00112.97           N  
ANISOU 2729  NH2 ARG A1147    15787  13804  13333  -2181   3036   1353       N  
ATOM   2730  N   ASP A1148      57.555  -2.025   6.724  1.00 58.38           N  
ANISOU 2730  N   ASP A1148     8021   8025   6137   -781   2212    615       N  
ATOM   2731  CA  ASP A1148      56.741  -1.011   7.388  1.00 65.58           C  
ANISOU 2731  CA  ASP A1148     8676   9227   7013   -769   2299    421       C  
ATOM   2732  C   ASP A1148      56.410   0.157   6.462  1.00 60.13           C  
ANISOU 2732  C   ASP A1148     7632   8629   6587   -689   2098    169       C  
ATOM   2733  O   ASP A1148      55.254   0.563   6.342  1.00 64.06           O  
ANISOU 2733  O   ASP A1148     7850   9288   7202   -804   2195    -20       O  
ATOM   2734  CB  ASP A1148      57.457  -0.488   8.637  1.00 77.13           C  
ANISOU 2734  CB  ASP A1148    10288  10828   8191   -538   2262    454       C  
ATOM   2735  CG  ASP A1148      57.656  -1.561   9.691  1.00 96.68           C  
ANISOU 2735  CG  ASP A1148    13135  13242  10356   -594   2475    696       C  
ATOM   2736  OD1 ASP A1148      56.730  -2.374   9.898  1.00103.16           O  
ANISOU 2736  OD1 ASP A1148    14003  14049  11145   -866   2766    776       O  
ATOM   2737  OD2 ASP A1148      58.739  -1.592  10.313  1.00103.18           O  
ANISOU 2737  OD2 ASP A1148    14210  14027  10966   -365   2349    802       O  
ATOM   2738  N   ILE A1149      57.436   0.694   5.812  1.00 46.64           N  
ANISOU 2738  N   ILE A1149     5942   6817   4964   -488   1820    163       N  
ATOM   2739  CA  ILE A1149      57.289   1.874   4.969  1.00 44.87           C  
ANISOU 2739  CA  ILE A1149     5447   6644   4956   -382   1610    -44       C  
ATOM   2740  C   ILE A1149      56.504   1.592   3.691  1.00 46.24           C  
ANISOU 2740  C   ILE A1149     5457   6733   5378   -533   1598   -123       C  
ATOM   2741  O   ILE A1149      55.583   2.331   3.338  1.00 42.73           O  
ANISOU 2741  O   ILE A1149     4742   6418   5077   -543   1568   -338       O  
ATOM   2742  CB  ILE A1149      58.665   2.447   4.581  1.00 47.13           C  
ANISOU 2742  CB  ILE A1149     5820   6820   5266   -160   1344     -5       C  
ATOM   2743  CG1 ILE A1149      59.477   2.774   5.834  1.00 50.03           C  
ANISOU 2743  CG1 ILE A1149     6328   7280   5403     13   1318     35       C  
ATOM   2744  CG2 ILE A1149      58.507   3.679   3.701  1.00 48.48           C  
ANISOU 2744  CG2 ILE A1149     5755   7014   5651    -65   1141   -193       C  
ATOM   2745  CD1 ILE A1149      60.920   3.116   5.549  1.00 46.54           C  
ANISOU 2745  CD1 ILE A1149     5979   6724   4978    203   1083     82       C  
ATOM   2746  N   ILE A1150      56.873   0.513   3.009  1.00 41.68           N  
ANISOU 2746  N   ILE A1150     5049   5940   4847   -628   1605     34       N  
ATOM   2747  CA  ILE A1150      56.369   0.234   1.668  1.00 37.10           C  
ANISOU 2747  CA  ILE A1150     4348   5252   4498   -725   1537    -39       C  
ATOM   2748  C   ILE A1150      55.105  -0.624   1.653  1.00 49.52           C  
ANISOU 2748  C   ILE A1150     5825   6844   6147   -999   1761    -89       C  
ATOM   2749  O   ILE A1150      55.038  -1.668   2.304  1.00 50.32           O  
ANISOU 2749  O   ILE A1150     6111   6877   6130  -1164   1970     66       O  
ATOM   2750  CB  ILE A1150      57.453  -0.462   0.821  1.00 37.29           C  
ANISOU 2750  CB  ILE A1150     4588   5033   4548   -667   1404    126       C  
ATOM   2751  CG1 ILE A1150      58.693   0.426   0.716  1.00 29.43           C  
ANISOU 2751  CG1 ILE A1150     3640   4028   3515   -421   1190    148       C  
ATOM   2752  CG2 ILE A1150      56.924  -0.805  -0.565  1.00 36.15           C  
ANISOU 2752  CG2 ILE A1150     4336   4780   4619   -753   1331     45       C  
ATOM   2753  CD1 ILE A1150      59.881  -0.271   0.114  1.00 40.63           C  
ANISOU 2753  CD1 ILE A1150     5270   5252   4916   -347   1086    308       C  
ATOM   2754  N   THR A1151      54.106  -0.166   0.905  1.00 58.28           N  
ANISOU 2754  N   THR A1151     6645   8041   7457  -1046   1712   -315       N  
ATOM   2755  CA  THR A1151      52.898  -0.942   0.655  1.00 61.86           C  
ANISOU 2755  CA  THR A1151     6949   8509   8044  -1310   1886   -413       C  
ATOM   2756  C   THR A1151      52.809  -1.266  -0.834  1.00 69.20           C  
ANISOU 2756  C   THR A1151     7828   9277   9188  -1315   1709   -480       C  
ATOM   2757  O   THR A1151      53.666  -0.851  -1.614  1.00 64.89           O  
ANISOU 2757  O   THR A1151     7369   8625   8661  -1114   1477   -437       O  
ATOM   2758  CB  THR A1151      51.632  -0.192   1.102  1.00 60.34           C  
ANISOU 2758  CB  THR A1151     6414   8603   7909  -1362   1988   -678       C  
ATOM   2759  OG1 THR A1151      51.432   0.955   0.267  1.00 57.14           O  
ANISOU 2759  OG1 THR A1151     5792   8271   7648  -1156   1727   -897       O  
ATOM   2760  CG2 THR A1151      51.765   0.256   2.553  1.00 59.28           C  
ANISOU 2760  CG2 THR A1151     6327   8654   7541  -1313   2141   -632       C  
ATOM   2761  N   ASN A1152      51.774  -2.000  -1.232  1.00 80.41           N  
ANISOU 2761  N   ASN A1152     9103  10684  10766  -1547   1823   -594       N  
ATOM   2762  CA  ASN A1152      51.631  -2.412  -2.626  1.00 78.59           C  
ANISOU 2762  CA  ASN A1152     8830  10301  10729  -1552   1654   -676       C  
ATOM   2763  C   ASN A1152      51.263  -1.249  -3.545  1.00 77.43           C  
ANISOU 2763  C   ASN A1152     8441  10268  10709  -1341   1402   -917       C  
ATOM   2764  O   ASN A1152      51.279  -1.389  -4.769  1.00 78.88           O  
ANISOU 2764  O   ASN A1152     8615  10339  11017  -1272   1216   -984       O  
ATOM   2765  CB  ASN A1152      50.587  -3.524  -2.750  1.00 76.72           C  
ANISOU 2765  CB  ASN A1152     8490  10018  10645  -1871   1841   -760       C  
ATOM   2766  CG  ASN A1152      49.181  -3.038  -2.468  1.00 86.61           C  
ANISOU 2766  CG  ASN A1152     9352  11536  12019  -1994   1955  -1052       C  
ATOM   2767  OD1 ASN A1152      48.791  -2.864  -1.313  1.00 92.74           O  
ANISOU 2767  OD1 ASN A1152    10062  12489  12688  -2099   2185  -1049       O  
ATOM   2768  ND2 ASN A1152      48.407  -2.822  -3.526  1.00 90.13           N  
ANISOU 2768  ND2 ASN A1152     9536  12028  12683  -1967   1790  -1322       N  
ATOM   2769  N   GLU A1153      50.932  -0.104  -2.952  1.00 72.28           N  
ANISOU 2769  N   GLU A1153     7615   9835  10013  -1222   1387  -1050       N  
ATOM   2770  CA  GLU A1153      50.632   1.101  -3.719  1.00 64.30           C  
ANISOU 2770  CA  GLU A1153     6420   8915   9098   -990   1134  -1265       C  
ATOM   2771  C   GLU A1153      51.845   2.022  -3.806  1.00 55.16           C  
ANISOU 2771  C   GLU A1153     5450   7683   7824   -731    947  -1126       C  
ATOM   2772  O   GLU A1153      51.864   2.958  -4.605  1.00 63.67           O  
ANISOU 2772  O   GLU A1153     6471   8755   8964   -529    716  -1236       O  
ATOM   2773  CB  GLU A1153      49.454   1.862  -3.104  1.00 72.00           C  
ANISOU 2773  CB  GLU A1153     7069  10169  10119   -996   1200  -1541       C  
ATOM   2774  CG  GLU A1153      48.107   1.166  -3.233  1.00 89.39           C  
ANISOU 2774  CG  GLU A1153     8993  12482  12489  -1236   1347  -1763       C  
ATOM   2775  CD  GLU A1153      47.809   0.235  -2.072  1.00 99.52           C  
ANISOU 2775  CD  GLU A1153    10296  13822  13693  -1542   1710  -1655       C  
ATOM   2776  OE1 GLU A1153      48.691   0.059  -1.205  1.00103.32           O  
ANISOU 2776  OE1 GLU A1153    11044  14242  13972  -1544   1828  -1393       O  
ATOM   2777  OE2 GLU A1153      46.688  -0.316  -2.026  1.00 97.51           O  
ANISOU 2777  OE2 GLU A1153     9890  13627  13531  -1721   1814  -1790       O  
ATOM   2778  N   THR A1154      52.853   1.759  -2.980  1.00 41.52           N  
ANISOU 2778  N   THR A1154     3952   5894   5930   -739   1046   -890       N  
ATOM   2779  CA  THR A1154      54.027   2.623  -2.918  1.00 48.40           C  
ANISOU 2779  CA  THR A1154     4973   6712   6704   -521    892   -776       C  
ATOM   2780  C   THR A1154      55.337   1.858  -3.096  1.00 54.26           C  
ANISOU 2780  C   THR A1154     6003   7255   7357   -513    884   -515       C  
ATOM   2781  O   THR A1154      56.330   2.150  -2.429  1.00 55.23           O  
ANISOU 2781  O   THR A1154     6267   7368   7349   -418    875   -384       O  
ATOM   2782  CB  THR A1154      54.085   3.387  -1.583  1.00 56.13           C  
ANISOU 2782  CB  THR A1154     5912   7862   7553   -460    968   -803       C  
ATOM   2783  OG1 THR A1154      54.121   2.452  -0.497  1.00 63.14           O  
ANISOU 2783  OG1 THR A1154     6910   8781   8299   -625   1216   -667       O  
ATOM   2784  CG2 THR A1154      52.870   4.291  -1.431  1.00 59.04           C  
ANISOU 2784  CG2 THR A1154     5985   8441   8005   -417    943  -1088       C  
ATOM   2785  N   GLY A1155      55.336   0.881  -3.997  1.00 50.80           N  
ANISOU 2785  N   GLY A1155     5641   6668   6994   -598    873   -463       N  
ATOM   2786  CA  GLY A1155      56.540   0.133  -4.304  1.00 30.74           C  
ANISOU 2786  CA  GLY A1155     3357   3943   4380   -564    843   -248       C  
ATOM   2787  C   GLY A1155      56.281  -1.333  -4.586  1.00 34.93           C  
ANISOU 2787  C   GLY A1155     3992   4332   4949   -745    949   -181       C  
ATOM   2788  O   GLY A1155      55.132  -1.766  -4.676  1.00 44.13           O  
ANISOU 2788  O   GLY A1155     5011   5533   6225   -917   1042   -312       O  
ATOM   2789  N   ILE A1156      57.359  -2.097  -4.729  1.00 37.00           N  
ANISOU 2789  N   ILE A1156     4500   4430   5130   -704    927      6       N  
ATOM   2790  CA  ILE A1156      57.267  -3.527  -4.996  1.00 35.20           C  
ANISOU 2790  CA  ILE A1156     4422   4023   4930   -853   1003     85       C  
ATOM   2791  C   ILE A1156      58.054  -4.315  -3.953  1.00 43.41           C  
ANISOU 2791  C   ILE A1156     5731   4969   5793   -878   1123    300       C  
ATOM   2792  O   ILE A1156      59.242  -4.066  -3.744  1.00 49.83           O  
ANISOU 2792  O   ILE A1156     6683   5766   6485   -699   1037    414       O  
ATOM   2793  CB  ILE A1156      57.794  -3.876  -6.403  1.00 37.71           C  
ANISOU 2793  CB  ILE A1156     4808   4199   5321   -745    826     83       C  
ATOM   2794  CG1 ILE A1156      57.010  -3.112  -7.471  1.00 36.53           C  
ANISOU 2794  CG1 ILE A1156     4428   4133   5316   -691    690   -127       C  
ATOM   2795  CG2 ILE A1156      57.710  -5.372  -6.650  1.00 40.92           C  
ANISOU 2795  CG2 ILE A1156     5382   4403   5763   -887    886    148       C  
ATOM   2796  CD1 ILE A1156      57.884  -2.341  -8.431  1.00 40.24           C  
ANISOU 2796  CD1 ILE A1156     4933   4596   5760   -459    498   -109       C  
ATOM   2797  N   LEU A1157      57.390  -5.263  -3.300  1.00 42.53           N  
ANISOU 2797  N   LEU A1157     5698   4793   5667  -1101   1320    351       N  
ATOM   2798  CA  LEU A1157      58.031  -6.058  -2.258  1.00 45.08           C  
ANISOU 2798  CA  LEU A1157     6320   5010   5800  -1124   1440    565       C  
ATOM   2799  C   LEU A1157      58.414  -7.447  -2.755  1.00 47.75           C  
ANISOU 2799  C   LEU A1157     6916   5071   6156  -1180   1421    684       C  
ATOM   2800  O   LEU A1157      57.737  -8.021  -3.607  1.00 48.20           O  
ANISOU 2800  O   LEU A1157     6901   5023   6388  -1320   1414    590       O  
ATOM   2801  CB  LEU A1157      57.118  -6.170  -1.035  1.00 41.92           C  
ANISOU 2801  CB  LEU A1157     5893   4713   5322  -1331   1700    580       C  
ATOM   2802  CG  LEU A1157      57.002  -4.899  -0.193  1.00 37.15           C  
ANISOU 2802  CG  LEU A1157     5120   4377   4621  -1228   1725    502       C  
ATOM   2803  CD1 LEU A1157      55.979  -5.078   0.914  1.00 42.53           C  
ANISOU 2803  CD1 LEU A1157     5751   5181   5226  -1449   2007    494       C  
ATOM   2804  CD2 LEU A1157      58.359  -4.520   0.384  1.00 41.39           C  
ANISOU 2804  CD2 LEU A1157     5848   4919   4959   -975   1610    634       C  
ATOM   2805  N   VAL A1158      59.511  -7.974  -2.218  1.00 54.27           N  
ANISOU 2805  N   VAL A1158     8041   5778   6801  -1050   1394    870       N  
ATOM   2806  CA  VAL A1158      60.018  -9.288  -2.605  1.00 50.18           C  
ANISOU 2806  CA  VAL A1158     7809   4982   6274  -1054   1351    987       C  
ATOM   2807  C   VAL A1158      60.570 -10.052  -1.413  1.00 56.73           C  
ANISOU 2807  C   VAL A1158     8994   5685   6875  -1038   1451   1204       C  
ATOM   2808  O   VAL A1158      60.814  -9.475  -0.355  1.00 65.05           O  
ANISOU 2808  O   VAL A1158    10075   6888   7754   -962   1514   1263       O  
ATOM   2809  CB  VAL A1158      61.135  -9.183  -3.660  1.00 45.86           C  
ANISOU 2809  CB  VAL A1158     7281   4393   5753   -796   1105    961       C  
ATOM   2810  CG1 VAL A1158      60.564  -8.786  -5.002  1.00 39.02           C  
ANISOU 2810  CG1 VAL A1158     6156   3573   5096   -820   1004    775       C  
ATOM   2811  CG2 VAL A1158      62.201  -8.197  -3.204  1.00 43.48           C  
ANISOU 2811  CG2 VAL A1158     6950   4260   5311   -548   1007    989       C  
ATOM   2812  N   LYS A1159      60.772 -11.354  -1.593  1.00 65.62           N  
ANISOU 2812  N   LYS A1159    10365   6564   8003  -1070   1418   1292       N  
ATOM   2813  CA  LYS A1159      61.411 -12.165  -0.566  1.00 66.22           C  
ANISOU 2813  CA  LYS A1159    10711   6569   7879   -964   1398   1442       C  
ATOM   2814  C   LYS A1159      62.878 -11.755  -0.465  1.00 68.16           C  
ANISOU 2814  C   LYS A1159    11042   6879   7977   -623   1200   1471       C  
ATOM   2815  O   LYS A1159      63.535 -11.523  -1.482  1.00 68.87           O  
ANISOU 2815  O   LYS A1159    11066   6954   8148   -470   1037   1401       O  
ATOM   2816  CB  LYS A1159      61.269 -13.656  -0.875  1.00 63.88           C  
ANISOU 2816  CB  LYS A1159    10603   6015   7653  -1055   1368   1489       C  
ATOM   2817  CG  LYS A1159      61.390 -14.545   0.351  1.00 68.32           C  
ANISOU 2817  CG  LYS A1159    11431   6492   8037  -1066   1441   1645       C  
ATOM   2818  CD  LYS A1159      60.614 -15.845   0.183  1.00 75.05           C  
ANISOU 2818  CD  LYS A1159    12398   7110   9008  -1302   1524   1683       C  
ATOM   2819  CE  LYS A1159      61.258 -16.762  -0.843  1.00 74.73           C  
ANISOU 2819  CE  LYS A1159    12482   6849   9064  -1180   1320   1652       C  
ATOM   2820  NZ  LYS A1159      60.547 -18.067  -0.929  1.00 77.49           N  
ANISOU 2820  NZ  LYS A1159    12969   6947   9526  -1404   1392   1695       N  
ATOM   2821  N   ALA A1160      63.374 -11.671   0.767  1.00 72.17           N  
ANISOU 2821  N   ALA A1160    11682   7468   8271   -504   1215   1559       N  
ATOM   2822  CA  ALA A1160      64.657 -11.037   1.079  1.00 63.67           C  
ANISOU 2822  CA  ALA A1160    10624   6511   7055   -199   1050   1551       C  
ATOM   2823  C   ALA A1160      65.845 -11.536   0.254  1.00 68.59           C  
ANISOU 2823  C   ALA A1160    11304   7045   7714     29    819   1509       C  
ATOM   2824  O   ALA A1160      66.602 -10.732  -0.295  1.00 73.46           O  
ANISOU 2824  O   ALA A1160    11776   7775   8361    203    693   1430       O  
ATOM   2825  CB  ALA A1160      64.960 -11.203   2.558  1.00 54.54           C  
ANISOU 2825  CB  ALA A1160     9651   5407   5663   -114   1090   1645       C  
ATOM   2826  N   GLY A1161      66.019 -12.851   0.174  1.00 56.15           N  
ANISOU 2826  N   GLY A1161     9929   5274   6134     30    771   1555       N  
ATOM   2827  CA  GLY A1161      67.180 -13.401  -0.502  1.00 57.94           C  
ANISOU 2827  CA  GLY A1161    10210   5434   6368    260    561   1499       C  
ATOM   2828  C   GLY A1161      66.863 -14.319  -1.666  1.00 62.30           C  
ANISOU 2828  C   GLY A1161    10788   5800   7083    174    520   1462       C  
ATOM   2829  O   GLY A1161      67.529 -15.337  -1.855  1.00 65.90           O  
ANISOU 2829  O   GLY A1161    11408   6125   7508    300    400   1460       O  
ATOM   2830  N   ASP A1162      65.850 -13.959  -2.449  1.00 56.94           N  
ANISOU 2830  N   ASP A1162     9951   5108   6576    -31    610   1416       N  
ATOM   2831  CA  ASP A1162      65.462 -14.755  -3.610  1.00 53.36           C  
ANISOU 2831  CA  ASP A1162     9506   4477   6290   -117    563   1356       C  
ATOM   2832  C   ASP A1162      65.694 -13.970  -4.899  1.00 55.18           C  
ANISOU 2832  C   ASP A1162     9525   4800   6639    -24    464   1230       C  
ATOM   2833  O   ASP A1162      64.891 -13.106  -5.255  1.00 56.41           O  
ANISOU 2833  O   ASP A1162     9509   5026   6899   -165    554   1182       O  
ATOM   2834  CB  ASP A1162      63.995 -15.186  -3.503  1.00 55.02           C  
ANISOU 2834  CB  ASP A1162     9720   4562   6624   -453    748   1381       C  
ATOM   2835  CG  ASP A1162      63.648 -16.339  -4.436  1.00 68.96           C  
ANISOU 2835  CG  ASP A1162    11565   6092   8546   -541    687   1331       C  
ATOM   2836  OD1 ASP A1162      64.213 -16.409  -5.549  1.00 69.61           O  
ANISOU 2836  OD1 ASP A1162    11604   6151   8695   -381    523   1231       O  
ATOM   2837  OD2 ASP A1162      62.808 -17.181  -4.050  1.00 69.77           O  
ANISOU 2837  OD2 ASP A1162    11772   6036   8704   -769    806   1385       O  
ATOM   2838  N   PRO A1163      66.796 -14.275  -5.604  1.00 49.07           N  
ANISOU 2838  N   PRO A1163     8766   4033   5845    216    285   1168       N  
ATOM   2839  CA  PRO A1163      67.163 -13.594  -6.852  1.00 38.04           C  
ANISOU 2839  CA  PRO A1163     7184   2736   4531    335    187   1053       C  
ATOM   2840  C   PRO A1163      66.121 -13.787  -7.950  1.00 49.19           C  
ANISOU 2840  C   PRO A1163     8546   4020   6124    171    208    975       C  
ATOM   2841  O   PRO A1163      65.962 -12.915  -8.804  1.00 57.94           O  
ANISOU 2841  O   PRO A1163     9492   5217   7307    197    186    894       O  
ATOM   2842  CB  PRO A1163      68.489 -14.258  -7.241  1.00 38.81           C  
ANISOU 2842  CB  PRO A1163     7346   2845   4555    594     19   1002       C  
ATOM   2843  CG  PRO A1163      69.011 -14.853  -5.972  1.00 38.97           C  
ANISOU 2843  CG  PRO A1163     7552   2831   4425    656     18   1088       C  
ATOM   2844  CD  PRO A1163      67.794 -15.285  -5.217  1.00 43.55           C  
ANISOU 2844  CD  PRO A1163     8262   3261   5026    397    173   1194       C  
ATOM   2845  N   GLY A1164      65.424 -14.919  -7.925  1.00 45.93           N  
ANISOU 2845  N   GLY A1164     8275   3391   5784      8    243    988       N  
ATOM   2846  CA  GLY A1164      64.366 -15.180  -8.884  1.00 40.84           C  
ANISOU 2846  CA  GLY A1164     7579   2608   5331   -172    256    883       C  
ATOM   2847  C   GLY A1164      63.215 -14.211  -8.702  1.00 47.04           C  
ANISOU 2847  C   GLY A1164     8180   3479   6212   -407    412    848       C  
ATOM   2848  O   GLY A1164      62.734 -13.610  -9.666  1.00 59.41           O  
ANISOU 2848  O   GLY A1164     9493   5179   7902   -416    357    691       O  
ATOM   2849  N   GLU A1165      62.781 -14.057  -7.455  1.00 53.92           N  
ANISOU 2849  N   GLU A1165     9083   4384   7019   -566    584    959       N  
ATOM   2850  CA  GLU A1165      61.711 -13.127  -7.116  1.00 53.53           C  
ANISOU 2850  CA  GLU A1165     8774   4517   7048   -770    734    896       C  
ATOM   2851  C   GLU A1165      62.101 -11.690  -7.441  1.00 54.85           C  
ANISOU 2851  C   GLU A1165     8671   4980   7191   -593    655    816       C  
ATOM   2852  O   GLU A1165      61.276 -10.906  -7.913  1.00 60.58           O  
ANISOU 2852  O   GLU A1165     9122   5856   8039   -676    666    675       O  
ATOM   2853  CB  GLU A1165      61.344 -13.247  -5.634  1.00 59.80           C  
ANISOU 2853  CB  GLU A1165     9696   5297   7727   -937    943   1047       C  
ATOM   2854  CG  GLU A1165      60.643 -14.544  -5.261  1.00 74.65           C  
ANISOU 2854  CG  GLU A1165    11705   6995   9665  -1154   1029   1090       C  
ATOM   2855  CD  GLU A1165      59.222 -14.622  -5.794  1.00 86.49           C  
ANISOU 2855  CD  GLU A1165    13003   8457  11403  -1464   1140    940       C  
ATOM   2856  OE1 GLU A1165      58.693 -13.588  -6.255  1.00 91.45           O  
ANISOU 2856  OE1 GLU A1165    13353   9259  12134  -1507   1160    792       O  
ATOM   2857  OE2 GLU A1165      58.631 -15.722  -5.749  1.00 91.99           O  
ANISOU 2857  OE2 GLU A1165    13778   8982  12192  -1646   1184    946       O  
ATOM   2858  N   LEU A1166      63.361 -11.348  -7.190  1.00 42.93           N  
ANISOU 2858  N   LEU A1166     7242   3543   5526   -347    568    896       N  
ATOM   2859  CA  LEU A1166      63.851 -10.005  -7.479  1.00 39.40           C  
ANISOU 2859  CA  LEU A1166     6564   3345   5060   -191    498    833       C  
ATOM   2860  C   LEU A1166      63.871  -9.738  -8.983  1.00 41.41           C  
ANISOU 2860  C   LEU A1166     6669   3641   5426   -103    367    697       C  
ATOM   2861  O   LEU A1166      63.485  -8.660  -9.430  1.00 35.14           O  
ANISOU 2861  O   LEU A1166     5645   3013   4694   -103    350    604       O  
ATOM   2862  CB  LEU A1166      65.247  -9.796  -6.888  1.00 29.44           C  
ANISOU 2862  CB  LEU A1166     5414   2144   3629     39    433    929       C  
ATOM   2863  CG  LEU A1166      65.880  -8.434  -7.188  1.00 29.60           C  
ANISOU 2863  CG  LEU A1166     5207   2397   3644    184    364    867       C  
ATOM   2864  CD1 LEU A1166      64.942  -7.299  -6.801  1.00 26.26           C  
ANISOU 2864  CD1 LEU A1166     4563   2132   3281     47    453    809       C  
ATOM   2865  CD2 LEU A1166      67.215  -8.289  -6.476  1.00 29.48           C  
ANISOU 2865  CD2 LEU A1166     5279   2444   3480    387    306    935       C  
ATOM   2866  N   ALA A1167      64.323 -10.719  -9.758  1.00 28.75           N  
ANISOU 2866  N   ALA A1167     5215   1878   3829    -12    266    684       N  
ATOM   2867  CA  ALA A1167      64.353 -10.589 -11.211  1.00 32.22           C  
ANISOU 2867  CA  ALA A1167     5546   2353   4343     89    142    554       C  
ATOM   2868  C   ALA A1167      62.937 -10.457 -11.770  1.00 40.23           C  
ANISOU 2868  C   ALA A1167     6397   3367   5522    -95    162    414       C  
ATOM   2869  O   ALA A1167      62.689  -9.670 -12.694  1.00 45.61           O  
ANISOU 2869  O   ALA A1167     6902   4179   6249    -28     89    303       O  
ATOM   2870  CB  ALA A1167      65.063 -11.772 -11.835  1.00 28.94           C  
ANISOU 2870  CB  ALA A1167     5337   1764   3896    228     31    552       C  
ATOM   2871  N   ASN A1168      62.013 -11.225 -11.200  1.00 38.43           N  
ANISOU 2871  N   ASN A1168     6232   2992   5380   -325    261    415       N  
ATOM   2872  CA  ASN A1168      60.604 -11.120 -11.564  1.00 36.22           C  
ANISOU 2872  CA  ASN A1168     5760   2729   5275   -525    294    256       C  
ATOM   2873  C   ASN A1168      60.051  -9.735 -11.257  1.00 43.64           C  
ANISOU 2873  C   ASN A1168     6441   3911   6227   -554    348    200       C  
ATOM   2874  O   ASN A1168      59.297  -9.168 -12.050  1.00 51.50           O  
ANISOU 2874  O   ASN A1168     7234   5007   7329   -554    277     32       O  
ATOM   2875  CB  ASN A1168      59.778 -12.182 -10.838  1.00 36.09           C  
ANISOU 2875  CB  ASN A1168     5852   2514   5347   -805    434    283       C  
ATOM   2876  CG  ASN A1168      60.084 -13.584 -11.316  1.00 49.47           C  
ANISOU 2876  CG  ASN A1168     7794   3925   7075   -798    354    294       C  
ATOM   2877  OD1 ASN A1168      60.479 -13.787 -12.464  1.00 57.28           O  
ANISOU 2877  OD1 ASN A1168     8792   4889   8084   -622    181    195       O  
ATOM   2878  ND2 ASN A1168      59.902 -14.562 -10.437  1.00 58.63           N  
ANISOU 2878  ND2 ASN A1168     9178   4866   8235   -983    480    414       N  
ATOM   2879  N   ALA A1169      60.435  -9.194 -10.105  1.00 34.09           N  
ANISOU 2879  N   ALA A1169     5253   2793   4904   -556    454    329       N  
ATOM   2880  CA  ALA A1169      60.002  -7.859  -9.701  1.00 32.57           C  
ANISOU 2880  CA  ALA A1169     4839   2824   4714   -562    496    277       C  
ATOM   2881  C   ALA A1169      60.565  -6.784 -10.626  1.00 35.98           C  
ANISOU 2881  C   ALA A1169     5163   3386   5121   -343    348    225       C  
ATOM   2882  O   ALA A1169      59.901  -5.791 -10.911  1.00 47.29           O  
ANISOU 2882  O   ALA A1169     6397   4955   6616   -338    316    108       O  
ATOM   2883  CB  ALA A1169      60.412  -7.583  -8.272  1.00 30.36           C  
ANISOU 2883  CB  ALA A1169     4633   2602   4299   -583    624    421       C  
ATOM   2884  N   ILE A1170      61.797  -6.983 -11.079  1.00 31.11           N  
ANISOU 2884  N   ILE A1170     4685   2728   4409   -162    264    311       N  
ATOM   2885  CA  ILE A1170      62.432  -6.055 -12.006  1.00 32.48           C  
ANISOU 2885  CA  ILE A1170     4785   3009   4545     27    153    285       C  
ATOM   2886  C   ILE A1170      61.705  -6.076 -13.351  1.00 32.99           C  
ANISOU 2886  C   ILE A1170     4771   3063   4700     54     44    133       C  
ATOM   2887  O   ILE A1170      61.417  -5.021 -13.928  1.00 29.93           O  
ANISOU 2887  O   ILE A1170     4257   2788   4326    125    -19     61       O  
ATOM   2888  CB  ILE A1170      63.924  -6.392 -12.195  1.00 27.43           C  
ANISOU 2888  CB  ILE A1170     4294   2342   3786    202    108    393       C  
ATOM   2889  CG1 ILE A1170      64.700  -6.069 -10.917  1.00 22.77           C  
ANISOU 2889  CG1 ILE A1170     3744   1806   3100    222    178    511       C  
ATOM   2890  CG2 ILE A1170      64.509  -5.628 -13.366  1.00 22.08           C  
ANISOU 2890  CG2 ILE A1170     3554   1760   3077    366     18    360       C  
ATOM   2891  CD1 ILE A1170      66.162  -6.469 -10.968  1.00 34.34           C  
ANISOU 2891  CD1 ILE A1170     5333   3258   4458    398    129    589       C  
ATOM   2892  N   LEU A1171      61.400  -7.278 -13.837  1.00 25.47           N  
ANISOU 2892  N   LEU A1171     3909   1963   3804      6     10     77       N  
ATOM   2893  CA  LEU A1171      60.606  -7.433 -15.056  1.00 28.09           C  
ANISOU 2893  CA  LEU A1171     4165   2278   4229     29   -108    -99       C  
ATOM   2894  C   LEU A1171      59.247  -6.736 -14.927  1.00 37.00           C  
ANISOU 2894  C   LEU A1171     5074   3505   5480    -91    -98   -250       C  
ATOM   2895  O   LEU A1171      58.803  -6.023 -15.839  1.00 45.06           O  
ANISOU 2895  O   LEU A1171     5988   4614   6521     18   -217   -377       O  
ATOM   2896  CB  LEU A1171      60.408  -8.917 -15.381  1.00 28.47           C  
ANISOU 2896  CB  LEU A1171     4342   2128   4346    -40   -139   -151       C  
ATOM   2897  CG  LEU A1171      61.621  -9.692 -15.903  1.00 27.83           C  
ANISOU 2897  CG  LEU A1171     4467   1950   4158    135   -210    -75       C  
ATOM   2898  CD1 LEU A1171      61.369 -11.186 -15.836  1.00 29.87           C  
ANISOU 2898  CD1 LEU A1171     4881   1971   4498     28   -220   -106       C  
ATOM   2899  CD2 LEU A1171      61.948  -9.277 -17.328  1.00 27.22           C  
ANISOU 2899  CD2 LEU A1171     4363   1964   4017    355   -350   -163       C  
ATOM   2900  N   LYS A1172      58.601  -6.938 -13.782  1.00 39.98           N  
ANISOU 2900  N   LYS A1172     5392   3874   5926   -302     43   -239       N  
ATOM   2901  CA  LYS A1172      57.305  -6.329 -13.506  1.00 41.87           C  
ANISOU 2901  CA  LYS A1172     5396   4230   6285   -427     76   -400       C  
ATOM   2902  C   LYS A1172      57.416  -4.807 -13.492  1.00 38.15           C  
ANISOU 2902  C   LYS A1172     4810   3936   5751   -282     26   -406       C  
ATOM   2903  O   LYS A1172      56.514  -4.108 -13.952  1.00 46.67           O  
ANISOU 2903  O   LYS A1172     5712   5115   6907   -247    -60   -583       O  
ATOM   2904  CB  LYS A1172      56.749  -6.840 -12.171  1.00 45.38           C  
ANISOU 2904  CB  LYS A1172     5818   4647   6777   -684    279   -357       C  
ATOM   2905  CG  LYS A1172      55.249  -6.633 -11.979  1.00 55.61           C  
ANISOU 2905  CG  LYS A1172     6848   6043   8237   -865    334   -570       C  
ATOM   2906  CD  LYS A1172      54.924  -5.277 -11.365  1.00 66.91           C  
ANISOU 2906  CD  LYS A1172     8098   7692   9634   -815    364   -612       C  
ATOM   2907  CE  LYS A1172      53.422  -5.043 -11.295  1.00 77.25           C  
ANISOU 2907  CE  LYS A1172     9110   9130  11110   -958    394   -869       C  
ATOM   2908  NZ  LYS A1172      52.794  -5.051 -12.646  1.00 81.84           N  
ANISOU 2908  NZ  LYS A1172     9570   9710  11814   -861    188  -1100       N  
ATOM   2909  N   ALA A1173      58.527  -4.305 -12.961  1.00 39.00           N  
ANISOU 2909  N   ALA A1173     5024   4072   5724   -190     68   -226       N  
ATOM   2910  CA  ALA A1173      58.783  -2.870 -12.903  1.00 30.52           C  
ANISOU 2910  CA  ALA A1173     3873   3128   4594    -63     24   -212       C  
ATOM   2911  C   ALA A1173      59.000  -2.306 -14.298  1.00 31.06           C  
ANISOU 2911  C   ALA A1173     3962   3206   4634    129   -140   -262       C  
ATOM   2912  O   ALA A1173      58.662  -1.157 -14.567  1.00 33.16           O  
ANISOU 2912  O   ALA A1173     4142   3556   4902    220   -217   -327       O  
ATOM   2913  CB  ALA A1173      59.987  -2.578 -12.024  1.00 22.85           C  
ANISOU 2913  CB  ALA A1173     3007   2171   3504    -24    102    -25       C  
ATOM   2914  N   LEU A1174      59.579  -3.118 -15.175  1.00 32.74           N  
ANISOU 2914  N   LEU A1174     4310   3327   4803    203   -194   -227       N  
ATOM   2915  CA  LEU A1174      59.768  -2.736 -16.569  1.00 28.18           C  
ANISOU 2915  CA  LEU A1174     3779   2759   4169    389   -335   -271       C  
ATOM   2916  C   LEU A1174      58.423  -2.595 -17.277  1.00 33.83           C  
ANISOU 2916  C   LEU A1174     4368   3503   4983    406   -462   -495       C  
ATOM   2917  O   LEU A1174      58.092  -1.530 -17.833  1.00 43.46           O  
ANISOU 2917  O   LEU A1174     5546   4792   6174    538   -567   -559       O  
ATOM   2918  CB  LEU A1174      60.647  -3.767 -17.282  1.00 27.64           C  
ANISOU 2918  CB  LEU A1174     3875   2601   4026    467   -357   -208       C  
ATOM   2919  CG  LEU A1174      60.704  -3.758 -18.812  1.00 35.12           C  
ANISOU 2919  CG  LEU A1174     4890   3552   4904    652   -497   -282       C  
ATOM   2920  CD1 LEU A1174      61.115  -2.401 -19.357  1.00 41.22           C  
ANISOU 2920  CD1 LEU A1174     5681   4413   5567    798   -532   -216       C  
ATOM   2921  CD2 LEU A1174      61.659  -4.830 -19.297  1.00 25.33           C  
ANISOU 2921  CD2 LEU A1174     3801   2238   3586    726   -496   -223       C  
ATOM   2922  N   GLU A1175      57.645  -3.676 -17.242  1.00 37.47           N  
ANISOU 2922  N   GLU A1175     4774   3900   5564    275   -459   -624       N  
ATOM   2923  CA  GLU A1175      56.329  -3.678 -17.873  1.00 44.39           C  
ANISOU 2923  CA  GLU A1175     5493   4811   6561    277   -586   -879       C  
ATOM   2924  C   GLU A1175      55.474  -2.553 -17.307  1.00 41.54           C  
ANISOU 2924  C   GLU A1175     4939   4584   6261    258   -588   -982       C  
ATOM   2925  O   GLU A1175      54.660  -1.959 -18.013  1.00 60.30           O  
ANISOU 2925  O   GLU A1175     7210   7029   8671    381   -746  -1171       O  
ATOM   2926  CB  GLU A1175      55.630  -5.026 -17.678  1.00 54.10           C  
ANISOU 2926  CB  GLU A1175     6666   5942   7947     74   -543  -1001       C  
ATOM   2927  CG  GLU A1175      56.488  -6.242 -18.015  1.00 67.45           C  
ANISOU 2927  CG  GLU A1175     8564   7473   9591     77   -533   -897       C  
ATOM   2928  CD  GLU A1175      57.015  -6.231 -19.442  1.00 72.39           C  
ANISOU 2928  CD  GLU A1175     9314   8091  10102    332   -706   -928       C  
ATOM   2929  OE1 GLU A1175      56.336  -5.678 -20.334  1.00 69.91           O  
ANISOU 2929  OE1 GLU A1175     8914   7853   9794    467   -864  -1100       O  
ATOM   2930  OE2 GLU A1175      58.115  -6.781 -19.668  1.00 68.31           O  
ANISOU 2930  OE2 GLU A1175     8983   7499   9474    412   -686   -786       O  
ATOM   2931  N   LEU A1176      55.679  -2.257 -16.029  1.00 35.16           N  
ANISOU 2931  N   LEU A1176     4094   3815   5452    128   -425   -867       N  
ATOM   2932  CA  LEU A1176      54.990  -1.158 -15.370  1.00 38.45           C  
ANISOU 2932  CA  LEU A1176     4336   4366   5909    124   -417   -957       C  
ATOM   2933  C   LEU A1176      55.520   0.186 -15.869  1.00 45.12           C  
ANISOU 2933  C   LEU A1176     5260   5245   6638    350   -536   -892       C  
ATOM   2934  O   LEU A1176      54.795   1.181 -15.897  1.00 47.86           O  
ANISOU 2934  O   LEU A1176     5487   5679   7018    439   -632  -1030       O  
ATOM   2935  CB  LEU A1176      55.153  -1.268 -13.852  1.00 39.77           C  
ANISOU 2935  CB  LEU A1176     4469   4565   6077    -63   -207   -845       C  
ATOM   2936  CG  LEU A1176      53.982  -0.830 -12.973  1.00 43.41           C  
ANISOU 2936  CG  LEU A1176     4683   5170   6640   -181   -135  -1016       C  
ATOM   2937  CD1 LEU A1176      52.683  -1.424 -13.484  1.00 56.72           C  
ANISOU 2937  CD1 LEU A1176     6173   6884   8493   -273   -187  -1281       C  
ATOM   2938  CD2 LEU A1176      54.228  -1.262 -11.541  1.00 45.16           C  
ANISOU 2938  CD2 LEU A1176     4927   5402   6829   -376     96   -879       C  
ATOM   2939  N   SER A1177      56.789   0.204 -16.270  1.00 42.73           N  
ANISOU 2939  N   SER A1177     5162   4868   6205    441   -527   -688       N  
ATOM   2940  CA  SER A1177      57.435   1.432 -16.721  1.00 34.66           C  
ANISOU 2940  CA  SER A1177     4244   3853   5074    615   -601   -590       C  
ATOM   2941  C   SER A1177      57.097   1.713 -18.177  1.00 39.13           C  
ANISOU 2941  C   SER A1177     4881   4400   5586    813   -788   -685       C  
ATOM   2942  O   SER A1177      57.453   2.761 -18.712  1.00 36.70           O  
ANISOU 2942  O   SER A1177     4681   4081   5182    965   -864   -617       O  
ATOM   2943  CB  SER A1177      58.953   1.353 -16.545  1.00 25.35           C  
ANISOU 2943  CB  SER A1177     3226   2623   3782    615   -495   -347       C  
ATOM   2944  OG  SER A1177      59.543   0.559 -17.560  1.00 40.75           O  
ANISOU 2944  OG  SER A1177     5313   4513   5658    688   -525   -297       O  
ATOM   2945  N   ARG A1178      56.416   0.773 -18.823  1.00 38.97           N  
ANISOU 2945  N   ARG A1178     4816   4366   5623    811   -865   -843       N  
ATOM   2946  CA  ARG A1178      55.924   1.028 -20.178  1.00 41.11           C  
ANISOU 2946  CA  ARG A1178     5142   4638   5839   1024  -1071   -978       C  
ATOM   2947  C   ARG A1178      54.835   2.114 -20.221  1.00 46.62           C  
ANISOU 2947  C   ARG A1178     5716   5410   6586   1138  -1222  -1166       C  
ATOM   2948  O   ARG A1178      54.561   2.685 -21.279  1.00 45.37           O  
ANISOU 2948  O   ARG A1178     5654   5246   6338   1364  -1409  -1239       O  
ATOM   2949  CB  ARG A1178      55.395  -0.261 -20.804  1.00 33.00           C  
ANISOU 2949  CB  ARG A1178     4073   3581   4883    995  -1138  -1143       C  
ATOM   2950  CG  ARG A1178      56.414  -1.378 -20.817  1.00 41.78           C  
ANISOU 2950  CG  ARG A1178     5321   4605   5947    914  -1020   -986       C  
ATOM   2951  CD  ARG A1178      56.040  -2.485 -21.784  1.00 51.67           C  
ANISOU 2951  CD  ARG A1178     6597   5806   7231    963  -1139  -1148       C  
ATOM   2952  NE  ARG A1178      56.947  -3.620 -21.647  1.00 61.65           N  
ANISOU 2952  NE  ARG A1178     7982   6973   8470    879  -1030  -1017       N  
ATOM   2953  CZ  ARG A1178      58.177  -3.658 -22.150  1.00 60.17           C  
ANISOU 2953  CZ  ARG A1178     7986   6766   8110   1005   -998   -840       C  
ATOM   2954  NH1 ARG A1178      58.651  -2.624 -22.834  1.00 57.37           N  
ANISOU 2954  NH1 ARG A1178     7734   6474   7591   1192  -1043   -751       N  
ATOM   2955  NH2 ARG A1178      58.933  -4.733 -21.974  1.00 51.41           N  
ANISOU 2955  NH2 ARG A1178     6971   5572   6990    945   -919   -756       N  
ATOM   2956  N   SER A1179      54.218   2.398 -19.076  1.00 43.56           N  
ANISOU 2956  N   SER A1179     5129   5096   6326   1001  -1148  -1250       N  
ATOM   2957  CA  SER A1179      53.189   3.435 -19.002  1.00 42.52           C  
ANISOU 2957  CA  SER A1179     4857   5050   6249   1120  -1292  -1451       C  
ATOM   2958  C   SER A1179      53.533   4.524 -17.988  1.00 40.29           C  
ANISOU 2958  C   SER A1179     4568   4789   5951   1097  -1211  -1339       C  
ATOM   2959  O   SER A1179      54.602   4.502 -17.376  1.00 46.98           O  
ANISOU 2959  O   SER A1179     5519   5587   6742    992  -1049  -1105       O  
ATOM   2960  CB  SER A1179      51.829   2.822 -18.657  1.00 39.05           C  
ANISOU 2960  CB  SER A1179     4118   4720   6001   1005  -1313  -1754       C  
ATOM   2961  OG  SER A1179      51.250   2.197 -19.789  1.00 54.22           O  
ANISOU 2961  OG  SER A1179     6023   6632   7949   1107  -1484  -1945       O  
ATOM   2962  N   ASP A1180      52.614   5.472 -17.823  1.00 35.67           N  
ANISOU 2962  N   ASP A1180     3854   4279   5418   1214  -1344  -1532       N  
ATOM   2963  CA  ASP A1180      52.788   6.598 -16.907  1.00 40.10           C  
ANISOU 2963  CA  ASP A1180     4400   4861   5975   1227  -1310  -1479       C  
ATOM   2964  C   ASP A1180      52.960   6.135 -15.461  1.00 50.09           C  
ANISOU 2964  C   ASP A1180     5518   6202   7312    977  -1073  -1424       C  
ATOM   2965  O   ASP A1180      52.179   5.325 -14.963  1.00 59.89           O  
ANISOU 2965  O   ASP A1180     6545   7547   8664    821   -984  -1577       O  
ATOM   2966  CB  ASP A1180      51.594   7.554 -17.020  1.00 44.38           C  
ANISOU 2966  CB  ASP A1180     4804   5485   6575   1419  -1521  -1756       C  
ATOM   2967  CG  ASP A1180      51.679   8.722 -16.053  1.00 60.37           C  
ANISOU 2967  CG  ASP A1180     6803   7530   8606   1449  -1507  -1740       C  
ATOM   2968  OD1 ASP A1180      52.806   9.125 -15.690  1.00 65.93           O  
ANISOU 2968  OD1 ASP A1180     7683   8133   9235   1398  -1405  -1486       O  
ATOM   2969  OD2 ASP A1180      50.613   9.242 -15.660  1.00 62.66           O  
ANISOU 2969  OD2 ASP A1180     6887   7943   8978   1525  -1604  -2000       O  
ATOM   2970  N   LEU A1181      53.987   6.659 -14.795  1.00 44.68           N  
ANISOU 2970  N   LEU A1181     4954   5465   6559    938   -969  -1209       N  
ATOM   2971  CA  LEU A1181      54.302   6.278 -13.419  1.00 40.46           C  
ANISOU 2971  CA  LEU A1181     4329   4994   6049    737   -757  -1133       C  
ATOM   2972  C   LEU A1181      54.104   7.429 -12.431  1.00 49.81           C  
ANISOU 2972  C   LEU A1181     5425   6253   7249    782   -767  -1198       C  
ATOM   2973  O   LEU A1181      54.550   7.351 -11.286  1.00 50.51           O  
ANISOU 2973  O   LEU A1181     5485   6387   7321    660   -612  -1111       O  
ATOM   2974  CB  LEU A1181      55.744   5.771 -13.325  1.00 28.50           C  
ANISOU 2974  CB  LEU A1181     3009   3377   4443    654   -626   -851       C  
ATOM   2975  CG  LEU A1181      56.086   4.406 -13.921  1.00 32.54           C  
ANISOU 2975  CG  LEU A1181     3599   3827   4936    571   -563   -773       C  
ATOM   2976  CD1 LEU A1181      57.596   4.227 -13.993  1.00 22.56           C  
ANISOU 2976  CD1 LEU A1181     2534   2471   3568    564   -484   -518       C  
ATOM   2977  CD2 LEU A1181      55.457   3.295 -13.098  1.00 24.82           C  
ANISOU 2977  CD2 LEU A1181     2476   2915   4041    366   -416   -849       C  
ATOM   2978  N   SER A1182      53.434   8.489 -12.877  1.00 43.16           N  
ANISOU 2978  N   SER A1182     4553   5417   6428    978   -966  -1360       N  
ATOM   2979  CA  SER A1182      53.246   9.696 -12.071  1.00 42.36           C  
ANISOU 2979  CA  SER A1182     4393   5361   6342   1064  -1020  -1443       C  
ATOM   2980  C   SER A1182      52.547   9.430 -10.735  1.00 43.65           C  
ANISOU 2980  C   SER A1182     4296   5721   6566    931   -873  -1595       C  
ATOM   2981  O   SER A1182      53.069   9.770  -9.667  1.00 45.78           O  
ANISOU 2981  O   SER A1182     4570   6022   6802    872   -767  -1515       O  
ATOM   2982  CB  SER A1182      52.452  10.736 -12.867  1.00 47.31           C  
ANISOU 2982  CB  SER A1182     5031   5958   6986   1321  -1285  -1632       C  
ATOM   2983  OG  SER A1182      53.103  11.058 -14.084  1.00 50.45           O  
ANISOU 2983  OG  SER A1182     5705   6168   7296   1450  -1408  -1472       O  
ATOM   2984  N   LYS A1183      51.362   8.830 -10.810  1.00 44.95           N  
ANISOU 2984  N   LYS A1183     5594   7242   4242     19    539      8       N  
ATOM   2985  CA  LYS A1183      50.563   8.504  -9.632  1.00 43.85           C  
ANISOU 2985  CA  LYS A1183     5341   7150   4169    172    568   -132       C  
ATOM   2986  C   LYS A1183      51.369   7.681  -8.627  1.00 48.97           C  
ANISOU 2986  C   LYS A1183     5851   7815   4942     44    722    -83       C  
ATOM   2987  O   LYS A1183      51.302   7.909  -7.416  1.00 45.63           O  
ANISOU 2987  O   LYS A1183     5454   7331   4552     96    689   -108       O  
ATOM   2988  CB  LYS A1183      49.295   7.752 -10.055  1.00 39.15           C  
ANISOU 2988  CB  LYS A1183     4561   6742   3574    315    647   -322       C  
ATOM   2989  CG  LYS A1183      48.590   6.981  -8.946  1.00 49.89           C  
ANISOU 2989  CG  LYS A1183     5736   8215   5005    383    761   -474       C  
ATOM   2990  CD  LYS A1183      47.862   7.901  -7.980  1.00 67.47           C  
ANISOU 2990  CD  LYS A1183     8063  10390   7181    564    601   -582       C  
ATOM   2991  CE  LYS A1183      47.028   7.100  -6.989  1.00 69.07           C  
ANISOU 2991  CE  LYS A1183     8069  10748   7425    610    728   -763       C  
ATOM   2992  NZ  LYS A1183      46.404   7.964  -5.952  1.00 64.78           N  
ANISOU 2992  NZ  LYS A1183     7600  10176   6835    773    581   -878       N  
ATOM   2993  N   PHE A1184      52.147   6.738  -9.149  1.00 44.39           N  
ANISOU 2993  N   PHE A1184     5131   7313   4421   -115    877    -22       N  
ATOM   2994  CA  PHE A1184      52.993   5.879  -8.332  1.00 40.06           C  
ANISOU 2994  CA  PHE A1184     4463   6778   3979   -222   1008     17       C  
ATOM   2995  C   PHE A1184      54.018   6.698  -7.541  1.00 35.35           C  
ANISOU 2995  C   PHE A1184     4010   6038   3384   -303    915    137       C  
ATOM   2996  O   PHE A1184      54.138   6.561  -6.315  1.00 34.39           O  
ANISOU 2996  O   PHE A1184     3876   5870   3322   -276    928    124       O  
ATOM   2997  CB  PHE A1184      53.699   4.854  -9.224  1.00 34.87           C  
ANISOU 2997  CB  PHE A1184     3662   6209   3377   -351   1139     50       C  
ATOM   2998  CG  PHE A1184      53.972   3.540  -8.551  1.00 42.45           C  
ANISOU 2998  CG  PHE A1184     4569   7009   4550   -331   1175     12       C  
ATOM   2999  CD1 PHE A1184      54.013   3.445  -7.171  1.00 42.65           C  
ANISOU 2999  CD1 PHE A1184     4613   6981   4613   -301   1183      1       C  
ATOM   3000  CD2 PHE A1184      54.189   2.397  -9.305  1.00 50.90           C  
ANISOU 3000  CD2 PHE A1184     5600   7992   5748   -335   1195     -2       C  
ATOM   3001  CE1 PHE A1184      54.265   2.238  -6.555  1.00 46.01           C  
ANISOU 3001  CE1 PHE A1184     5029   7273   5181   -286   1215    -17       C  
ATOM   3002  CE2 PHE A1184      54.443   1.184  -8.694  1.00 51.21           C  
ANISOU 3002  CE2 PHE A1184     5633   7903   5920   -306   1222    -16       C  
ATOM   3003  CZ  PHE A1184      54.481   1.104  -7.316  1.00 50.46           C  
ANISOU 3003  CZ  PHE A1184     5567   7762   5844   -285   1233    -20       C  
ATOM   3004  N   ARG A1185      54.745   7.555  -8.255  1.00 32.11           N  
ANISOU 3004  N   ARG A1185     3743   5562   2896   -418    824    251       N  
ATOM   3005  CA  ARG A1185      55.777   8.395  -7.656  1.00 29.16           C  
ANISOU 3005  CA  ARG A1185     3513   5063   2501   -533    739    364       C  
ATOM   3006  C   ARG A1185      55.193   9.327  -6.602  1.00 30.04           C  
ANISOU 3006  C   ARG A1185     3789   5033   2591   -392    593    341       C  
ATOM   3007  O   ARG A1185      55.795   9.539  -5.543  1.00 43.92           O  
ANISOU 3007  O   ARG A1185     5576   6719   4392   -427    576    381       O  
ATOM   3008  CB  ARG A1185      56.500   9.206  -8.736  1.00 29.95           C  
ANISOU 3008  CB  ARG A1185     3769   5126   2483   -709    665    475       C  
ATOM   3009  CG  ARG A1185      57.180   8.349  -9.791  1.00 29.75           C  
ANISOU 3009  CG  ARG A1185     3571   5264   2469   -866    806    489       C  
ATOM   3010  CD  ARG A1185      58.120   9.158 -10.668  1.00 31.13           C  
ANISOU 3010  CD  ARG A1185     3895   5420   2514  -1101    750    601       C  
ATOM   3011  NE  ARG A1185      59.142   8.308 -11.279  1.00 36.98           N  
ANISOU 3011  NE  ARG A1185     4423   6344   3283  -1281    897    600       N  
ATOM   3012  CZ  ARG A1185      59.091   7.838 -12.521  1.00 50.06           C  
ANISOU 3012  CZ  ARG A1185     5991   8119   4909  -1339    961    579       C  
ATOM   3013  NH1 ARG A1185      58.072   8.145 -13.311  1.00 70.45           N  
ANISOU 3013  NH1 ARG A1185     8683  10672   7411  -1252    904    573       N  
ATOM   3014  NH2 ARG A1185      60.070   7.069 -12.976  1.00 45.79           N  
ANISOU 3014  NH2 ARG A1185     5287   7606   4506  -1374    993    511       N  
ATOM   3015  N   GLU A1186      54.015   9.873  -6.889  1.00 34.74           N  
ANISOU 3015  N   GLU A1186     4484   5599   3116   -219    480    261       N  
ATOM   3016  CA  GLU A1186      53.358  10.768  -5.945  1.00 43.94           C  
ANISOU 3016  CA  GLU A1186     5796   6649   4251    -54    324    206       C  
ATOM   3017  C   GLU A1186      52.939  10.009  -4.686  1.00 36.84           C  
ANISOU 3017  C   GLU A1186     4721   5822   3456     33    426    102       C  
ATOM   3018  O   GLU A1186      53.080  10.516  -3.566  1.00 44.90           O  
ANISOU 3018  O   GLU A1186     5817   6750   4494     70    356    110       O  
ATOM   3019  CB  GLU A1186      52.151  11.447  -6.593  1.00 54.04           C  
ANISOU 3019  CB  GLU A1186     7202   7910   5422    143    168    106       C  
ATOM   3020  CG  GLU A1186      51.733  12.740  -5.903  1.00 73.21           C  
ANISOU 3020  CG  GLU A1186     9871  10171   7773    298    -62     79       C  
ATOM   3021  CD  GLU A1186      52.846  13.776  -5.874  1.00 79.84           C  
ANISOU 3021  CD  GLU A1186    10982  10808   8547    133   -184    258       C  
ATOM   3022  OE1 GLU A1186      53.633  13.839  -6.844  1.00 86.74           O  
ANISOU 3022  OE1 GLU A1186    11932  11661   9365    -67   -157    383       O  
ATOM   3023  OE2 GLU A1186      52.936  14.526  -4.879  1.00 77.09           O  
ANISOU 3023  OE2 GLU A1186    10768  10332   8193    188   -302    267       O  
ATOM   3024  N   ASN A1187      52.437   8.789  -4.876  1.00 28.35           N  
ANISOU 3024  N   ASN A1187     3425   4909   2438     50    591      6       N  
ATOM   3025  CA  ASN A1187      52.098   7.918  -3.754  1.00 27.45           C  
ANISOU 3025  CA  ASN A1187     3162   4865   2403     83    710    -85       C  
ATOM   3026  C   ASN A1187      53.308   7.648  -2.868  1.00 37.51           C  
ANISOU 3026  C   ASN A1187     4434   6064   3753    -46    763     26       C  
ATOM   3027  O   ASN A1187      53.204   7.666  -1.640  1.00 43.00           O  
ANISOU 3027  O   ASN A1187     5137   6721   4480     -5    757     -7       O  
ATOM   3028  CB  ASN A1187      51.520   6.591  -4.247  1.00 26.81           C  
ANISOU 3028  CB  ASN A1187     2877   4954   2354     72    887   -186       C  
ATOM   3029  CG  ASN A1187      50.141   6.742  -4.854  1.00 52.33           C  
ANISOU 3029  CG  ASN A1187     6070   8298   5513    223    849   -347       C  
ATOM   3030  OD1 ASN A1187      49.732   5.941  -5.693  1.00 63.53           O  
ANISOU 3030  OD1 ASN A1187     7359   9847   6932    206    958   -409       O  
ATOM   3031  ND2 ASN A1187      49.418   7.776  -4.437  1.00 56.25           N  
ANISOU 3031  ND2 ASN A1187     6675   8755   5942    383    685   -430       N  
ATOM   3032  N   CYS A1188      54.453   7.399  -3.500  1.00 34.96           N  
ANISOU 3032  N   CYS A1188     4093   5738   3453   -199    812    142       N  
ATOM   3033  CA  CYS A1188      55.695   7.188  -2.761  1.00 30.01           C  
ANISOU 3033  CA  CYS A1188     3454   5060   2886   -311    846    230       C  
ATOM   3034  C   CYS A1188      56.091   8.424  -1.959  1.00 35.81           C  
ANISOU 3034  C   CYS A1188     4366   5649   3591   -310    698    297       C  
ATOM   3035  O   CYS A1188      56.429   8.322  -0.775  1.00 38.04           O  
ANISOU 3035  O   CYS A1188     4645   5884   3925   -301    704    301       O  
ATOM   3036  CB  CYS A1188      56.826   6.803  -3.711  1.00 35.52           C  
ANISOU 3036  CB  CYS A1188     4083   5821   3591   -471    910    308       C  
ATOM   3037  SG  CYS A1188      56.571   5.221  -4.528  1.00 36.39           S  
ANISOU 3037  SG  CYS A1188     3981   6094   3752   -477   1087    231       S  
ATOM   3038  N   LYS A1189      56.045   9.588  -2.604  1.00 27.86           N  
ANISOU 3038  N   LYS A1189     3533   4561   2490   -321    558    350       N  
ATOM   3039  CA  LYS A1189      56.361  10.842  -1.923  1.00 30.53           C  
ANISOU 3039  CA  LYS A1189     4076   4741   2781   -322    399    413       C  
ATOM   3040  C   LYS A1189      55.492  11.041  -0.683  1.00 34.79           C  
ANISOU 3040  C   LYS A1189     4631   5239   3347   -144    343    317       C  
ATOM   3041  O   LYS A1189      56.000  11.273   0.424  1.00 41.45           O  
ANISOU 3041  O   LYS A1189     5507   6013   4230   -161    320    348       O  
ATOM   3042  CB  LYS A1189      56.190  12.033  -2.869  1.00 30.06           C  
ANISOU 3042  CB  LYS A1189     4250   4580   2591   -336    236    466       C  
ATOM   3043  CG  LYS A1189      57.175  12.069  -4.028  1.00 49.14           C  
ANISOU 3043  CG  LYS A1189     6693   7026   4949   -560    274    573       C  
ATOM   3044  CD  LYS A1189      57.169  13.433  -4.709  1.00 59.81           C  
ANISOU 3044  CD  LYS A1189     8358   8223   6146   -613     86    651       C  
ATOM   3045  CE  LYS A1189      58.045  13.446  -5.953  1.00 71.26           C  
ANISOU 3045  CE  LYS A1189     9839   9725   7510   -863    135    745       C  
ATOM   3046  NZ  LYS A1189      57.500  12.573  -7.031  1.00 74.90           N  
ANISOU 3046  NZ  LYS A1189    10140  10335   7984   -821    238    687       N  
ATOM   3047  N   LYS A1190      54.181  10.931  -0.872  1.00 28.56           N  
ANISOU 3047  N   LYS A1190     3806   4516   2532     23    326    185       N  
ATOM   3048  CA  LYS A1190      53.237  11.179   0.211  1.00 28.66           C  
ANISOU 3048  CA  LYS A1190     3819   4527   2544    192    267     58       C  
ATOM   3049  C   LYS A1190      53.335  10.133   1.326  1.00 39.17           C  
ANISOU 3049  C   LYS A1190     4987   5930   3966    159    421     17       C  
ATOM   3050  O   LYS A1190      53.135  10.449   2.504  1.00 55.39           O  
ANISOU 3050  O   LYS A1190     7072   7943   6029    223    374    -26       O  
ATOM   3051  CB  LYS A1190      51.815  11.246  -0.344  1.00 29.29           C  
ANISOU 3051  CB  LYS A1190     3864   4707   2558    371    220   -107       C  
ATOM   3052  CG  LYS A1190      51.631  12.379  -1.343  1.00 36.88           C  
ANISOU 3052  CG  LYS A1190     5037   5565   3409    442     26    -77       C  
ATOM   3053  CD  LYS A1190      50.179  12.803  -1.471  1.00 63.51           C  
ANISOU 3053  CD  LYS A1190     8420   9007   6702    692    -98   -276       C  
ATOM   3054  CE  LYS A1190      50.060  14.091  -2.276  1.00 76.74           C  
ANISOU 3054  CE  LYS A1190    10380  10525   8251    790   -343   -240       C  
ATOM   3055  NZ  LYS A1190      48.661  14.600  -2.330  1.00 82.70           N  
ANISOU 3055  NZ  LYS A1190    11158  11345   8919   1080   -505   -462       N  
ATOM   3056  N   ARG A1191      53.659   8.896   0.961  1.00 32.24           N  
ANISOU 3056  N   ARG A1191     3958   5150   3144     58    594     29       N  
ATOM   3057  CA  ARG A1191      53.873   7.848   1.955  1.00 30.26           C  
ANISOU 3057  CA  ARG A1191     3602   4934   2962     12    728      6       C  
ATOM   3058  C   ARG A1191      55.114   8.136   2.801  1.00 31.50           C  
ANISOU 3058  C   ARG A1191     3829   4974   3164    -66    691    124       C  
ATOM   3059  O   ARG A1191      55.082   8.006   4.028  1.00 32.23           O  
ANISOU 3059  O   ARG A1191     3930   5034   3282    -41    699     97       O  
ATOM   3060  CB  ARG A1191      53.997   6.480   1.282  1.00 29.91           C  
ANISOU 3060  CB  ARG A1191     3415   4996   2955    -68    896     -6       C  
ATOM   3061  CG  ARG A1191      54.474   5.369   2.210  1.00 35.48           C  
ANISOU 3061  CG  ARG A1191     4067   5695   3718   -130   1011     -2       C  
ATOM   3062  CD  ARG A1191      53.562   5.208   3.415  1.00 42.99           C  
ANISOU 3062  CD  ARG A1191     5026   6662   4646    -75   1033   -112       C  
ATOM   3063  NE  ARG A1191      54.118   4.277   4.392  1.00 54.33           N  
ANISOU 3063  NE  ARG A1191     6471   8053   6120   -140   1114    -88       N  
ATOM   3064  CZ  ARG A1191      53.653   4.125   5.628  1.00 53.03           C  
ANISOU 3064  CZ  ARG A1191     6345   7874   5932   -132   1131   -151       C  
ATOM   3065  NH1 ARG A1191      52.622   4.849   6.043  1.00 50.21           N  
ANISOU 3065  NH1 ARG A1191     5989   7569   5518    -57   1078   -257       N  
ATOM   3066  NH2 ARG A1191      54.221   3.254   6.451  1.00 47.89           N  
ANISOU 3066  NH2 ARG A1191     5735   7160   5301   -193   1192   -119       N  
ATOM   3067  N   ALA A1192      56.203   8.526   2.143  1.00 25.90           N  
ANISOU 3067  N   ALA A1192     3166   4218   2456   -171    654    243       N  
ATOM   3068  CA  ALA A1192      57.433   8.870   2.853  1.00 34.35           C  
ANISOU 3068  CA  ALA A1192     4290   5204   3557   -256    615    339       C  
ATOM   3069  C   ALA A1192      57.203  10.029   3.823  1.00 41.06           C  
ANISOU 3069  C   ALA A1192     5287   5934   4379   -184    473    343       C  
ATOM   3070  O   ALA A1192      57.580   9.958   5.002  1.00 42.34           O  
ANISOU 3070  O   ALA A1192     5453   6051   4582   -177    473    349       O  
ATOM   3071  CB  ALA A1192      58.534   9.215   1.869  1.00 31.56           C  
ANISOU 3071  CB  ALA A1192     3957   4857   3179   -404    597    439       C  
ATOM   3072  N   MET A1193      56.572  11.090   3.322  1.00 37.26           N  
ANISOU 3072  N   MET A1193     4938   5397   3821   -118    340    333       N  
ATOM   3073  CA  MET A1193      56.270  12.257   4.147  1.00 32.84           C  
ANISOU 3073  CA  MET A1193     4537   4716   3223    -25    179    321       C  
ATOM   3074  C   MET A1193      55.375  11.894   5.335  1.00 40.15           C  
ANISOU 3074  C   MET A1193     5387   5689   4178    108    207    195       C  
ATOM   3075  O   MET A1193      55.585  12.374   6.455  1.00 43.15           O  
ANISOU 3075  O   MET A1193     5829   5993   4573    136    143    202       O  
ATOM   3076  CB  MET A1193      55.622  13.350   3.296  1.00 39.32           C  
ANISOU 3076  CB  MET A1193     5532   5467   3941     55     15    308       C  
ATOM   3077  CG  MET A1193      56.575  13.940   2.261  1.00 72.37           C  
ANISOU 3077  CG  MET A1193     9856   9576   8065   -114    -38    447       C  
ATOM   3078  SD  MET A1193      55.815  15.096   1.103  1.00 89.77           S  
ANISOU 3078  SD  MET A1193    12309  11676  10122    -28   -237    440       S  
ATOM   3079  CE  MET A1193      57.242  15.584   0.134  1.00 84.87           C  
ANISOU 3079  CE  MET A1193    11840  10982   9426   -324   -245    622       C  
ATOM   3080  N   SER A1194      54.390  11.034   5.090  1.00 35.92           N  
ANISOU 3080  N   SER A1194     4715   5290   3642    172    310     74       N  
ATOM   3081  CA  SER A1194      53.515  10.556   6.159  1.00 30.38           C  
ANISOU 3081  CA  SER A1194     3929   4669   2947    252    367    -62       C  
ATOM   3082  C   SER A1194      54.296   9.798   7.236  1.00 33.44           C  
ANISOU 3082  C   SER A1194     4276   5029   3400    156    468     -7       C  
ATOM   3083  O   SER A1194      54.086  10.004   8.434  1.00 33.85           O  
ANISOU 3083  O   SER A1194     4351   5058   3451    199    440    -53       O  
ATOM   3084  CB  SER A1194      52.418   9.660   5.585  1.00 28.79           C  
ANISOU 3084  CB  SER A1194     3583   4638   2718    287    483   -202       C  
ATOM   3085  OG  SER A1194      51.586   9.154   6.613  1.00 43.12           O  
ANISOU 3085  OG  SER A1194     5315   6552   4515    319    555   -345       O  
ATOM   3086  N   PHE A1195      55.197   8.924   6.797  1.00 36.01           N  
ANISOU 3086  N   PHE A1195     4545   5361   3776     39    575     82       N  
ATOM   3087  CA  PHE A1195      56.022   8.134   7.707  1.00 27.28           C  
ANISOU 3087  CA  PHE A1195     3417   4222   2725    -31    652    129       C  
ATOM   3088  C   PHE A1195      56.902   9.026   8.583  1.00 33.24           C  
ANISOU 3088  C   PHE A1195     4272   4857   3499    -38    541    211       C  
ATOM   3089  O   PHE A1195      56.977   8.844   9.807  1.00 39.49           O  
ANISOU 3089  O   PHE A1195     5084   5613   4307    -22    548    194       O  
ATOM   3090  CB  PHE A1195      56.884   7.154   6.913  1.00 24.62           C  
ANISOU 3090  CB  PHE A1195     3004   3920   2429   -125    751    191       C  
ATOM   3091  CG  PHE A1195      57.425   6.024   7.730  1.00 34.56           C  
ANISOU 3091  CG  PHE A1195     4242   5164   3727   -160    838    193       C  
ATOM   3092  CD1 PHE A1195      56.631   4.926   8.024  1.00 37.65           C  
ANISOU 3092  CD1 PHE A1195     4604   5605   4097   -161    950    107       C  
ATOM   3093  CD2 PHE A1195      58.729   6.050   8.195  1.00 40.88           C  
ANISOU 3093  CD2 PHE A1195     5065   5900   4569   -195    800    272       C  
ATOM   3094  CE1 PHE A1195      57.127   3.875   8.775  1.00 44.05           C  
ANISOU 3094  CE1 PHE A1195     5445   6370   4922   -192   1010    114       C  
ATOM   3095  CE2 PHE A1195      59.233   5.004   8.947  1.00 43.78           C  
ANISOU 3095  CE2 PHE A1195     5436   6240   4960   -198    854    265       C  
ATOM   3096  CZ  PHE A1195      58.430   3.914   9.238  1.00 43.87           C  
ANISOU 3096  CZ  PHE A1195     5455   6269   4944   -194    953    193       C  
ATOM   3097  N   SER A1196      57.561   9.994   7.950  1.00 31.88           N  
ANISOU 3097  N   SER A1196     4175   4623   3315    -77    440    298       N  
ATOM   3098  CA  SER A1196      58.385  10.960   8.675  1.00 35.98           C  
ANISOU 3098  CA  SER A1196     4801   5030   3838   -102    328    373       C  
ATOM   3099  C   SER A1196      57.559  11.733   9.701  1.00 36.62           C  
ANISOU 3099  C   SER A1196     4965   5055   3893     17    228    305       C  
ATOM   3100  O   SER A1196      57.984  11.936  10.851  1.00 47.88           O  
ANISOU 3100  O   SER A1196     6427   6422   5344     22    197    321       O  
ATOM   3101  CB  SER A1196      59.045  11.925   7.696  1.00 37.78           C  
ANISOU 3101  CB  SER A1196     5126   5205   4023   -192    236    464       C  
ATOM   3102  OG  SER A1196      59.766  11.209   6.711  1.00 50.97           O  
ANISOU 3102  OG  SER A1196     6698   6961   5708   -308    333    505       O  
ATOM   3103  N   LYS A 294      56.375  12.157   9.268  1.00 31.87           N  
ANISOU 3103  N   LYS A 294     4387   4486   3236    125    172    213       N  
ATOM   3104  CA  LYS A 294      55.415  12.818  10.143  1.00 32.19           C  
ANISOU 3104  CA  LYS A 294     4474   4518   3239    266     75    101       C  
ATOM   3105  C   LYS A 294      55.158  11.974  11.393  1.00 35.83           C  
ANISOU 3105  C   LYS A 294     4843   5044   3729    266    182     31       C  
ATOM   3106  O   LYS A 294      55.220  12.471  12.529  1.00 37.91           O  
ANISOU 3106  O   LYS A 294     5157   5252   3993    305    116     16       O  
ATOM   3107  CB  LYS A 294      54.105  13.070   9.394  1.00 30.21           C  
ANISOU 3107  CB  LYS A 294     4207   4351   2920    395     25    -32       C  
ATOM   3108  CG  LYS A 294      53.319  14.265   9.893  1.00 45.56           C  
ANISOU 3108  CG  LYS A 294     6256   6252   4801    567   -162   -137       C  
ATOM   3109  CD  LYS A 294      54.050  15.555   9.566  1.00 69.55           C  
ANISOU 3109  CD  LYS A 294     9518   9099   7810    560   -347    -14       C  
ATOM   3110  CE  LYS A 294      53.319  16.767  10.116  1.00 75.73           C  
ANISOU 3110  CE  LYS A 294    10436   9812   8526    751   -559   -121       C  
ATOM   3111  NZ  LYS A 294      54.023  18.031   9.766  1.00 76.50           N  
ANISOU 3111  NZ  LYS A 294    10799   9695   8575    725   -750      5       N  
ATOM   3112  N   GLN A 295      54.886  10.690  11.169  1.00 31.68           N  
ANISOU 3112  N   GLN A 295     4197   4625   3215    210    345    -10       N  
ATOM   3113  CA  GLN A 295      54.618   9.755  12.258  1.00 30.32           C  
ANISOU 3113  CA  GLN A 295     3972   4504   3043    177    458    -73       C  
ATOM   3114  C   GLN A 295      55.802   9.657  13.216  1.00 35.85           C  
ANISOU 3114  C   GLN A 295     4734   5092   3796    118    449     37       C  
ATOM   3115  O   GLN A 295      55.622   9.615  14.440  1.00 48.51           O  
ANISOU 3115  O   GLN A 295     6363   6684   5385    131    450     -6       O  
ATOM   3116  CB  GLN A 295      54.280   8.371  11.704  1.00 39.82           C  
ANISOU 3116  CB  GLN A 295     5080   5810   4240    101    626   -114       C  
ATOM   3117  CG  GLN A 295      53.976   7.335  12.776  1.00 58.28           C  
ANISOU 3117  CG  GLN A 295     7410   8185   6550     35    744   -175       C  
ATOM   3118  CD  GLN A 295      53.828   5.934  12.212  1.00 72.94           C  
ANISOU 3118  CD  GLN A 295     9218  10103   8395    -58    899   -192       C  
ATOM   3119  OE1 GLN A 295      54.068   5.701  11.027  1.00 80.52           O  
ANISOU 3119  OE1 GLN A 295    10129  11081   9384    -67    923   -151       O  
ATOM   3120  NE2 GLN A 295      53.433   4.992  13.062  1.00 70.46           N  
ANISOU 3120  NE2 GLN A 295     8931   9814   8026   -140   1003   -254       N  
ATOM   3121  N   ILE A 296      57.011   9.623  12.659  1.00 27.71           N  
ANISOU 3121  N   ILE A 296     3718   3996   2816     54    440    163       N  
ATOM   3122  CA  ILE A 296      58.214   9.582  13.488  1.00 30.79           C  
ANISOU 3122  CA  ILE A 296     4149   4299   3250     11    418    249       C  
ATOM   3123  C   ILE A 296      58.297  10.807  14.401  1.00 41.24           C  
ANISOU 3123  C   ILE A 296     5564   5539   4566     63    284    259       C  
ATOM   3124  O   ILE A 296      58.546  10.683  15.610  1.00 47.43           O  
ANISOU 3124  O   ILE A 296     6377   6284   5361     72    280    256       O  
ATOM   3125  CB  ILE A 296      59.487   9.500  12.634  1.00 36.57           C  
ANISOU 3125  CB  ILE A 296     4857   5018   4022    -68    418    350       C  
ATOM   3126  CG1 ILE A 296      59.463   8.239  11.769  1.00 44.87           C  
ANISOU 3126  CG1 ILE A 296     5814   6150   5082   -107    543    332       C  
ATOM   3127  CG2 ILE A 296      60.725   9.514  13.520  1.00 33.87           C  
ANISOU 3127  CG2 ILE A 296     4539   4614   3717    -97    384    409       C  
ATOM   3128  CD1 ILE A 296      60.622   8.143  10.800  1.00 41.53           C  
ANISOU 3128  CD1 ILE A 296     5338   5756   4686   -184    547    401       C  
ATOM   3129  N   ARG A 297      58.073  11.985  13.826  1.00 26.03           N  
ANISOU 3129  N   ARG A 297     3701   3577   2613    100    166    269       N  
ATOM   3130  CA  ARG A 297      58.099  13.216  14.613  1.00 33.48           C  
ANISOU 3130  CA  ARG A 297     4754   4426   3541    158     20    273       C  
ATOM   3131  C   ARG A 297      57.051  13.203  15.736  1.00 43.60           C  
ANISOU 3131  C   ARG A 297     6020   5753   4795    259     15    146       C  
ATOM   3132  O   ARG A 297      57.339  13.592  16.881  1.00 47.54           O  
ANISOU 3132  O   ARG A 297     6565   6193   5304    278    -38    151       O  
ATOM   3133  CB  ARG A 297      57.895  14.426  13.698  1.00 41.87           C  
ANISOU 3133  CB  ARG A 297     5929   5425   4555    189   -121    293       C  
ATOM   3134  CG  ARG A 297      59.120  14.764  12.850  1.00 40.16           C  
ANISOU 3134  CG  ARG A 297     5769   5147   4342     48   -143    427       C  
ATOM   3135  CD  ARG A 297      58.806  15.827  11.807  1.00 48.24           C  
ANISOU 3135  CD  ARG A 297     6940   6099   5291     58   -275    449       C  
ATOM   3136  NE  ARG A 297      58.560  15.246  10.490  1.00 58.76           N  
ANISOU 3136  NE  ARG A 297     8206   7514   6605     19   -197    450       N  
ATOM   3137  CZ  ARG A 297      57.752  15.775   9.576  1.00 56.96           C  
ANISOU 3137  CZ  ARG A 297     8065   7269   6308     91   -283    413       C  
ATOM   3138  NH1 ARG A 297      57.097  16.899   9.836  1.00 57.88           N  
ANISOU 3138  NH1 ARG A 297     8345   7285   6361    222   -462    364       N  
ATOM   3139  NH2 ARG A 297      57.592  15.176   8.404  1.00 61.37           N  
ANISOU 3139  NH2 ARG A 297     8551   7912   6855     48   -200    416       N  
ATOM   3140  N   ALA A 298      55.845  12.740  15.411  1.00 36.01           N  
ANISOU 3140  N   ALA A 298     4981   4912   3790    311     76     20       N  
ATOM   3141  CA  ALA A 298      54.779  12.623  16.409  1.00 39.46           C  
ANISOU 3141  CA  ALA A 298     5373   5443   4178    378     94   -133       C  
ATOM   3142  C   ALA A 298      55.180  11.714  17.576  1.00 43.73           C  
ANISOU 3142  C   ALA A 298     5901   5981   4734    293    202   -113       C  
ATOM   3143  O   ALA A 298      55.028  12.078  18.762  1.00 38.39           O  
ANISOU 3143  O   ALA A 298     5254   5294   4039    325    158   -160       O  
ATOM   3144  CB  ALA A 298      53.507  12.108  15.758  1.00 32.66           C  
ANISOU 3144  CB  ALA A 298     4405   4747   3256    413    170   -284       C  
ATOM   3145  N   ARG A 299      55.688  10.533  17.231  1.00 31.82           N  
ANISOU 3145  N   ARG A 299     4362   4477   3251    191    332    -48       N  
ATOM   3146  CA  ARG A 299      56.162   9.581  18.229  1.00 25.80           C  
ANISOU 3146  CA  ARG A 299     3630   3682   2491    117    418    -19       C  
ATOM   3147  C   ARG A 299      57.238  10.207  19.107  1.00 28.10           C  
ANISOU 3147  C   ARG A 299     3999   3849   2829    134    319     75       C  
ATOM   3148  O   ARG A 299      57.286   9.958  20.315  1.00 35.28           O  
ANISOU 3148  O   ARG A 299     4953   4734   3717    121    332     58       O  
ATOM   3149  CB  ARG A 299      56.690   8.314  17.554  1.00 25.37           C  
ANISOU 3149  CB  ARG A 299     3557   3624   2458     35    533     41       C  
ATOM   3150  CG  ARG A 299      55.606   7.292  17.255  1.00 25.52           C  
ANISOU 3150  CG  ARG A 299     3529   3759   2408    -23    669    -66       C  
ATOM   3151  CD  ARG A 299      56.003   6.343  16.136  1.00 37.96           C  
ANISOU 3151  CD  ARG A 299     5072   5339   4011    -73    751    -15       C  
ATOM   3152  NE  ARG A 299      55.739   4.952  16.490  1.00 58.04           N  
ANISOU 3152  NE  ARG A 299     7664   7892   6498   -165    878    -50       N  
ATOM   3153  CZ  ARG A 299      54.535   4.387  16.472  1.00 81.71           C  
ANISOU 3153  CZ  ARG A 299    10634  11005   9406   -234    985   -173       C  
ATOM   3154  NH1 ARG A 299      53.468   5.093  16.118  1.00 84.37           N  
ANISOU 3154  NH1 ARG A 299    10868  11479   9708   -194    975   -289       N  
ATOM   3155  NH2 ARG A 299      54.395   3.113  16.815  1.00 87.90           N  
ANISOU 3155  NH2 ARG A 299    11506  11770  10124   -346   1094   -191       N  
ATOM   3156  N   ARG A 300      58.088  11.033  18.503  1.00 25.70           N  
ANISOU 3156  N   ARG A 300     3716   3473   2577    148    223    169       N  
ATOM   3157  CA  ARG A 300      59.087  11.769  19.271  1.00 25.80           C  
ANISOU 3157  CA  ARG A 300     3795   3382   2625    154    124    245       C  
ATOM   3158  C   ARG A 300      58.446  12.716  20.286  1.00 35.72           C  
ANISOU 3158  C   ARG A 300     5100   4622   3851    232     28    175       C  
ATOM   3159  O   ARG A 300      58.878  12.777  21.442  1.00 37.05           O  
ANISOU 3159  O   ARG A 300     5308   4740   4027    235      4    190       O  
ATOM   3160  CB  ARG A 300      60.008  12.551  18.340  1.00 25.95           C  
ANISOU 3160  CB  ARG A 300     3834   3348   2677    117     45    341       C  
ATOM   3161  CG  ARG A 300      61.013  11.680  17.621  1.00 38.20           C  
ANISOU 3161  CG  ARG A 300     5326   4925   4265     36    124    407       C  
ATOM   3162  CD  ARG A 300      61.782  12.477  16.594  1.00 46.83           C  
ANISOU 3162  CD  ARG A 300     6431   6001   5363    -36     61    480       C  
ATOM   3163  NE  ARG A 300      62.747  11.651  15.878  1.00 48.61           N  
ANISOU 3163  NE  ARG A 300     6569   6288   5615   -113    136    516       N  
ATOM   3164  CZ  ARG A 300      63.470  12.078  14.850  1.00 53.80           C  
ANISOU 3164  CZ  ARG A 300     7208   6973   6262   -212    117    566       C  
ATOM   3165  NH1 ARG A 300      63.331  13.324  14.415  1.00 55.36           N  
ANISOU 3165  NH1 ARG A 300     7504   7113   6418   -254     20    603       N  
ATOM   3166  NH2 ARG A 300      64.327  11.261  14.255  1.00 62.42           N  
ANISOU 3166  NH2 ARG A 300     8194   8150   7373   -272    187    570       N  
ATOM   3167  N   LYS A 301      57.418  13.450  19.859  1.00 26.72           N  
ANISOU 3167  N   LYS A 301     3956   3526   2669    310    -37     87       N  
ATOM   3168  CA  LYS A 301      56.717  14.358  20.771  1.00 34.77           C  
ANISOU 3168  CA  LYS A 301     5010   4551   3651    410   -143    -12       C  
ATOM   3169  C   LYS A 301      56.117  13.623  21.974  1.00 38.61           C  
ANISOU 3169  C   LYS A 301     5449   5126   4094    393    -50   -111       C  
ATOM   3170  O   LYS A 301      56.363  13.997  23.133  1.00 47.07           O  
ANISOU 3170  O   LYS A 301     6564   6154   5167    411   -102   -114       O  
ATOM   3171  CB  LYS A 301      55.613  15.120  20.037  1.00 28.06           C  
ANISOU 3171  CB  LYS A 301     4155   3759   2748    525   -236   -127       C  
ATOM   3172  CG  LYS A 301      56.117  16.101  18.999  1.00 31.28           C  
ANISOU 3172  CG  LYS A 301     4670   4048   3168    546   -368    -34       C  
ATOM   3173  CD  LYS A 301      54.958  16.804  18.311  1.00 44.19           C  
ANISOU 3173  CD  LYS A 301     6324   5730   4735    691   -481   -164       C  
ATOM   3174  CE  LYS A 301      55.407  17.474  17.024  1.00 53.28           C  
ANISOU 3174  CE  LYS A 301     7600   6767   5876    676   -579    -61       C  
ATOM   3175  NZ  LYS A 301      55.934  16.475  16.052  1.00 59.27           N  
ANISOU 3175  NZ  LYS A 301     8282   7568   6670    537   -426     34       N  
ATOM   3176  N   THR A 302      55.334  12.579  21.701  1.00 29.01           N  
ANISOU 3176  N   THR A 302     4156   4037   2831    341     88   -195       N  
ATOM   3177  CA  THR A 302      54.702  11.825  22.786  1.00 31.13           C  
ANISOU 3177  CA  THR A 302     4401   4398   3027    280    191   -297       C  
ATOM   3178  C   THR A 302      55.729  11.185  23.712  1.00 31.34           C  
ANISOU 3178  C   THR A 302     4516   4314   3079    199    231   -182       C  
ATOM   3179  O   THR A 302      55.586  11.213  24.942  1.00 31.76           O  
ANISOU 3179  O   THR A 302     4605   4373   3089    185    228   -226       O  
ATOM   3180  CB  THR A 302      53.772  10.722  22.257  1.00 33.18           C  
ANISOU 3180  CB  THR A 302     4585   4806   3216    196    346   -398       C  
ATOM   3181  OG1 THR A 302      54.393  10.063  21.147  1.00 67.10           O  
ANISOU 3181  OG1 THR A 302     8884   9045   7567    149    404   -284       O  
ATOM   3182  CG2 THR A 302      52.452  11.317  21.813  1.00 32.31           C  
ANISOU 3182  CG2 THR A 302     4367   4867   3042    286    310   -587       C  
ATOM   3183  N   ALA A 303      56.772  10.615  23.122  1.00 26.58           N  
ANISOU 3183  N   ALA A 303     3944   3616   2539    157    260    -47       N  
ATOM   3184  CA  ALA A 303      57.799   9.969  23.923  1.00 29.99           C  
ANISOU 3184  CA  ALA A 303     4460   3945   2989    112    278     45       C  
ATOM   3185  C   ALA A 303      58.519  10.990  24.824  1.00 30.44           C  
ANISOU 3185  C   ALA A 303     4563   3914   3088    173    151     92       C  
ATOM   3186  O   ALA A 303      58.785  10.704  25.995  1.00 30.25           O  
ANISOU 3186  O   ALA A 303     4608   3849   3038    157    153     97       O  
ATOM   3187  CB  ALA A 303      58.781   9.227  23.026  1.00 25.95           C  
ANISOU 3187  CB  ALA A 303     3949   3377   2533     83    314    147       C  
ATOM   3188  N   ARG A 304      58.801  12.184  24.299  1.00 26.45           N  
ANISOU 3188  N   ARG A 304     4040   3377   2635    235     36    124       N  
ATOM   3189  CA  ARG A 304      59.394  13.254  25.111  1.00 26.66           C  
ANISOU 3189  CA  ARG A 304     4117   3321   2691    285    -91    159       C  
ATOM   3190  C   ARG A 304      58.481  13.661  26.272  1.00 30.20           C  
ANISOU 3190  C   ARG A 304     4576   3818   3082    332   -121     46       C  
ATOM   3191  O   ARG A 304      58.944  13.826  27.410  1.00 44.99           O  
ANISOU 3191  O   ARG A 304     6498   5639   4957    337   -158     64       O  
ATOM   3192  CB  ARG A 304      59.715  14.480  24.249  1.00 34.64           C  
ANISOU 3192  CB  ARG A 304     5144   4279   3740    319   -212    205       C  
ATOM   3193  CG  ARG A 304      60.376  15.629  25.008  1.00 39.00           C  
ANISOU 3193  CG  ARG A 304     5768   4735   4316    351   -347    245       C  
ATOM   3194  CD  ARG A 304      60.931  16.669  24.049  1.00 56.20           C  
ANISOU 3194  CD  ARG A 304     8002   6837   6513    331   -453    317       C  
ATOM   3195  NE  ARG A 304      59.890  17.217  23.185  1.00 74.09           N  
ANISOU 3195  NE  ARG A 304    10289   9125   8737    395   -508    253       N  
ATOM   3196  CZ  ARG A 304      59.335  18.412  23.350  1.00 83.02           C  
ANISOU 3196  CZ  ARG A 304    11508  10201   9833    491   -659    197       C  
ATOM   3197  NH1 ARG A 304      59.727  19.196  24.345  1.00 85.93           N  
ANISOU 3197  NH1 ARG A 304    11949  10491  10210    519   -760    206       N  
ATOM   3198  NH2 ARG A 304      58.392  18.827  22.514  1.00 85.31           N  
ANISOU 3198  NH2 ARG A 304    11822  10515  10077    573   -721    124       N  
ATOM   3199  N   MET A 305      57.191  13.824  25.983  1.00 22.69           N  
ANISOU 3199  N   MET A 305     3536   2339   2747   -161    569     44       N  
ATOM   3200  CA  MET A 305      56.215  14.123  27.032  1.00 21.72           C  
ANISOU 3200  CA  MET A 305     3311   2224   2716   -139    409    -46       C  
ATOM   3201  C   MET A 305      56.268  13.084  28.151  1.00 32.81           C  
ANISOU 3201  C   MET A 305     4549   3718   4198    -94    470    -92       C  
ATOM   3202  O   MET A 305      56.390  13.424  29.335  1.00 30.24           O  
ANISOU 3202  O   MET A 305     4083   3437   3969   -104    430   -108       O  
ATOM   3203  CB  MET A 305      54.803  14.185  26.451  1.00 33.85           C  
ANISOU 3203  CB  MET A 305     4970   3686   4204   -106    253   -119       C  
ATOM   3204  CG  MET A 305      53.730  14.495  27.483  1.00 35.59           C  
ANISOU 3204  CG  MET A 305     5085   3899   4537    -72    109   -204       C  
ATOM   3205  SD  MET A 305      52.061  14.482  26.802  1.00 46.11           S  
ANISOU 3205  SD  MET A 305     6520   5153   5845    -30    -77   -271       S  
ATOM   3206  CE  MET A 305      51.899  12.758  26.352  1.00 37.91           C  
ANISOU 3206  CE  MET A 305     5516   4157   4729     -5     15   -322       C  
ATOM   3207  N   LEU A 306      56.190  11.815  27.763  1.00 34.08           N  
ANISOU 3207  N   LEU A 306     4744   3899   4306    -48    573   -113       N  
ATOM   3208  CA  LEU A 306      56.222  10.712  28.721  1.00 36.09           C  
ANISOU 3208  CA  LEU A 306     4859   4228   4624      5    651   -150       C  
ATOM   3209  C   LEU A 306      57.497  10.702  29.562  1.00 33.81           C  
ANISOU 3209  C   LEU A 306     4405   4030   4410    -10    757    -65       C  
ATOM   3210  O   LEU A 306      57.450  10.470  30.775  1.00 35.53           O  
ANISOU 3210  O   LEU A 306     4479   4310   4708     12    735    -94       O  
ATOM   3211  CB  LEU A 306      56.071   9.380  27.988  1.00 35.88           C  
ANISOU 3211  CB  LEU A 306     4927   4190   4517     47    773   -173       C  
ATOM   3212  CG  LEU A 306      54.739   9.236  27.255  1.00 30.97           C  
ANISOU 3212  CG  LEU A 306     4453   3491   3825     51    645   -265       C  
ATOM   3213  CD1 LEU A 306      54.729   7.991  26.382  1.00 26.72           C  
ANISOU 3213  CD1 LEU A 306     4048   2926   3179     67    775   -284       C  
ATOM   3214  CD2 LEU A 306      53.588   9.224  28.252  1.00 19.18           C  
ANISOU 3214  CD2 LEU A 306     2849   2003   2435     83    507   -363       C  
ATOM   3215  N   MET A 307      58.634  10.954  28.918  1.00 34.95           N  
ANISOU 3215  N   MET A 307     4568   4181   4529    -49    872     46       N  
ATOM   3216  CA  MET A 307      59.904  11.018  29.634  1.00 32.56           C  
ANISOU 3216  CA  MET A 307     4091   3967   4312    -75    958    146       C  
ATOM   3217  C   MET A 307      59.890  12.137  30.665  1.00 23.96           C  
ANISOU 3217  C   MET A 307     2904   2901   3299   -139    802    131       C  
ATOM   3218  O   MET A 307      60.386  11.970  31.781  1.00 26.84           O  
ANISOU 3218  O   MET A 307     3107   3353   3739   -146    798    154       O  
ATOM   3219  CB  MET A 307      61.068  11.218  28.665  1.00 28.33           C  
ANISOU 3219  CB  MET A 307     3596   3417   3753   -112   1110    274       C  
ATOM   3220  CG  MET A 307      61.342  10.026  27.777  1.00 28.55           C  
ANISOU 3220  CG  MET A 307     3712   3424   3712    -48   1314    307       C  
ATOM   3221  SD  MET A 307      62.600  10.388  26.546  1.00 40.17           S  
ANISOU 3221  SD  MET A 307     5265   4848   5149    -90   1509    454       S  
ATOM   3222  CE  MET A 307      62.427   8.960  25.478  1.00 41.40           C  
ANISOU 3222  CE  MET A 307     5610   4939   5180     -8   1720    437       C  
ATOM   3223  N   VAL A 308      59.316  13.275  30.287  1.00 22.80           N  
ANISOU 3223  N   VAL A 308     2869   2670   3126   -187    673     94       N  
ATOM   3224  CA  VAL A 308      59.217  14.402  31.206  1.00 28.78           C  
ANISOU 3224  CA  VAL A 308     3569   3421   3944   -252    535     69       C  
ATOM   3225  C   VAL A 308      58.334  14.052  32.405  1.00 25.30           C  
ANISOU 3225  C   VAL A 308     3062   3004   3548   -204    449    -36       C  
ATOM   3226  O   VAL A 308      58.665  14.385  33.548  1.00 28.66           O  
ANISOU 3226  O   VAL A 308     3383   3478   4028   -244    401    -39       O  
ATOM   3227  CB  VAL A 308      58.670  15.657  30.499  1.00 28.68           C  
ANISOU 3227  CB  VAL A 308     3707   3293   3896   -295    430     52       C  
ATOM   3228  CG1 VAL A 308      58.280  16.724  31.514  1.00 25.92           C  
ANISOU 3228  CG1 VAL A 308     3328   2913   3609   -344    293     -3       C  
ATOM   3229  CG2 VAL A 308      59.707  16.199  29.529  1.00 22.40           C  
ANISOU 3229  CG2 VAL A 308     2968   2474   3071   -362    520    165       C  
ATOM   3230  N   VAL A 309      57.227  13.361  32.148  1.00 23.82           N  
ANISOU 3230  N   VAL A 309     2938   2779   3332   -123    433   -119       N  
ATOM   3231  CA  VAL A 309      56.354  12.930  33.237  1.00 23.16           C  
ANISOU 3231  CA  VAL A 309     2792   2710   3299    -69    379   -215       C  
ATOM   3232  C   VAL A 309      57.111  12.004  34.184  1.00 21.01           C  
ANISOU 3232  C   VAL A 309     2376   2549   3059    -47    474   -182       C  
ATOM   3233  O   VAL A 309      57.035  12.153  35.405  1.00 24.60           O  
ANISOU 3233  O   VAL A 309     2754   3037   3558    -53    423   -215       O  
ATOM   3234  CB  VAL A 309      55.092  12.220  32.717  1.00 26.09           C  
ANISOU 3234  CB  VAL A 309     3240   3026   3648      6    358   -300       C  
ATOM   3235  CG1 VAL A 309      54.275  11.672  33.877  1.00 16.82           C  
ANISOU 3235  CG1 VAL A 309     1986   1866   2540     64    336   -390       C  
ATOM   3236  CG2 VAL A 309      54.253  13.176  31.889  1.00 31.02           C  
ANISOU 3236  CG2 VAL A 309     3991   3545   4250    -10    235   -325       C  
ATOM   3237  N   LEU A 310      57.857  11.063  33.612  1.00 37.08           N  
ANISOU 3237  N   LEU A 310     4385   4635   5067    -18    617   -109       N  
ATOM   3238  CA  LEU A 310      58.667  10.142  34.402  1.00 29.10           C  
ANISOU 3238  CA  LEU A 310     3231   3731   4094     16    720    -50       C  
ATOM   3239  C   LEU A 310      59.669  10.883  35.283  1.00 35.52           C  
ANISOU 3239  C   LEU A 310     3922   4618   4957    -64    667     25       C  
ATOM   3240  O   LEU A 310      59.828  10.568  36.466  1.00 33.37           O  
ANISOU 3240  O   LEU A 310     3545   4417   4718    -53    643     23       O  
ATOM   3241  CB  LEU A 310      59.406   9.167  33.489  1.00 24.12           C  
ANISOU 3241  CB  LEU A 310     2605   3123   3435     58    903     36       C  
ATOM   3242  CG  LEU A 310      60.274   8.143  34.218  1.00 24.84           C  
ANISOU 3242  CG  LEU A 310     2540   3320   3577    111   1028    118       C  
ATOM   3243  CD1 LEU A 310      59.422   7.336  35.182  1.00 19.17           C  
ANISOU 3243  CD1 LEU A 310     1793   2618   2874    186   1009     26       C  
ATOM   3244  CD2 LEU A 310      60.984   7.233  33.230  1.00 27.12           C  
ANISOU 3244  CD2 LEU A 310     2851   3607   3845    161   1237    207       C  
ATOM   3245  N   LEU A 311      60.341  11.871  34.698  1.00 26.17           N  
ANISOU 3245  N   LEU A 311     2759   3412   3772   -153    645     92       N  
ATOM   3246  CA  LEU A 311      61.320  12.674  35.424  1.00 27.45           C  
ANISOU 3246  CA  LEU A 311     2811   3635   3983   -256    582    165       C  
ATOM   3247  C   LEU A 311      60.683  13.439  36.581  1.00 34.03           C  
ANISOU 3247  C   LEU A 311     3662   4446   4822   -302    424     69       C  
ATOM   3248  O   LEU A 311      61.233  13.486  37.686  1.00 28.91           O  
ANISOU 3248  O   LEU A 311     2909   3877   4200   -349    373     95       O  
ATOM   3249  CB  LEU A 311      62.013  13.653  34.477  1.00 31.10           C  
ANISOU 3249  CB  LEU A 311     3317   4052   4446   -348    594    242       C  
ATOM   3250  CG  LEU A 311      62.902  14.704  35.144  1.00 30.39           C  
ANISOU 3250  CG  LEU A 311     3137   4001   4410   -484    505    301       C  
ATOM   3251  CD1 LEU A 311      64.061  14.044  35.870  1.00 29.87           C  
ANISOU 3251  CD1 LEU A 311     2863   4075   4410   -497    552    414       C  
ATOM   3252  CD2 LEU A 311      63.405  15.708  34.120  1.00 35.31           C  
ANISOU 3252  CD2 LEU A 311     3830   4552   5034   -570    526    363       C  
ATOM   3253  N   VAL A 312      59.524  14.038  36.321  1.00 25.28           N  
ANISOU 3253  N   VAL A 312     2693   3225   3688   -289    349    -37       N  
ATOM   3254  CA  VAL A 312      58.827  14.821  37.335  1.00 25.29           C  
ANISOU 3254  CA  VAL A 312     2737   3175   3698   -323    226   -132       C  
ATOM   3255  C   VAL A 312      58.338  13.920  38.467  1.00 30.66           C  
ANISOU 3255  C   VAL A 312     3362   3904   4385   -248    234   -193       C  
ATOM   3256  O   VAL A 312      58.338  14.312  39.633  1.00 29.74           O  
ANISOU 3256  O   VAL A 312     3234   3799   4269   -293    163   -229       O  
ATOM   3257  CB  VAL A 312      57.645  15.593  36.726  1.00 18.86           C  
ANISOU 3257  CB  VAL A 312     2071   2221   2874   -303    162   -215       C  
ATOM   3258  CG1 VAL A 312      56.815  16.261  37.811  1.00 25.45           C  
ANISOU 3258  CG1 VAL A 312     2952   2987   3730   -312     71   -315       C  
ATOM   3259  CG2 VAL A 312      58.156  16.623  35.738  1.00 19.74           C  
ANISOU 3259  CG2 VAL A 312     2252   2275   2972   -384    147   -150       C  
ATOM   3260  N   PHE A 313      57.936  12.705  38.114  1.00 32.51           N  
ANISOU 3260  N   PHE A 313     3578   4158   4615   -140    328   -205       N  
ATOM   3261  CA  PHE A 313      57.532  11.709  39.098  1.00 29.58           C  
ANISOU 3261  CA  PHE A 313     3153   3833   4253    -61    364   -250       C  
ATOM   3262  C   PHE A 313      58.712  11.323  39.992  1.00 30.92           C  
ANISOU 3262  C   PHE A 313     3191   4131   4426    -92    381   -157       C  
ATOM   3263  O   PHE A 313      58.612  11.346  41.225  1.00 29.88           O  
ANISOU 3263  O   PHE A 313     3041   4028   4286   -101    328   -191       O  
ATOM   3264  CB  PHE A 313      56.963  10.474  38.392  1.00 20.92           C  
ANISOU 3264  CB  PHE A 313     2070   2726   3153     48    474   -273       C  
ATOM   3265  CG  PHE A 313      56.536   9.380  39.325  1.00 26.89           C  
ANISOU 3265  CG  PHE A 313     2776   3519   3924    135    533   -316       C  
ATOM   3266  CD1 PHE A 313      57.430   8.394  39.717  1.00 35.97           C  
ANISOU 3266  CD1 PHE A 313     3819   4774   5073    173    631   -229       C  
ATOM   3267  CD2 PHE A 313      55.238   9.330  39.803  1.00 29.59           C  
ANISOU 3267  CD2 PHE A 313     3172   3782   4288    184    500   -435       C  
ATOM   3268  CE1 PHE A 313      57.039   7.386  40.576  1.00 32.87           C  
ANISOU 3268  CE1 PHE A 313     3392   4409   4691    257    693   -263       C  
ATOM   3269  CE2 PHE A 313      54.839   8.321  40.658  1.00 36.78           C  
ANISOU 3269  CE2 PHE A 313     4044   4717   5214    263    570   -472       C  
ATOM   3270  CZ  PHE A 313      55.740   7.351  41.047  1.00 37.01           C  
ANISOU 3270  CZ  PHE A 313     3983   4850   5229    299    665   -388       C  
ATOM   3271  N   ALA A 314      59.826  10.968  39.355  1.00 24.69           N  
ANISOU 3271  N   ALA A 314     2315   3417   3650   -105    459    -33       N  
ATOM   3272  CA  ALA A 314      61.042  10.578  40.060  1.00 25.75           C  
ANISOU 3272  CA  ALA A 314     2294   3681   3807   -131    475     87       C  
ATOM   3273  C   ALA A 314      61.486  11.663  41.032  1.00 20.36           C  
ANISOU 3273  C   ALA A 314     1591   3026   3118   -261    321     91       C  
ATOM   3274  O   ALA A 314      61.799  11.386  42.198  1.00 34.19           O  
ANISOU 3274  O   ALA A 314     3274   4857   4859   -272    270    111       O  
ATOM   3275  CB  ALA A 314      62.153  10.271  39.063  1.00 19.79           C  
ANISOU 3275  CB  ALA A 314     1452   2977   3089   -135    590    228       C  
ATOM   3276  N   ILE A 315      61.502  12.900  40.546  1.00 20.19           N  
ANISOU 3276  N   ILE A 315     1646   2931   3096   -364    248     71       N  
ATOM   3277  CA  ILE A 315      61.862  14.040  41.376  1.00 27.84           C  
ANISOU 3277  CA  ILE A 315     2629   3898   4052   -506    104     59       C  
ATOM   3278  C   ILE A 315      60.889  14.207  42.541  1.00 25.20           C  
ANISOU 3278  C   ILE A 315     2396   3510   3668   -491     29    -71       C  
ATOM   3279  O   ILE A 315      61.305  14.351  43.688  1.00 24.68           O  
ANISOU 3279  O   ILE A 315     2302   3504   3572   -560    -57    -63       O  
ATOM   3280  CB  ILE A 315      61.904  15.338  40.553  1.00 28.02           C  
ANISOU 3280  CB  ILE A 315     2742   3821   4083   -608     62     50       C  
ATOM   3281  CG1 ILE A 315      63.077  15.298  39.571  1.00 29.46           C  
ANISOU 3281  CG1 ILE A 315     2817   4060   4316   -650    138    194       C  
ATOM   3282  CG2 ILE A 315      62.015  16.548  41.469  1.00 22.41           C  
ANISOU 3282  CG2 ILE A 315     2093   3073   3349   -753    -81      2       C  
ATOM   3283  CD1 ILE A 315      63.124  16.478  38.622  1.00 29.86           C  
ANISOU 3283  CD1 ILE A 315     2968   4006   4372   -735    123    195       C  
ATOM   3284  N   CYS A 316      59.595  14.169  42.244  1.00 24.34           N  
ANISOU 3284  N   CYS A 316     2406   3288   3553   -402     63   -184       N  
ATOM   3285  CA  CYS A 316      58.568  14.375  43.261  1.00 29.97           C  
ANISOU 3285  CA  CYS A 316     3225   3926   4238   -376     20   -308       C  
ATOM   3286  C   CYS A 316      58.573  13.311  44.356  1.00 30.37           C  
ANISOU 3286  C   CYS A 316     3217   4060   4261   -308     51   -308       C  
ATOM   3287  O   CYS A 316      58.158  13.584  45.483  1.00 30.90           O  
ANISOU 3287  O   CYS A 316     3362   4093   4284   -328      2   -381       O  
ATOM   3288  CB  CYS A 316      57.182  14.428  42.613  1.00 34.94           C  
ANISOU 3288  CB  CYS A 316     3957   4424   4896   -281     62   -408       C  
ATOM   3289  SG  CYS A 316      56.746  16.035  41.918  1.00 38.60           S  
ANISOU 3289  SG  CYS A 316     4553   4738   5375   -359    -12   -451       S  
ATOM   3290  N   TYR A 317      59.035  12.105  44.035  1.00 33.95           N  
ANISOU 3290  N   TYR A 317     3551   4613   4735   -225    143   -225       N  
ATOM   3291  CA  TYR A 317      59.009  11.023  45.018  1.00 25.76           C  
ANISOU 3291  CA  TYR A 317     2463   3649   3675   -145    187   -216       C  
ATOM   3292  C   TYR A 317      60.370  10.719  45.645  1.00 29.09           C  
ANISOU 3292  C   TYR A 317     2748   4224   4082   -200    143    -79       C  
ATOM   3293  O   TYR A 317      60.452   9.938  46.595  1.00 26.13           O  
ANISOU 3293  O   TYR A 317     2337   3916   3675   -146    156    -57       O  
ATOM   3294  CB  TYR A 317      58.434   9.751  44.391  1.00 24.54           C  
ANISOU 3294  CB  TYR A 317     2281   3487   3557      4    335   -226       C  
ATOM   3295  CG  TYR A 317      56.923   9.717  44.408  1.00 26.06           C  
ANISOU 3295  CG  TYR A 317     2590   3550   3762     77    366   -369       C  
ATOM   3296  CD1 TYR A 317      56.184  10.283  43.376  1.00 32.16           C  
ANISOU 3296  CD1 TYR A 317     3436   4218   4568     75    356   -430       C  
ATOM   3297  CD2 TYR A 317      56.235   9.135  45.466  1.00 20.31           C  
ANISOU 3297  CD2 TYR A 317     1895   2804   3019    148    403   -436       C  
ATOM   3298  CE1 TYR A 317      54.801  10.264  43.394  1.00 38.82           C  
ANISOU 3298  CE1 TYR A 317     4359   4947   5445    141    374   -546       C  
ATOM   3299  CE2 TYR A 317      54.852   9.110  45.491  1.00 26.18           C  
ANISOU 3299  CE2 TYR A 317     2724   3425   3798    213    440   -558       C  
ATOM   3300  CZ  TYR A 317      54.140   9.676  44.452  1.00 40.01           C  
ANISOU 3300  CZ  TYR A 317     4524   5080   5598    209    421   -610       C  
ATOM   3301  OH  TYR A 317      52.764   9.655  44.471  1.00 45.63           O  
ANISOU 3301  OH  TYR A 317     5295   5675   6367    275    448   -717       O  
ATOM   3302  N   LEU A 318      61.432  11.334  45.132  1.00 20.53           N  
ANISOU 3302  N   LEU A 318     1582   3194   3027   -308     89     22       N  
ATOM   3303  CA  LEU A 318      62.762  11.115  45.705  1.00 25.88           C  
ANISOU 3303  CA  LEU A 318     2101   4022   3712   -372     29    168       C  
ATOM   3304  C   LEU A 318      62.889  11.535  47.189  1.00 33.34           C  
ANISOU 3304  C   LEU A 318     3092   5003   4573   -464   -123    141       C  
ATOM   3305  O   LEU A 318      63.351  10.735  48.004  1.00 34.99           O  
ANISOU 3305  O   LEU A 318     3214   5323   4760   -424   -137    218       O  
ATOM   3306  CB  LEU A 318      63.832  11.830  44.868  1.00 27.45           C  
ANISOU 3306  CB  LEU A 318     2201   4255   3973   -487      0    277       C  
ATOM   3307  CG  LEU A 318      65.272  11.659  45.360  1.00 33.07           C  
ANISOU 3307  CG  LEU A 318     2714   5127   4725   -564    -69    449       C  
ATOM   3308  CD1 LEU A 318      65.725  10.209  45.233  1.00 31.96           C  
ANISOU 3308  CD1 LEU A 318     2417   5088   4638   -414     70    574       C  
ATOM   3309  CD2 LEU A 318      66.220  12.590  44.621  1.00 32.00           C  
ANISOU 3309  CD2 LEU A 318     2499   5002   4660   -704   -109    536       C  
ATOM   3310  N   PRO A 319      62.483  12.774  47.550  1.00 29.53           N  
ANISOU 3310  N   PRO A 319     2759   4422   4037   -586   -234     33       N  
ATOM   3311  CA  PRO A 319      62.672  13.189  48.949  1.00 27.99           C  
ANISOU 3311  CA  PRO A 319     2635   4255   3743   -691   -377      6       C  
ATOM   3312  C   PRO A 319      61.989  12.294  49.987  1.00 28.25           C  
ANISOU 3312  C   PRO A 319     2737   4292   3703   -575   -335    -48       C  
ATOM   3313  O   PRO A 319      62.635  11.904  50.960  1.00 34.26           O  
ANISOU 3313  O   PRO A 319     3447   5165   4403   -606   -418     27       O  
ATOM   3314  CB  PRO A 319      62.057  14.591  48.979  1.00 24.37           C  
ANISOU 3314  CB  PRO A 319     2370   3643   3247   -805   -443   -128       C  
ATOM   3315  CG  PRO A 319      62.202  15.083  47.596  1.00 24.00           C  
ANISOU 3315  CG  PRO A 319     2278   3550   3291   -820   -393    -99       C  
ATOM   3316  CD  PRO A 319      61.940  13.882  46.742  1.00 25.36           C  
ANISOU 3316  CD  PRO A 319     2351   3756   3530   -644   -238    -55       C  
ATOM   3317  N   ILE A 320      60.713  11.980  49.788  1.00 27.55           N  
ANISOU 3317  N   ILE A 320     2760   4084   3625   -447   -212   -168       N  
ATOM   3318  CA  ILE A 320      59.982  11.146  50.740  1.00 23.82           C  
ANISOU 3318  CA  ILE A 320     2361   3595   3094   -334   -147   -225       C  
ATOM   3319  C   ILE A 320      60.566   9.732  50.787  1.00 21.85           C  
ANISOU 3319  C   ILE A 320     1948   3484   2871   -219    -72    -96       C  
ATOM   3320  O   ILE A 320      60.532   9.071  51.827  1.00 31.40           O  
ANISOU 3320  O   ILE A 320     3181   4738   4010   -169    -71    -81       O  
ATOM   3321  CB  ILE A 320      58.469  11.086  50.402  1.00 29.54           C  
ANISOU 3321  CB  ILE A 320     3210   4157   3856   -221    -20   -372       C  
ATOM   3322  CG1 ILE A 320      57.687  10.423  51.539  1.00 30.62           C  
ANISOU 3322  CG1 ILE A 320     3448   4255   3931   -128     47   -442       C  
ATOM   3323  CG2 ILE A 320      58.227  10.368  49.083  1.00 19.30           C  
ANISOU 3323  CG2 ILE A 320     1808   2859   2665   -109    105   -343       C  
ATOM   3324  CD1 ILE A 320      57.839  11.124  52.875  1.00 40.93           C  
ANISOU 3324  CD1 ILE A 320     4903   5544   5107   -239    -66   -483       C  
ATOM   3325  N   SER A 321      61.121   9.285  49.664  1.00 21.52           N  
ANISOU 3325  N   SER A 321     1751   3500   2926   -177      0      3       N  
ATOM   3326  CA  SER A 321      61.756   7.977  49.588  1.00 29.32           C  
ANISOU 3326  CA  SER A 321     2578   4608   3955    -64     93    139       C  
ATOM   3327  C   SER A 321      63.003   7.944  50.453  1.00 37.47           C  
ANISOU 3327  C   SER A 321     3492   5796   4951   -143    -42    287       C  
ATOM   3328  O   SER A 321      63.148   7.080  51.317  1.00 43.67           O  
ANISOU 3328  O   SER A 321     4248   6654   5693    -68    -30    346       O  
ATOM   3329  CB  SER A 321      62.113   7.631  48.143  1.00 28.02           C  
ANISOU 3329  CB  SER A 321     2297   4451   3896    -15    211    211       C  
ATOM   3330  OG  SER A 321      60.965   7.651  47.319  1.00 33.08           O  
ANISOU 3330  OG  SER A 321     3050   4955   4562     49    311     80       O  
ATOM   3331  N   ILE A 322      63.900   8.897  50.214  1.00 38.60           N  
ANISOU 3331  N   ILE A 322     3565   5988   5116   -300   -174    352       N  
ATOM   3332  CA  ILE A 322      65.145   8.982  50.967  1.00 35.86           C  
ANISOU 3332  CA  ILE A 322     3082   5794   4749   -404   -333    502       C  
ATOM   3333  C   ILE A 322      64.872   9.172  52.455  1.00 48.46           C  
ANISOU 3333  C   ILE A 322     4822   7395   6194   -461   -471    440       C  
ATOM   3334  O   ILE A 322      65.536   8.566  53.296  1.00 55.82           O  
ANISOU 3334  O   ILE A 322     5667   8457   7087   -449   -546    561       O  
ATOM   3335  CB  ILE A 322      66.032  10.134  50.463  1.00 33.04           C  
ANISOU 3335  CB  ILE A 322     2647   5463   4444   -590   -459    557       C  
ATOM   3336  CG1 ILE A 322      66.278  10.000  48.959  1.00 37.37           C  
ANISOU 3336  CG1 ILE A 322     3082   5989   5128   -534   -308    615       C  
ATOM   3337  CG2 ILE A 322      67.348  10.165  51.222  1.00 38.88           C  
ANISOU 3337  CG2 ILE A 322     3217   6373   5183   -704   -636    727       C  
ATOM   3338  CD1 ILE A 322      66.801   8.643  48.539  1.00 36.42           C  
ANISOU 3338  CD1 ILE A 322     2776   5963   5099   -372   -150    767       C  
ATOM   3339  N   LEU A 323      63.887  10.006  52.774  1.00 41.20           N  
ANISOU 3339  N   LEU A 323     4133   6329   5191   -518   -496    258       N  
ATOM   3340  CA  LEU A 323      63.522  10.252  54.165  1.00 37.49           C  
ANISOU 3340  CA  LEU A 323     3848   5833   4563   -574   -600    179       C  
ATOM   3341  C   LEU A 323      63.008   8.980  54.830  1.00 38.20           C  
ANISOU 3341  C   LEU A 323     3965   5941   4608   -397   -485    187       C  
ATOM   3342  O   LEU A 323      63.429   8.635  55.939  1.00 46.87           O  
ANISOU 3342  O   LEU A 323     5082   7128   5600   -416   -584    252       O  
ATOM   3343  CB  LEU A 323      62.471  11.361  54.263  1.00 26.94           C  
ANISOU 3343  CB  LEU A 323     2759   4308   3168   -643   -598    -19       C  
ATOM   3344  CG  LEU A 323      62.984  12.795  54.126  1.00 29.28           C  
ANISOU 3344  CG  LEU A 323     3104   4573   3448   -859   -754    -44       C  
ATOM   3345  CD1 LEU A 323      61.836  13.781  54.241  1.00 31.73           C  
ANISOU 3345  CD1 LEU A 323     3670   4679   3709   -893   -714   -236       C  
ATOM   3346  CD2 LEU A 323      64.053  13.088  55.171  1.00 30.37           C  
ANISOU 3346  CD2 LEU A 323     3224   4836   3478  -1030   -973     44       C  
ATOM   3347  N   ASN A 324      62.104   8.282  54.148  1.00 30.44           N  
ANISOU 3347  N   ASN A 324     2989   4872   3704   -231   -281    123       N  
ATOM   3348  CA  ASN A 324      61.560   7.038  54.680  1.00 27.93           C  
ANISOU 3348  CA  ASN A 324     2696   4555   3362    -59   -145    125       C  
ATOM   3349  C   ASN A 324      62.639   5.983  54.879  1.00 31.86           C  
ANISOU 3349  C   ASN A 324     2994   5226   3883      9   -152    327       C  
ATOM   3350  O   ASN A 324      62.631   5.269  55.873  1.00 37.62           O  
ANISOU 3350  O   ASN A 324     3764   6002   4529     77   -150    369       O  
ATOM   3351  CB  ASN A 324      60.463   6.488  53.769  1.00 23.32           C  
ANISOU 3351  CB  ASN A 324     2132   3851   2878     87     68     28       C  
ATOM   3352  CG  ASN A 324      59.095   7.055  54.093  1.00 30.65           C  
ANISOU 3352  CG  ASN A 324     3278   4602   3767     90    116   -166       C  
ATOM   3353  OD1 ASN A 324      58.856   7.542  55.199  1.00 36.52           O  
ANISOU 3353  OD1 ASN A 324     4182   5304   4391     28     42   -229       O  
ATOM   3354  ND2 ASN A 324      58.185   6.988  53.128  1.00 38.20           N  
ANISOU 3354  ND2 ASN A 324     4243   5448   4824    164    243   -256       N  
ATOM   3355  N   VAL A 325      63.568   5.889  53.935  1.00 33.79           N  
ANISOU 3355  N   VAL A 325     3029   5563   4248     -3   -149    460       N  
ATOM   3356  CA  VAL A 325      64.646   4.911  54.038  1.00 35.40           C  
ANISOU 3356  CA  VAL A 325     3019   5928   4504     71   -140    672       C  
ATOM   3357  C   VAL A 325      65.599   5.254  55.186  1.00 43.57           C  
ANISOU 3357  C   VAL A 325     4013   7099   5443    -54   -378    787       C  
ATOM   3358  O   VAL A 325      65.994   4.380  55.956  1.00 45.14           O  
ANISOU 3358  O   VAL A 325     4152   7398   5602     28   -391    909       O  
ATOM   3359  CB  VAL A 325      65.431   4.805  52.719  1.00 34.87           C  
ANISOU 3359  CB  VAL A 325     2740   5910   4597     83    -63    791       C  
ATOM   3360  CG1 VAL A 325      66.672   3.948  52.900  1.00 35.18           C  
ANISOU 3360  CG1 VAL A 325     2540   6119   4707    144    -69   1032       C  
ATOM   3361  CG2 VAL A 325      64.542   4.233  51.626  1.00 28.49           C  
ANISOU 3361  CG2 VAL A 325     1979   4980   3866    220    173    696       C  
ATOM   3362  N   LEU A 326      65.956   6.529  55.307  1.00 42.72           N  
ANISOU 3362  N   LEU A 326     3947   6992   5293   -258   -570    749       N  
ATOM   3363  CA  LEU A 326      66.829   6.977  56.390  1.00 32.32           C  
ANISOU 3363  CA  LEU A 326     2614   5797   3871   -413   -825    840       C  
ATOM   3364  C   LEU A 326      66.207   6.733  57.760  1.00 32.77           C  
ANISOU 3364  C   LEU A 326     2895   5822   3736   -391   -874    763       C  
ATOM   3365  O   LEU A 326      66.882   6.283  58.686  1.00 45.21           O  
ANISOU 3365  O   LEU A 326     4418   7529   5232   -400  -1006    898       O  
ATOM   3366  CB  LEU A 326      67.159   8.463  56.239  1.00 41.89           C  
ANISOU 3366  CB  LEU A 326     3873   6978   5063   -650  -1004    776       C  
ATOM   3367  CG  LEU A 326      68.166   8.846  55.155  1.00 43.41           C  
ANISOU 3367  CG  LEU A 326     3821   7244   5428   -728  -1026    903       C  
ATOM   3368  CD1 LEU A 326      68.345  10.351  55.116  1.00 34.50           C  
ANISOU 3368  CD1 LEU A 326     2787   6060   4264   -968  -1193    815       C  
ATOM   3369  CD2 LEU A 326      69.496   8.155  55.400  1.00 50.03           C  
ANISOU 3369  CD2 LEU A 326     4376   8288   6345   -718  -1119   1158       C  
ATOM   3370  N   LYS A 327      64.918   7.031  57.886  1.00 33.39           N  
ANISOU 3370  N   LYS A 327     3223   5723   3742   -358   -764    554       N  
ATOM   3371  CA  LYS A 327      64.226   6.893  59.163  1.00 38.46           C  
ANISOU 3371  CA  LYS A 327     4111   6303   4200   -340   -780    462       C  
ATOM   3372  C   LYS A 327      63.935   5.436  59.527  1.00 41.64           C  
ANISOU 3372  C   LYS A 327     4483   6736   4601   -123   -619    532       C  
ATOM   3373  O   LYS A 327      64.253   4.985  60.629  1.00 39.39           O  
ANISOU 3373  O   LYS A 327     4252   6530   4185   -113   -710    612       O  
ATOM   3374  CB  LYS A 327      62.917   7.687  59.146  1.00 35.00           C  
ANISOU 3374  CB  LYS A 327     3935   5650   3713   -363   -687    224       C  
ATOM   3375  CG  LYS A 327      62.063   7.489  60.392  1.00 45.30           C  
ANISOU 3375  CG  LYS A 327     5509   6860   4844   -319   -644    118       C  
ATOM   3376  CD  LYS A 327      60.672   8.080  60.226  1.00 52.12           C  
ANISOU 3376  CD  LYS A 327     6589   7501   5714   -294   -491    -99       C  
ATOM   3377  CE  LYS A 327      59.791   7.753  61.423  1.00 57.23           C  
ANISOU 3377  CE  LYS A 327     7491   8043   6210   -224   -401   -194       C  
ATOM   3378  NZ  LYS A 327      58.410   8.290  61.270  1.00 61.63           N  
ANISOU 3378  NZ  LYS A 327     8236   8378   6802   -185   -232   -391       N  
ATOM   3379  N   ARG A 328      63.333   4.708  58.592  1.00 42.83           N  
ANISOU 3379  N   ARG A 328     4560   6820   4894     43   -383    502       N  
ATOM   3380  CA  ARG A 328      62.799   3.373  58.856  1.00 35.62           C  
ANISOU 3380  CA  ARG A 328     3659   5887   3987    250   -187    525       C  
ATOM   3381  C   ARG A 328      63.814   2.245  58.676  1.00 39.13           C  
ANISOU 3381  C   ARG A 328     3858   6493   4518    363   -156    754       C  
ATOM   3382  O   ARG A 328      63.675   1.183  59.282  1.00 50.78           O  
ANISOU 3382  O   ARG A 328     5352   7988   5953    506    -59    818       O  
ATOM   3383  CB  ARG A 328      61.592   3.107  57.952  1.00 31.39           C  
ANISOU 3383  CB  ARG A 328     3176   5190   3561    364     52    373       C  
ATOM   3384  CG  ARG A 328      60.397   4.010  58.211  1.00 34.17           C  
ANISOU 3384  CG  ARG A 328     3771   5364   3849    302     70    155       C  
ATOM   3385  CD  ARG A 328      59.753   3.688  59.546  1.00 47.39           C  
ANISOU 3385  CD  ARG A 328     5659   6975   5372    350    107     93       C  
ATOM   3386  NE  ARG A 328      58.507   4.419  59.748  1.00 56.11           N  
ANISOU 3386  NE  ARG A 328     6987   7889   6444    323    179   -111       N  
ATOM   3387  CZ  ARG A 328      57.739   4.295  60.826  1.00 59.68           C  
ANISOU 3387  CZ  ARG A 328     7659   8240   6777    362    250   -198       C  
ATOM   3388  NH1 ARG A 328      58.092   3.467  61.799  1.00 60.74           N  
ANISOU 3388  NH1 ARG A 328     7831   8451   6796    426    245   -101       N  
ATOM   3389  NH2 ARG A 328      56.619   4.998  60.931  1.00 62.98           N  
ANISOU 3389  NH2 ARG A 328     8261   8476   7194    344    333   -374       N  
ATOM   3390  N   VAL A 329      64.823   2.460  57.839  1.00 36.49           N  
ANISOU 3390  N   VAL A 329     3294   6263   4309    308   -220    884       N  
ATOM   3391  CA  VAL A 329      65.808   1.414  57.584  1.00 44.20           C  
ANISOU 3391  CA  VAL A 329     4020   7380   5393    426   -166   1113       C  
ATOM   3392  C   VAL A 329      67.102   1.644  58.364  1.00 49.64           C  
ANISOU 3392  C   VAL A 329     4571   8256   6035    318   -424   1310       C  
ATOM   3393  O   VAL A 329      67.670   0.706  58.925  1.00 51.36           O  
ANISOU 3393  O   VAL A 329     4681   8586   6248    426   -426   1489       O  
ATOM   3394  CB  VAL A 329      66.137   1.300  56.081  1.00 39.44           C  
ANISOU 3394  CB  VAL A 329     3230   6770   4985    465    -23   1158       C  
ATOM   3395  CG1 VAL A 329      67.123   0.172  55.835  1.00 32.59           C  
ANISOU 3395  CG1 VAL A 329     2116   6029   4238    604     71   1399       C  
ATOM   3396  CG2 VAL A 329      64.865   1.085  55.278  1.00 38.18           C  
ANISOU 3396  CG2 VAL A 329     3208   6433   4866    556    203    967       C  
ATOM   3397  N   PHE A 330      67.562   2.890  58.409  1.00 46.60           N  
ANISOU 3397  N   PHE A 330     4187   7902   5615    101   -647   1283       N  
ATOM   3398  CA  PHE A 330      68.827   3.201  59.068  1.00 47.05           C  
ANISOU 3398  CA  PHE A 330     4094   8140   5642    -33   -918   1470       C  
ATOM   3399  C   PHE A 330      68.633   3.891  60.417  1.00 47.85           C  
ANISOU 3399  C   PHE A 330     4435   8239   5507   -188  -1153   1385       C  
ATOM   3400  O   PHE A 330      69.599   4.314  61.051  1.00 51.04           O  
ANISOU 3400  O   PHE A 330     4758   8783   5853   -341  -1421   1512       O  
ATOM   3401  CB  PHE A 330      69.697   4.060  58.152  1.00 42.80           C  
ANISOU 3401  CB  PHE A 330     3355   7658   5249   -183  -1013   1535       C  
ATOM   3402  CG  PHE A 330      70.058   3.383  56.864  1.00 53.79           C  
ANISOU 3402  CG  PHE A 330     4511   9063   6864    -40   -789   1645       C  
ATOM   3403  CD1 PHE A 330      71.036   2.402  56.834  1.00 63.67           C  
ANISOU 3403  CD1 PHE A 330     5567  10400   8224     74   -725   1861       C  
ATOM   3404  CD2 PHE A 330      69.412   3.715  55.686  1.00 57.29           C  
ANISOU 3404  CD2 PHE A 330     5011   9366   7391    -22   -609   1501       C  
ATOM   3405  CE1 PHE A 330      71.369   1.769  55.651  1.00 57.88           C  
ANISOU 3405  CE1 PHE A 330     4775   9563   7654    191   -469   1894       C  
ATOM   3406  CE2 PHE A 330      69.741   3.086  54.500  1.00 60.69           C  
ANISOU 3406  CE2 PHE A 330     5305   9762   7994    100   -387   1575       C  
ATOM   3407  CZ  PHE A 330      70.721   2.112  54.483  1.00 61.06           C  
ANISOU 3407  CZ  PHE A 330     5256   9829   8116    200   -307   1744       C  
ATOM   3408  N   GLY A 331      67.381   3.998  60.848  1.00 48.69           N  
ANISOU 3408  N   GLY A 331     4840   8181   5479   -152  -1049   1174       N  
ATOM   3409  CA  GLY A 331      67.063   4.484  62.178  1.00 52.18           C  
ANISOU 3409  CA  GLY A 331     5555   8592   5678   -264  -1214   1084       C  
ATOM   3410  C   GLY A 331      67.548   5.881  62.518  1.00 49.21           C  
ANISOU 3410  C   GLY A 331     5260   8233   5203   -541  -1488   1033       C  
ATOM   3411  O   GLY A 331      67.733   6.207  63.690  1.00 58.61           O  
ANISOU 3411  O   GLY A 331     6622   9459   6188   -663  -1691   1031       O  
ATOM   3412  N   MET A 332      67.753   6.712  61.503  1.00 47.70           N  
ANISOU 3412  N   MET A 332     4964   8012   5150   -647  -1494    990       N  
ATOM   3413  CA  MET A 332      68.140   8.096  61.743  1.00 57.73           C  
ANISOU 3413  CA  MET A 332     6326   9271   6338   -916  -1729    923       C  
ATOM   3414  C   MET A 332      66.955   8.883  62.294  1.00 73.31           C  
ANISOU 3414  C   MET A 332     8681  11039   8136   -981  -1686    667       C  
ATOM   3415  O   MET A 332      65.854   8.344  62.430  1.00 82.48           O  
ANISOU 3415  O   MET A 332    10003  12074   9262   -813  -1472    554       O  
ATOM   3416  CB  MET A 332      68.669   8.745  60.463  1.00 58.11           C  
ANISOU 3416  CB  MET A 332     6160   9330   6590  -1000  -1720    953       C  
ATOM   3417  CG  MET A 332      69.920   8.077  59.916  1.00 70.01           C  
ANISOU 3417  CG  MET A 332     7285  11031   8283   -952  -1756   1214       C  
ATOM   3418  SD  MET A 332      70.769   9.071  58.675  1.00 84.42           S  
ANISOU 3418  SD  MET A 332     8883  12881  10312  -1118  -1809   1265       S  
ATOM   3419  CE  MET A 332      72.110   7.973  58.220  1.00 86.84           C  
ANISOU 3419  CE  MET A 332     8825  13332  10837   -972  -1732   1548       C  
ATOM   3420  N   PHE A 333      67.192  10.153  62.614  1.00 70.83           N  
ANISOU 3420  N   PHE A 333     8507  10686   7721  -1227  -1880    583       N  
ATOM   3421  CA  PHE A 333      66.177  11.026  63.206  1.00 66.39           C  
ANISOU 3421  CA  PHE A 333     8319   9920   6985  -1311  -1849    350       C  
ATOM   3422  C   PHE A 333      65.669  10.450  64.525  1.00 68.70           C  
ANISOU 3422  C   PHE A 333     8863  10184   7054  -1243  -1842    315       C  
ATOM   3423  O   PHE A 333      64.512  10.643  64.894  1.00 78.58           O  
ANISOU 3423  O   PHE A 333    10400  11246   8210  -1187  -1682    132       O  
ATOM   3424  CB  PHE A 333      65.005  11.245  62.243  1.00 58.00           C  
ANISOU 3424  CB  PHE A 333     7322   8663   6051  -1188  -1578    183       C  
ATOM   3425  CG  PHE A 333      65.422  11.468  60.815  1.00 61.50           C  
ANISOU 3425  CG  PHE A 333     7501   9140   6727  -1186  -1529    242       C  
ATOM   3426  CD1 PHE A 333      66.478  12.313  60.505  1.00 55.68           C  
ANISOU 3426  CD1 PHE A 333     6631   8489   6036  -1396  -1729    319       C  
ATOM   3427  CD2 PHE A 333      64.761  10.822  59.782  1.00 60.08           C  
ANISOU 3427  CD2 PHE A 333     7213   8902   6715   -981  -1280    221       C  
ATOM   3428  CE1 PHE A 333      66.863  12.511  59.191  1.00 47.53           C  
ANISOU 3428  CE1 PHE A 333     5369   7477   5212  -1389  -1665    377       C  
ATOM   3429  CE2 PHE A 333      65.140  11.016  58.467  1.00 56.98           C  
ANISOU 3429  CE2 PHE A 333     6605   8531   6514   -979  -1229    275       C  
ATOM   3430  CZ  PHE A 333      66.192  11.862  58.170  1.00 53.49           C  
ANISOU 3430  CZ  PHE A 333     6038   8169   6116  -1178  -1412    354       C  
ATOM   3431  N   ALA A 334      66.542   9.735  65.228  1.00 63.89           N  
ANISOU 3431  N   ALA A 334     8143   9762   6370  -1243  -2010    500       N  
ATOM   3432  CA  ALA A 334      66.203   9.179  66.530  1.00 70.35           C  
ANISOU 3432  CA  ALA A 334     9202  10570   6956  -1190  -2030    493       C  
ATOM   3433  C   ALA A 334      66.437  10.215  67.622  1.00 78.66           C  
ANISOU 3433  C   ALA A 334    10552  11591   7744  -1453  -2283    411       C  
ATOM   3434  O   ALA A 334      66.135   9.980  68.793  1.00 74.33           O  
ANISOU 3434  O   ALA A 334    10276  11009   6957  -1452  -2320    378       O  
ATOM   3435  CB  ALA A 334      67.015   7.922  66.801  1.00 72.50           C  
ANISOU 3435  CB  ALA A 334     9234  11053   7260  -1061  -2096    740       C  
ATOM   3436  N   HIS A 335      66.978  11.363  67.225  1.00 85.24           N  
ANISOU 3436  N   HIS A 335    11346  12425   8616  -1683  -2449    377       N  
ATOM   3437  CA  HIS A 335      67.265  12.452  68.151  1.00 81.05           C  
ANISOU 3437  CA  HIS A 335    11070  11809   7915  -1905  -2618    280       C  
ATOM   3438  C   HIS A 335      66.449  13.694  67.807  1.00 73.77           C  
ANISOU 3438  C   HIS A 335    10386  10651   6994  -2003  -2496     48       C  
ATOM   3439  O   HIS A 335      66.882  14.819  68.052  1.00 68.40           O  
ANISOU 3439  O   HIS A 335     9791   9895   6303  -2181  -2592    -12       O  
ATOM   3440  CB  HIS A 335      68.758  12.785  68.140  1.00 80.33           C  
ANISOU 3440  CB  HIS A 335    10712  11866   7943  -2042  -2844    441       C  
ATOM   3441  N   ASP A 338      67.048  18.090  67.533  1.00 76.89           N  
ANISOU 3441  N   ASP A 338    11108  10632   7475  -2561  -2597   -270       N  
ATOM   3442  CA  ASP A 338      66.335  18.895  66.546  1.00 82.46           C  
ANISOU 3442  CA  ASP A 338    11853  11170   8308  -2548  -2422   -398       C  
ATOM   3443  C   ASP A 338      65.327  18.053  65.755  1.00 84.83           C  
ANISOU 3443  C   ASP A 338    12095  11445   8690  -2343  -2224   -437       C  
ATOM   3444  O   ASP A 338      65.704  17.239  64.910  1.00 85.48           O  
ANISOU 3444  O   ASP A 338    11873  11689   8915  -2263  -2242   -309       O  
ATOM   3445  CB  ASP A 338      67.331  19.567  65.597  1.00 86.42           C  
ANISOU 3445  CB  ASP A 338    12090  11743   9001  -2666  -2516   -310       C  
ATOM   3446  CG  ASP A 338      66.750  20.790  64.904  1.00 93.92           C  
ANISOU 3446  CG  ASP A 338    13165  12489  10031  -2711  -2376   -451       C  
ATOM   3447  OD1 ASP A 338      65.567  20.759  64.499  1.00 97.09           O  
ANISOU 3447  OD1 ASP A 338    13690  12745  10455  -2582  -2172   -572       O  
ATOM   3448  OD2 ASP A 338      67.487  21.789  64.761  1.00 95.70           O  
ANISOU 3448  OD2 ASP A 338    13361  12700  10302  -2872  -2467   -436       O  
ATOM   3449  N   ARG A 339      64.043  18.264  66.031  1.00 77.44           N  
ANISOU 3449  N   ARG A 339    11450  10299   7675  -2257  -2022   -610       N  
ATOM   3450  CA  ARG A 339      62.976  17.494  65.397  1.00 69.42           C  
ANISOU 3450  CA  ARG A 339    10424   9230   6721  -2064  -1818   -671       C  
ATOM   3451  C   ARG A 339      62.181  18.326  64.395  1.00 68.17           C  
ANISOU 3451  C   ARG A 339    10299   8884   6719  -2031  -1638   -797       C  
ATOM   3452  O   ARG A 339      61.662  17.800  63.408  1.00 64.19           O  
ANISOU 3452  O   ARG A 339     9637   8378   6373  -1880  -1496   -796       O  
ATOM   3453  CB  ARG A 339      62.033  16.932  66.461  1.00 68.49           C  
ANISOU 3453  CB  ARG A 339    10595   9006   6421  -1943  -1682   -761       C  
ATOM   3454  CG  ARG A 339      61.637  17.954  67.519  1.00 84.33           C  
ANISOU 3454  CG  ARG A 339    12935  10812   8294  -2023  -1630   -883       C  
ATOM   3455  CD  ARG A 339      60.389  17.529  68.271  1.00 88.76           C  
ANISOU 3455  CD  ARG A 339    13767  11205   8753  -1861  -1396   -995       C  
ATOM   3456  NE  ARG A 339      59.234  17.443  67.384  1.00 91.70           N  
ANISOU 3456  NE  ARG A 339    14118  11432   9290  -1690  -1138  -1094       N  
ATOM   3457  CZ  ARG A 339      57.999  17.167  67.791  1.00 93.38           C  
ANISOU 3457  CZ  ARG A 339    14509  11471   9500  -1518   -879  -1191       C  
ATOM   3458  NH1 ARG A 339      57.755  16.953  69.076  1.00 95.24           N  
ANISOU 3458  NH1 ARG A 339    14975  11651   9561  -1499   -838  -1206       N  
ATOM   3459  NH2 ARG A 339      57.008  17.108  66.912  1.00 91.30           N  
ANISOU 3459  NH2 ARG A 339    14174  11088   9429  -1359   -658  -1261       N  
ATOM   3460  N   GLU A 340      62.089  19.625  64.661  1.00 74.19           N  
ANISOU 3460  N   GLU A 340    11239   9484   7466  -2137  -1618   -884       N  
ATOM   3461  CA  GLU A 340      61.289  20.531  63.844  1.00 66.51           C  
ANISOU 3461  CA  GLU A 340    10323   8316   6632  -2095  -1441   -994       C  
ATOM   3462  C   GLU A 340      61.783  20.582  62.401  1.00 56.74           C  
ANISOU 3462  C   GLU A 340     8792   7171   5598  -2110  -1481   -919       C  
ATOM   3463  O   GLU A 340      60.986  20.712  61.474  1.00 63.27           O  
ANISOU 3463  O   GLU A 340     9592   7886   6561  -2004  -1320   -983       O  
ATOM   3464  CB  GLU A 340      61.285  21.936  64.456  1.00 71.52           C  
ANISOU 3464  CB  GLU A 340    11186   8790   7197  -2222  -1437  -1069       C  
ATOM   3465  CG  GLU A 340      62.659  22.571  64.617  1.00 83.50           C  
ANISOU 3465  CG  GLU A 340    12615  10427   8685  -2439  -1672   -977       C  
ATOM   3466  CD  GLU A 340      62.592  23.953  65.240  1.00 95.11           C  
ANISOU 3466  CD  GLU A 340    14340  11728  10070  -2569  -1655  -1062       C  
ATOM   3467  OE1 GLU A 340      61.536  24.298  65.813  1.00 96.81           O  
ANISOU 3467  OE1 GLU A 340    14817  11752  10215  -2492  -1478  -1176       O  
ATOM   3468  OE2 GLU A 340      63.593  24.695  65.155  1.00101.06           O  
ANISOU 3468  OE2 GLU A 340    15028  12537  10834  -2746  -1810  -1009       O  
ATOM   3469  N   THR A 341      63.094  20.465  62.215  1.00 42.55           N  
ANISOU 3469  N   THR A 341     6126   5808   4234  -2632   -744   -333       N  
ATOM   3470  CA  THR A 341      63.685  20.458  60.880  1.00 47.80           C  
ANISOU 3470  CA  THR A 341     6633   6498   5029  -2591   -743   -280       C  
ATOM   3471  C   THR A 341      63.297  19.196  60.116  1.00 44.22           C  
ANISOU 3471  C   THR A 341     6007   6114   4682  -2452   -732   -233       C  
ATOM   3472  O   THR A 341      62.880  19.261  58.956  1.00 45.88           O  
ANISOU 3472  O   THR A 341     6172   6280   4979  -2377   -667   -244       O  
ATOM   3473  CB  THR A 341      65.221  20.569  60.948  1.00 47.88           C  
ANISOU 3473  CB  THR A 341     6528   6608   5056  -2684   -844   -196       C  
ATOM   3474  OG1 THR A 341      65.585  21.897  61.342  1.00 56.88           O  
ANISOU 3474  OG1 THR A 341     7833   7667   6112  -2824   -845   -238       O  
ATOM   3475  CG2 THR A 341      65.845  20.262  59.598  1.00 34.56           C  
ANISOU 3475  CG2 THR A 341     4644   4985   3502  -2623   -840   -130       C  
ATOM   3476  N   VAL A 342      63.432  18.051  60.780  1.00 40.23           N  
ANISOU 3476  N   VAL A 342     5423   5705   4157  -2422   -799   -178       N  
ATOM   3477  CA  VAL A 342      63.064  16.766  60.196  1.00 36.57           C  
ANISOU 3477  CA  VAL A 342     4826   5298   3771  -2298   -801   -128       C  
ATOM   3478  C   VAL A 342      61.581  16.748  59.835  1.00 44.82           C  
ANISOU 3478  C   VAL A 342     5948   6263   4820  -2234   -696   -201       C  
ATOM   3479  O   VAL A 342      61.192  16.315  58.742  1.00 55.18           O  
ANISOU 3479  O   VAL A 342     7169   7569   6228  -2141   -657   -186       O  
ATOM   3480  CB  VAL A 342      63.372  15.604  61.160  1.00 36.40           C  
ANISOU 3480  CB  VAL A 342     4764   5369   3696  -2291   -894    -63       C  
ATOM   3481  CG1 VAL A 342      63.066  14.268  60.502  1.00 35.38           C  
ANISOU 3481  CG1 VAL A 342     4520   5284   3640  -2168   -906     -5       C  
ATOM   3482  CG2 VAL A 342      64.822  15.661  61.610  1.00 42.24           C  
ANISOU 3482  CG2 VAL A 342     5426   6202   4423  -2358  -1005      4       C  
ATOM   3483  N   TYR A 343      60.761  17.242  60.758  1.00 36.25           N  
ANISOU 3483  N   TYR A 343     5029   5121   3621  -2287   -648   -284       N  
ATOM   3484  CA  TYR A 343      59.319  17.291  60.557  1.00 37.20           C  
ANISOU 3484  CA  TYR A 343     5220   5186   3728  -2221   -537   -362       C  
ATOM   3485  C   TYR A 343      58.958  18.218  59.400  1.00 38.75           C  
ANISOU 3485  C   TYR A 343     5435   5282   4005  -2138   -442   -406       C  
ATOM   3486  O   TYR A 343      58.029  17.942  58.641  1.00 40.36           O  
ANISOU 3486  O   TYR A 343     5589   5465   4279  -1990   -356   -411       O  
ATOM   3487  CB  TYR A 343      58.613  17.742  61.837  1.00 34.19           C  
ANISOU 3487  CB  TYR A 343     5021   4773   3196  -2274   -488   -444       C  
ATOM   3488  CG  TYR A 343      57.122  17.500  61.810  1.00 50.85           C  
ANISOU 3488  CG  TYR A 343     7151   6871   5300  -2137   -353   -487       C  
ATOM   3489  CD1 TYR A 343      56.593  16.274  62.191  1.00 55.85           C  
ANISOU 3489  CD1 TYR A 343     7714   7588   5918  -2105   -355   -438       C  
ATOM   3490  CD2 TYR A 343      56.244  18.493  61.392  1.00 60.76           C  
ANISOU 3490  CD2 TYR A 343     8492   8037   6558  -2041   -226   -571       C  
ATOM   3491  CE1 TYR A 343      55.230  16.043  62.162  1.00 60.05           C  
ANISOU 3491  CE1 TYR A 343     8241   8134   6443  -2002   -232   -469       C  
ATOM   3492  CE2 TYR A 343      54.879  18.272  61.361  1.00 60.93           C  
ANISOU 3492  CE2 TYR A 343     8498   8079   6575  -1910   -104   -604       C  
ATOM   3493  CZ  TYR A 343      54.378  17.046  61.746  1.00 63.25           C  
ANISOU 3493  CZ  TYR A 343     8699   8475   6857  -1902   -107   -552       C  
ATOM   3494  OH  TYR A 343      53.021  16.820  61.714  1.00 68.16           O  
ANISOU 3494  OH  TYR A 343     9285   9141   7472  -1794     13   -578       O  
ATOM   3495  N   ALA A 344      59.701  19.314  59.269  1.00 29.84           N  
ANISOU 3495  N   ALA A 344     4386   4092   2860  -2244   -466   -434       N  
ATOM   3496  CA  ALA A 344      59.491  20.255  58.175  1.00 32.05           C  
ANISOU 3496  CA  ALA A 344     4711   4263   3204  -2182   -387   -468       C  
ATOM   3497  C   ALA A 344      59.833  19.612  56.829  1.00 38.36           C  
ANISOU 3497  C   ALA A 344     5321   5107   4148  -2090   -395   -387       C  
ATOM   3498  O   ALA A 344      59.089  19.761  55.851  1.00 38.87           O  
ANISOU 3498  O   ALA A 344     5378   5109   4282  -1949   -309   -402       O  
ATOM   3499  CB  ALA A 344      60.318  21.512  58.389  1.00 31.03           C  
ANISOU 3499  CB  ALA A 344     4725   4055   3010  -2348   -422   -504       C  
ATOM   3500  N   TRP A 345      60.957  18.897  56.788  1.00 33.09           N  
ANISOU 3500  N   TRP A 345     4505   4551   3518  -2159   -499   -300       N  
ATOM   3501  CA  TRP A 345      61.349  18.149  55.597  1.00 34.08           C  
ANISOU 3501  CA  TRP A 345     4453   4730   3765  -2060   -506   -219       C  
ATOM   3502  C   TRP A 345      60.273  17.144  55.203  1.00 36.77           C  
ANISOU 3502  C   TRP A 345     4745   5073   4155  -1885   -454   -208       C  
ATOM   3503  O   TRP A 345      59.954  16.988  54.019  1.00 36.83           O  
ANISOU 3503  O   TRP A 345     4696   5047   4249  -1765   -402   -190       O  
ATOM   3504  CB  TRP A 345      62.679  17.425  55.821  1.00 36.52           C  
ANISOU 3504  CB  TRP A 345     4611   5172   4092  -2097   -614   -123       C  
ATOM   3505  CG  TRP A 345      63.876  18.249  55.470  1.00 45.45           C  
ANISOU 3505  CG  TRP A 345     5707   6322   5241  -2178   -634    -92       C  
ATOM   3506  CD1 TRP A 345      64.739  18.857  56.337  1.00 45.75           C  
ANISOU 3506  CD1 TRP A 345     5785   6391   5207  -2299   -691    -86       C  
ATOM   3507  CD2 TRP A 345      64.344  18.562  54.152  1.00 43.90           C  
ANISOU 3507  CD2 TRP A 345     5429   6121   5131  -2158   -596    -60       C  
ATOM   3508  NE1 TRP A 345      65.715  19.526  55.639  1.00 47.73           N  
ANISOU 3508  NE1 TRP A 345     5977   6663   5496  -2361   -692    -51       N  
ATOM   3509  CE2 TRP A 345      65.495  19.361  54.297  1.00 49.28           C  
ANISOU 3509  CE2 TRP A 345     6099   6838   5788  -2276   -629    -34       C  
ATOM   3510  CE3 TRP A 345      63.900  18.243  52.865  1.00 36.94           C  
ANISOU 3510  CE3 TRP A 345     4487   5211   4339  -2061   -536    -47       C  
ATOM   3511  CZ2 TRP A 345      66.208  19.847  53.201  1.00 47.81           C  
ANISOU 3511  CZ2 TRP A 345     5840   6664   5661  -2301   -597      4       C  
ATOM   3512  CZ3 TRP A 345      64.610  18.725  51.780  1.00 44.04           C  
ANISOU 3512  CZ3 TRP A 345     5322   6115   5295  -2080   -504    -10       C  
ATOM   3513  CH2 TRP A 345      65.750  19.519  51.955  1.00 46.07           C  
ANISOU 3513  CH2 TRP A 345     5567   6412   5525  -2200   -530     15       C  
ATOM   3514  N   PHE A 346      59.707  16.472  56.202  1.00 26.14           N  
ANISOU 3514  N   PHE A 346     3426   3764   2741  -1886   -470   -217       N  
ATOM   3515  CA  PHE A 346      58.648  15.501  55.952  1.00 27.44           C  
ANISOU 3515  CA  PHE A 346     3553   3939   2935  -1758   -427   -204       C  
ATOM   3516  C   PHE A 346      57.375  16.150  55.412  1.00 24.77           C  
ANISOU 3516  C   PHE A 346     3277   3520   2615  -1657   -307   -274       C  
ATOM   3517  O   PHE A 346      56.783  15.649  54.455  1.00 31.92           O  
ANISOU 3517  O   PHE A 346     4115   4418   3595  -1539   -273   -252       O  
ATOM   3518  CB  PHE A 346      58.333  14.712  57.224  1.00 28.77           C  
ANISOU 3518  CB  PHE A 346     3755   4167   3009  -1808   -465   -196       C  
ATOM   3519  CG  PHE A 346      59.063  13.404  57.316  1.00 33.24           C  
ANISOU 3519  CG  PHE A 346     4227   4812   3591  -1802   -570   -100       C  
ATOM   3520  CD1 PHE A 346      58.554  12.270  56.702  1.00 27.45           C  
ANISOU 3520  CD1 PHE A 346     3437   4084   2909  -1695   -564    -51       C  
ATOM   3521  CD2 PHE A 346      60.260  13.308  58.008  1.00 35.10           C  
ANISOU 3521  CD2 PHE A 346     4440   5114   3781  -1901   -682    -58       C  
ATOM   3522  CE1 PHE A 346      59.223  11.062  56.778  1.00 24.65           C  
ANISOU 3522  CE1 PHE A 346     3029   3781   2557  -1671   -660     36       C  
ATOM   3523  CE2 PHE A 346      60.935  12.104  58.088  1.00 33.34           C  
ANISOU 3523  CE2 PHE A 346     4136   4964   3567  -1866   -781     33       C  
ATOM   3524  CZ  PHE A 346      60.415  10.979  57.472  1.00 26.16           C  
ANISOU 3524  CZ  PHE A 346     3194   4041   2706  -1743   -766     78       C  
ATOM   3525  N   THR A 347      56.953  17.258  56.019  1.00 25.60           N  
ANISOU 3525  N   THR A 347     3518   3564   2643  -1694   -249   -358       N  
ATOM   3526  CA  THR A 347      55.747  17.951  55.566  1.00 32.84           C  
ANISOU 3526  CA  THR A 347     4496   4412   3568  -1574   -136   -427       C  
ATOM   3527  C   THR A 347      55.920  18.415  54.126  1.00 24.92           C  
ANISOU 3527  C   THR A 347     3464   3340   2665  -1493   -114   -412       C  
ATOM   3528  O   THR A 347      55.013  18.265  53.290  1.00 37.96           O  
ANISOU 3528  O   THR A 347     5073   4979   4373  -1356    -59   -415       O  
ATOM   3529  CB  THR A 347      55.403  19.164  56.456  1.00 35.11           C  
ANISOU 3529  CB  THR A 347     4967   4629   3745  -1612    -77   -523       C  
ATOM   3530  OG1 THR A 347      56.531  20.042  56.536  1.00 51.60           O  
ANISOU 3530  OG1 THR A 347     7148   6651   5806  -1741   -130   -533       O  
ATOM   3531  CG2 THR A 347      55.022  18.710  57.856  1.00 27.44           C  
ANISOU 3531  CG2 THR A 347     4036   3727   2662  -1673    -76   -544       C  
ATOM   3532  N   PHE A 348      57.098  18.959  53.836  1.00 25.27           N  
ANISOU 3532  N   PHE A 348     3527   3350   2723  -1587   -162   -391       N  
ATOM   3533  CA  PHE A 348      57.401  19.393  52.480  1.00 26.69           C  
ANISOU 3533  CA  PHE A 348     3686   3467   2986  -1531   -141   -368       C  
ATOM   3534  C   PHE A 348      57.339  18.230  51.505  1.00 27.39           C  
ANISOU 3534  C   PHE A 348     3621   3617   3171  -1428   -159   -295       C  
ATOM   3535  O   PHE A 348      56.755  18.349  50.429  1.00 31.09           O  
ANISOU 3535  O   PHE A 348     4083   4035   3697  -1308   -110   -297       O  
ATOM   3536  CB  PHE A 348      58.777  20.047  52.401  1.00 25.63           C  
ANISOU 3536  CB  PHE A 348     3575   3319   2846  -1683   -193   -343       C  
ATOM   3537  CG  PHE A 348      59.221  20.326  50.997  1.00 33.09           C  
ANISOU 3537  CG  PHE A 348     4479   4222   3873  -1641   -171   -303       C  
ATOM   3538  CD1 PHE A 348      58.678  21.383  50.285  1.00 35.54           C  
ANISOU 3538  CD1 PHE A 348     4923   4398   4182  -1578    -97   -350       C  
ATOM   3539  CD2 PHE A 348      60.168  19.523  50.381  1.00 35.85           C  
ANISOU 3539  CD2 PHE A 348     4666   4666   4290  -1652   -220   -215       C  
ATOM   3540  CE1 PHE A 348      59.077  21.642  48.989  1.00 40.90           C  
ANISOU 3540  CE1 PHE A 348     5580   5034   4924  -1545    -74   -310       C  
ATOM   3541  CE2 PHE A 348      60.572  19.777  49.083  1.00 43.35           C  
ANISOU 3541  CE2 PHE A 348     5585   5584   5304  -1612   -187   -177       C  
ATOM   3542  CZ  PHE A 348      60.025  20.839  48.386  1.00 39.71           C  
ANISOU 3542  CZ  PHE A 348     5264   4985   4839  -1568   -115   -224       C  
ATOM   3543  N   SER A 349      57.948  17.110  51.885  1.00 29.36           N  
ANISOU 3543  N   SER A 349     3763   3965   3428  -1470   -234   -231       N  
ATOM   3544  CA  SER A 349      57.984  15.929  51.026  1.00 29.55           C  
ANISOU 3544  CA  SER A 349     3670   4033   3525  -1373   -259   -161       C  
ATOM   3545  C   SER A 349      56.582  15.411  50.723  1.00 30.57           C  
ANISOU 3545  C   SER A 349     3798   4148   3667  -1258   -213   -181       C  
ATOM   3546  O   SER A 349      56.272  15.058  49.579  1.00 38.65           O  
ANISOU 3546  O   SER A 349     4781   5148   4755  -1156   -197   -155       O  
ATOM   3547  CB  SER A 349      58.827  14.831  51.669  1.00 31.01           C  
ANISOU 3547  CB  SER A 349     3772   4317   3694  -1426   -351    -93       C  
ATOM   3548  OG  SER A 349      60.166  15.267  51.825  1.00 28.27           O  
ANISOU 3548  OG  SER A 349     3388   4012   3342  -1527   -402    -64       O  
ATOM   3549  N   HIS A 350      55.738  15.373  51.750  1.00 22.17           N  
ANISOU 3549  N   HIS A 350     2777   3109   2537  -1283   -191   -224       N  
ATOM   3550  CA  HIS A 350      54.341  14.990  51.574  1.00 27.63           C  
ANISOU 3550  CA  HIS A 350     3452   3816   3232  -1196   -140   -245       C  
ATOM   3551  C   HIS A 350      53.662  15.903  50.555  1.00 30.29           C  
ANISOU 3551  C   HIS A 350     3815   4082   3612  -1083    -71   -287       C  
ATOM   3552  O   HIS A 350      53.067  15.429  49.567  1.00 31.34           O  
ANISOU 3552  O   HIS A 350     3892   4216   3801   -989    -67   -263       O  
ATOM   3553  CB  HIS A 350      53.595  15.035  52.912  1.00 27.86           C  
ANISOU 3553  CB  HIS A 350     3524   3893   3167  -1248   -106   -291       C  
ATOM   3554  CG  HIS A 350      54.103  14.053  53.921  1.00 33.13           C  
ANISOU 3554  CG  HIS A 350     4180   4627   3780  -1352   -177   -246       C  
ATOM   3555  ND1 HIS A 350      53.792  14.132  55.262  1.00 41.53           N  
ANISOU 3555  ND1 HIS A 350     5305   5732   4742  -1431   -160   -280       N  
ATOM   3556  CD2 HIS A 350      54.902  12.967  53.785  1.00 25.79           C  
ANISOU 3556  CD2 HIS A 350     3199   3726   2875  -1377   -266   -167       C  
ATOM   3557  CE1 HIS A 350      54.377  13.140  55.907  1.00 33.21           C  
ANISOU 3557  CE1 HIS A 350     4240   4727   3652  -1510   -242   -221       C  
ATOM   3558  NE2 HIS A 350      55.056  12.418  55.036  1.00 33.73           N  
ANISOU 3558  NE2 HIS A 350     4237   4785   3794  -1471   -309   -151       N  
ATOM   3559  N   TRP A 351      53.775  17.212  50.785  1.00 30.96           N  
ANISOU 3559  N   TRP A 351     4003   4097   3662  -1094    -25   -347       N  
ATOM   3560  CA  TRP A 351      53.179  18.184  49.871  1.00 30.48           C  
ANISOU 3560  CA  TRP A 351     3999   3952   3629   -977     37   -387       C  
ATOM   3561  C   TRP A 351      53.664  18.001  48.437  1.00 30.27           C  
ANISOU 3561  C   TRP A 351     3930   3884   3685   -924     12   -333       C  
ATOM   3562  O   TRP A 351      52.894  18.159  47.497  1.00 29.93           O  
ANISOU 3562  O   TRP A 351     3882   3810   3679   -802     40   -339       O  
ATOM   3563  CB  TRP A 351      53.473  19.619  50.313  1.00 33.28           C  
ANISOU 3563  CB  TRP A 351     4513   4208   3922  -1013     77   -454       C  
ATOM   3564  CG  TRP A 351      53.037  20.618  49.283  1.00 30.13           C  
ANISOU 3564  CG  TRP A 351     4199   3701   3548   -891    129   -483       C  
ATOM   3565  CD1 TRP A 351      51.802  21.187  49.164  1.00 36.21           C  
ANISOU 3565  CD1 TRP A 351     5015   4447   4297   -739    197   -538       C  
ATOM   3566  CD2 TRP A 351      53.825  21.143  48.207  1.00 28.14           C  
ANISOU 3566  CD2 TRP A 351     3995   3358   3340   -901    116   -453       C  
ATOM   3567  NE1 TRP A 351      51.776  22.042  48.089  1.00 31.30           N  
ANISOU 3567  NE1 TRP A 351     4483   3710   3701   -647    218   -544       N  
ATOM   3568  CE2 TRP A 351      53.005  22.031  47.482  1.00 26.68           C  
ANISOU 3568  CE2 TRP A 351     3906   3077   3153   -754    173   -492       C  
ATOM   3569  CE3 TRP A 351      55.144  20.951  47.787  1.00 32.18           C  
ANISOU 3569  CE3 TRP A 351     4471   3870   3886  -1015     67   -392       C  
ATOM   3570  CZ2 TRP A 351      53.461  22.726  46.366  1.00 34.42           C  
ANISOU 3570  CZ2 TRP A 351     4972   3946   4161   -732    179   -473       C  
ATOM   3571  CZ3 TRP A 351      55.595  21.640  46.676  1.00 35.94           C  
ANISOU 3571  CZ3 TRP A 351     5013   4251   4391   -999     84   -373       C  
ATOM   3572  CH2 TRP A 351      54.757  22.517  45.980  1.00 37.28           C  
ANISOU 3572  CH2 TRP A 351     5302   4310   4554   -865    138   -413       C  
ATOM   3573  N   LEU A 352      54.945  17.681  48.279  1.00 32.80           N  
ANISOU 3573  N   LEU A 352     4220   4214   4030  -1012    -41   -279       N  
ATOM   3574  CA  LEU A 352      55.555  17.512  46.962  1.00 25.72           C  
ANISOU 3574  CA  LEU A 352     3286   3286   3200   -968    -54   -226       C  
ATOM   3575  C   LEU A 352      54.967  16.298  46.246  1.00 30.67           C  
ANISOU 3575  C   LEU A 352     3826   3955   3872   -873    -78   -183       C  
ATOM   3576  O   LEU A 352      54.610  16.352  45.050  1.00 29.22           O  
ANISOU 3576  O   LEU A 352     3649   3725   3730   -774    -61   -171       O  
ATOM   3577  CB  LEU A 352      57.071  17.373  47.111  1.00 21.35           C  
ANISOU 3577  CB  LEU A 352     2691   2770   2652  -1083   -100   -174       C  
ATOM   3578  CG  LEU A 352      57.945  17.289  45.863  1.00 29.14           C  
ANISOU 3578  CG  LEU A 352     3633   3744   3694  -1056    -99   -115       C  
ATOM   3579  CD1 LEU A 352      57.847  18.564  45.045  1.00 28.93           C  
ANISOU 3579  CD1 LEU A 352     3715   3606   3670  -1038    -39   -145       C  
ATOM   3580  CD2 LEU A 352      59.383  17.021  46.270  1.00 29.20           C  
ANISOU 3580  CD2 LEU A 352     3558   3837   3699  -1170   -148    -62       C  
ATOM   3581  N   VAL A 353      54.866  15.205  46.999  1.00 23.09           N  
ANISOU 3581  N   VAL A 353     2806   3075   2894   -912   -122   -158       N  
ATOM   3582  CA  VAL A 353      54.225  13.991  46.515  1.00 22.68           C  
ANISOU 3582  CA  VAL A 353     2699   3055   2863   -851   -153   -121       C  
ATOM   3583  C   VAL A 353      52.827  14.303  45.997  1.00 26.16           C  
ANISOU 3583  C   VAL A 353     3145   3482   3313   -761   -113   -159       C  
ATOM   3584  O   VAL A 353      52.454  13.870  44.908  1.00 32.49           O  
ANISOU 3584  O   VAL A 353     3930   4263   4151   -684   -129   -134       O  
ATOM   3585  CB  VAL A 353      54.146  12.916  47.616  1.00 25.04           C  
ANISOU 3585  CB  VAL A 353     2967   3428   3118   -925   -201    -98       C  
ATOM   3586  CG1 VAL A 353      53.192  11.802  47.215  1.00 19.43           C  
ANISOU 3586  CG1 VAL A 353     2230   2740   2413   -887   -226    -71       C  
ATOM   3587  CG2 VAL A 353      55.527  12.365  47.905  1.00 24.65           C  
ANISOU 3587  CG2 VAL A 353     2896   3403   3066   -977   -260    -42       C  
ATOM   3588  N   TYR A 354      52.059  15.076  46.758  1.00 25.01           N  
ANISOU 3588  N   TYR A 354     3024   3352   3128   -762    -63   -221       N  
ATOM   3589  CA  TYR A 354      50.723  15.433  46.286  1.00 27.00           C  
ANISOU 3589  CA  TYR A 354     3259   3614   3386   -656    -23   -255       C  
ATOM   3590  C   TYR A 354      50.777  16.403  45.105  1.00 30.93           C  
ANISOU 3590  C   TYR A 354     3819   4015   3919   -551      1   -268       C  
ATOM   3591  O   TYR A 354      49.865  16.438  44.274  1.00 33.25           O  
ANISOU 3591  O   TYR A 354     4087   4312   4235   -446      3   -270       O  
ATOM   3592  CB  TYR A 354      49.889  16.024  47.424  1.00 21.21           C  
ANISOU 3592  CB  TYR A 354     2535   2933   2592   -658     38   -318       C  
ATOM   3593  CG  TYR A 354      49.529  15.001  48.476  1.00 27.15           C  
ANISOU 3593  CG  TYR A 354     3222   3793   3300   -752     22   -301       C  
ATOM   3594  CD1 TYR A 354      48.757  13.892  48.157  1.00 24.50           C  
ANISOU 3594  CD1 TYR A 354     2796   3534   2978   -758    -12   -260       C  
ATOM   3595  CD2 TYR A 354      49.967  15.137  49.784  1.00 25.20           C  
ANISOU 3595  CD2 TYR A 354     3021   3566   2987   -850     35   -324       C  
ATOM   3596  CE1 TYR A 354      48.431  12.951  49.112  1.00 34.53           C  
ANISOU 3596  CE1 TYR A 354     4027   4894   4199   -862    -25   -239       C  
ATOM   3597  CE2 TYR A 354      49.645  14.202  50.746  1.00 29.15           C  
ANISOU 3597  CE2 TYR A 354     3480   4159   3437   -941     22   -304       C  
ATOM   3598  CZ  TYR A 354      48.877  13.111  50.406  1.00 37.00           C  
ANISOU 3598  CZ  TYR A 354     4389   5224   4446   -948     -5   -260       C  
ATOM   3599  OH  TYR A 354      48.557  12.177  51.366  1.00 32.76           O  
ANISOU 3599  OH  TYR A 354     3830   4771   3848  -1056    -17   -234       O  
ATOM   3600  N   ALA A 355      51.857  17.172  45.025  1.00 32.45           N  
ANISOU 3600  N   ALA A 355     4093   4126   4111   -591     14   -271       N  
ATOM   3601  CA  ALA A 355      52.014  18.169  43.975  1.00 25.59           C  
ANISOU 3601  CA  ALA A 355     3312   3150   3261   -515     42   -280       C  
ATOM   3602  C   ALA A 355      52.201  17.500  42.621  1.00 28.47           C  
ANISOU 3602  C   ALA A 355     3642   3499   3677   -459      6   -222       C  
ATOM   3603  O   ALA A 355      51.806  18.051  41.591  1.00 29.67           O  
ANISOU 3603  O   ALA A 355     3847   3584   3842   -358     21   -225       O  
ATOM   3604  CB  ALA A 355      53.185  19.090  44.281  1.00 21.10           C  
ANISOU 3604  CB  ALA A 355     2841   2507   2670   -612     61   -290       C  
ATOM   3605  N   ASN A 356      52.809  16.315  42.626  1.00 24.24           N  
ANISOU 3605  N   ASN A 356     3034   3017   3159   -517    -41   -169       N  
ATOM   3606  CA  ASN A 356      52.962  15.533  41.393  1.00 28.10           C  
ANISOU 3606  CA  ASN A 356     3505   3489   3682   -457    -74   -117       C  
ATOM   3607  C   ASN A 356      51.649  15.379  40.604  1.00 34.11           C  
ANISOU 3607  C   ASN A 356     4261   4250   4451   -352    -90   -126       C  
ATOM   3608  O   ASN A 356      51.601  15.565  39.367  1.00 46.71           O  
ANISOU 3608  O   ASN A 356     5903   5783   6061   -270    -94   -109       O  
ATOM   3609  CB  ASN A 356      53.531  14.152  41.728  1.00 30.34           C  
ANISOU 3609  CB  ASN A 356     3727   3834   3967   -514   -127    -67       C  
ATOM   3610  CG  ASN A 356      53.802  13.319  40.493  1.00 35.55           C  
ANISOU 3610  CG  ASN A 356     4398   4464   4647   -446   -157    -16       C  
ATOM   3611  OD1 ASN A 356      54.878  13.400  39.903  1.00 46.44           O  
ANISOU 3611  OD1 ASN A 356     5792   5815   6039   -435   -139     17       O  
ATOM   3612  ND2 ASN A 356      52.825  12.511  40.095  1.00 24.25           N  
ANISOU 3612  ND2 ASN A 356     2961   3043   3211   -407   -200    -10       N  
ATOM   3613  N   SER A 357      50.589  15.049  41.341  1.00 28.28           N  
ANISOU 3613  N   SER A 357     3459   3592   3695   -360   -101   -151       N  
ATOM   3614  CA  SER A 357      49.256  14.849  40.780  1.00 40.18           C  
ANISOU 3614  CA  SER A 357     4923   5140   5205   -280   -125   -157       C  
ATOM   3615  C   SER A 357      48.739  16.081  40.044  1.00 41.85           C  
ANISOU 3615  C   SER A 357     5189   5291   5420   -153    -92   -189       C  
ATOM   3616  O   SER A 357      47.980  15.965  39.082  1.00 42.10           O  
ANISOU 3616  O   SER A 357     5208   5327   5460    -67   -128   -177       O  
ATOM   3617  CB  SER A 357      48.271  14.466  41.886  1.00 44.13           C  
ANISOU 3617  CB  SER A 357     5329   5760   5678   -328   -122   -180       C  
ATOM   3618  OG  SER A 357      48.666  13.268  42.531  1.00 52.54           O  
ANISOU 3618  OG  SER A 357     6363   6870   6729   -446   -161   -144       O  
ATOM   3619  N   ALA A 358      49.138  17.259  40.509  1.00 37.26           N  
ANISOU 3619  N   ALA A 358     4686   4649   4823   -143    -31   -229       N  
ATOM   3620  CA  ALA A 358      48.757  18.497  39.845  1.00 40.22           C  
ANISOU 3620  CA  ALA A 358     5156   4938   5189    -17      2   -258       C  
ATOM   3621  C   ALA A 358      49.733  18.807  38.719  1.00 33.47           C  
ANISOU 3621  C   ALA A 358     4407   3964   4348    -13      0   -221       C  
ATOM   3622  O   ALA A 358      49.403  19.526  37.776  1.00 41.12           O  
ANISOU 3622  O   ALA A 358     5461   4854   5310     96      4   -223       O  
ATOM   3623  CB  ALA A 358      48.704  19.647  40.840  1.00 32.53           C  
ANISOU 3623  CB  ALA A 358     4258   3929   4175     -8     68   -320       C  
ATOM   3624  N   ALA A 359      50.937  18.254  38.822  1.00 29.65           N  
ANISOU 3624  N   ALA A 359     3915   3476   3876   -128     -4   -185       N  
ATOM   3625  CA  ALA A 359      51.972  18.488  37.824  1.00 28.05           C  
ANISOU 3625  CA  ALA A 359     3791   3186   3681   -138      9   -145       C  
ATOM   3626  C   ALA A 359      51.648  17.813  36.497  1.00 32.38           C  
ANISOU 3626  C   ALA A 359     4339   3722   4241    -53    -32   -105       C  
ATOM   3627  O   ALA A 359      51.854  18.406  35.440  1.00 33.45           O  
ANISOU 3627  O   ALA A 359     4574   3768   4367      5    -14    -89       O  
ATOM   3628  CB  ALA A 359      53.322  18.012  38.334  1.00 22.21           C  
ANISOU 3628  CB  ALA A 359     3010   2480   2950   -270     16   -113       C  
ATOM   3629  N   ASN A 360      51.149  16.580  36.540  1.00 26.11           N  
ANISOU 3629  N   ASN A 360     3453   3009   3458    -56    -89    -87       N  
ATOM   3630  CA  ASN A 360      50.915  15.852  35.282  1.00 23.00           C  
ANISOU 3630  CA  ASN A 360     3082   2594   3062      7   -138    -50       C  
ATOM   3631  C   ASN A 360      50.027  16.567  34.228  1.00 30.20           C  
ANISOU 3631  C   ASN A 360     4063   3451   3959    132   -155    -59       C  
ATOM   3632  O   ASN A 360      50.440  16.700  33.066  1.00 31.65           O  
ANISOU 3632  O   ASN A 360     4342   3555   4129    180   -151    -30       O  
ATOM   3633  CB  ASN A 360      50.336  14.465  35.578  1.00 23.14           C  
ANISOU 3633  CB  ASN A 360     3014   2698   3080    -31   -208    -35       C  
ATOM   3634  CG  ASN A 360      51.354  13.532  36.187  1.00 24.96           C  
ANISOU 3634  CG  ASN A 360     3216   2954   3313   -121   -208     -7       C  
ATOM   3635  OD1 ASN A 360      52.555  13.689  35.975  1.00 31.04           O  
ANISOU 3635  OD1 ASN A 360     4021   3685   4088   -133   -168     16       O  
ATOM   3636  ND2 ASN A 360      50.882  12.552  36.949  1.00 46.18           N  
ANISOU 3636  ND2 ASN A 360     5838   5715   5993   -184   -255     -4       N  
ATOM   3637  N   PRO A 361      48.818  17.033  34.612  1.00 27.37           N  
ANISOU 3637  N   PRO A 361     3659   3142   3598    194   -171    -96       N  
ATOM   3638  CA  PRO A 361      47.957  17.626  33.575  1.00 24.19           C  
ANISOU 3638  CA  PRO A 361     3312   2700   3178    330   -203    -97       C  
ATOM   3639  C   PRO A 361      48.531  18.874  32.883  1.00 29.86           C  
ANISOU 3639  C   PRO A 361     4194   3277   3875    395   -150    -97       C  
ATOM   3640  O   PRO A 361      48.321  19.042  31.676  1.00 34.05           O  
ANISOU 3640  O   PRO A 361     4810   3744   4383    481   -182    -72       O  
ATOM   3641  CB  PRO A 361      46.679  17.984  34.345  1.00 23.69           C  
ANISOU 3641  CB  PRO A 361     3147   2738   3115    392   -212   -139       C  
ATOM   3642  CG  PRO A 361      46.684  17.086  35.534  1.00 21.03           C  
ANISOU 3642  CG  PRO A 361     2685   2514   2793    267   -210   -146       C  
ATOM   3643  CD  PRO A 361      48.127  16.972  35.914  1.00 27.51           C  
ANISOU 3643  CD  PRO A 361     3566   3266   3620    158   -164   -134       C  
ATOM   3644  N   ILE A 362      49.240  19.731  33.616  1.00 23.82           N  
ANISOU 3644  N   ILE A 362     3488   2457   3106    343    -76   -121       N  
ATOM   3645  CA  ILE A 362      49.828  20.917  32.992  1.00 37.54           C  
ANISOU 3645  CA  ILE A 362     5402   4050   4813    373    -25   -115       C  
ATOM   3646  C   ILE A 362      50.999  20.519  32.086  1.00 31.29           C  
ANISOU 3646  C   ILE A 362     4664   3206   4017    304     -6    -60       C  
ATOM   3647  O   ILE A 362      51.277  21.184  31.078  1.00 38.32           O  
ANISOU 3647  O   ILE A 362     5698   3988   4873    348     16    -36       O  
ATOM   3648  CB  ILE A 362      50.285  21.959  34.045  1.00 40.78           C  
ANISOU 3648  CB  ILE A 362     5882   4407   5208    310     43   -157       C  
ATOM   3649  CG1 ILE A 362      49.098  22.544  34.805  1.00 51.32           C  
ANISOU 3649  CG1 ILE A 362     7141   5794   6563    134     71   -147       C  
ATOM   3650  CG2 ILE A 362      51.078  23.075  33.379  1.00 42.50           C  
ANISOU 3650  CG2 ILE A 362     6056   4677   5417    403     39   -215       C  
ATOM   3651  CD1 ILE A 362      49.499  23.360  36.012  1.00 60.69           C  
ANISOU 3651  CD1 ILE A 362     8384   6948   7727     54    119   -193       C  
ATOM   3652  N   ILE A 363      51.667  19.422  32.437  1.00 20.69           N  
ANISOU 3652  N   ILE A 363     3213   1946   2702    206    -11    -38       N  
ATOM   3653  CA  ILE A 363      52.681  18.836  31.571  1.00 20.41           C  
ANISOU 3653  CA  ILE A 363     3203   1891   2660    171      9     15       C  
ATOM   3654  C   ILE A 363      52.039  18.439  30.252  1.00 35.06           C  
ANISOU 3654  C   ILE A 363     5121   3712   4489    283    -43     38       C  
ATOM   3655  O   ILE A 363      52.563  18.754  29.184  1.00 28.36           O  
ANISOU 3655  O   ILE A 363     4388   2783   3606    310    -10     71       O  
ATOM   3656  CB  ILE A 363      53.350  17.601  32.205  1.00 23.82           C  
ANISOU 3656  CB  ILE A 363     3508   2422   3120     86     -1     33       C  
ATOM   3657  CG1 ILE A 363      54.216  18.008  33.397  1.00 25.92           C  
ANISOU 3657  CG1 ILE A 363     3721   2724   3403    -37     46     22       C  
ATOM   3658  CG2 ILE A 363      54.193  16.860  31.175  1.00 19.61           C  
ANISOU 3658  CG2 ILE A 363     3004   1876   2571    101     15     86       C  
ATOM   3659  CD1 ILE A 363      54.822  16.830  34.129  1.00 25.53           C  
ANISOU 3659  CD1 ILE A 363     3548   2776   3376   -106     26     41       C  
ATOM   3660  N   TYR A 364      50.897  17.756  30.330  1.00 32.67           N  
ANISOU 3660  N   TYR A 364     4744   3474   4194    335   -127     22       N  
ATOM   3661  CA  TYR A 364      50.148  17.396  29.124  1.00 25.34           C  
ANISOU 3661  CA  TYR A 364     3874   2522   3233    431   -198     41       C  
ATOM   3662  C   TYR A 364      49.740  18.635  28.339  1.00 26.48           C  
ANISOU 3662  C   TYR A 364     4151   2569   3342    538   -192     39       C  
ATOM   3663  O   TYR A 364      49.678  18.614  27.107  1.00 27.43           O  
ANISOU 3663  O   TYR A 364     4381   2623   3416    604   -219     69       O  
ATOM   3664  CB  TYR A 364      48.894  16.593  29.465  1.00 26.80           C  
ANISOU 3664  CB  TYR A 364     3941   2813   3431    444   -296     25       C  
ATOM   3665  CG  TYR A 364      49.142  15.340  30.263  1.00 31.64           C  
ANISOU 3665  CG  TYR A 364     4446   3510   4066    337   -314     29       C  
ATOM   3666  CD1 TYR A 364      50.373  14.697  30.232  1.00 31.16           C  
ANISOU 3666  CD1 TYR A 364     4414   3423   4005    277   -272     56       C  
ATOM   3667  CD2 TYR A 364      48.138  14.799  31.051  1.00 21.72           C  
ANISOU 3667  CD2 TYR A 364     3061   2365   2825    301   -373      9       C  
ATOM   3668  CE1 TYR A 364      50.592  13.549  30.971  1.00 25.44           C  
ANISOU 3668  CE1 TYR A 364     3611   2762   3291    197   -296     63       C  
ATOM   3669  CE2 TYR A 364      48.347  13.663  31.791  1.00 19.59           C  
ANISOU 3669  CE2 TYR A 364     2721   2158   2566    197   -393     17       C  
ATOM   3670  CZ  TYR A 364      49.571  13.037  31.746  1.00 22.30           C  
ANISOU 3670  CZ  TYR A 364     3113   2454   2904    151   -359     44       C  
ATOM   3671  OH  TYR A 364      49.769  11.897  32.486  1.00 27.38           O  
ANISOU 3671  OH  TYR A 364     3706   3148   3549     64   -386     55       O  
ATOM   3672  N   ASN A 365      49.446  19.711  29.058  1.00 21.98           N  
ANISOU 3672  N   ASN A 365     3590   1979   2780    562   -158      4       N  
ATOM   3673  CA  ASN A 365      49.043  20.947  28.409  1.00 28.19           C  
ANISOU 3673  CA  ASN A 365     4528   2657   3525    678   -153      1       C  
ATOM   3674  C   ASN A 365      50.176  21.544  27.582  1.00 29.18           C  
ANISOU 3674  C   ASN A 365     4828   2649   3609    639    -81     39       C  
ATOM   3675  O   ASN A 365      49.968  21.959  26.442  1.00 35.21           O  
ANISOU 3675  O   ASN A 365     5734   3323   4320    728   -101     65       O  
ATOM   3676  CB  ASN A 365      48.558  21.962  29.442  1.00 25.92           C  
ANISOU 3676  CB  ASN A 365     4238   2364   3245    718   -123    -49       C  
ATOM   3677  CG  ASN A 365      48.079  23.249  28.807  1.00 34.96           C  
ANISOU 3677  CG  ASN A 365     5563   3382   4337    864   -123    -53       C  
ATOM   3678  OD1 ASN A 365      46.942  23.342  28.343  1.00 37.66           O  
ANISOU 3678  OD1 ASN A 365     5890   3757   4665   1017   -198    -56       O  
ATOM   3679  ND2 ASN A 365      48.948  24.253  28.780  1.00 52.01           N  
ANISOU 3679  ND2 ASN A 365     7900   5400   6463    813    -45    -50       N  
ATOM   3680  N   PHE A 366      51.378  21.574  28.148  1.00 32.34           N  
ANISOU 3680  N   PHE A 366     5214   3048   4026    499      1     45       N  
ATOM   3681  CA  PHE A 366      52.500  22.210  27.458  1.00 38.93           C  
ANISOU 3681  CA  PHE A 366     6194   3779   4820    436     83     85       C  
ATOM   3682  C   PHE A 366      53.208  21.296  26.456  1.00 36.61           C  
ANISOU 3682  C   PHE A 366     5899   3506   4507    417     99    137       C  
ATOM   3683  O   PHE A 366      53.862  21.779  25.532  1.00 36.26           O  
ANISOU 3683  O   PHE A 366     5991   3376   4409    405    158    177       O  
ATOM   3684  CB  PHE A 366      53.517  22.739  28.473  1.00 33.27           C  
ANISOU 3684  CB  PHE A 366     5456   3064   4120    281    162     75       C  
ATOM   3685  CG  PHE A 366      53.021  23.913  29.268  1.00 36.24           C  
ANISOU 3685  CG  PHE A 366     5918   3368   4484    296    168     26       C  
ATOM   3686  CD1 PHE A 366      52.700  25.105  28.639  1.00 48.74           C  
ANISOU 3686  CD1 PHE A 366     7717   4797   6005    374    179     27       C  
ATOM   3687  CD2 PHE A 366      52.881  23.828  30.643  1.00 40.43           C  
ANISOU 3687  CD2 PHE A 366     6336   3973   5052    240    164    -21       C  
ATOM   3688  CE1 PHE A 366      52.241  26.189  29.364  1.00 50.16           C  
ANISOU 3688  CE1 PHE A 366     8005   4893   6161    410    187    -21       C  
ATOM   3689  CE2 PHE A 366      52.425  24.909  31.375  1.00 40.91           C  
ANISOU 3689  CE2 PHE A 366     6498   3958   5087    268    177    -72       C  
ATOM   3690  CZ  PHE A 366      52.104  26.090  30.734  1.00 51.47           C  
ANISOU 3690  CZ  PHE A 366     8058   5137   6363    359    189    -73       C  
ATOM   3691  N   LEU A 367      53.074  19.985  26.623  1.00 36.40           N  
ANISOU 3691  N   LEU A 367     5734   3583   4512    418     52    137       N  
ATOM   3692  CA  LEU A 367      53.822  19.047  25.792  1.00 26.08           C  
ANISOU 3692  CA  LEU A 367     4435   2294   3181    411     76    180       C  
ATOM   3693  C   LEU A 367      52.941  18.177  24.896  1.00 29.59           C  
ANISOU 3693  C   LEU A 367     4915   2737   3592    514    -18    184       C  
ATOM   3694  O   LEU A 367      53.437  17.276  24.220  1.00 29.25           O  
ANISOU 3694  O   LEU A 367     4896   2700   3517    525     -8    212       O  
ATOM   3695  CB  LEU A 367      54.698  18.157  26.672  1.00 25.75           C  
ANISOU 3695  CB  LEU A 367     4238   2360   3185    316    108    184       C  
ATOM   3696  CG  LEU A 367      55.883  18.872  27.322  1.00 30.25           C  
ANISOU 3696  CG  LEU A 367     4773   2947   3773    192    205    197       C  
ATOM   3697  CD1 LEU A 367      56.632  17.939  28.259  1.00 34.83           C  
ANISOU 3697  CD1 LEU A 367     5185   3650   4399    118    214    202       C  
ATOM   3698  CD2 LEU A 367      56.816  19.421  26.256  1.00 27.71           C  
ANISOU 3698  CD2 LEU A 367     4566   2565   3396    172    298    247       C  
ATOM   3699  N   SER A 368      51.639  18.444  24.888  1.00 33.67           N  
ANISOU 3699  N   SER A 368     5436   3248   4108    593   -112    158       N  
ATOM   3700  CA  SER A 368      50.729  17.735  23.992  1.00 35.00           C  
ANISOU 3700  CA  SER A 368     5642   3419   4236    676   -219    165       C  
ATOM   3701  C   SER A 368      49.709  18.681  23.376  1.00 33.10           C  
ANISOU 3701  C   SER A 368     5499   3120   3958    791   -282    161       C  
ATOM   3702  O   SER A 368      48.913  19.296  24.084  1.00 33.90           O  
ANISOU 3702  O   SER A 368     5532   3256   4094    830   -312    130       O  
ATOM   3703  CB  SER A 368      50.010  16.605  24.728  1.00 44.92           C  
ANISOU 3703  CB  SER A 368     6744   4791   5534    641   -307    142       C  
ATOM   3704  OG  SER A 368      48.980  16.057  23.924  1.00 40.52           O  
ANISOU 3704  OG  SER A 368     6219   4243   4934    702   -427    147       O  
ATOM   3705  N   GLY A 369      49.738  18.786  22.051  1.00 34.06           N  
ANISOU 3705  N   GLY A 369     5785   3154   4003    857   -299    194       N  
ATOM   3706  CA  GLY A 369      48.842  19.667  21.327  1.00 24.99           C  
ANISOU 3706  CA  GLY A 369     4752   1939   2803    981   -367    200       C  
ATOM   3707  C   GLY A 369      47.376  19.309  21.482  1.00 38.68           C  
ANISOU 3707  C   GLY A 369     6369   3773   4554   1055   -513    179       C  
ATOM   3708  O   GLY A 369      46.533  20.188  21.674  1.00 43.61           O  
ANISOU 3708  O   GLY A 369     6984   4403   5184   1157   -554    164       O  
ATOM   3709  N   LYS A 370      47.067  18.019  21.405  1.00 24.91           N  
ANISOU 3709  N   LYS A 370     4538   2114   2813   1003   -591    179       N  
ATOM   3710  CA  LYS A 370      45.682  17.570  21.488  1.00 36.57           C  
ANISOU 3710  CA  LYS A 370     5891   3707   4298   1040   -737    166       C  
ATOM   3711  C   LYS A 370      45.088  17.843  22.869  1.00 34.05           C  
ANISOU 3711  C   LYS A 370     5369   3509   4061   1028   -728    129       C  
ATOM   3712  O   LYS A 370      43.988  18.404  22.988  1.00 52.65           O  
ANISOU 3712  O   LYS A 370     7649   5934   6422   1129   -797    118       O  
ATOM   3713  CB  LYS A 370      45.584  16.084  21.141  1.00 38.82           C  
ANISOU 3713  CB  LYS A 370     6155   4039   4556    952   -818    176       C  
ATOM   3714  CG  LYS A 370      45.902  15.776  19.686  1.00 46.04           C  
ANISOU 3714  CG  LYS A 370     7282   4843   5369    987   -851    208       C  
ATOM   3715  CD  LYS A 370      45.418  14.390  19.288  1.00 55.63           C  
ANISOU 3715  CD  LYS A 370     8496   6102   6538    917   -974    211       C  
ATOM   3716  CE  LYS A 370      45.609  14.144  17.800  1.00 52.91           C  
ANISOU 3716  CE  LYS A 370     8384   5645   6076    965  -1018    238       C  
ATOM   3717  NZ  LYS A 370      45.023  12.842  17.367  1.00 57.18           N  
ANISOU 3717  NZ  LYS A 370     8955   6215   6555    891  -1158    238       N  
ATOM   3718  N   PHE A 371      45.823  17.458  23.908  1.00 24.20           N  
ANISOU 3718  N   PHE A 371     4034   2291   2869    914   -640    110       N  
ATOM   3719  CA  PHE A 371      45.404  17.729  25.280  1.00 28.55           C  
ANISOU 3719  CA  PHE A 371     4415   2946   3487    892   -612     73       C  
ATOM   3720  C   PHE A 371      45.210  19.224  25.507  1.00 30.09           C  
ANISOU 3720  C   PHE A 371     4666   3084   3683   1009   -559     54       C  
ATOM   3721  O   PHE A 371      44.243  19.641  26.142  1.00 32.52           O  
ANISOU 3721  O   PHE A 371     4858   3483   4013   1084   -587     26       O  
ATOM   3722  CB  PHE A 371      46.420  17.178  26.282  1.00 32.18           C  
ANISOU 3722  CB  PHE A 371     4814   3421   3993    754   -522     62       C  
ATOM   3723  CG  PHE A 371      46.182  15.745  26.666  1.00 34.93           C  
ANISOU 3723  CG  PHE A 371     5047   3870   4355    647   -584     65       C  
ATOM   3724  CD1 PHE A 371      45.100  15.399  27.461  1.00 30.02           C  
ANISOU 3724  CD1 PHE A 371     4253   3391   3762    618   -646     45       C  
ATOM   3725  CD2 PHE A 371      47.049  14.746  26.247  1.00 27.87           C  
ANISOU 3725  CD2 PHE A 371     4227   2926   3438    576   -575     89       C  
ATOM   3726  CE1 PHE A 371      44.877  14.081  27.822  1.00 27.51           C  
ANISOU 3726  CE1 PHE A 371     3852   3153   3445    499   -705     53       C  
ATOM   3727  CE2 PHE A 371      46.833  13.426  26.606  1.00 24.16           C  
ANISOU 3727  CE2 PHE A 371     3689   2524   2968    480   -637     93       C  
ATOM   3728  CZ  PHE A 371      45.744  13.094  27.395  1.00 30.94           C  
ANISOU 3728  CZ  PHE A 371     4389   3513   3852    429   -705     77       C  
ATOM   3729  N   ARG A 372      46.131  20.024  24.978  1.00 35.32           N  
ANISOU 3729  N   ARG A 372     5514   3593   4311   1027   -480     69       N  
ATOM   3730  CA  ARG A 372      46.052  21.473  25.117  1.00 34.34           C  
ANISOU 3730  CA  ARG A 372     5502   3376   4170   1128   -429     54       C  
ATOM   3731  C   ARG A 372      44.799  22.017  24.447  1.00 39.91           C  
ANISOU 3731  C   ARG A 372     6237   4091   4836   1314   -531     60       C  
ATOM   3732  O   ARG A 372      44.143  22.911  24.981  1.00 46.70           O  
ANISOU 3732  O   ARG A 372     7083   4961   5700   1433   -525     31       O  
ATOM   3733  CB  ARG A 372      47.295  22.144  24.529  1.00 25.65           C  
ANISOU 3733  CB  ARG A 372     4612   2108   3027   1082   -333     82       C  
ATOM   3734  CG  ARG A 372      47.266  23.660  24.607  1.00 26.72           C  
ANISOU 3734  CG  ARG A 372     4913   2112   3127   1169   -284     70       C  
ATOM   3735  CD  ARG A 372      48.616  24.273  24.272  1.00 43.66           C  
ANISOU 3735  CD  ARG A 372     7244   4111   5235   1063   -173     98       C  
ATOM   3736  NE  ARG A 372      49.068  23.936  22.925  1.00 51.58           N  
ANISOU 3736  NE  ARG A 372     8367   5052   6178   1058   -179    152       N  
ATOM   3737  CZ  ARG A 372      49.994  23.022  22.654  1.00 53.86           C  
ANISOU 3737  CZ  ARG A 372     8610   5381   6475    940   -134    179       C  
ATOM   3738  NH1 ARG A 372      50.572  22.348  23.639  1.00 54.49           N  
ANISOU 3738  NH1 ARG A 372     8521   5560   6622    817    -90    159       N  
ATOM   3739  NH2 ARG A 372      50.342  22.781  21.397  1.00 47.00           N  
ANISOU 3739  NH2 ARG A 372     7870   4450   5537    957   -131    224       N  
ATOM   3740  N   GLU A 373      44.466  21.471  23.281  1.00 38.80           N  
ANISOU 3740  N   GLU A 373     6142   3951   4649   1349   -627     97       N  
ATOM   3741  CA  GLU A 373      43.287  21.920  22.548  1.00 38.25           C  
ANISOU 3741  CA  GLU A 373     6095   3905   4535   1526   -744    111       C  
ATOM   3742  C   GLU A 373      42.000  21.558  23.287  1.00 36.41           C  
ANISOU 3742  C   GLU A 373     5607   3879   4349   1575   -828     86       C  
ATOM   3743  O   GLU A 373      41.053  22.348  23.325  1.00 41.28           O  
ANISOU 3743  O   GLU A 373     6192   4539   4953   1750   -873     78       O  
ATOM   3744  CB  GLU A 373      43.268  21.329  21.137  1.00 42.48           C  
ANISOU 3744  CB  GLU A 373     6742   4398   4999   1528   -837    157       C  
ATOM   3745  CG  GLU A 373      42.051  21.733  20.317  1.00 57.35           C  
ANISOU 3745  CG  GLU A 373     8646   6318   6829   1706   -980    178       C  
ATOM   3746  CD  GLU A 373      41.884  23.238  20.223  1.00 82.24           C  
ANISOU 3746  CD  GLU A 373    11949   9354   9946   1887   -947    179       C  
ATOM   3747  OE1 GLU A 373      42.869  23.927  19.883  1.00 89.17           O  
ANISOU 3747  OE1 GLU A 373    13055  10044  10782   1867   -846    193       O  
ATOM   3748  OE2 GLU A 373      40.767  23.732  20.493  1.00 87.04           O  
ANISOU 3748  OE2 GLU A 373    12451  10058  10561   2050  -1019    167       O  
ATOM   3749  N   GLU A 374      41.960  20.369  23.878  1.00 38.14           N  
ANISOU 3749  N   GLU A 374     5647   4230   4616   1424   -845     76       N  
ATOM   3750  CA  GLU A 374      40.765  19.967  24.613  1.00 41.66           C  
ANISOU 3750  CA  GLU A 374     5840   4890   5101   1438   -913     58       C  
ATOM   3751  C   GLU A 374      40.617  20.758  25.915  1.00 43.24           C  
ANISOU 3751  C   GLU A 374     5950   5134   5346   1495   -812     11       C  
ATOM   3752  O   GLU A 374      39.502  21.129  26.298  1.00 54.79           O  
ANISOU 3752  O   GLU A 374     7264   6736   6816   1622   -850     -3       O  
ATOM   3753  CB  GLU A 374      40.783  18.463  24.890  1.00 44.67           C  
ANISOU 3753  CB  GLU A 374     6085   5381   5506   1243   -959     65       C  
ATOM   3754  CG  GLU A 374      40.735  17.611  23.627  1.00 61.92           C  
ANISOU 3754  CG  GLU A 374     8361   7535   7632   1194  -1076    105       C  
ATOM   3755  CD  GLU A 374      39.636  18.040  22.664  1.00 78.95           C  
ANISOU 3755  CD  GLU A 374    10518   9743   9737   1344  -1214    131       C  
ATOM   3756  OE1 GLU A 374      38.520  18.362  23.128  1.00 86.11           O  
ANISOU 3756  OE1 GLU A 374    11233  10817  10668   1432  -1266    122       O  
ATOM   3757  OE2 GLU A 374      39.891  18.057  21.439  1.00 78.19           O  
ANISOU 3757  OE2 GLU A 374    10611   9528   9571   1381  -1269    161       O  
ATOM   3758  N   PHE A 375      41.737  21.026  26.583  1.00 34.12           N  
ANISOU 3758  N   PHE A 375     4885   3866   4212   1404   -684    -11       N  
ATOM   3759  CA  PHE A 375      41.736  21.893  27.760  1.00 28.27           C  
ANISOU 3759  CA  PHE A 375     4120   3125   3494   1453   -583    -59       C  
ATOM   3760  C   PHE A 375      41.233  23.277  27.372  1.00 33.19           C  
ANISOU 3760  C   PHE A 375     4879   3658   4071   1682   -584    -67       C  
ATOM   3761  O   PHE A 375      40.516  23.930  28.129  1.00 33.52           O  
ANISOU 3761  O   PHE A 375     4849   3769   4117   1812   -555   -104       O  
ATOM   3762  CB  PHE A 375      43.136  22.003  28.375  1.00 32.03           C  
ANISOU 3762  CB  PHE A 375     4704   3478   3988   1303   -463    -75       C  
ATOM   3763  CG  PHE A 375      43.669  20.710  28.926  1.00 47.13           C  
ANISOU 3763  CG  PHE A 375     6489   5475   5943   1103   -455    -70       C  
ATOM   3764  CD1 PHE A 375      42.815  19.672  29.262  1.00 42.25           C  
ANISOU 3764  CD1 PHE A 375     5665   5039   5350   1053   -528    -68       C  
ATOM   3765  CD2 PHE A 375      45.032  20.535  29.109  1.00 51.30           C  
ANISOU 3765  CD2 PHE A 375     7106   5906   6481    963   -377    -63       C  
ATOM   3766  CE1 PHE A 375      43.310  18.484  29.767  1.00 39.83           C  
ANISOU 3766  CE1 PHE A 375     5276   4788   5070    875   -525    -60       C  
ATOM   3767  CE2 PHE A 375      45.532  19.350  29.614  1.00 42.18           C  
ANISOU 3767  CE2 PHE A 375     5846   4823   5357    805   -375    -55       C  
ATOM   3768  CZ  PHE A 375      44.671  18.324  29.944  1.00 42.64           C  
ANISOU 3768  CZ  PHE A 375     5732   5036   5435    764   -449    -54       C  
ATOM   3769  N   LYS A 376      41.622  23.710  26.178  1.00 35.01           N  
ANISOU 3769  N   LYS A 376     5322   3731   4249   1737   -612    -30       N  
ATOM   3770  CA  LYS A 376      41.204  24.992  25.633  1.00 40.60           C  
ANISOU 3770  CA  LYS A 376     6206   4322   4897   1957   -626    -26       C  
ATOM   3771  C   LYS A 376      39.692  25.025  25.439  1.00 46.44           C  
ANISOU 3771  C   LYS A 376     6780   5236   5630   2157   -741    -21       C  
ATOM   3772  O   LYS A 376      39.028  25.985  25.830  1.00 51.45           O  
ANISOU 3772  O   LYS A 376     7427   5877   6246   2359   -724    -48       O  
ATOM   3773  CB  LYS A 376      41.924  25.255  24.308  1.00 49.42           C  
ANISOU 3773  CB  LYS A 376     7578   5249   5949   1947   -642     23       C  
ATOM   3774  CG  LYS A 376      41.822  26.676  23.795  1.00 59.63           C  
ANISOU 3774  CG  LYS A 376     9129   6361   7168   2137   -631     31       C  
ATOM   3775  CD  LYS A 376      43.088  27.058  23.052  1.00 64.29           C  
ANISOU 3775  CD  LYS A 376     9978   6746   7704   2006   -557     64       C  
ATOM   3776  CE  LYS A 376      44.307  26.913  23.956  1.00 69.70           C  
ANISOU 3776  CE  LYS A 376    10675   7375   8434   1805   -429     40       C  
ATOM   3777  NZ  LYS A 376      45.581  27.281  23.271  1.00 72.11           N  
ANISOU 3777  NZ  LYS A 376    11201   7511   8687   1666   -348     78       N  
ATOM   3778  N   ALA A 377      39.153  23.967  24.840  1.00 51.60           N  
ANISOU 3778  N   ALA A 377     7280   6034   6292   2100   -860     13       N  
ATOM   3779  CA  ALA A 377      37.714  23.862  24.620  1.00 52.03           C  
ANISOU 3779  CA  ALA A 377     7136   6293   6341   2255   -986     27       C  
ATOM   3780  C   ALA A 377      36.951  23.828  25.942  1.00 54.38           C  
ANISOU 3780  C   ALA A 377     7173   6797   6691   2290   -939    -17       C  
ATOM   3781  O   ALA A 377      35.835  24.340  26.039  1.00 63.74           O  
ANISOU 3781  O   ALA A 377     8231   8121   7865   2500   -985    -20       O  
ATOM   3782  CB  ALA A 377      37.395  22.625  23.792  1.00 42.86           C  
ANISOU 3782  CB  ALA A 377     5869   5242   5173   2129  -1125     71       C  
ATOM   3783  N   ALA A 378      37.563  23.228  26.959  1.00 43.61           N  
ANISOU 3783  N   ALA A 378     5731   5459   5378   2091   -844    -47       N  
ATOM   3784  CA  ALA A 378      36.927  23.103  28.267  1.00 44.19           C  
ANISOU 3784  CA  ALA A 378     5570   5727   5493   2092   -785    -88       C  
ATOM   3785  C   ALA A 378      36.699  24.456  28.941  1.00 49.04           C  
ANISOU 3785  C   ALA A 378     6264   6283   6084   2314   -687   -136       C  
ATOM   3786  O   ALA A 378      35.597  24.748  29.404  1.00 61.56           O  
ANISOU 3786  O   ALA A 378     7668   8054   7670   2484   -693   -152       O  
ATOM   3787  CB  ALA A 378      37.761  22.206  29.169  1.00 46.27           C  
ANISOU 3787  CB  ALA A 378     5781   5997   5802   1830   -707   -107       C  
ATOM   3788  N   PHE A 379      37.744  25.277  28.991  1.00 52.41           N  
ANISOU 3788  N   PHE A 379     6971   6457   6486   2311   -595   -157       N  
ATOM   3789  CA  PHE A 379      37.697  26.544  29.719  1.00 57.73           C  
ANISOU 3789  CA  PHE A 379     7778   7031   7125   2486   -492   -210       C  
ATOM   3790  C   PHE A 379      37.069  27.691  28.931  1.00 65.26           C  
ANISOU 3790  C   PHE A 379     8891   7893   8013   2788   -541   -197       C  
ATOM   3791  O   PHE A 379      37.145  28.845  29.351  1.00 71.26           O  
ANISOU 3791  O   PHE A 379     9843   8508   8725   2946   -462   -238       O  
ATOM   3792  CB  PHE A 379      39.106  26.954  30.157  1.00 49.19           C  
ANISOU 3792  CB  PHE A 379     6941   5715   6035   2325   -380   -236       C  
ATOM   3793  CG  PHE A 379      39.544  26.336  31.452  1.00 56.01           C  
ANISOU 3793  CG  PHE A 379     7670   6665   6944   2125   -294   -275       C  
ATOM   3794  CD1 PHE A 379      39.012  26.771  32.655  1.00 63.61           C  
ANISOU 3794  CD1 PHE A 379     8556   7715   7898   2218   -214   -334       C  
ATOM   3795  CD2 PHE A 379      40.496  25.330  31.470  1.00 45.98           C  
ANISOU 3795  CD2 PHE A 379     6365   5388   5715   1859   -293   -252       C  
ATOM   3796  CE1 PHE A 379      39.413  26.209  33.852  1.00 60.64           C  
ANISOU 3796  CE1 PHE A 379     8072   7415   7552   2032   -140   -368       C  
ATOM   3797  CE2 PHE A 379      40.903  24.764  32.664  1.00 48.37           C  
ANISOU 3797  CE2 PHE A 379     6558   5768   6053   1686   -224   -283       C  
ATOM   3798  CZ  PHE A 379      40.361  25.204  33.856  1.00 54.33           C  
ANISOU 3798  CZ  PHE A 379     7240   6607   6797   1764   -150   -340       C  
ATOM   3799  N   SER A 380      36.452  27.382  27.796  1.00 69.79           N  
ANISOU 3799  N   SER A 380     9403   8540   8574   2870   -678   -141       N  
ATOM   3800  CA  SER A 380      35.823  28.415  26.980  1.00 77.75           C  
ANISOU 3800  CA  SER A 380    10547   9481   9512   3091   -727   -121       C  
ATOM   3801  C   SER A 380      34.389  28.693  27.425  1.00 89.66           C  
ANISOU 3801  C   SER A 380    11813  11235  11020   3291   -744   -135       C  
ATOM   3802  O   SER A 380      33.459  27.980  27.046  1.00 89.41           O  
ANISOU 3802  O   SER A 380    11518  11441  11012   3315   -857    -99       O  
ATOM   3803  CB  SER A 380      35.850  28.020  25.503  1.00 76.72           C  
ANISOU 3803  CB  SER A 380    10482   9314   9354   3043   -856    -53       C  
ATOM   3804  OG  SER A 380      37.175  28.037  25.002  1.00 76.29           O  
ANISOU 3804  OG  SER A 380    10694   9015   9280   2877   -814    -38       O  
ATOM   3805  N   CYS A 381      34.221  29.736  28.232  1.00 94.89           N  
ANISOU 3805  N   CYS A 381    12568  11839  11646   3419   -632   -186       N  
ATOM   3806  CA  CYS A 381      32.907  30.128  28.728  1.00 91.36           C  
ANISOU 3806  CA  CYS A 381    11916  11609  11187   3623   -623   -202       C  
ATOM   3807  C   CYS A 381      32.396  31.365  27.998  1.00 95.11           C  
ANISOU 3807  C   CYS A 381    12585  11977  11577   3824   -649   -187       C  
ATOM   3808  O   CYS A 381      33.041  32.413  28.012  1.00 99.38           O  
ANISOU 3808  O   CYS A 381    13448  12263  12050   3848   -579   -209       O  
ATOM   3809  CB  CYS A 381      32.955  30.390  30.235  1.00 91.03           C  
ANISOU 3809  CB  CYS A 381    11830  11603  11153   3646   -476   -273       C  
ATOM   3810  SG  CYS A 381      33.460  28.967  31.231  1.00 91.72           S  
ANISOU 3810  SG  CYS A 381    11670  11847  11331   3428   -436   -299       S  
TER    3811      CYS A 381                                                      
HETATM 3812  C1  SUV A2001      51.065   6.873  55.061  1.00 28.86           C  
HETATM 3813  N1  SUV A2001      51.928   5.873  54.855  1.00 29.78           N  
HETATM 3814  O1  SUV A2001      50.274   7.311  54.118  1.00 31.92           O  
HETATM 3815 CL1  SUV A2001      47.586  11.394  57.073  1.00 41.55          CL  
HETATM 3816  N2  SUV A2001      50.868   7.553  56.183  1.00 34.08           N  
HETATM 3817  O2  SUV A2001      55.542   8.030  54.017  1.00 34.54           O  
HETATM 3818  C3  SUV A2001      49.914   8.446  55.906  1.00 34.98           C  
HETATM 3819  N3  SUV A2001      54.068   6.441  53.433  1.00 36.48           N  
HETATM 3820  C4  SUV A2001      49.332   9.378  56.660  1.00 21.58           C  
HETATM 3821  N4  SUV A2001      54.727   8.096  50.464  1.00 40.50           N  
HETATM 3822  C5  SUV A2001      48.345  10.192  56.121  1.00 22.65           C  
HETATM 3823  N5  SUV A2001      54.437   7.845  49.303  1.00 45.50           N  
HETATM 3824  C6  SUV A2001      47.973  10.028  54.796  1.00 30.72           C  
HETATM 3825  N6  SUV A2001      55.807   7.587  50.753  1.00 38.01           N  
HETATM 3826  C7  SUV A2001      48.611   9.044  54.061  1.00 28.58           C  
HETATM 3827  C8  SUV A2001      49.552   8.289  54.626  1.00 32.15           C  
HETATM 3828  C11 SUV A2001      51.895   5.284  53.512  1.00 27.27           C  
HETATM 3829  C12 SUV A2001      52.842   6.111  52.661  1.00 31.25           C  
HETATM 3830  C14 SUV A2001      54.848   5.528  54.313  1.00 29.80           C  
HETATM 3831  C15 SUV A2001      53.978   4.624  55.193  1.00 21.84           C  
HETATM 3832  C16 SUV A2001      52.881   5.438  55.890  1.00 20.33           C  
HETATM 3833  C17 SUV A2001      54.550   7.695  53.369  1.00 37.43           C  
HETATM 3834  C19 SUV A2001      53.863   8.668  52.642  1.00 35.50           C  
HETATM 3835  C20 SUV A2001      53.959   8.848  51.254  1.00 36.96           C  
HETATM 3836  C21 SUV A2001      53.213   9.857  50.648  1.00 23.40           C  
HETATM 3837  C22 SUV A2001      52.386  10.692  51.393  1.00 13.97           C  
HETATM 3838  C23 SUV A2001      52.297  10.514  52.766  1.00 21.68           C  
HETATM 3839  C24 SUV A2001      53.034   9.511  53.379  1.00 28.54           C  
HETATM 3840  C27 SUV A2001      55.382   7.090  48.757  1.00 32.50           C  
HETATM 3841  C28 SUV A2001      56.281   6.922  49.707  1.00 34.66           C  
HETATM 3842  C29 SUV A2001      51.476  11.336  53.529  1.00 31.10           C  
HETATM 3843  C30 SUV A2001      55.815   4.670  53.495  1.00 23.16           C  
HETATM 3844  C1  OLA A2002      57.305  21.848  32.533  1.00 62.33           C  
HETATM 3845  O1  OLA A2002      56.801  21.949  31.381  1.00 62.63           O1-
HETATM 3846  O2  OLA A2002      58.437  21.335  32.739  1.00 64.65           O  
HETATM 3847  C2  OLA A2002      56.491  22.381  33.767  1.00 49.19           C  
HETATM 3848  C3  OLA A2002      56.313  21.385  34.916  1.00 44.33           C  
HETATM 3849  C4  OLA A2002      55.286  21.753  36.007  1.00 34.96           C  
HETATM 3850  C5  OLA A2002      55.837  22.587  37.158  1.00 34.83           C  
HETATM 3851  C6  OLA A2002      54.819  22.881  38.240  1.00 27.64           C  
HETATM 3852  O   HOH A4001      52.671  18.070  54.208  1.00 28.11           O  
HETATM 3853  O   HOH A4002      47.791  12.018  34.054  1.00 37.41           O  
HETATM 3854  O   HOH A4003      58.583  13.753  48.186  1.00 22.37           O  
HETATM 3855  O   HOH A4004      52.581  14.807  23.372  1.00 25.65           O  
HETATM 3856  O   HOH A4005      62.961   8.826 -14.095  1.00 31.74           O  
HETATM 3857  O   HOH A4006      56.355  16.352  23.578  1.00 37.48           O  
HETATM 3858  O   HOH A4007      39.051  -1.168  58.273  1.00 37.56           O  
HETATM 3859  O   HOH A4008      38.759  -1.440  60.992  1.00 36.60           O  
HETATM 3860  O   HOH A4009      75.414  -5.861  -0.115  1.00 47.06           O  
HETATM 3861  O   HOH A4010      41.337   9.690  66.264  1.00 30.89           O  
HETATM 3862  O   HOH A4011      53.073   2.333 -15.117  1.00 34.19           O  
HETATM 3863  O   HOH A4012      69.086   0.246  -2.923  1.00 44.45           O  
HETATM 3864  O   HOH A4013      55.701   8.795 -15.802  1.00 35.96           O  
HETATM 3865  O   HOH A4014      58.200  11.931  60.967  1.00 28.73           O  
HETATM 3866  O   HOH A4015      61.285   4.144 -18.820  1.00 31.46           O  
HETATM 3867  O   HOH A4016      61.750  15.497  15.456  1.00 40.87           O  
HETATM 3868  O   HOH A4017      32.736  25.831  27.616  1.00 53.73           O  
HETATM 3869  O   HOH A4018      60.631   1.434 -20.166  1.00 38.41           O  
HETATM 3870  O   HOH A4019      49.235  15.523  21.123  1.00 35.86           O  
HETATM 3871  O   HOH A4020      69.741  -3.163   0.475  1.00 35.43           O  
HETATM 3872  O   HOH A4021      57.036   5.873  57.481  1.00 39.03           O  
HETATM 3873  O   HOH A4022      50.958   3.048  66.204  1.00 44.68           O  
HETATM 3874  O   HOH A4023      40.491   0.993  29.520  1.00 47.15           O  
HETATM 3875  O   HOH A4024      73.577  13.436 -11.583  1.00 46.38           O  
HETATM 3876  O   HOH A4025      55.853   9.838  56.024  1.00 27.64           O  
HETATM 3877  O   HOH A4026      68.859  -9.715 -23.335  1.00 56.04           O  
HETATM 3878  O   HOH A4027      49.032  10.530  24.606  1.00 44.07           O  
HETATM 3879  O   HOH A4028      55.937   6.016  31.359  1.00 25.57           O  
CONECT  619 1189                                                                
CONECT 1189  619                                                                
CONECT 3812 3813 3814 3816                                                      
CONECT 3813 3812 3828 3832                                                      
CONECT 3814 3812 3827                                                           
CONECT 3815 3822                                                                
CONECT 3816 3812 3818                                                           
CONECT 3817 3833                                                                
CONECT 3818 3816 3820 3827                                                      
CONECT 3819 3829 3830 3833                                                      
CONECT 3820 3818 3822                                                           
CONECT 3821 3823 3825 3835                                                      
CONECT 3822 3815 3820 3824                                                      
CONECT 3823 3821 3840                                                           
CONECT 3824 3822 3826                                                           
CONECT 3825 3821 3841                                                           
CONECT 3826 3824 3827                                                           
CONECT 3827 3814 3818 3826                                                      
CONECT 3828 3813 3829                                                           
CONECT 3829 3819 3828                                                           
CONECT 3830 3819 3831 3843                                                      
CONECT 3831 3830 3832                                                           
CONECT 3832 3813 3831                                                           
CONECT 3833 3817 3819 3834                                                      
CONECT 3834 3833 3835 3839                                                      
CONECT 3835 3821 3834 3836                                                      
CONECT 3836 3835 3837                                                           
CONECT 3837 3836 3838                                                           
CONECT 3838 3837 3839 3842                                                      
CONECT 3839 3834 3838                                                           
CONECT 3840 3823 3841                                                           
CONECT 3841 3825 3840                                                           
CONECT 3842 3838                                                                
CONECT 3843 3830                                                                
CONECT 3844 3845 3846 3847                                                      
CONECT 3845 3844                                                                
CONECT 3846 3844                                                                
CONECT 3847 3844 3848                                                           
CONECT 3848 3847 3849                                                           
CONECT 3849 3848 3850                                                           
CONECT 3850 3849 3851                                                           
CONECT 3851 3850                                                                
MASTER      638    0    2   21    8    0    3    6 3878    1   42   43          
END                                                                             



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